paragraph_index int64 | sec string | p_has_citation int64 | cites string | citeids list | pmid int64 | cited_id string | sentences string | all_sent_cites list | sent_len int64 | sentence_batch_index int64 | sent_has_citation float64 | qc_fail bool | cited_sentence string | cites_in_sentence list | cln_sentence string | is_cap bool | is_alpha bool | ends_wp bool | cit_qc bool | lgtm bool | __index_level_0__ int64 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
4 | DISCUSSION | 1 | 37 | [
"B40",
"B51",
"B52",
"B53",
"B37"
] | 20,562,439 | pmid-15020582|pmid-11425866|pmid-14690611|pmid-15525516|pmid-17597150 | Moreover, dissociation of (H2A-H2B) dimers has been detected in vitro by FRET over increased salt concentrations (37). | [
"40",
"51",
"52",
"53",
"37"
] | 118 | 37,316 | 1 | false | Moreover, dissociation of (H2A-H2B) dimers has been detected in vitro by FRET over increased salt concentrations. | [
"37"
] | Moreover, dissociation of (H2A-H2B) dimers has been detected in vitro by FRET over increased salt concentrations. | true | true | true | true | true | 6,398 |
4 | DISCUSSION | 1 | 40 | [
"B40",
"B51",
"B52",
"B53",
"B37"
] | 20,562,439 | pmid-15020582|pmid-11425866|pmid-14690611|pmid-15525516|pmid-17597150 | Using this technique, we found that both UV irradiated NCPs and NCPs containing a single UV lesion are significantly less stable to salt-induced dissociation (Figs. | [
"40",
"51",
"52",
"53",
"37"
] | 164 | 37,317 | 0 | false | Using this technique, we found that both UV irradiated NCPs and NCPs containing a single UV lesion are significantly less stable to salt-induced dissociation (Figs. | [] | Using this technique, we found that both UV irradiated NCPs and NCPs containing a single UV lesion are significantly less stable to salt-induced dissociation (Figs. | true | true | true | true | true | 6,398 |
4 | DISCUSSION | 1 | 40 | [
"B40",
"B51",
"B52",
"B53",
"B37"
] | 20,562,439 | pmid-15020582|pmid-11425866|pmid-14690611|pmid-15525516|pmid-17597150 | 4, 6, D and E). | [
"40",
"51",
"52",
"53",
"37"
] | 15 | 37,318 | 0 | false | 4, 6, D and E). | [] | 4, 6, D and E). | false | false | true | true | false | 6,398 |
4 | DISCUSSION | 1 | 40 | [
"B40",
"B51",
"B52",
"B53",
"B37"
] | 20,562,439 | pmid-15020582|pmid-11425866|pmid-14690611|pmid-15525516|pmid-17597150 | It is possible that, UV-damaged NCPs undergo conformational changes more easily, and/or preferentially release (H2A-H2B) dimers, with increased salt, both of which would facilitate DNA lesion access by repair proteins. | [
"40",
"51",
"52",
"53",
"37"
] | 218 | 37,319 | 0 | false | It is possible that, UV-damaged NCPs undergo conformational changes more easily, and/or preferentially release (H2A-H2B) dimers, with increased salt, both of which would facilitate DNA lesion access by repair proteins. | [] | It is possible that, UV-damaged NCPs undergo conformational changes more easily, and/or preferentially release (H2A-H2B) dimers, with increased salt, both of which would facilitate DNA lesion access by repair proteins. | true | true | true | true | true | 6,398 |
5 | DISCUSSION | 1 | 54 | [
"B54",
"B54"
] | 20,562,439 | pmid-12051916|pmid-12051916 | Enhanced unwrapping of damaged nucleosomes may provide sufficient time for passive binding of repair proteins. | [
"54",
"54"
] | 110 | 37,320 | 0 | false | Enhanced unwrapping of damaged nucleosomes may provide sufficient time for passive binding of repair proteins. | [] | Enhanced unwrapping of damaged nucleosomes may provide sufficient time for passive binding of repair proteins. | true | true | true | true | true | 6,399 |
5 | DISCUSSION | 1 | 54 | [
"B54",
"B54"
] | 20,562,439 | pmid-12051916|pmid-12051916 | Indeed, Suter and Thoma have shown that the single-subunit protein, UV photolyase, is strongly inhibited by nucleosomes in vitro, yet is capable of gaining rapid access to CPDs in nucleosomes of intact yeast cells (54). | [
"54",
"54"
] | 219 | 37,321 | 1 | false | Indeed, Suter and Thoma have shown that the single-subunit protein, UV photolyase, is strongly inhibited by nucleosomes in vitro, yet is capable of gaining rapid access to CPDs in nucleosomes of intact yeast cells. | [
"54"
] | Indeed, Suter and Thoma have shown that the single-subunit protein, UV photolyase, is strongly inhibited by nucleosomes in vitro, yet is capable of gaining rapid access to CPDs in nucleosomes of intact yeast cells. | true | true | true | true | true | 6,399 |
5 | DISCUSSION | 1 | 54 | [
"B54",
"B54"
] | 20,562,439 | pmid-12051916|pmid-12051916 | Importantly, these authors found that repair rates are slower in the central regions of nucleosome DNA and faster near the terminal ends (54). | [
"54",
"54"
] | 142 | 37,322 | 1 | false | Importantly, these authors found that repair rates are slower in the central regions of nucleosome DNA and faster near the terminal ends. | [
"54"
] | Importantly, these authors found that repair rates are slower in the central regions of nucleosome DNA and faster near the terminal ends. | true | true | true | true | true | 6,399 |
5 | DISCUSSION | 1 | 54 | [
"B54",
"B54"
] | 20,562,439 | pmid-12051916|pmid-12051916 | These observations are consistent with the intrinsic site-exposure model and the dynamic enhancement of damaged nucleosomes yielding more time for UV photolyase proteins to recognize CPDs in chromatin. | [
"54",
"54"
] | 201 | 37,323 | 0 | false | These observations are consistent with the intrinsic site-exposure model and the dynamic enhancement of damaged nucleosomes yielding more time for UV photolyase proteins to recognize CPDs in chromatin. | [] | These observations are consistent with the intrinsic site-exposure model and the dynamic enhancement of damaged nucleosomes yielding more time for UV photolyase proteins to recognize CPDs in chromatin. | true | true | true | true | true | 6,399 |
5 | DISCUSSION | 1 | 54 | [
"B54",
"B54"
] | 20,562,439 | pmid-12051916|pmid-12051916 | Access and binding to nucleosomes by UV photolyase may be possible through the spontaneous “trapping” of partially unwrapped nucleosomes, in which the terminal DNA is transiently released from the histone surface. | [
"54",
"54"
] | 213 | 37,324 | 0 | false | Access and binding to nucleosomes by UV photolyase may be possible through the spontaneous “trapping” of partially unwrapped nucleosomes, in which the terminal DNA is transiently released from the histone surface. | [] | Access and binding to nucleosomes by UV photolyase may be possible through the spontaneous “trapping” of partially unwrapped nucleosomes, in which the terminal DNA is transiently released from the histone surface. | true | true | true | true | true | 6,399 |
5 | DISCUSSION | 1 | 54 | [
"B54",
"B54"
] | 20,562,439 | pmid-12051916|pmid-12051916 | Thus, compared with nucleosome sliding or histone eviction, the site-exposure mechanism is a rapid, energy-efficient way for repair proteins to gain access to DNA lesions, at least near the ends of nucleosome DNA. | [
"54",
"54"
] | 213 | 37,325 | 0 | false | Thus, compared with nucleosome sliding or histone eviction, the site-exposure mechanism is a rapid, energy-efficient way for repair proteins to gain access to DNA lesions, at least near the ends of nucleosome DNA. | [] | Thus, compared with nucleosome sliding or histone eviction, the site-exposure mechanism is a rapid, energy-efficient way for repair proteins to gain access to DNA lesions, at least near the ends of nucleosome DNA. | true | true | true | true | true | 6,399 |
6 | DISCUSSION | 1 | 5 | [
"B5",
"B55",
"B56",
"B14",
"B20",
"B21",
"B5"
] | 20,562,439 | NA|pmid-279912|pmid-1892653|pmid-12637512|pmid-17013386|pmid-15939881|NA | Nucleotide excision repair is the main pathway used in most organisms (including human) to repair UV lesions (5), and nucleosome rearrangements occur during nucleotide excision repair in chromatin (55, 56). | [
"5",
"55",
"56",
"14",
"20",
"21",
"5"
] | 206 | 37,326 | 1 | false | Nucleotide excision repair is the main pathway used in most organisms (including human) to repair UV lesions, and nucleosome rearrangements occur during nucleotide excision repair in chromatin. | [
"5",
"55, 56"
] | Nucleotide excision repair is the main pathway used in most organisms (including human) to repair UV lesions, and nucleosome rearrangements occur during nucleotide excision repair in chromatin. | true | true | true | true | true | 6,400 |
6 | DISCUSSION | 1 | 5 | [
"B5",
"B55",
"B56",
"B14",
"B20",
"B21",
"B5"
] | 20,562,439 | NA|pmid-279912|pmid-1892653|pmid-12637512|pmid-17013386|pmid-15939881|NA | Furthermore, it has been shown that ATP-dependent chromatin remodeling factors and histone modification are involved in the DNA repair process (14, 20, 21). | [
"5",
"55",
"56",
"14",
"20",
"21",
"5"
] | 156 | 37,327 | 0 | false | Furthermore, it has been shown that ATP-dependent chromatin remodeling factors and histone modification are involved in the DNA repair process. | [
"14, 20, 21"
] | Furthermore, it has been shown that ATP-dependent chromatin remodeling factors and histone modification are involved in the DNA repair process. | true | true | true | true | true | 6,400 |
6 | DISCUSSION | 1 | 5 | [
"B5",
"B55",
"B56",
"B14",
"B20",
"B21",
"B5"
] | 20,562,439 | NA|pmid-279912|pmid-1892653|pmid-12637512|pmid-17013386|pmid-15939881|NA | However, it is unclear how these remodeling and modification factors are recruited to sites of damaged DNA associated with nucleosomes. | [
"5",
"55",
"56",
"14",
"20",
"21",
"5"
] | 135 | 37,328 | 0 | false | However, it is unclear how these remodeling and modification factors are recruited to sites of damaged DNA associated with nucleosomes. | [] | However, it is unclear how these remodeling and modification factors are recruited to sites of damaged DNA associated with nucleosomes. | true | true | true | true | true | 6,400 |
6 | DISCUSSION | 1 | 5 | [
"B5",
"B55",
"B56",
"B14",
"B20",
"B21",
"B5"
] | 20,562,439 | NA|pmid-279912|pmid-1892653|pmid-12637512|pmid-17013386|pmid-15939881|NA | Our data implies that intrinsic nucleosome dynamics, especially increased unwrapping of UV-damaged NCPs, facilitate the invasion of factors involved in repair and/or those involved in remodeling or histone modifications. | [
"5",
"55",
"56",
"14",
"20",
"21",
"5"
] | 220 | 37,329 | 0 | false | Our data implies that intrinsic nucleosome dynamics, especially increased unwrapping of UV-damaged NCPs, facilitate the invasion of factors involved in repair and/or those involved in remodeling or histone modifications. | [] | Our data implies that intrinsic nucleosome dynamics, especially increased unwrapping of UV-damaged NCPs, facilitate the invasion of factors involved in repair and/or those involved in remodeling or histone modifications. | true | true | true | true | true | 6,400 |
