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PMC1779780_F1_8745.jpg | What is the principal component of this image? | Confocal microscopy analysis of intracellular distribution of TAT-SA or SA at 4 h post transduction or injection. (A-C) Human cancer cell lines (HeLa, A549) and a non-cancer cell line (MRC-5) were transduced with TAT-SA prior to PFA fixation, permeabilization with Triton-X and immunolabeling with rabbit SA Ab followed by Alexa-488-conjugated goat anti-rabbit IgG (green). (D-E) Living HeLa cells were transduced or (F) injected to the cytoplasm with TAT-SA-A488 (green), or (G-H) transduced or (I) injected with SA-A488 (green). Scale bars, 10 μm. |
PMC1779780_F1_8744.jpg | What is being portrayed in this visual content? | Confocal microscopy analysis of intracellular distribution of TAT-SA or SA at 4 h post transduction or injection. (A-C) Human cancer cell lines (HeLa, A549) and a non-cancer cell line (MRC-5) were transduced with TAT-SA prior to PFA fixation, permeabilization with Triton-X and immunolabeling with rabbit SA Ab followed by Alexa-488-conjugated goat anti-rabbit IgG (green). (D-E) Living HeLa cells were transduced or (F) injected to the cytoplasm with TAT-SA-A488 (green), or (G-H) transduced or (I) injected with SA-A488 (green). Scale bars, 10 μm. |
PMC1779780_F4_8751.jpg | Describe the main subject of this image. | Colocalization of TAT-SA with endocytic markers in living cells. (A) HeLa cells were transduced first with TAT-SA-A488 (green) and then with TRITC-labeled transferrin (TRITC-Tf, red), a marker clathrin-mediated endocytosis, prior to analysis with confocal microscope at 15 min post transduction. (B) Cells transduced with TAT-SA-A488 and fluid-phase endosomal marker TRITC-labeled dextran (10 kD, red) were monitored at 15 min and (C) at 4 h post transduction. The white rectangles show the close-ups of representative structures. Scale bars, 10 μm. |
PMC1779780_F4_8755.jpg | What is the dominant medical problem in this image? | Colocalization of TAT-SA with endocytic markers in living cells. (A) HeLa cells were transduced first with TAT-SA-A488 (green) and then with TRITC-labeled transferrin (TRITC-Tf, red), a marker clathrin-mediated endocytosis, prior to analysis with confocal microscope at 15 min post transduction. (B) Cells transduced with TAT-SA-A488 and fluid-phase endosomal marker TRITC-labeled dextran (10 kD, red) were monitored at 15 min and (C) at 4 h post transduction. The white rectangles show the close-ups of representative structures. Scale bars, 10 μm. |
PMC1779780_F4_8753.jpg | What can you see in this picture? | Colocalization of TAT-SA with endocytic markers in living cells. (A) HeLa cells were transduced first with TAT-SA-A488 (green) and then with TRITC-labeled transferrin (TRITC-Tf, red), a marker clathrin-mediated endocytosis, prior to analysis with confocal microscope at 15 min post transduction. (B) Cells transduced with TAT-SA-A488 and fluid-phase endosomal marker TRITC-labeled dextran (10 kD, red) were monitored at 15 min and (C) at 4 h post transduction. The white rectangles show the close-ups of representative structures. Scale bars, 10 μm. |
PMC1779780_F4_8752.jpg | What object or scene is depicted here? | Colocalization of TAT-SA with endocytic markers in living cells. (A) HeLa cells were transduced first with TAT-SA-A488 (green) and then with TRITC-labeled transferrin (TRITC-Tf, red), a marker clathrin-mediated endocytosis, prior to analysis with confocal microscope at 15 min post transduction. (B) Cells transduced with TAT-SA-A488 and fluid-phase endosomal marker TRITC-labeled dextran (10 kD, red) were monitored at 15 min and (C) at 4 h post transduction. The white rectangles show the close-ups of representative structures. Scale bars, 10 μm. |
PMC1779780_F4_8749.jpg | What's the most prominent thing you notice in this picture? | Colocalization of TAT-SA with endocytic markers in living cells. (A) HeLa cells were transduced first with TAT-SA-A488 (green) and then with TRITC-labeled transferrin (TRITC-Tf, red), a marker clathrin-mediated endocytosis, prior to analysis with confocal microscope at 15 min post transduction. (B) Cells transduced with TAT-SA-A488 and fluid-phase endosomal marker TRITC-labeled dextran (10 kD, red) were monitored at 15 min and (C) at 4 h post transduction. The white rectangles show the close-ups of representative structures. Scale bars, 10 μm. |