6 | DISCUSSION | 1 | 5 | [
"B5",
"B55",
"B56",
"B14",
"B20",
"B21",
"B5"
] | 20,562,439 | NA|pmid-279912|pmid-1892653|pmid-12637512|pmid-17013386|pmid-15939881|NA | The binding of damage specific factors should further shift the equilibrium toward the unwrapped states. | [
"5",
"55",
"56",
"14",
"20",
"21",
"5"
] | 104 | 37,330 | 0 | false | The binding of damage specific factors should further shift the equilibrium toward the unwrapped states. | [] | The binding of damage specific factors should further shift the equilibrium toward the unwrapped states. | true | true | true | true | true | 6,400 |
6 | DISCUSSION | 1 | 5 | [
"B5",
"B55",
"B56",
"B14",
"B20",
"B21",
"B5"
] | 20,562,439 | NA|pmid-279912|pmid-1892653|pmid-12637512|pmid-17013386|pmid-15939881|NA | Thus, once repair recognition factors and/or remodeling factors are recruited to the damaged nucleosomes, disruption of local chromatin structure could initiate the “cascade” of recruitment of nucleotide excision repair proteins (5). | [
"5",
"55",
"56",
"14",
"20",
"21",
"5"
] | 233 | 37,331 | 1 | false | Thus, once repair recognition factors and/or remodeling factors are recruited to the damaged nucleosomes, disruption of local chromatin structure could initiate the “cascade” of recruitment of nucleotide excision repair proteins. | [
"5"
] | Thus, once repair recognition factors and/or remodeling factors are recruited to the damaged nucleosomes, disruption of local chromatin structure could initiate the “cascade” of recruitment of nucleotide excision repair proteins. | true | true | true | true | true | 6,400 |
0 | INTRODUCTION | 1 | 1 | [
"DDQ002C1",
"DDQ002C2",
"DDQ002C3",
"DDQ002C4",
"DDQ002C5"
] | 20,053,669 | pmid-2862839|pmid-11758801|pmid-11331908|pmid-2225059|pmid-18174896|pmid-17263664|pmid-15232570|pmid-10339406|pmid-16055927|pmid-17934217|pmid-11750097|pmid-15704001|pmid-14981507|pmid-14981506|pmid-16977310 | Mitochondria are essential, complex organelles of eukaryotic organisms required for a variety of metabolic processes including the generation of energy by oxidative phosphorylation (1). | [
"1",
"2",
"3",
"4",
"5"
] | 185 | 37,332 | 1 | false | Mitochondria are essential, complex organelles of eukaryotic organisms required for a variety of metabolic processes including the generation of energy by oxidative phosphorylation. | [
"1"
] | Mitochondria are essential, complex organelles of eukaryotic organisms required for a variety of metabolic processes including the generation of energy by oxidative phosphorylation. | true | true | true | true | true | 6,401 |
0 | INTRODUCTION | 1 | 1 | [
"DDQ002C1",
"DDQ002C2",
"DDQ002C3",
"DDQ002C4",
"DDQ002C5"
] | 20,053,669 | pmid-2862839|pmid-11758801|pmid-11331908|pmid-2225059|pmid-18174896|pmid-17263664|pmid-15232570|pmid-10339406|pmid-16055927|pmid-17934217|pmid-11750097|pmid-15704001|pmid-14981507|pmid-14981506|pmid-16977310 | Normal mitochondrial function requires 500–2000 different types of proteins depending on the species. | [
"1",
"2",
"3",
"4",
"5"
] | 101 | 37,333 | 0 | false | Normal mitochondrial function requires 500–2000 different types of proteins depending on the species. | [] | Normal mitochondrial function requires 500–2000 different types of proteins depending on the species. | true | true | true | true | true | 6,401 |
0 | INTRODUCTION | 1 | 1 | [
"DDQ002C1",
"DDQ002C2",
"DDQ002C3",
"DDQ002C4",
"DDQ002C5"
] | 20,053,669 | pmid-2862839|pmid-11758801|pmid-11331908|pmid-2225059|pmid-18174896|pmid-17263664|pmid-15232570|pmid-10339406|pmid-16055927|pmid-17934217|pmid-11750097|pmid-15704001|pmid-14981507|pmid-14981506|pmid-16977310 | However, mitochondrial genome of yeast and human cells encodes only 8 and 13 proteins, respectively (2,3). | [
"1",
"2",
"3",
"4",
"5"
] | 106 | 37,334 | 0 | false | However, mitochondrial genome of yeast and human cells encodes only 8 and 13 proteins, respectively. | [
"2,3"
] | However, mitochondrial genome of yeast and human cells encodes only 8 and 13 proteins, respectively. | true | true | true | true | true | 6,401 |
0 | INTRODUCTION | 1 | 1 | [
"DDQ002C1",
"DDQ002C2",
"DDQ002C3",
"DDQ002C4",
"DDQ002C5"
] | 20,053,669 | pmid-2862839|pmid-11758801|pmid-11331908|pmid-2225059|pmid-18174896|pmid-17263664|pmid-15232570|pmid-10339406|pmid-16055927|pmid-17934217|pmid-11750097|pmid-15704001|pmid-14981507|pmid-14981506|pmid-16977310 | Thus, the vast majority of proteins that comprise mitochondria are encoded by the nuclear genome and mitochondrial function requires the import and folding of a large number of proteins synthesized on cytosolic ribosomes (4,5). | [
"1",
"2",
"3",
"4",
"5"
] | 227 | 37,335 | 0 | false | Thus, the vast majority of proteins that comprise mitochondria are encoded by the nuclear genome and mitochondrial function requires the import and folding of a large number of proteins synthesized on cytosolic ribosomes. | [
"4,5"
] | Thus, the vast majority of proteins that comprise mitochondria are encoded by the nuclear genome and mitochondrial function requires the import and folding of a large number of proteins synthesized on cytosolic ribosomes. | true | true | true | true | true | 6,401 |
1 | INTRODUCTION | 1 | 6 | [
"DDQ002C6",
"DDQ002C10",
"DDQ002C6",
"DDQ002C8",
"DDQ002C10",
"DDQ002C7",
"DDQ002C10",
"DDQ002C9",
"DDQ002C11",
"DDQ002C12",
"DDQ002C13",
"DDQ002C14",
"DDQ002C15",
"DDQ002C7",
"DDQ002C9"
] | 20,053,669 | pmid-17514892|pmid-11450972|pmid-17514892|pmid-17263664|pmid-11450972|pmid-12154367|pmid-11450972|pmid-15232570|pmid-18692467|pmid-12191765|pmid-12437924|pmid-1833391|pmid-8631295|pmid-12154367|pmid-15232570|pmid-14981507|pmid-14981506 | Owing to distinct compartmentalization into an outer and inner membrane, mitochondria have evolved an efficient system for recognition and transport of precursor proteins across membranes. | [
"6",
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"8",
"10",
"7",
"10",
"9",
"11",
"12",
"13",
"14",
"15",
"7",
"9"
] | 188 | 37,336 | 0 | false | Owing to distinct compartmentalization into an outer and inner membrane, mitochondria have evolved an efficient system for recognition and transport of precursor proteins across membranes. | [] | Owing to distinct compartmentalization into an outer and inner membrane, mitochondria have evolved an efficient system for recognition and transport of precursor proteins across membranes. | true | true | true | true | true | 6,402 |
1 | INTRODUCTION | 1 | 6 | [
"DDQ002C6",
"DDQ002C10",
"DDQ002C6",
"DDQ002C8",
"DDQ002C10",
"DDQ002C7",
"DDQ002C10",
"DDQ002C9",
"DDQ002C11",
"DDQ002C12",
"DDQ002C13",
"DDQ002C14",
"DDQ002C15",
"DDQ002C7",
"DDQ002C9"
] | 20,053,669 | pmid-17514892|pmid-11450972|pmid-17514892|pmid-17263664|pmid-11450972|pmid-12154367|pmid-11450972|pmid-15232570|pmid-18692467|pmid-12191765|pmid-12437924|pmid-1833391|pmid-8631295|pmid-12154367|pmid-15232570|pmid-14981507|pmid-14981506 | Import of nuclear encoded proteins into the mitochondrial membranes is a multistep process involving machinery of cytosol, mitochondrial membranes and mitochondrial matrix (6–10). | [
"6",
"10",
"6",
"8",
"10",
"7",
"10",
"9",
"11",
"12",
"13",
"14",
"15",
"7",
"9"
] | 179 | 37,337 | 0 | false | Import of nuclear encoded proteins into the mitochondrial membranes is a multistep process involving machinery of cytosol, mitochondrial membranes and mitochondrial matrix. | [
"6–10"
] | Import of nuclear encoded proteins into the mitochondrial membranes is a multistep process involving machinery of cytosol, mitochondrial membranes and mitochondrial matrix. | true | true | true | true | true | 6,402 |
1 | INTRODUCTION | 1 | 6 | [
"DDQ002C6",
"DDQ002C10",
"DDQ002C6",
"DDQ002C8",
"DDQ002C10",
"DDQ002C7",
"DDQ002C10",
"DDQ002C9",
"DDQ002C11",
"DDQ002C12",
"DDQ002C13",
"DDQ002C14",
"DDQ002C15",
"DDQ002C7",
"DDQ002C9"
] | 20,053,669 | pmid-17514892|pmid-11450972|pmid-17514892|pmid-17263664|pmid-11450972|pmid-12154367|pmid-11450972|pmid-15232570|pmid-18692467|pmid-12191765|pmid-12437924|pmid-1833391|pmid-8631295|pmid-12154367|pmid-15232570|pmid-14981507|pmid-14981506 | As a first step in the translocation process, the cytosolic facing receptors recognize the mitochondrial targeting sequence of a precursor protein and transfer them to the protein complex of the outer membrane, where Tom40 forms a pore and allows passage of the precursor protein through the membrane (6,8,10). | [
"6",
"10",
"6",
"8",
"10",
"7",
"10",
"9",
"11",
"12",
"13",
"14",
"15",
"7",
"9"
] | 310 | 37,338 | 0 | false | As a first step in the translocation process, the cytosolic facing receptors recognize the mitochondrial targeting sequence of a precursor protein and transfer them to the protein complex of the outer membrane, where Tom40 forms a pore and allows passage of the precursor protein through the membrane. | [
"6,8,10"
] | As a first step in the translocation process, the cytosolic facing receptors recognize the mitochondrial targeting sequence of a precursor protein and transfer them to the protein complex of the outer membrane, where Tom40 forms a pore and allows passage of the precursor protein through the membrane. | true | true | true | true | true | 6,402 |
1 | INTRODUCTION | 1 | 6 | [
"DDQ002C6",
"DDQ002C10",
"DDQ002C6",
"DDQ002C8",
"DDQ002C10",
"DDQ002C7",
"DDQ002C10",
"DDQ002C9",
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"DDQ002C12",
"DDQ002C13",
"DDQ002C14",
"DDQ002C15",
"DDQ002C7",
"DDQ002C9"
] | 20,053,669 | pmid-17514892|pmid-11450972|pmid-17514892|pmid-17263664|pmid-11450972|pmid-12154367|pmid-11450972|pmid-15232570|pmid-18692467|pmid-12191765|pmid-12437924|pmid-1833391|pmid-8631295|pmid-12154367|pmid-15232570|pmid-14981507|pmid-14981506 | After passage through TOM complex, a major portion of precursor proteins are targeted into mitochondrial matrix; and this process is mediated by presequence translocase (TIM23 complex) of the inner membrane (7–10). | [
"6",
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"8",
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"7",
"10",
"9",
"11",
"12",
"13",
"14",
"15",
"7",
"9"
] | 214 | 37,339 | 0 | false | After passage through TOM complex, a major portion of precursor proteins are targeted into mitochondrial matrix; and this process is mediated by presequence translocase (TIM23 complex) of the inner membrane. | [
"7–10"
] | After passage through TOM complex, a major portion of precursor proteins are targeted into mitochondrial matrix; and this process is mediated by presequence translocase (TIM23 complex) of the inner membrane. | true | true | true | true | true | 6,402 |
1 | INTRODUCTION | 1 | 13 | [
"DDQ002C6",
"DDQ002C10",
"DDQ002C6",
"DDQ002C8",
"DDQ002C10",
"DDQ002C7",
"DDQ002C10",
"DDQ002C9",
"DDQ002C11",
"DDQ002C12",
"DDQ002C13",
"DDQ002C14",
"DDQ002C15",
"DDQ002C7",
"DDQ002C9"
] | 20,053,669 | pmid-17514892|pmid-11450972|pmid-17514892|pmid-17263664|pmid-11450972|pmid-12154367|pmid-11450972|pmid-15232570|pmid-18692467|pmid-12191765|pmid-12437924|pmid-1833391|pmid-8631295|pmid-12154367|pmid-15232570|pmid-14981507|pmid-14981506 | The TIM23 complex consists mainly two set of components: (i) channel-forming components which include integral membrane proteins Tim23 and Tim17 that comprise the translocation channel (9,11,12) and (ii) the associated peripheral membrane protein Tim50 (13). | [
"6",
"10",
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"8",
"10",
"7",
"10",
"9",
"11",
"12",
"13",
"14",
"15",
"7",
"9"
] | 258 | 37,340 | 1 | false | The TIM23 complex consists mainly two set of components: (i) channel-forming components which include integral membrane proteins Tim23 and Tim17 that comprise the translocation channel and (ii) the associated peripheral membrane protein Tim50. | [
"9,11,12",
"13"
] | The TIM23 complex consists mainly two set of components: (i) channel-forming components which include integral membrane proteins Tim23 and Tim17 that comprise the translocation channel and (ii) the associated peripheral membrane protein Tim50. | true | true | true | true | true | 6,402 |
1 | INTRODUCTION | 1 | 6 | [
"DDQ002C6",
"DDQ002C10",
"DDQ002C6",
"DDQ002C8",
"DDQ002C10",
"DDQ002C7",
"DDQ002C10",
"DDQ002C9",
"DDQ002C11",
"DDQ002C12",
"DDQ002C13",
"DDQ002C14",
"DDQ002C15",
"DDQ002C7",
"DDQ002C9"
] | 20,053,669 | pmid-17514892|pmid-11450972|pmid-17514892|pmid-17263664|pmid-11450972|pmid-12154367|pmid-11450972|pmid-15232570|pmid-18692467|pmid-12191765|pmid-12437924|pmid-1833391|pmid-8631295|pmid-12154367|pmid-15232570|pmid-14981507|pmid-14981506 | The movement of the presequence through the inner membrane requires a membrane potential (14,15), whereas import of the rest of the protein requires translocation channel associated ‘import motor machinery’ (7,9). | [
"6",
"10",
"6",
"8",
"10",
"7",
"10",
"9",
"11",
"12",
"13",
"14",
"15",
"7",
"9"
] | 213 | 37,341 | 0 | false | The movement of the presequence through the inner membrane requires a membrane potential, whereas import of the rest of the protein requires translocation channel associated ‘import motor machinery’. | [
"14,15",
"7,9"
] | The movement of the presequence through the inner membrane requires a membrane potential, whereas import of the rest of the protein requires translocation channel associated ‘import motor machinery’. | true | true | true | true | true | 6,402 |
2 | INTRODUCTION | 1 | 8 | [
"DDQ002C8",
"DDQ002C16",
"DDQ002C20",
"DDQ002C21",
"DDQ002C23",
"DDQ002C24",
"DDQ002C25",
"DDQ002C26",
"DDQ002C24",
"DDQ002C27"
] | 20,053,669 | pmid-17263664|pmid-14981507|pmid-8246957|pmid-16943180|pmid-16790493|pmid-12677068|pmid-8408191|pmid-11733493|pmid-12677068|pmid-18426906 | The yeast import motor consists of five essential subunits namely, mtHsp70 (Ssc1), Tim44, Pam18, Pam16, Mge1 (8,16–20), and two non-essential subunits, Pam17 and Tam41 (21–23). | [
"8",
"16",
"20",
"21",
"23",
"24",
"25",
"26",
"24",
"27"
] | 176 | 37,342 | 0 | false | The yeast import motor consists of five essential subunits namely, mtHsp70 (Ssc1), Tim44, Pam18, Pam16, Mge1, and two non-essential subunits, Pam17 and Tam41. | [
"8,16–20",
"21–23"
] | The yeast import motor consists of five essential subunits namely, mtHsp70 (Ssc1), Tim44, Pam18, Pam16, Mge1, and two non-essential subunits, Pam17 and Tam41. | true | true | true | true | true | 6,403 |
2 | INTRODUCTION | 1 | 8 | [
"DDQ002C8",
"DDQ002C16",
"DDQ002C20",
"DDQ002C21",
"DDQ002C23",
"DDQ002C24",
"DDQ002C25",
"DDQ002C26",
"DDQ002C24",
"DDQ002C27"
] | 20,053,669 | pmid-17263664|pmid-14981507|pmid-8246957|pmid-16943180|pmid-16790493|pmid-12677068|pmid-8408191|pmid-11733493|pmid-12677068|pmid-18426906 | A critical core component of this machinery is the major mitochondrial 70 kDa heat shock protein (mtHsp70; Ssc1 in yeast), which binds short hydrophobic segments of incoming polypeptide chains (24,25). | [
"8",
"16",
"20",
"21",
"23",
"24",
"25",
"26",
"24",
"27"
] | 201 | 37,343 | 0 | false | A critical core component of this machinery is the major mitochondrial 70 kDa heat shock protein (mtHsp70; Ssc1 in yeast), which binds short hydrophobic segments of incoming polypeptide chains. | [
"24,25"
] | A critical core component of this machinery is the major mitochondrial 70 kDa heat shock protein (mtHsp70; Ssc1 in yeast), which binds short hydrophobic segments of incoming polypeptide chains. | true | true | true | true | true | 6,403 |
2 | INTRODUCTION | 1 | 26 | [
"DDQ002C8",
"DDQ002C16",
"DDQ002C20",
"DDQ002C21",
"DDQ002C23",
"DDQ002C24",
"DDQ002C25",
"DDQ002C26",
"DDQ002C24",
"DDQ002C27"
] | 20,053,669 | pmid-17263664|pmid-14981507|pmid-8246957|pmid-16943180|pmid-16790493|pmid-12677068|pmid-8408191|pmid-11733493|pmid-12677068|pmid-18426906 | MtHsp70 is tethered to the import channel via its interaction with an essential peripheral membrane component of the channel, Tim44 (26). | [
"8",
"16",
"20",
"21",
"23",
"24",
"25",
"26",
"24",
"27"
] | 137 | 37,344 | 1 | false | MtHsp70 is tethered to the import channel via its interaction with an essential peripheral membrane component of the channel, Tim44. | [
"26"
] | MtHsp70 is tethered to the import channel via its interaction with an essential peripheral membrane component of the channel, Tim44. | true | true | true | true | true | 6,403 |
2 | INTRODUCTION | 1 | 8 | [
"DDQ002C8",
"DDQ002C16",
"DDQ002C20",
"DDQ002C21",
"DDQ002C23",
"DDQ002C24",
"DDQ002C25",
"DDQ002C26",
"DDQ002C24",
"DDQ002C27"
] | 20,053,669 | pmid-17263664|pmid-14981507|pmid-8246957|pmid-16943180|pmid-16790493|pmid-12677068|pmid-8408191|pmid-11733493|pmid-12677068|pmid-18426906 | This interaction is destabilized upon binding a translocating precursor polypeptide (24,27). | [
"8",
"16",
"20",
"21",
"23",
"24",
"25",
"26",
"24",
"27"
] | 92 | 37,345 | 0 | false | This interaction is destabilized upon binding a translocating precursor polypeptide. | [
"24,27"
] | This interaction is destabilized upon binding a translocating precursor polypeptide. | true | true | true | true | true | 6,403 |
3 | INTRODUCTION | 1 | 28 | [
"DDQ002C28",
"DDQ002C30",
"DDQ002C16",
"DDQ002C17",
"DDQ002C31",
"DDQ002C16",
"DDQ002C17",
"DDQ002C28",
"DDQ002C30",
"DDQ002C31",
"DDQ002C33",
"DDQ002C31",
"DDQ002C34",
"DDQ002C35",
"DDQ002C36"
] | 20,053,669 | pmid-14517234|pmid-14605210|pmid-14981507|pmid-14981506|pmid-16105940|pmid-14981507|pmid-14981506|pmid-14517234|pmid-14605210|pmid-16105940|pmid-19564938|pmid-16105940|pmid-15218029|pmid-17242434|pmid-18003975 | Recently, two additional critical components of the import motor, a J-protein (Pam18) (28–30) and J-like protein (Pam16) (16,17,31) have been identified. | [
"28",
"30",
"16",
"17",
"31",
"16",
"17",
"28",
"30",
"31",
"33",
"31",
"34",
"35",
"36"
] | 153 | 37,346 | 0 | false | Recently, two additional critical components of the import motor, a J-protein (Pam18) and J-like protein have been identified. | [
"28–30",
"Pam16",
"16,17,31"
] | Recently, two additional critical components of the import motor, a J-protein and J-like protein have been identified. | true | true | true | true | true | 6,404 |
3 | INTRODUCTION | 1 | 28 | [
"DDQ002C28",
"DDQ002C30",
"DDQ002C16",
"DDQ002C17",
"DDQ002C31",
"DDQ002C16",
"DDQ002C17",
"DDQ002C28",
"DDQ002C30",
"DDQ002C31",
"DDQ002C33",
"DDQ002C31",
"DDQ002C34",
"DDQ002C35",
"DDQ002C36"
] | 20,053,669 | pmid-14517234|pmid-14605210|pmid-14981507|pmid-14981506|pmid-16105940|pmid-14981507|pmid-14981506|pmid-14517234|pmid-14605210|pmid-16105940|pmid-19564938|pmid-16105940|pmid-15218029|pmid-17242434|pmid-18003975 | Pam18 and Pam16 proteins are highly conserved (16,17). | [
"28",
"30",
"16",
"17",
"31",
"16",
"17",
"28",
"30",
"31",
"33",
"31",
"34",
"35",
"36"
] | 54 | 37,347 | 0 | false | Pam18 and Pam16 proteins are highly conserved. | [
"16,17"
] | Pam18 and Pam16 proteins are highly conserved. | true | true | true | true | true | 6,404 |
3 | INTRODUCTION | 1 | 28 | [
"DDQ002C28",
"DDQ002C30",
"DDQ002C16",
"DDQ002C17",
"DDQ002C31",
"DDQ002C16",
"DDQ002C17",
"DDQ002C28",
"DDQ002C30",
"DDQ002C31",
"DDQ002C33",
"DDQ002C31",
"DDQ002C34",
"DDQ002C35",
"DDQ002C36"
] | 20,053,669 | pmid-14517234|pmid-14605210|pmid-14981507|pmid-14981506|pmid-16105940|pmid-14981507|pmid-14981506|pmid-14517234|pmid-14605210|pmid-16105940|pmid-19564938|pmid-16105940|pmid-15218029|pmid-17242434|pmid-18003975 | As expected of a J-protein, Pam18 stimulates Ssc1's ATPase activity and stabilizes the interaction with precursor proteins, thus carries out an essential function during the translocation process (28–30). | [
"28",
"30",
"16",
"17",
"31",
"16",
"17",
"28",
"30",
"31",
"33",
"31",
"34",
"35",
"36"
] | 204 | 37,348 | 0 | false | As expected of a J-protein, Pam18 stimulates Ssc1's ATPase activity and stabilizes the interaction with precursor proteins, thus carries out an essential function during the translocation process. | [
"28–30"
] | As expected of a J-protein, Pam18 stimulates Ssc1's ATPase activity and stabilizes the interaction with precursor proteins, thus carries out an essential function during the translocation process. | true | true | true | true | true | 6,404 |
3 | INTRODUCTION | 1 | 28 | [
"DDQ002C28",
"DDQ002C30",
"DDQ002C16",
"DDQ002C17",
"DDQ002C31",
"DDQ002C16",
"DDQ002C17",
"DDQ002C28",
"DDQ002C30",
"DDQ002C31",
"DDQ002C33",
"DDQ002C31",
"DDQ002C34",
"DDQ002C35",
"DDQ002C36"
] | 20,053,669 | pmid-14517234|pmid-14605210|pmid-14981507|pmid-14981506|pmid-16105940|pmid-14981507|pmid-14981506|pmid-14517234|pmid-14605210|pmid-16105940|pmid-19564938|pmid-16105940|pmid-15218029|pmid-17242434|pmid-18003975 | Pam16 regulates Pam18's ATPase stimulating activity by forming a functional heterodimer through its C-terminal domain (31–33). | [
"28",
"30",
"16",
"17",
"31",
"16",
"17",
"28",
"30",
"31",
"33",
"31",
"34",
"35",
"36"
] | 126 | 37,349 | 0 | false | Pam16 regulates Pam18's ATPase stimulating activity by forming a functional heterodimer through its C-terminal domain. | [
"31–33"
] | Pam16 regulates Pam18's ATPase stimulating activity by forming a functional heterodimer through its C-terminal domain. | true | true | true | true | true | 6,404 |
3 | INTRODUCTION | 1 | 28 | [
"DDQ002C28",
"DDQ002C30",
"DDQ002C16",
"DDQ002C17",
"DDQ002C31",
"DDQ002C16",
"DDQ002C17",
"DDQ002C28",
"DDQ002C30",
"DDQ002C31",
"DDQ002C33",
"DDQ002C31",
"DDQ002C34",
"DDQ002C35",
"DDQ002C36"