PMC1779780_F4_8748.jpg | What is being portrayed in this visual content? | Colocalization of TAT-SA with endocytic markers in living cells. (A) HeLa cells were transduced first with TAT-SA-A488 (green) and then with TRITC-labeled transferrin (TRITC-Tf, red), a marker clathrin-mediated endocytosis, prior to analysis with confocal microscope at 15 min post transduction. (B) Cells transduced with TAT-SA-A488 and fluid-phase endosomal marker TRITC-labeled dextran (10 kD, red) were monitored at 15 min and (C) at 4 h post transduction. The white rectangles show the close-ups of representative structures. Scale bars, 10 μm. |
PMC1779780_F4_8757.jpg | What is the focal point of this photograph? | Colocalization of TAT-SA with endocytic markers in living cells. (A) HeLa cells were transduced first with TAT-SA-A488 (green) and then with TRITC-labeled transferrin (TRITC-Tf, red), a marker clathrin-mediated endocytosis, prior to analysis with confocal microscope at 15 min post transduction. (B) Cells transduced with TAT-SA-A488 and fluid-phase endosomal marker TRITC-labeled dextran (10 kD, red) were monitored at 15 min and (C) at 4 h post transduction. The white rectangles show the close-ups of representative structures. Scale bars, 10 μm. |
PMC1779780_F4_8750.jpg | What's the most prominent thing you notice in this picture? | Colocalization of TAT-SA with endocytic markers in living cells. (A) HeLa cells were transduced first with TAT-SA-A488 (green) and then with TRITC-labeled transferrin (TRITC-Tf, red), a marker clathrin-mediated endocytosis, prior to analysis with confocal microscope at 15 min post transduction. (B) Cells transduced with TAT-SA-A488 and fluid-phase endosomal marker TRITC-labeled dextran (10 kD, red) were monitored at 15 min and (C) at 4 h post transduction. The white rectangles show the close-ups of representative structures. Scale bars, 10 μm. |
PMC1779780_F4_8754.jpg | What is the main focus of this visual representation? | Colocalization of TAT-SA with endocytic markers in living cells. (A) HeLa cells were transduced first with TAT-SA-A488 (green) and then with TRITC-labeled transferrin (TRITC-Tf, red), a marker clathrin-mediated endocytosis, prior to analysis with confocal microscope at 15 min post transduction. (B) Cells transduced with TAT-SA-A488 and fluid-phase endosomal marker TRITC-labeled dextran (10 kD, red) were monitored at 15 min and (C) at 4 h post transduction. The white rectangles show the close-ups of representative structures. Scale bars, 10 μm. |
PMC1779780_F4_8758.jpg | What is being portrayed in this visual content? | Colocalization of TAT-SA with endocytic markers in living cells. (A) HeLa cells were transduced first with TAT-SA-A488 (green) and then with TRITC-labeled transferrin (TRITC-Tf, red), a marker clathrin-mediated endocytosis, prior to analysis with confocal microscope at 15 min post transduction. (B) Cells transduced with TAT-SA-A488 and fluid-phase endosomal marker TRITC-labeled dextran (10 kD, red) were monitored at 15 min and (C) at 4 h post transduction. The white rectangles show the close-ups of representative structures. Scale bars, 10 μm. |
PMC1779781_F2_8764.jpg | What is the principal component of this image? | Imaging of location-based biosensors with subcellular resolution. A) Images of GFP-actin (top panel) and GFP-PH (lower panel) were collected from the medial section of cells using a confocal microscope. Note that GFP-PH translocated from the membrane to the cytosol in cells following UV-A exposure, but not in non-exposed (control) cells. The post-irradiation time is indicated in the images. |
PMC1779781_F2_8761.jpg | What stands out most in this visual? | Imaging of location-based biosensors with subcellular resolution. A) Images of GFP-actin (top panel) and GFP-PH (lower panel) were collected from the medial section of cells using a confocal microscope. Note that GFP-PH translocated from the membrane to the cytosol in cells following UV-A exposure, but not in non-exposed (control) cells. The post-irradiation time is indicated in the images. |
PMC1779781_F2_8763.jpg | What key item or scene is captured in this photo? | Imaging of location-based biosensors with subcellular resolution. A) Images of GFP-actin (top panel) and GFP-PH (lower panel) were collected from the medial section of cells using a confocal microscope. Note that GFP-PH translocated from the membrane to the cytosol in cells following UV-A exposure, but not in non-exposed (control) cells. The post-irradiation time is indicated in the images. |
PMC1779781_F2_8766.jpg | What is the core subject represented in this visual? | Imaging of location-based biosensors with subcellular resolution. A) Images of GFP-actin (top panel) and GFP-PH (lower panel) were collected from the medial section of cells using a confocal microscope. Note that GFP-PH translocated from the membrane to the cytosol in cells following UV-A exposure, but not in non-exposed (control) cells. The post-irradiation time is indicated in the images. |
PMC1779781_F2_8760.jpg | What stands out most in this visual? | Imaging of location-based biosensors with subcellular resolution. A) Images of GFP-actin (top panel) and GFP-PH (lower panel) were collected from the medial section of cells using a confocal microscope. Note that GFP-PH translocated from the membrane to the cytosol in cells following UV-A exposure, but not in non-exposed (control) cells. The post-irradiation time is indicated in the images. |
PMC1779781_F2_8765.jpg | What's the most prominent thing you notice in this picture? | Imaging of location-based biosensors with subcellular resolution. A) Images of GFP-actin (top panel) and GFP-PH (lower panel) were collected from the medial section of cells using a confocal microscope. Note that GFP-PH translocated from the membrane to the cytosol in cells following UV-A exposure, but not in non-exposed (control) cells. The post-irradiation time is indicated in the images. |
PMC1779781_F2_8762.jpg | What is being portrayed in this visual content? | Imaging of location-based biosensors with subcellular resolution. A) Images of GFP-actin (top panel) and GFP-PH (lower panel) were collected from the medial section of cells using a confocal microscope. Note that GFP-PH translocated from the membrane to the cytosol in cells following UV-A exposure, but not in non-exposed (control) cells. The post-irradiation time is indicated in the images. |
PMC1779783_F4_8801.jpg | What is shown in this image? | Expression of the IRM-linked H40Y- and V163L-actin mutants. EGFP-tagged H40Y- (A-C) and V163L- (D, E) actin mutantswere expressed in C2C12 myoblasts (A) and differentiatedmyotubes.(B-E). EGFP fluorescence showed intranuclear (A; long arrows) and cytoplasmic aggregates (A; short arrow) formed by the H40Y-mutant in undifferentiated cells, with some co-staining with phalloidin (A"; arrows), but not with alpha-actinin (A'; arrows). A similar phenotype was observed for the V163L-isoform (not shown). In myotubes, some integration of EGFP-actin into stress fibres or sarcomeric structures was observed for both, H40Y- actin (B-B"; long arrows) and V163L-actin mutants (E, inset). However, in many differentiated cells, aberrant stress fibres were produced with a thickened and wavy appearance (C, C" long arrows; E, E", short arrows). The H40Y mutant might also induce fragmentation of stress fibres (B, B"; short arrow), but this could also be a short cytoplasmic rod. The V163L-mutant also formed nuclear aggregates in some myotubes (D; long arrow) that co-stained with phalloidin (D"; long arrow) and also very faintly with alpha-actinin (D'; long arrow). Nuclear aggregates were never found with the H40Y-mutant after differentiation. (Scale bars: 5 μm) |