] | 20,053,669 | pmid-14517234|pmid-14605210|pmid-14981507|pmid-14981506|pmid-16105940|pmid-14981507|pmid-14981506|pmid-14517234|pmid-14605210|pmid-16105940|pmid-19564938|pmid-16105940|pmid-15218029|pmid-17242434|pmid-18003975 | A stable heterodimer is required for the protein translocation and viability of yeast cells (31,34,35). | [
"28",
"30",
"16",
"17",
"31",
"16",
"17",
"28",
"30",
"31",
"33",
"31",
"34",
"35",
"36"
] | 103 | 37,350 | 0 | false | A stable heterodimer is required for the protein translocation and viability of yeast cells. | [
"31,34,35"
] | A stable heterodimer is required for the protein translocation and viability of yeast cells. | true | true | true | true | true | 6,404 |
3 | INTRODUCTION | 1 | 36 | [
"DDQ002C28",
"DDQ002C30",
"DDQ002C16",
"DDQ002C17",
"DDQ002C31",
"DDQ002C16",
"DDQ002C17",
"DDQ002C28",
"DDQ002C30",
"DDQ002C31",
"DDQ002C33",
"DDQ002C31",
"DDQ002C34",
"DDQ002C35",
"DDQ002C36"
] | 20,053,669 | pmid-14517234|pmid-14605210|pmid-14981507|pmid-14981506|pmid-16105940|pmid-14981507|pmid-14981506|pmid-14517234|pmid-14605210|pmid-16105940|pmid-19564938|pmid-16105940|pmid-15218029|pmid-17242434|pmid-18003975 | Pam18:Pam16 heterodimer is tethered to the translocon via multiple interactions with other components of the translocation channel and regulates the import motor activity (36). | [
"28",
"30",
"16",
"17",
"31",
"16",
"17",
"28",
"30",
"31",
"33",
"31",
"34",
"35",
"36"
] | 176 | 37,351 | 1 | false | Pam18:Pam16 heterodimer is tethered to the translocon via multiple interactions with other components of the translocation channel and regulates the import motor activity. | [
"36"
] | Pam18:Pam16 heterodimer is tethered to the translocon via multiple interactions with other components of the translocation channel and regulates the import motor activity. | true | true | true | true | true | 6,404 |
3 | INTRODUCTION | 1 | 28 | [
"DDQ002C28",
"DDQ002C30",
"DDQ002C16",
"DDQ002C17",
"DDQ002C31",
"DDQ002C16",
"DDQ002C17",
"DDQ002C28",
"DDQ002C30",
"DDQ002C31",
"DDQ002C33",
"DDQ002C31",
"DDQ002C34",
"DDQ002C35",
"DDQ002C36"
] | 20,053,669 | pmid-14517234|pmid-14605210|pmid-14981507|pmid-14981506|pmid-16105940|pmid-14981507|pmid-14981506|pmid-14517234|pmid-14605210|pmid-16105940|pmid-19564938|pmid-16105940|pmid-15218029|pmid-17242434|pmid-18003975 | However, the precise mechanism of regulation of the import motor by Pam16 is not clearly understood. | [
"28",
"30",
"16",
"17",
"31",
"16",
"17",
"28",
"30",
"31",
"33",
"31",
"34",
"35",
"36"
] | 100 | 37,352 | 0 | false | However, the precise mechanism of regulation of the import motor by Pam16 is not clearly understood. | [] | However, the precise mechanism of regulation of the import motor by Pam16 is not clearly understood. | true | true | true | true | true | 6,404 |
4 | INTRODUCTION | 1 | 37 | [
"DDQ002C37",
"DDQ002C38",
"DDQ002C39",
"DDQ002C40",
"DDQ002C41",
"DDQ002C40",
"DDQ002C42",
"DDQ002C41",
"DDQ002C43"
] | 20,053,669 | pmid-15984936|pmid-11179663|pmid-11099034|pmid-12704206|pmid-11750097|pmid-12704206|pmid-15704001|pmid-11750097|pmid-18451534|pmid-18003975|pmid-18003975 | The proteins homologous to yeast Pam16 have been reported in other organisms (37). | [
"37",
"38",
"39",
"40",
"41",
"40",
"42",
"41",
"43"
] | 82 | 37,353 | 1 | false | The proteins homologous to yeast Pam16 have been reported in other organisms. | [
"37"
] | The proteins homologous to yeast Pam16 have been reported in other organisms. | true | true | true | true | true | 6,405 |
4 | INTRODUCTION | 1 | 38 | [
"DDQ002C37",
"DDQ002C38",
"DDQ002C39",
"DDQ002C40",
"DDQ002C41",
"DDQ002C40",
"DDQ002C42",
"DDQ002C41",
"DDQ002C43"
] | 20,053,669 | pmid-15984936|pmid-11179663|pmid-11099034|pmid-12704206|pmid-11750097|pmid-12704206|pmid-15704001|pmid-11750097|pmid-18451534|pmid-18003975|pmid-18003975 | A homologous deletion mutant in Drosophila was found to be lethal at the first instar larval stage (38). | [
"37",
"38",
"39",
"40",
"41",
"40",
"42",
"41",
"43"
] | 104 | 37,354 | 1 | false | A homologous deletion mutant in Drosophila was found to be lethal at the first instar larval stage. | [
"38"
] | A homologous deletion mutant in Drosophila was found to be lethal at the first instar larval stage. | true | true | true | true | true | 6,405 |
4 | INTRODUCTION | 1 | 37 | [
"DDQ002C37",
"DDQ002C38",
"DDQ002C39",
"DDQ002C40",
"DDQ002C41",
"DDQ002C40",
"DDQ002C42",
"DDQ002C41",
"DDQ002C43"
] | 20,053,669 | pmid-15984936|pmid-11179663|pmid-11099034|pmid-12704206|pmid-11750097|pmid-12704206|pmid-15704001|pmid-11750097|pmid-18451534|pmid-18003975|pmid-18003975 | Magmas-like proteins are found essential for the development of murine and Caenorhabditis elegans (39,40). | [
"37",
"38",
"39",
"40",
"41",
"40",
"42",
"41",
"43"
] | 106 | 37,355 | 0 | false | Magmas-like proteins are found essential for the development of murine and Caenorhabditis elegans. | [
"39,40"
] | Magmas-like proteins are found essential for the development of murine and Caenorhabditis elegans. | true | true | true | true | true | 6,405 |
4 | INTRODUCTION | 1 | 37 | [
"DDQ002C37",
"DDQ002C38",
"DDQ002C39",
"DDQ002C40",
"DDQ002C41",
"DDQ002C40",
"DDQ002C42",
"DDQ002C41",
"DDQ002C43"
] | 20,053,669 | pmid-15984936|pmid-11179663|pmid-11099034|pmid-12704206|pmid-11750097|pmid-12704206|pmid-15704001|pmid-11750097|pmid-18451534|pmid-18003975|pmid-18003975 | In humans, mitochondria-associated granulocyte-macrophage colony-stimulating factor (GM-CSF) signaling molecule (referred as ‘Magmas’, ortholog of yeast Pam16) was first reported as a protein upregulated in PGMD1 cells cultured in a GM-CSF rich medium and not in cells exposed to Interleukin-3. | [
"37",
"38",
"39",
"40",
"41",
"40",
"42",
"41",
"43"
] | 294 | 37,356 | 0 | false | In humans, mitochondria-associated granulocyte-macrophage colony-stimulating factor (GM-CSF) signaling molecule (referred as ‘Magmas’, ortholog of yeast Pam16) was first reported as a protein upregulated in PGMD1 cells cultured in a GM-CSF rich medium and not in cells exposed to Interleukin-3. | [] | In humans, mitochondria-associated granulocyte-macrophage colony-stimulating factor (GM-CSF) signaling molecule (referred as ‘Magmas’, ortholog of yeast Pam16) was first reported as a protein upregulated in PGMD1 cells cultured in a GM-CSF rich medium and not in cells exposed to Interleukin-3. | true | true | true | true | true | 6,405 |
4 | INTRODUCTION | 1 | 41 | [
"DDQ002C37",
"DDQ002C38",
"DDQ002C39",
"DDQ002C40",
"DDQ002C41",
"DDQ002C40",
"DDQ002C42",
"DDQ002C41",
"DDQ002C43"
] | 20,053,669 | pmid-15984936|pmid-11179663|pmid-11099034|pmid-12704206|pmid-11750097|pmid-12704206|pmid-15704001|pmid-11750097|pmid-18451534|pmid-18003975|pmid-18003975 | Reduced Magmas expression in PGMD1 cells under GM-CSF resulted in decreased proliferative rates in a dose-responsive manner (41). | [
"37",
"38",
"39",
"40",
"41",
"40",
"42",
"41",
"43"
] | 129 | 37,357 | 1 | false | Reduced Magmas expression in PGMD1 cells under GM-CSF resulted in decreased proliferative rates in a dose-responsive manner. | [
"41"
] | Reduced Magmas expression in PGMD1 cells under GM-CSF resulted in decreased proliferative rates in a dose-responsive manner. | true | true | true | true | true | 6,405 |
4 | INTRODUCTION | 1 | 40 | [
"DDQ002C37",
"DDQ002C38",
"DDQ002C39",
"DDQ002C40",
"DDQ002C41",
"DDQ002C40",
"DDQ002C42",
"DDQ002C41",
"DDQ002C43"
] | 20,053,669 | pmid-15984936|pmid-11179663|pmid-11099034|pmid-12704206|pmid-11750097|pmid-12704206|pmid-15704001|pmid-11750097|pmid-18451534|pmid-18003975|pmid-18003975 | During the developmental stages of animals, expression of Magmas was upregulated in muscle, testis, intestinal mucosa and liver (40). | [
"37",
"38",
"39",
"40",
"41",
"40",
"42",
"41",
"43"
] | 133 | 37,358 | 1 | false | During the developmental stages of animals, expression of Magmas was upregulated in muscle, testis, intestinal mucosa and liver. | [
"40"
] | During the developmental stages of animals, expression of Magmas was upregulated in muscle, testis, intestinal mucosa and liver. | true | true | true | true | true | 6,405 |
4 | INTRODUCTION | 1 | 42 | [
"DDQ002C37",
"DDQ002C38",
"DDQ002C39",
"DDQ002C40",
"DDQ002C41",
"DDQ002C40",
"DDQ002C42",
"DDQ002C41",
"DDQ002C43"
] | 20,053,669 | pmid-15984936|pmid-11179663|pmid-11099034|pmid-12704206|pmid-11750097|pmid-12704206|pmid-15704001|pmid-11750097|pmid-18451534|pmid-18003975|pmid-18003975 | Magmas levels were also found to be upregulated in neoplastic prostate in humans, though its expression is restricted only to a subset of tumors (42). | [
"37",
"38",
"39",
"40",
"41",
"40",
"42",
"41",
"43"
] | 150 | 37,359 | 1 | false | Magmas levels were also found to be upregulated in neoplastic prostate in humans, though its expression is restricted only to a subset of tumors. | [
"42"
] | Magmas levels were also found to be upregulated in neoplastic prostate in humans, though its expression is restricted only to a subset of tumors. | true | true | true | true | true | 6,405 |
4 | INTRODUCTION | 1 | 37 | [
"DDQ002C37",
"DDQ002C38",
"DDQ002C39",
"DDQ002C40",
"DDQ002C41",
"DDQ002C40",
"DDQ002C42",
"DDQ002C41",
"DDQ002C43"
] | 20,053,669 | pmid-15984936|pmid-11179663|pmid-11099034|pmid-12704206|pmid-11750097|pmid-12704206|pmid-15704001|pmid-11750097|pmid-18451534|pmid-18003975|pmid-18003975 | On the basis of these observations, it has been proposed that Magmas functions as a ‘signaling molecule’ and perhaps controls anaerobic metabolism, resistance to apoptosis or altered growth sensitivity in mammalian system (41–43). | [
"37",
"38",
"39",
"40",
"41",
"40",
"42",
"41",
"43"
] | 230 | 37,360 | 0 | false | On the basis of these observations, it has been proposed that Magmas functions as a ‘signaling molecule’ and perhaps controls anaerobic metabolism, resistance to apoptosis or altered growth sensitivity in mammalian system. | [
"41–43"
] | On the basis of these observations, it has been proposed that Magmas functions as a ‘signaling molecule’ and perhaps controls anaerobic metabolism, resistance to apoptosis or altered growth sensitivity in mammalian system. | true | true | true | true | true | 6,405 |
5 | INTRODUCTION | 0 | null | null | 20,053,669 | pmid-11750097|pmid-15704001|pmid-16055927|pmid-16055927|pmid-16055927 | Although Magmas levels are upregulated in different developmental stages and various pathophysiological conditions including prostate cancer, little functional information about human Magmas is available. | null | 204 | 37,361 | 0 | false | null | null | Although Magmas levels are upregulated in different developmental stages and various pathophysiological conditions including prostate cancer, little functional information about human Magmas is available. | true | true | true | true | true | 6,406 |
5 | INTRODUCTION | 0 | null | null | 20,053,669 | pmid-11750097|pmid-15704001|pmid-16055927|pmid-16055927|pmid-16055927 | On the basis of a weak sequence and predicted structural fold similarity with yPam16's J-like domain, we sought to determine the function of Magmas in humans. | null | 158 | 37,362 | 0 | false | null | null | On the basis of a weak sequence and predicted structural fold similarity with yPam16's J-like domain, we sought to determine the function of Magmas in humans. | true | true | true | true | true | 6,406 |
5 | INTRODUCTION | 0 | null | null | 20,053,669 | pmid-11750097|pmid-15704001|pmid-16055927|pmid-16055927|pmid-16055927 | We found that Magmas is an ortholog of yeast Pam16 and has similar functions; and it complements the growth of yeast cells deleted for Pam16. | null | 141 | 37,363 | 0 | false | null | null | We found that Magmas is an ortholog of yeast Pam16 and has similar functions; and it complements the growth of yeast cells deleted for Pam16. | true | true | true | true | true | 6,406 |
5 | INTRODUCTION | 0 | null | null | 20,053,669 | pmid-11750097|pmid-15704001|pmid-16055927|pmid-16055927|pmid-16055927 | Moreover, Magmas interacts with yeast Pam18 as well as human DnaJC19 (ortholog of yeast Pam18) both in vivo and in vitro conditions to form a heterodimeric subcomplex. | null | 167 | 37,364 | 0 | false | null | null | Moreover, Magmas interacts with yeast Pam18 as well as human DnaJC19 (ortholog of yeast Pam18) both in vivo and in vitro conditions to form a heterodimeric subcomplex. | true | true | true | true | true | 6,406 |
5 | INTRODUCTION | 0 | null | null | 20,053,669 | pmid-11750097|pmid-15704001|pmid-16055927|pmid-16055927|pmid-16055927 | The residues critical for the association of Magmas with yPam18, DnaJC19 and translocation channel were identified. | null | 115 | 37,365 | 0 | false | null | null | The residues critical for the association of Magmas with yPam18, DnaJC19 and translocation channel were identified. | true | true | true | true | true | 6,406 |
5 | INTRODUCTION | 0 | null | null | 20,053,669 | pmid-11750097|pmid-15704001|pmid-16055927|pmid-16055927|pmid-16055927 | Our results are consistent with the existence of stable interaction between Magmas and DnaJC19 that plays a crucial role in tethering of DnaJC19 at the translocon and perhaps regulating human import motor activity. | null | 214 | 37,366 | 0 | false | null | null | Our results are consistent with the existence of stable interaction between Magmas and DnaJC19 that plays a crucial role in tethering of DnaJC19 at the translocon and perhaps regulating human import motor activity. | true | true | true | true | true | 6,406 |
5 | INTRODUCTION | 0 | null | null | 20,053,669 | pmid-11750097|pmid-15704001|pmid-16055927|pmid-16055927|pmid-16055927 | We have identified the minimal region of DnaJC19 essential for its association with Magmas. | null | 91 | 37,367 | 0 | false | null | null | We have identified the minimal region of DnaJC19 essential for its association with Magmas. | true | true | true | true | true | 6,406 |
5 | INTRODUCTION | 0 | null | null | 20,053,669 | pmid-11750097|pmid-15704001|pmid-16055927|pmid-16055927|pmid-16055927 | Thus, our study underlines the possible molecular mechanism for the physiological symptoms of dilated cardiomyopathy with ataxia (DCM) syndrome which is associated with a truncated DnaJC19 protein. | null | 197 | 37,368 | 0 | false | null | null | Thus, our study underlines the possible molecular mechanism for the physiological symptoms of dilated cardiomyopathy with ataxia (DCM) syndrome which is associated with a truncated DnaJC19 protein. | true | true | true | true | true | 6,406 |
0 | DISCUSSION | 1 | 8 | [
"DDQ002C8",
"DDQ002C9",
"DDQ002C46",
"DDQ002C47",
"DDQ002C49",
"DDQ002C41",
"DDQ002C42",
"DDQ002C16",
"DDQ002C17",
"DDQ002C32"
] | 20,053,669 | pmid-2862839|pmid-11758801|pmid-11331908|pmid-2225059|pmid-18174896|pmid-17263664|pmid-15232570|pmid-10339406|pmid-16055927|pmid-17934217|pmid-11750097|pmid-15704001|pmid-14981507|pmid-14981506|pmid-16977310 | Protein transport is a highly regulated process that depends on the critical functioning of inner mitochondrial ‘import motor’ components (8,9). | [
"8",
"9",
"46",
"47",
"49",
"41",
"42",
"16",
"17",
"32"
] | 144 | 37,369 | 0 | false | Protein transport is a highly regulated process that depends on the critical functioning of inner mitochondrial ‘import motor’ components. | [
"8,9"
] | Protein transport is a highly regulated process that depends on the critical functioning of inner mitochondrial ‘import motor’ components. | true | true | true | true | true | 6,407 |
0 | DISCUSSION | 1 | 46 | [
"DDQ002C8",
"DDQ002C9",
"DDQ002C46",
"DDQ002C47",
"DDQ002C49",
"DDQ002C41",
"DDQ002C42",
"DDQ002C16",
"DDQ002C17",
"DDQ002C32"
] | 20,053,669 | pmid-2862839|pmid-11758801|pmid-11331908|pmid-2225059|pmid-18174896|pmid-17263664|pmid-15232570|pmid-10339406|pmid-16055927|pmid-17934217|pmid-11750097|pmid-15704001|pmid-14981507|pmid-14981506|pmid-16977310 | The proteins related to the yeast import motor are conserved in mammalian mitochondria including humans (46). | [
"8",
"9",
"46",
"47",
"49",
"41",
"42",
"16",
"17",
"32"
] | 109 | 37,370 | 1 | false | The proteins related to the yeast import motor are conserved in mammalian mitochondria including humans. | [
"46"
] | The proteins related to the yeast import motor are conserved in mammalian mitochondria including humans. | true | true | true | true | true | 6,407 |
0 | DISCUSSION | 1 | 8 | [
"DDQ002C8",
"DDQ002C9",
"DDQ002C46",
"DDQ002C47",
"DDQ002C49",
"DDQ002C41",
"DDQ002C42",
"DDQ002C16",
"DDQ002C17",
"DDQ002C32"
] | 20,053,669 | pmid-2862839|pmid-11758801|pmid-11331908|pmid-2225059|pmid-18174896|pmid-17263664|pmid-15232570|pmid-10339406|pmid-16055927|pmid-17934217|pmid-11750097|pmid-15704001|pmid-14981507|pmid-14981506|pmid-16977310 | Depending upon the metabolic state of the cell, the expression of human import motor components is highly regulated, thus controlling the import process. | [
"8",
"9",
"46",
"47",
"49",
"41",
"42",
"16",
"17",
"32"
] | 153 | 37,371 | 0 | false | Depending upon the metabolic state of the cell, the expression of human import motor components is highly regulated, thus controlling the import process. | [] | Depending upon the metabolic state of the cell, the expression of human import motor components is highly regulated, thus controlling the import process. | true | true | true | true | true | 6,407 |
0 | DISCUSSION | 1 | 8 | [
"DDQ002C8",
"DDQ002C9",
"DDQ002C46",
"DDQ002C47",
"DDQ002C49",
"DDQ002C41",
"DDQ002C42",
"DDQ002C16",
"DDQ002C17",
"DDQ002C32"
] | 20,053,669 | pmid-2862839|pmid-11758801|pmid-11331908|pmid-2225059|pmid-18174896|pmid-17263664|pmid-15232570|pmid-10339406|pmid-16055927|pmid-17934217|pmid-11750097|pmid-15704001|pmid-14981507|pmid-14981506|pmid-16977310 | The mechanism of regulation of the import process in humans is largely unknown; however, altered regulation leads to severe mitochondrial disorders including neuromuscular diseases and malignancy (47–49). | [
"8",
"9",
"46",
"47",
"49",
"41",
"42",
"16",
"17",
"32"
] | 204 | 37,372 | 0 | false | The mechanism of regulation of the import process in humans is largely unknown; however, altered regulation leads to severe mitochondrial disorders including neuromuscular diseases and malignancy. | [
"47–49"
] | The mechanism of regulation of the import process in humans is largely unknown; however, altered regulation leads to severe mitochondrial disorders including neuromuscular diseases and malignancy. | true | true | true | true | true | 6,407 |
0 | DISCUSSION | 1 | 8 | [
"DDQ002C8",
"DDQ002C9",
"DDQ002C46",
"DDQ002C47",
"DDQ002C49",
"DDQ002C41",
"DDQ002C42",
"DDQ002C16",
"DDQ002C17",
"DDQ002C32"
] | 20,053,669 | pmid-2862839|pmid-11758801|pmid-11331908|pmid-2225059|pmid-18174896|pmid-17263664|pmid-15232570|pmid-10339406|pmid-16055927|pmid-17934217|pmid-11750097|pmid-15704001|pmid-14981507|pmid-14981506|pmid-16977310 | Mammalian Magmas proteins are ubiquitously expressed; and in humans, it was identified as GM-CSF specific signaling molecule which gets overexpressed in neoplastic prostate (41,42). | [
"8",
"9",
"46",
"47",
"49",
"41",
"42",
"16",
"17",
"32"
] | 181 | 37,373 | 0 | false | Mammalian Magmas proteins are ubiquitously expressed; and in humans, it was identified as GM-CSF specific signaling molecule which gets overexpressed in neoplastic prostate. | [
"41,42"
] | Mammalian Magmas proteins are ubiquitously expressed; and in humans, it was identified as GM-CSF specific signaling molecule which gets overexpressed in neoplastic prostate. | true | true | true | true | true | 6,407 |
0 | DISCUSSION | 1 | 8 | [
"DDQ002C8",
"DDQ002C9",
"DDQ002C46",
"DDQ002C47",
"DDQ002C49",
"DDQ002C41",
"DDQ002C42",
"DDQ002C16",
"DDQ002C17",
"DDQ002C32"
] | 20,053,669 | pmid-2862839|pmid-11758801|pmid-11331908|pmid-2225059|pmid-18174896|pmid-17263664|pmid-15232570|pmid-10339406|pmid-16055927|pmid-17934217|pmid-11750097|pmid-15704001|pmid-14981507|pmid-14981506|pmid-16977310 | Although it has been assumed that Magmas proteins are predicted homologs of yeast Pam16 (16,17), the primary function and mechanism of regulation in mammalian system was still elusive. | [
"8",
"9",
"46",
"47",
"49",
"41",
"42",
"16",
"17",
"32"
] | 184 | 37,374 | 0 | false | Although it has been assumed that Magmas proteins are predicted homologs of yeast Pam16, the primary function and mechanism of regulation in mammalian system was still elusive. | [
"16,17"
] | Although it has been assumed that Magmas proteins are predicted homologs of yeast Pam16, the primary function and mechanism of regulation in mammalian system was still elusive. | true | true | true | true | true | 6,407 |
0 | DISCUSSION | 1 | 8 | [
"DDQ002C8",
"DDQ002C9",
"DDQ002C46",
"DDQ002C47",
"DDQ002C49",
"DDQ002C41",
"DDQ002C42",
"DDQ002C16",
"DDQ002C17",
"DDQ002C32"
] | 20,053,669 | pmid-2862839|pmid-11758801|pmid-11331908|pmid-2225059|pmid-18174896|pmid-17263664|pmid-15232570|pmid-10339406|pmid-16055927|pmid-17934217|pmid-11750097|pmid-15704001|pmid-14981507|pmid-14981506|pmid-16977310 | The data presented here on human Magmas provides first experimental evidences to show that the mammalian Magmas proteins are orthologs of yeast Pam16 having similar functions and are essential part of mammalian import motor. | [
"8",
"9",
"46",
"47",
"49",
"41",
"42",
"16",
"17",
"32"