PMC1779783_F4_8797.jpg | What is the core subject represented in this visual? | Expression of the IRM-linked H40Y- and V163L-actin mutants. EGFP-tagged H40Y- (A-C) and V163L- (D, E) actin mutantswere expressed in C2C12 myoblasts (A) and differentiatedmyotubes.(B-E). EGFP fluorescence showed intranuclear (A; long arrows) and cytoplasmic aggregates (A; short arrow) formed by the H40Y-mutant in undifferentiated cells, with some co-staining with phalloidin (A"; arrows), but not with alpha-actinin (A'; arrows). A similar phenotype was observed for the V163L-isoform (not shown). In myotubes, some integration of EGFP-actin into stress fibres or sarcomeric structures was observed for both, H40Y- actin (B-B"; long arrows) and V163L-actin mutants (E, inset). However, in many differentiated cells, aberrant stress fibres were produced with a thickened and wavy appearance (C, C" long arrows; E, E", short arrows). The H40Y mutant might also induce fragmentation of stress fibres (B, B"; short arrow), but this could also be a short cytoplasmic rod. The V163L-mutant also formed nuclear aggregates in some myotubes (D; long arrow) that co-stained with phalloidin (D"; long arrow) and also very faintly with alpha-actinin (D'; long arrow). Nuclear aggregates were never found with the H40Y-mutant after differentiation. (Scale bars: 5 μm) |
PMC1779783_F4_8804.jpg | What key item or scene is captured in this photo? | Expression of the IRM-linked H40Y- and V163L-actin mutants. EGFP-tagged H40Y- (A-C) and V163L- (D, E) actin mutantswere expressed in C2C12 myoblasts (A) and differentiatedmyotubes.(B-E). EGFP fluorescence showed intranuclear (A; long arrows) and cytoplasmic aggregates (A; short arrow) formed by the H40Y-mutant in undifferentiated cells, with some co-staining with phalloidin (A"; arrows), but not with alpha-actinin (A'; arrows). A similar phenotype was observed for the V163L-isoform (not shown). In myotubes, some integration of EGFP-actin into stress fibres or sarcomeric structures was observed for both, H40Y- actin (B-B"; long arrows) and V163L-actin mutants (E, inset). However, in many differentiated cells, aberrant stress fibres were produced with a thickened and wavy appearance (C, C" long arrows; E, E", short arrows). The H40Y mutant might also induce fragmentation of stress fibres (B, B"; short arrow), but this could also be a short cytoplasmic rod. The V163L-mutant also formed nuclear aggregates in some myotubes (D; long arrow) that co-stained with phalloidin (D"; long arrow) and also very faintly with alpha-actinin (D'; long arrow). Nuclear aggregates were never found with the H40Y-mutant after differentiation. (Scale bars: 5 μm) |
PMC1779783_F4_8807.jpg | Can you identify the primary element in this image? | Expression of the IRM-linked H40Y- and V163L-actin mutants. EGFP-tagged H40Y- (A-C) and V163L- (D, E) actin mutantswere expressed in C2C12 myoblasts (A) and differentiatedmyotubes.(B-E). EGFP fluorescence showed intranuclear (A; long arrows) and cytoplasmic aggregates (A; short arrow) formed by the H40Y-mutant in undifferentiated cells, with some co-staining with phalloidin (A"; arrows), but not with alpha-actinin (A'; arrows). A similar phenotype was observed for the V163L-isoform (not shown). In myotubes, some integration of EGFP-actin into stress fibres or sarcomeric structures was observed for both, H40Y- actin (B-B"; long arrows) and V163L-actin mutants (E, inset). However, in many differentiated cells, aberrant stress fibres were produced with a thickened and wavy appearance (C, C" long arrows; E, E", short arrows). The H40Y mutant might also induce fragmentation of stress fibres (B, B"; short arrow), but this could also be a short cytoplasmic rod. The V163L-mutant also formed nuclear aggregates in some myotubes (D; long arrow) that co-stained with phalloidin (D"; long arrow) and also very faintly with alpha-actinin (D'; long arrow). Nuclear aggregates were never found with the H40Y-mutant after differentiation. (Scale bars: 5 μm) |