] | 224 | 37,375 | 0 | false | The data presented here on human Magmas provides first experimental evidences to show that the mammalian Magmas proteins are orthologs of yeast Pam16 having similar functions and are essential part of mammalian import motor. | [] | The data presented here on human Magmas provides first experimental evidences to show that the mammalian Magmas proteins are orthologs of yeast Pam16 having similar functions and are essential part of mammalian import motor. | true | true | true | true | true | 6,407 |
0 | DISCUSSION | 1 | 8 | [
"DDQ002C8",
"DDQ002C9",
"DDQ002C46",
"DDQ002C47",
"DDQ002C49",
"DDQ002C41",
"DDQ002C42",
"DDQ002C16",
"DDQ002C17",
"DDQ002C32"
] | 20,053,669 | pmid-2862839|pmid-11758801|pmid-11331908|pmid-2225059|pmid-18174896|pmid-17263664|pmid-15232570|pmid-10339406|pmid-16055927|pmid-17934217|pmid-11750097|pmid-15704001|pmid-14981507|pmid-14981506|pmid-16977310 | The primary structure of human Magmas is related to yeast Pam16 and share a common domain organization. | [
"8",
"9",
"46",
"47",
"49",
"41",
"42",
"16",
"17",
"32"
] | 103 | 37,376 | 0 | false | The primary structure of human Magmas is related to yeast Pam16 and share a common domain organization. | [] | The primary structure of human Magmas is related to yeast Pam16 and share a common domain organization. | true | true | true | true | true | 6,407 |
0 | DISCUSSION | 1 | 8 | [
"DDQ002C8",
"DDQ002C9",
"DDQ002C46",
"DDQ002C47",
"DDQ002C49",
"DDQ002C41",
"DDQ002C42",
"DDQ002C16",
"DDQ002C17",
"DDQ002C32"
] | 20,053,669 | pmid-2862839|pmid-11758801|pmid-11331908|pmid-2225059|pmid-18174896|pmid-17263664|pmid-15232570|pmid-10339406|pmid-16055927|pmid-17934217|pmid-11750097|pmid-15704001|pmid-14981507|pmid-14981506|pmid-16977310 | It consists of predicted N-terminal membrane association domain (TM), middle targeting region (T) and C-terminal J-like domain (J). | [
"8",
"9",
"46",
"47",
"49",
"41",
"42",
"16",
"17",
"32"
] | 131 | 37,377 | 0 | false | It consists of predicted N-terminal membrane association domain (TM), middle targeting region (T) and C-terminal J-like domain (J). | [] | It consists of predicted N-terminal membrane association domain (TM), middle targeting region (T) and C-terminal J-like domain (J). | true | true | true | true | true | 6,407 |
0 | DISCUSSION | 1 | 32 | [
"DDQ002C8",
"DDQ002C9",
"DDQ002C46",
"DDQ002C47",
"DDQ002C49",
"DDQ002C41",
"DDQ002C42",
"DDQ002C16",
"DDQ002C17",
"DDQ002C32"
] | 20,053,669 | pmid-2862839|pmid-11758801|pmid-11331908|pmid-2225059|pmid-18174896|pmid-17263664|pmid-15232570|pmid-10339406|pmid-16055927|pmid-17934217|pmid-11750097|pmid-15704001|pmid-14981507|pmid-14981506|pmid-16977310 | However, it lacks C-terminal extension region of Pam16 which is functionally dispensable in yeast (32). | [
"8",
"9",
"46",
"47",
"49",
"41",
"42",
"16",
"17",
"32"
] | 103 | 37,378 | 1 | false | However, it lacks C-terminal extension region of Pam16 which is functionally dispensable in yeast. | [
"32"
] | However, it lacks C-terminal extension region of Pam16 which is functionally dispensable in yeast. | true | true | true | true | true | 6,407 |
1 | DISCUSSION | 1 | 16 | [
"DDQ002C16",
"DDQ002C17"
] | 20,053,669 | pmid-17514892|pmid-11450972|pmid-17514892|pmid-17263664|pmid-11450972|pmid-12154367|pmid-11450972|pmid-15232570|pmid-18692467|pmid-12191765|pmid-12437924|pmid-1833391|pmid-8631295|pmid-12154367|pmid-15232570|pmid-14981507|pmid-14981506 | Human Magmas is an ortholog of yeast Pam16 in several aspects and performs the similar function. | [
"16",
"17"
] | 96 | 37,379 | 0 | false | Human Magmas is an ortholog of yeast Pam16 in several aspects and performs the similar function. | [] | Human Magmas is an ortholog of yeast Pam16 in several aspects and performs the similar function. | true | true | true | true | true | 6,408 |
1 | DISCUSSION | 1 | 16 | [
"DDQ002C16",
"DDQ002C17"
] | 20,053,669 | pmid-17514892|pmid-11450972|pmid-17514892|pmid-17263664|pmid-11450972|pmid-12154367|pmid-11450972|pmid-15232570|pmid-18692467|pmid-12191765|pmid-12437924|pmid-1833391|pmid-8631295|pmid-12154367|pmid-15232570|pmid-14981507|pmid-14981506 | Several biochemical and genetic evidences are presented here to support this idea. | [
"16",
"17"
] | 82 | 37,380 | 0 | false | Several biochemical and genetic evidences are presented here to support this idea. | [] | Several biochemical and genetic evidences are presented here to support this idea. | true | true | true | true | true | 6,408 |
1 | DISCUSSION | 1 | 16 | [
"DDQ002C16",
"DDQ002C17"
] | 20,053,669 | pmid-17514892|pmid-11450972|pmid-17514892|pmid-17263664|pmid-11450972|pmid-12154367|pmid-11450972|pmid-15232570|pmid-18692467|pmid-12191765|pmid-12437924|pmid-1833391|pmid-8631295|pmid-12154367|pmid-15232570|pmid-14981507|pmid-14981506 | First, it shows a complete growth support of yeast cells deleted for essential PAM16 gene at all conditions. | [
"16",
"17"
] | 108 | 37,381 | 0 | false | First, it shows a complete growth support of yeast cells deleted for essential PAM16 gene at all conditions. | [] | First, it shows a complete growth support of yeast cells deleted for essential PAM16 gene at all conditions. | true | true | true | true | true | 6,408 |
1 | DISCUSSION | 1 | 16 | [
"DDQ002C16",
"DDQ002C17"
] | 20,053,669 | pmid-17514892|pmid-11450972|pmid-17514892|pmid-17263664|pmid-11450972|pmid-12154367|pmid-11450972|pmid-15232570|pmid-18692467|pmid-12191765|pmid-12437924|pmid-1833391|pmid-8631295|pmid-12154367|pmid-15232570|pmid-14981507|pmid-14981506 | These observations highlight a possible similar essential functional role for Magmas in humans. | [
"16",
"17"
] | 95 | 37,382 | 0 | false | These observations highlight a possible similar essential functional role for Magmas in humans. | [] | These observations highlight a possible similar essential functional role for Magmas in humans. | true | true | true | true | true | 6,408 |
1 | DISCUSSION | 1 | 16 | [
"DDQ002C16",
"DDQ002C17"
] | 20,053,669 | pmid-17514892|pmid-11450972|pmid-17514892|pmid-17263664|pmid-11450972|pmid-12154367|pmid-11450972|pmid-15232570|pmid-18692467|pmid-12191765|pmid-12437924|pmid-1833391|pmid-8631295|pmid-12154367|pmid-15232570|pmid-14981507|pmid-14981506 | Second, it localizes into mitochondria when expressed in Δpam16 cells as well as in human HeLa and HEK293T cells when expressed as GFP fusion proteins. | [
"16",
"17"
] | 151 | 37,383 | 0 | false | Second, it localizes into mitochondria when expressed in Δpam16 cells as well as in human HeLa and HEK293T cells when expressed as GFP fusion proteins. | [] | Second, it localizes into mitochondria when expressed in Δpam16 cells as well as in human HeLa and HEK293T cells when expressed as GFP fusion proteins. | true | true | true | true | true | 6,408 |
1 | DISCUSSION | 1 | 16 | [
"DDQ002C16",
"DDQ002C17"
] | 20,053,669 | pmid-17514892|pmid-11450972|pmid-17514892|pmid-17263664|pmid-11450972|pmid-12154367|pmid-11450972|pmid-15232570|pmid-18692467|pmid-12191765|pmid-12437924|pmid-1833391|pmid-8631295|pmid-12154367|pmid-15232570|pmid-14981507|pmid-14981506 | These observations were further supported by enrichment of the protein levels in purified mitochondria from yeast and human cell lines, respectively. | [
"16",
"17"
] | 149 | 37,384 | 0 | false | These observations were further supported by enrichment of the protein levels in purified mitochondria from yeast and human cell lines, respectively. | [] | These observations were further supported by enrichment of the protein levels in purified mitochondria from yeast and human cell lines, respectively. | true | true | true | true | true | 6,408 |
1 | DISCUSSION | 1 | 16 | [
"DDQ002C16",
"DDQ002C17"
] | 20,053,669 | pmid-17514892|pmid-11450972|pmid-17514892|pmid-17263664|pmid-11450972|pmid-12154367|pmid-11450972|pmid-15232570|pmid-18692467|pmid-12191765|pmid-12437924|pmid-1833391|pmid-8631295|pmid-12154367|pmid-15232570|pmid-14981507|pmid-14981506 | Third, in both yeast and human, Magmas is tightly associated with the inner mitochondrial membrane. | [
"16",
"17"
] | 99 | 37,385 | 0 | false | Third, in both yeast and human, Magmas is tightly associated with the inner mitochondrial membrane. | [] | Third, in both yeast and human, Magmas is tightly associated with the inner mitochondrial membrane. | true | true | true | true | true | 6,408 |
1 | DISCUSSION | 1 | 16 | [
"DDQ002C16",
"DDQ002C17"
] | 20,053,669 | pmid-17514892|pmid-11450972|pmid-17514892|pmid-17263664|pmid-11450972|pmid-12154367|pmid-11450972|pmid-15232570|pmid-18692467|pmid-12191765|pmid-12437924|pmid-1833391|pmid-8631295|pmid-12154367|pmid-15232570|pmid-14981507|pmid-14981506 | Similar to Pam16, Magmas was fractionated into inner membrane pellet fraction and resistant to high salt extraction. | [
"16",
"17"
] | 116 | 37,386 | 0 | false | Similar to Pam16, Magmas was fractionated into inner membrane pellet fraction and resistant to high salt extraction. | [] | Similar to Pam16, Magmas was fractionated into inner membrane pellet fraction and resistant to high salt extraction. | true | true | true | true | true | 6,408 |
1 | DISCUSSION | 1 | 16 | [
"DDQ002C16",
"DDQ002C17"
] | 20,053,669 | pmid-17514892|pmid-11450972|pmid-17514892|pmid-17263664|pmid-11450972|pmid-12154367|pmid-11450972|pmid-15232570|pmid-18692467|pmid-12191765|pmid-12437924|pmid-1833391|pmid-8631295|pmid-12154367|pmid-15232570|pmid-14981507|pmid-14981506 | However, majority of Magmas was extracted from pellet fraction at alkaline pH, indicating that it is a peripherally associated with inner mitochondrial membrane protein. | [
"16",
"17"
] | 169 | 37,387 | 0 | false | However, majority of Magmas was extracted from pellet fraction at alkaline pH, indicating that it is a peripherally associated with inner mitochondrial membrane protein. | [] | However, majority of Magmas was extracted from pellet fraction at alkaline pH, indicating that it is a peripherally associated with inner mitochondrial membrane protein. | true | true | true | true | true | 6,408 |
1 | DISCUSSION | 1 | 16 | [
"DDQ002C16",
"DDQ002C17"
] | 20,053,669 | pmid-17514892|pmid-11450972|pmid-17514892|pmid-17263664|pmid-11450972|pmid-12154367|pmid-11450972|pmid-15232570|pmid-18692467|pmid-12191765|pmid-12437924|pmid-1833391|pmid-8631295|pmid-12154367|pmid-15232570|pmid-14981507|pmid-14981506 | Fourth, like Pam16, Magmas is associated with mitochondrial TIM23 complex in Δpam16 yeast cells as well as in humans. | [
"16",
"17"
] | 117 | 37,388 | 0 | false | Fourth, like Pam16, Magmas is associated with mitochondrial TIM23 complex in Δpam16 yeast cells as well as in humans. | [] | Fourth, like Pam16, Magmas is associated with mitochondrial TIM23 complex in Δpam16 yeast cells as well as in humans. | true | true | true | true | true | 6,408 |
1 | DISCUSSION | 1 | 16 | [
"DDQ002C16",
"DDQ002C17"
] | 20,053,669 | pmid-17514892|pmid-11450972|pmid-17514892|pmid-17263664|pmid-11450972|pmid-12154367|pmid-11450972|pmid-15232570|pmid-18692467|pmid-12191765|pmid-12437924|pmid-1833391|pmid-8631295|pmid-12154367|pmid-15232570|pmid-14981507|pmid-14981506 | Fifth, Magmas regulates the ATPase stimulation activity of yPam18 as well as DnaJC19 in humans by forming a stable subcomplex through their C-terminal regions, thus regulating Ssc1 and human mtHsp70 (Mortalin) activity during the import process. | [
"16",
"17"
] | 245 | 37,389 | 0 | false | Fifth, Magmas regulates the ATPase stimulation activity of yPam18 as well as DnaJC19 in humans by forming a stable subcomplex through their C-terminal regions, thus regulating Ssc1 and human mtHsp70 (Mortalin) activity during the import process. | [] | Fifth, Magmas regulates the ATPase stimulation activity of yPam18 as well as DnaJC19 in humans by forming a stable subcomplex through their C-terminal regions, thus regulating Ssc1 and human mtHsp70 (Mortalin) activity during the import process. | true | true | true | true | true | 6,408 |
1 | DISCUSSION | 1 | 16 | [
"DDQ002C16",
"DDQ002C17"
] | 20,053,669 | pmid-17514892|pmid-11450972|pmid-17514892|pmid-17263664|pmid-11450972|pmid-12154367|pmid-11450972|pmid-15232570|pmid-18692467|pmid-12191765|pmid-12437924|pmid-1833391|pmid-8631295|pmid-12154367|pmid-15232570|pmid-14981507|pmid-14981506 | Sixth, like Pam16, Magmas plays an essential role in import of precursor proteins into the mitochondrial matrix. | [
"16",
"17"
] | 112 | 37,390 | 0 | false | Sixth, like Pam16, Magmas plays an essential role in import of precursor proteins into the mitochondrial matrix. | [] | Sixth, like Pam16, Magmas plays an essential role in import of precursor proteins into the mitochondrial matrix. | true | true | true | true | true | 6,408 |
1 | DISCUSSION | 1 | 16 | [
"DDQ002C16",
"DDQ002C17"
] | 20,053,669 | pmid-17514892|pmid-11450972|pmid-17514892|pmid-17263664|pmid-11450972|pmid-12154367|pmid-11450972|pmid-15232570|pmid-18692467|pmid-12191765|pmid-12437924|pmid-1833391|pmid-8631295|pmid-12154367|pmid-15232570|pmid-14981507|pmid-14981506 | Previously, it has been shown that downregulation of Pam16 level leads to the accumulation of precursor form of Hsp60 in yeast cells suggesting its essential role in protein import (16,17). | [
"16",
"17"
] | 189 | 37,391 | 0 | false | Previously, it has been shown that downregulation of Pam16 level leads to the accumulation of precursor form of Hsp60 in yeast cells suggesting its essential role in protein import. | [
"16,17"
] | Previously, it has been shown that downregulation of Pam16 level leads to the accumulation of precursor form of Hsp60 in yeast cells suggesting its essential role in protein import. | true | true | true | true | true | 6,408 |
1 | DISCUSSION | 1 | 16 | [
"DDQ002C16",
"DDQ002C17"
] | 20,053,669 | pmid-17514892|pmid-11450972|pmid-17514892|pmid-17263664|pmid-11450972|pmid-12154367|pmid-11450972|pmid-15232570|pmid-18692467|pmid-12191765|pmid-12437924|pmid-1833391|pmid-8631295|pmid-12154367|pmid-15232570|pmid-14981507|pmid-14981506 | Similarly, Δpam16 yeast cells expressing wt Magmas did not show the accumulation of precursor form of Hsp60 when exposed to non-permissive temperature, indicating that Magmas can complement the import function of Pam16. | [
"16",
"17"
] | 219 | 37,392 | 0 | false | Similarly, Δpam16 yeast cells expressing wt Magmas did not show the accumulation of precursor form of Hsp60 when exposed to non-permissive temperature, indicating that Magmas can complement the import function of Pam16. | [] | Similarly, Δpam16 yeast cells expressing wt Magmas did not show the accumulation of precursor form of Hsp60 when exposed to non-permissive temperature, indicating that Magmas can complement the import function of Pam16. | true | true | true | true | true | 6,408 |
1 | DISCUSSION | 1 | 16 | [
"DDQ002C16",
"DDQ002C17"
] | 20,053,669 | pmid-17514892|pmid-11450972|pmid-17514892|pmid-17263664|pmid-11450972|pmid-12154367|pmid-11450972|pmid-15232570|pmid-18692467|pmid-12191765|pmid-12437924|pmid-1833391|pmid-8631295|pmid-12154367|pmid-15232570|pmid-14981507|pmid-14981506 | In addition to that, Magmas also supported a wild-type level of protein import of model preprotein, Cytb2(47)-DHFR into the Δpam16 mitochondria. | [
"16",
"17"
] | 144 | 37,393 | 0 | false | In addition to that, Magmas also supported a wild-type level of protein import of model preprotein, Cytb2(47)-DHFR into the Δpam16 mitochondria. | [] | In addition to that, Magmas also supported a wild-type level of protein import of model preprotein, Cytb2(47)-DHFR into the Δpam16 mitochondria. | true | true | true | true | true | 6,408 |
2 | DISCUSSION | 0 | null | null | 20,053,669 | pmid-17263664|pmid-14981507|pmid-8246957|pmid-16943180|pmid-16790493|pmid-12677068|pmid-8408191|pmid-11733493|pmid-12677068|pmid-18426906 | Our results demonstrate that Magmas protein interacts with yPam18 and DnaJC19 via their J-like and J-domains to form a stable subcomplex. | null | 137 | 37,394 | 0 | false | null | null | Our results demonstrate that Magmas protein interacts with yPam18 and DnaJC19 via their J-like and J-domains to form a stable subcomplex. | true | true | true | true | true | 6,409 |
2 | DISCUSSION | 0 | null | null | 20,053,669 | pmid-17263664|pmid-14981507|pmid-8246957|pmid-16943180|pmid-16790493|pmid-12677068|pmid-8408191|pmid-11733493|pmid-12677068|pmid-18426906 | The J-like and J-domain of Magmas and yPam18/DnaJC19, respectively, are competent to form a subcomplex with similar affinities and a stable Magmas:yPam18 and Magmas:DnaJC19 subcomplex was co-immunoprecipitated in yeast and human mitochondrial lysates. | null | 251 | 37,395 | 0 | false | null | null | The J-like and J-domain of Magmas and yPam18/DnaJC19, respectively, are competent to form a subcomplex with similar affinities and a stable Magmas:yPam18 and Magmas:DnaJC19 subcomplex was co-immunoprecipitated in yeast and human mitochondrial lysates. | true | true | true | true | true | 6,409 |
2 | DISCUSSION | 0 | null | null | 20,053,669 | pmid-17263664|pmid-14981507|pmid-8246957|pmid-16943180|pmid-16790493|pmid-12677068|pmid-8408191|pmid-11733493|pmid-12677068|pmid-18426906 | Formation of a similar subcomplex between Pam16 and Pam18 was reported earlier in yeast. | null | 88 | 37,396 | 0 | false | null | null | Formation of a similar subcomplex between Pam16 and Pam18 was reported earlier in yeast. | true | true | true | true | true | 6,409 |
2 | DISCUSSION | 0 | null | null | 20,053,669 | pmid-17263664|pmid-14981507|pmid-8246957|pmid-16943180|pmid-16790493|pmid-12677068|pmid-8408191|pmid-11733493|pmid-12677068|pmid-18426906 | Hence, our findings clearly broaden the idea of evolutionary conserved existence of such subcomplex from yeast to human systems. | null | 128 | 37,397 | 0 | false | null | null | Hence, our findings clearly broaden the idea of evolutionary conserved existence of such subcomplex from yeast to human systems. | true | true | true | true | true | 6,409 |
3 | DISCUSSION | 0 | null | null | 20,053,669 | pmid-14517234|pmid-14605210|pmid-14981507|pmid-14981506|pmid-16105940|pmid-14981507|pmid-14981506|pmid-14517234|pmid-14605210|pmid-16105940|pmid-19564938|pmid-16105940|pmid-15218029|pmid-17242434|pmid-18003975 | A stable interaction between J-like domain of Magmas and J-domain of yPam18/DnaJC19 is required for in vivo function. | null | 117 | 37,398 | 0 | false | null | null | A stable interaction between J-like domain of Magmas and J-domain of yPam18/DnaJC19 is required for in vivo function. | true | true | true | true | true | 6,410 |
3 | DISCUSSION | 0 | null | null | 20,053,669 | pmid-14517234|pmid-14605210|pmid-14981507|pmid-14981506|pmid-16105940|pmid-14981507|pmid-14981506|pmid-14517234|pmid-14605210|pmid-16105940|pmid-19564938|pmid-16105940|pmid-15218029|pmid-17242434|pmid-18003975 | A single amino acid alteration in helix I and helix III region of the J-like domain of Magmas compromises growth of yeast cells and is associated with an unstable Magmas/yPam18 subcomplex. | null | 188 | 37,399 | 0 | false | null | null | A single amino acid alteration in helix I and helix III region of the J-like domain of Magmas compromises growth of yeast cells and is associated with an unstable Magmas/yPam18 subcomplex. | true | true | true | true | true | 6,410 |
3 | DISCUSSION | 0 | null | null | 20,053,669 | pmid-14517234|pmid-14605210|pmid-14981507|pmid-14981506|pmid-16105940|pmid-14981507|pmid-14981506|pmid-14517234|pmid-14605210|pmid-16105940|pmid-19564938|pmid-16105940|pmid-15218029|pmid-17242434|pmid-18003975 | The mutant proteins also showed a dramatic decrease in affinity for their interaction with yPam18 and human Pam18 ortholog DnaJC19 proteins; envisioning a similar defect in subcomplex formation in human mitochondria. | null | 216 | 37,400 | 0 | false | null | null | The mutant proteins also showed a dramatic decrease in affinity for their interaction with yPam18 and human Pam18 ortholog DnaJC19 proteins; envisioning a similar defect in subcomplex formation in human mitochondria. | true | true | true | true | true | 6,410 |
3 | DISCUSSION | 0 | null | null | 20,053,669 | pmid-14517234|pmid-14605210|pmid-14981507|pmid-14981506|pmid-16105940|pmid-14981507|pmid-14981506|pmid-14517234|pmid-14605210|pmid-16105940|pmid-19564938|pmid-16105940|pmid-15218029|pmid-17242434|pmid-18003975 | The corresponding in vivo and in organellar protein translocation defect associated with the Magmas mutants is consistent with the idea that the protein import and growth defects of cells expressing the mutant proteins are caused by instability of the subcomplex. | null | 263 | 37,401 | 0 | false | null | null | The corresponding in vivo and in organellar protein translocation defect associated with the Magmas mutants is consistent with the idea that the protein import and growth defects of cells expressing the mutant proteins are caused by instability of the subcomplex. | true | true | true | true | true | 6,410 |
4 | DISCUSSION | 1 | 36 | [
"DDQ002C36",
"DDQ002C36"
] | 20,053,669 | pmid-15984936|pmid-11179663|pmid-11099034|pmid-12704206|pmid-11750097|pmid-12704206|pmid-15704001|pmid-11750097|pmid-18451534|pmid-18003975|pmid-18003975 | Our findings support the hypothesis of Magmas playing a critical role in positioning of J-protein, Pam18/DnaJC19 to the translocon and perhaps regulating the import motor activity in mammalian system. | [
"36",
"36"
] | 200 | 37,402 | 0 | false | Our findings support the hypothesis of Magmas playing a critical role in positioning of J-protein, Pam18/DnaJC19 to the translocon and perhaps regulating the import motor activity in mammalian system. | [] | Our findings support the hypothesis of Magmas playing a critical role in positioning of J-protein, Pam18/DnaJC19 to the translocon and perhaps regulating the import motor activity in mammalian system. | true | true | true | true | true | 6,411 |