PMC1779783_F4_8809.jpg | Can you identify the primary element in this image? | Expression of the IRM-linked H40Y- and V163L-actin mutants. EGFP-tagged H40Y- (A-C) and V163L- (D, E) actin mutantswere expressed in C2C12 myoblasts (A) and differentiatedmyotubes.(B-E). EGFP fluorescence showed intranuclear (A; long arrows) and cytoplasmic aggregates (A; short arrow) formed by the H40Y-mutant in undifferentiated cells, with some co-staining with phalloidin (A"; arrows), but not with alpha-actinin (A'; arrows). A similar phenotype was observed for the V163L-isoform (not shown). In myotubes, some integration of EGFP-actin into stress fibres or sarcomeric structures was observed for both, H40Y- actin (B-B"; long arrows) and V163L-actin mutants (E, inset). However, in many differentiated cells, aberrant stress fibres were produced with a thickened and wavy appearance (C, C" long arrows; E, E", short arrows). The H40Y mutant might also induce fragmentation of stress fibres (B, B"; short arrow), but this could also be a short cytoplasmic rod. The V163L-mutant also formed nuclear aggregates in some myotubes (D; long arrow) that co-stained with phalloidin (D"; long arrow) and also very faintly with alpha-actinin (D'; long arrow). Nuclear aggregates were never found with the H40Y-mutant after differentiation. (Scale bars: 5 μm) |
PMC1779783_F4_8799.jpg | What key item or scene is captured in this photo? | Expression of the IRM-linked H40Y- and V163L-actin mutants. EGFP-tagged H40Y- (A-C) and V163L- (D, E) actin mutantswere expressed in C2C12 myoblasts (A) and differentiatedmyotubes.(B-E). EGFP fluorescence showed intranuclear (A; long arrows) and cytoplasmic aggregates (A; short arrow) formed by the H40Y-mutant in undifferentiated cells, with some co-staining with phalloidin (A"; arrows), but not with alpha-actinin (A'; arrows). A similar phenotype was observed for the V163L-isoform (not shown). In myotubes, some integration of EGFP-actin into stress fibres or sarcomeric structures was observed for both, H40Y- actin (B-B"; long arrows) and V163L-actin mutants (E, inset). However, in many differentiated cells, aberrant stress fibres were produced with a thickened and wavy appearance (C, C" long arrows; E, E", short arrows). The H40Y mutant might also induce fragmentation of stress fibres (B, B"; short arrow), but this could also be a short cytoplasmic rod. The V163L-mutant also formed nuclear aggregates in some myotubes (D; long arrow) that co-stained with phalloidin (D"; long arrow) and also very faintly with alpha-actinin (D'; long arrow). Nuclear aggregates were never found with the H40Y-mutant after differentiation. (Scale bars: 5 μm) |
PMC1779783_F4_8806.jpg | What is the dominant medical problem in this image? | Expression of the IRM-linked H40Y- and V163L-actin mutants. EGFP-tagged H40Y- (A-C) and V163L- (D, E) actin mutantswere expressed in C2C12 myoblasts (A) and differentiatedmyotubes.(B-E). EGFP fluorescence showed intranuclear (A; long arrows) and cytoplasmic aggregates (A; short arrow) formed by the H40Y-mutant in undifferentiated cells, with some co-staining with phalloidin (A"; arrows), but not with alpha-actinin (A'; arrows). A similar phenotype was observed for the V163L-isoform (not shown). In myotubes, some integration of EGFP-actin into stress fibres or sarcomeric structures was observed for both, H40Y- actin (B-B"; long arrows) and V163L-actin mutants (E, inset). However, in many differentiated cells, aberrant stress fibres were produced with a thickened and wavy appearance (C, C" long arrows; E, E", short arrows). The H40Y mutant might also induce fragmentation of stress fibres (B, B"; short arrow), but this could also be a short cytoplasmic rod. The V163L-mutant also formed nuclear aggregates in some myotubes (D; long arrow) that co-stained with phalloidin (D"; long arrow) and also very faintly with alpha-actinin (D'; long arrow). Nuclear aggregates were never found with the H40Y-mutant after differentiation. (Scale bars: 5 μm) |