4 | DISCUSSION | 1 | 36 | [
"DDQ002C36",
"DDQ002C36"
] | 20,053,669 | pmid-15984936|pmid-11179663|pmid-11099034|pmid-12704206|pmid-11750097|pmid-12704206|pmid-15704001|pmid-11750097|pmid-18451534|pmid-18003975|pmid-18003975 | In yeast, it was demonstrated that Pam16 plays a crucial role in tethering Pam18 to the translocon possibly by interacting through Tim44 with its N-terminal domain (36). | [
"36",
"36"
] | 169 | 37,403 | 1 | false | In yeast, it was demonstrated that Pam16 plays a crucial role in tethering Pam18 to the translocon possibly by interacting through Tim44 with its N-terminal domain. | [
"36"
] | In yeast, it was demonstrated that Pam16 plays a crucial role in tethering Pam18 to the translocon possibly by interacting through Tim44 with its N-terminal domain. | true | true | true | true | true | 6,411 |
4 | DISCUSSION | 1 | 36 | [
"DDQ002C36",
"DDQ002C36"
] | 20,053,669 | pmid-15984936|pmid-11179663|pmid-11099034|pmid-12704206|pmid-11750097|pmid-12704206|pmid-15704001|pmid-11750097|pmid-18451534|pmid-18003975|pmid-18003975 | Although the Ts mutants of Pam16 showed a compromised heterodimer subcomplex formation, a significantly reduced interaction of Pam18 at the translocon was observed, but Pam16 association remained unaffected (36). | [
"36",
"36"
] | 212 | 37,404 | 1 | false | Although the Ts mutants of Pam16 showed a compromised heterodimer subcomplex formation, a significantly reduced interaction of Pam18 at the translocon was observed, but Pam16 association remained unaffected. | [
"36"
] | Although the Ts mutants of Pam16 showed a compromised heterodimer subcomplex formation, a significantly reduced interaction of Pam18 at the translocon was observed, but Pam16 association remained unaffected. | true | true | true | true | true | 6,411 |
4 | DISCUSSION | 1 | 36 | [
"DDQ002C36",
"DDQ002C36"
] | 20,053,669 | pmid-15984936|pmid-11179663|pmid-11099034|pmid-12704206|pmid-11750097|pmid-12704206|pmid-15704001|pmid-11750097|pmid-18451534|pmid-18003975|pmid-18003975 | Supporting this data, Magmas Ts mutants also showed a similar reduced co-precipitation of yPam18, but not of Magmas with the translocon when Magmas:yPam18 subcomplex formation was compromised. | [
"36",
"36"
] | 192 | 37,405 | 0 | false | Supporting this data, Magmas Ts mutants also showed a similar reduced co-precipitation of yPam18, but not of Magmas with the translocon when Magmas:yPam18 subcomplex formation was compromised. | [] | Supporting this data, Magmas Ts mutants also showed a similar reduced co-precipitation of yPam18, but not of Magmas with the translocon when Magmas:yPam18 subcomplex formation was compromised. | true | true | true | true | true | 6,411 |
4 | DISCUSSION | 1 | 36 | [
"DDQ002C36",
"DDQ002C36"
] | 20,053,669 | pmid-15984936|pmid-11179663|pmid-11099034|pmid-12704206|pmid-11750097|pmid-12704206|pmid-15704001|pmid-11750097|pmid-18451534|pmid-18003975|pmid-18003975 | Owing to compromised heterodimer formation, the Magmas mutants were found to be defective in regulating ATPase activity of human import motor. | [
"36",
"36"
] | 142 | 37,406 | 0 | false | Owing to compromised heterodimer formation, the Magmas mutants were found to be defective in regulating ATPase activity of human import motor. | [] | Owing to compromised heterodimer formation, the Magmas mutants were found to be defective in regulating ATPase activity of human import motor. | true | true | true | true | true | 6,411 |
4 | DISCUSSION | 1 | 36 | [
"DDQ002C36",
"DDQ002C36"
] | 20,053,669 | pmid-15984936|pmid-11179663|pmid-11099034|pmid-12704206|pmid-11750097|pmid-12704206|pmid-15704001|pmid-11750097|pmid-18451534|pmid-18003975|pmid-18003975 | This is consistent with an important role for Magmas in tethering yPam18/DnaJC19 to the translocon. | [
"36",
"36"
] | 99 | 37,407 | 0 | false | This is consistent with an important role for Magmas in tethering yPam18/DnaJC19 to the translocon. | [] | This is consistent with an important role for Magmas in tethering yPam18/DnaJC19 to the translocon. | true | true | true | true | true | 6,411 |
4 | DISCUSSION | 1 | 36 | [
"DDQ002C36",
"DDQ002C36"
] | 20,053,669 | pmid-15984936|pmid-11179663|pmid-11099034|pmid-12704206|pmid-11750097|pmid-12704206|pmid-15704001|pmid-11750097|pmid-18451534|pmid-18003975|pmid-18003975 | On the basis of our analysis, we conclude that both Magmas and Pam16 share a common function across species and evolved precisely to alter Pam18's level at the translocon by forming subcomplex through their C-terminal regions, thus regulating the mitochondrial activity. | [
"36",
"36"
] | 270 | 37,408 | 0 | false | On the basis of our analysis, we conclude that both Magmas and Pam16 share a common function across species and evolved precisely to alter Pam18's level at the translocon by forming subcomplex through their C-terminal regions, thus regulating the mitochondrial activity. | [] | On the basis of our analysis, we conclude that both Magmas and Pam16 share a common function across species and evolved precisely to alter Pam18's level at the translocon by forming subcomplex through their C-terminal regions, thus regulating the mitochondrial activity. | true | true | true | true | true | 6,411 |
5 | DISCUSSION | 1 | 41 | [
"DDQ002C41",
"DDQ002C42",
"DDQ002C47",
"DDQ002C47",
"DDQ002C47"
] | 20,053,669 | pmid-11750097|pmid-15704001|pmid-16055927|pmid-16055927|pmid-16055927 | Although we have assigned a primary function for Magmas, understanding the mechanisms of regulation of Magmas as well as DnaJC19 is of utmost importance for the mitochondrial physiology. | [
"41",
"42",
"47",
"47",
"47"
] | 186 | 37,409 | 0 | false | Although we have assigned a primary function for Magmas, understanding the mechanisms of regulation of Magmas as well as DnaJC19 is of utmost importance for the mitochondrial physiology. | [] | Although we have assigned a primary function for Magmas, understanding the mechanisms of regulation of Magmas as well as DnaJC19 is of utmost importance for the mitochondrial physiology. | true | true | true | true | true | 6,412 |
5 | DISCUSSION | 1 | 41 | [
"DDQ002C41",
"DDQ002C42",
"DDQ002C47",
"DDQ002C47",
"DDQ002C47"
] | 20,053,669 | pmid-11750097|pmid-15704001|pmid-16055927|pmid-16055927|pmid-16055927 | There are numerous connections between altered Magmas levels and DnaJC19's function with mitochondrial pathophysiology: (i) Magmas levels is highly upregulated in prostate carcinoma and in response to GM-CSF treatment (41,42). | [
"41",
"42",
"47",
"47",
"47"
] | 226 | 37,410 | 0 | false | There are numerous connections between altered Magmas levels and DnaJC19's function with mitochondrial pathophysiology: (i) Magmas levels is highly upregulated in prostate carcinoma and in response to GM-CSF treatment. | [
"41,42"
] | There are numerous connections between altered Magmas levels and DnaJC19's function with mitochondrial pathophysiology: (i) Magmas levels is highly upregulated in prostate carcinoma and in response to GM-CSF treatment. | true | true | true | true | true | 6,412 |
5 | DISCUSSION | 1 | 47 | [
"DDQ002C41",
"DDQ002C42",
"DDQ002C47",
"DDQ002C47",
"DDQ002C47"
] | 20,053,669 | pmid-11750097|pmid-15704001|pmid-16055927|pmid-16055927|pmid-16055927 | (ii) Truncated DnaJC19 (devoid of its J-domain) protein causes a severe genetic disorder called DCM syndrome characterized by respiratory, cardiac and neurological symptoms (47). | [
"41",
"42",
"47",
"47",
"47"
] | 178 | 37,411 | 1 | false | (ii) Truncated DnaJC19 (devoid of its J-domain) protein causes a severe genetic disorder called DCM syndrome characterized by respiratory, cardiac and neurological symptoms. | [
"47"
] | (ii) Truncated DnaJC19 (devoid of its J-domain) protein causes a severe genetic disorder called DCM syndrome characterized by respiratory, cardiac and neurological symptoms. | false | false | true | true | false | 6,412 |
5 | DISCUSSION | 1 | 47 | [
"DDQ002C41",
"DDQ002C42",
"DDQ002C47",
"DDQ002C47",
"DDQ002C47"
] | 20,053,669 | pmid-11750097|pmid-15704001|pmid-16055927|pmid-16055927|pmid-16055927 | DCM syndrome is an autosomal recessive disorder prevalent in Canadian and ancestral European population and an IVS3-1G→C mutation was identified upon genotyping the disease haplotypes (47). | [
"41",
"42",
"47",
"47",
"47"
] | 189 | 37,412 | 1 | false | DCM syndrome is an autosomal recessive disorder prevalent in Canadian and ancestral European population and an IVS3-1G→C mutation was identified upon genotyping the disease haplotypes. | [
"47"
] | DCM syndrome is an autosomal recessive disorder prevalent in Canadian and ancestral European population and an IVS3-1G→C mutation was identified upon genotyping the disease haplotypes. | true | true | true | true | true | 6,412 |
5 | DISCUSSION | 1 | 41 | [
"DDQ002C41",
"DDQ002C42",
"DDQ002C47",
"DDQ002C47",
"DDQ002C47"
] | 20,053,669 | pmid-11750097|pmid-15704001|pmid-16055927|pmid-16055927|pmid-16055927 | The mutation causes abnormal splicing that result in the truncation of exon 4 followed by a stop codon. | [
"41",
"42",
"47",
"47",
"47"
] | 103 | 37,413 | 0 | false | The mutation causes abnormal splicing that result in the truncation of exon 4 followed by a stop codon. | [] | The mutation causes abnormal splicing that result in the truncation of exon 4 followed by a stop codon. | true | true | true | true | true | 6,412 |
5 | DISCUSSION | 1 | 47 | [
"DDQ002C41",
"DDQ002C42",
"DDQ002C47",
"DDQ002C47",
"DDQ002C47"
] | 20,053,669 | pmid-11750097|pmid-15704001|pmid-16055927|pmid-16055927|pmid-16055927 | Translation of the Δexon 4 transcript produces a protein having a truncated J-domain (47). | [
"41",
"42",
"47",
"47",
"47"
] | 90 | 37,414 | 1 | false | Translation of the Δexon 4 transcript produces a protein having a truncated J-domain. | [
"47"
] | Translation of the Δexon 4 transcript produces a protein having a truncated J-domain. | true | true | true | true | true | 6,412 |
5 | DISCUSSION | 1 | 41 | [
"DDQ002C41",
"DDQ002C42",
"DDQ002C47",
"DDQ002C47",
"DDQ002C47"
] | 20,053,669 | pmid-11750097|pmid-15704001|pmid-16055927|pmid-16055927|pmid-16055927 | On the basis of our studies, we propose the molecular etiology underlying the disorder. | [
"41",
"42",
"47",
"47",
"47"
] | 87 | 37,415 | 0 | false | On the basis of our studies, we propose the molecular etiology underlying the disorder. | [] | On the basis of our studies, we propose the molecular etiology underlying the disorder. | true | true | true | true | true | 6,412 |
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