PMC1779783_F4_8808.jpg | Describe the main subject of this image. | Expression of the IRM-linked H40Y- and V163L-actin mutants. EGFP-tagged H40Y- (A-C) and V163L- (D, E) actin mutantswere expressed in C2C12 myoblasts (A) and differentiatedmyotubes.(B-E). EGFP fluorescence showed intranuclear (A; long arrows) and cytoplasmic aggregates (A; short arrow) formed by the H40Y-mutant in undifferentiated cells, with some co-staining with phalloidin (A"; arrows), but not with alpha-actinin (A'; arrows). A similar phenotype was observed for the V163L-isoform (not shown). In myotubes, some integration of EGFP-actin into stress fibres or sarcomeric structures was observed for both, H40Y- actin (B-B"; long arrows) and V163L-actin mutants (E, inset). However, in many differentiated cells, aberrant stress fibres were produced with a thickened and wavy appearance (C, C" long arrows; E, E", short arrows). The H40Y mutant might also induce fragmentation of stress fibres (B, B"; short arrow), but this could also be a short cytoplasmic rod. The V163L-mutant also formed nuclear aggregates in some myotubes (D; long arrow) that co-stained with phalloidin (D"; long arrow) and also very faintly with alpha-actinin (D'; long arrow). Nuclear aggregates were never found with the H40Y-mutant after differentiation. (Scale bars: 5 μm) |
PMC1779783_F5_8792.jpg | What is the main focus of this visual representation? | Expression of the NEM-linked I64N- and N115S-actin mutants. EGFP-tagged I64N- (A, B) and N115S- (C, D) actin mutantswere expressed in C2C12 myoblasts (A, C) and differentiated myotubes (B, D). Both mutants showed poor integration in undifferentiated cells: EGFP fluorescence revealed delocalization in many myoblasts (A, C; short arrows). I64N-actin also produced large rods (A; long arrow), whereas N115S-actin formed smaller, punctuate aggregates in the cytoplasm of some cells (C; long arrow), in both cases not co-staining with phalloidin or alpha-actinin (A', A"; C', C"; long arrows). After differentiation both mutants incorporated into actin structures such as stress fibres (D-D"; long arrows) and sarcomeric thin filament bundles (B, B', inset). (Scale bars: 5 μm) |
PMC1779783_F5_8793.jpg | What stands out most in this visual? | Expression of the NEM-linked I64N- and N115S-actin mutants. EGFP-tagged I64N- (A, B) and N115S- (C, D) actin mutantswere expressed in C2C12 myoblasts (A, C) and differentiated myotubes (B, D). Both mutants showed poor integration in undifferentiated cells: EGFP fluorescence revealed delocalization in many myoblasts (A, C; short arrows). I64N-actin also produced large rods (A; long arrow), whereas N115S-actin formed smaller, punctuate aggregates in the cytoplasm of some cells (C; long arrow), in both cases not co-staining with phalloidin or alpha-actinin (A', A"; C', C"; long arrows). After differentiation both mutants incorporated into actin structures such as stress fibres (D-D"; long arrows) and sarcomeric thin filament bundles (B, B', inset). (Scale bars: 5 μm) |
PMC1779783_F5_8788.jpg | What key item or scene is captured in this photo? | Expression of the NEM-linked I64N- and N115S-actin mutants. EGFP-tagged I64N- (A, B) and N115S- (C, D) actin mutantswere expressed in C2C12 myoblasts (A, C) and differentiated myotubes (B, D). Both mutants showed poor integration in undifferentiated cells: EGFP fluorescence revealed delocalization in many myoblasts (A, C; short arrows). I64N-actin also produced large rods (A; long arrow), whereas N115S-actin formed smaller, punctuate aggregates in the cytoplasm of some cells (C; long arrow), in both cases not co-staining with phalloidin or alpha-actinin (A', A"; C', C"; long arrows). After differentiation both mutants incorporated into actin structures such as stress fibres (D-D"; long arrows) and sarcomeric thin filament bundles (B, B', inset). (Scale bars: 5 μm) |
PMC1779783_F5_8787.jpg | What object or scene is depicted here? | Expression of the NEM-linked I64N- and N115S-actin mutants. EGFP-tagged I64N- (A, B) and N115S- (C, D) actin mutantswere expressed in C2C12 myoblasts (A, C) and differentiated myotubes (B, D). Both mutants showed poor integration in undifferentiated cells: EGFP fluorescence revealed delocalization in many myoblasts (A, C; short arrows). I64N-actin also produced large rods (A; long arrow), whereas N115S-actin formed smaller, punctuate aggregates in the cytoplasm of some cells (C; long arrow), in both cases not co-staining with phalloidin or alpha-actinin (A', A"; C', C"; long arrows). After differentiation both mutants incorporated into actin structures such as stress fibres (D-D"; long arrows) and sarcomeric thin filament bundles (B, B', inset). (Scale bars: 5 μm) |
PMC1779783_F5_8795.jpg | What is the core subject represented in this visual? | Expression of the NEM-linked I64N- and N115S-actin mutants. EGFP-tagged I64N- (A, B) and N115S- (C, D) actin mutantswere expressed in C2C12 myoblasts (A, C) and differentiated myotubes (B, D). Both mutants showed poor integration in undifferentiated cells: EGFP fluorescence revealed delocalization in many myoblasts (A, C; short arrows). I64N-actin also produced large rods (A; long arrow), whereas N115S-actin formed smaller, punctuate aggregates in the cytoplasm of some cells (C; long arrow), in both cases not co-staining with phalloidin or alpha-actinin (A', A"; C', C"; long arrows). After differentiation both mutants incorporated into actin structures such as stress fibres (D-D"; long arrows) and sarcomeric thin filament bundles (B, B', inset). (Scale bars: 5 μm) |
PMC1779783_F5_8789.jpg | What can you see in this picture? | Expression of the NEM-linked I64N- and N115S-actin mutants. EGFP-tagged I64N- (A, B) and N115S- (C, D) actin mutantswere expressed in C2C12 myoblasts (A, C) and differentiated myotubes (B, D). Both mutants showed poor integration in undifferentiated cells: EGFP fluorescence revealed delocalization in many myoblasts (A, C; short arrows). I64N-actin also produced large rods (A; long arrow), whereas N115S-actin formed smaller, punctuate aggregates in the cytoplasm of some cells (C; long arrow), in both cases not co-staining with phalloidin or alpha-actinin (A', A"; C', C"; long arrows). After differentiation both mutants incorporated into actin structures such as stress fibres (D-D"; long arrows) and sarcomeric thin filament bundles (B, B', inset). (Scale bars: 5 μm) |
PMC1779783_F5_8791.jpg | Can you identify the primary element in this image? | Expression of the NEM-linked I64N- and N115S-actin mutants. EGFP-tagged I64N- (A, B) and N115S- (C, D) actin mutantswere expressed in C2C12 myoblasts (A, C) and differentiated myotubes (B, D). Both mutants showed poor integration in undifferentiated cells: EGFP fluorescence revealed delocalization in many myoblasts (A, C; short arrows). I64N-actin also produced large rods (A; long arrow), whereas N115S-actin formed smaller, punctuate aggregates in the cytoplasm of some cells (C; long arrow), in both cases not co-staining with phalloidin or alpha-actinin (A', A"; C', C"; long arrows). After differentiation both mutants incorporated into actin structures such as stress fibres (D-D"; long arrows) and sarcomeric thin filament bundles (B, B', inset). (Scale bars: 5 μm) |
PMC1779783_F5_8796.jpg | What key item or scene is captured in this photo? | Expression of the NEM-linked I64N- and N115S-actin mutants. EGFP-tagged I64N- (A, B) and N115S- (C, D) actin mutantswere expressed in C2C12 myoblasts (A, C) and differentiated myotubes (B, D). Both mutants showed poor integration in undifferentiated cells: EGFP fluorescence revealed delocalization in many myoblasts (A, C; short arrows). I64N-actin also produced large rods (A; long arrow), whereas N115S-actin formed smaller, punctuate aggregates in the cytoplasm of some cells (C; long arrow), in both cases not co-staining with phalloidin or alpha-actinin (A', A"; C', C"; long arrows). After differentiation both mutants incorporated into actin structures such as stress fibres (D-D"; long arrows) and sarcomeric thin filament bundles (B, B', inset). (Scale bars: 5 μm) |
PMC1779783_F5_8794.jpg | What key item or scene is captured in this photo? | Expression of the NEM-linked I64N- and N115S-actin mutants. EGFP-tagged I64N- (A, B) and N115S- (C, D) actin mutantswere expressed in C2C12 myoblasts (A, C) and differentiated myotubes (B, D). Both mutants showed poor integration in undifferentiated cells: EGFP fluorescence revealed delocalization in many myoblasts (A, C; short arrows). I64N-actin also produced large rods (A; long arrow), whereas N115S-actin formed smaller, punctuate aggregates in the cytoplasm of some cells (C; long arrow), in both cases not co-staining with phalloidin or alpha-actinin (A', A"; C', C"; long arrows). After differentiation both mutants incorporated into actin structures such as stress fibres (D-D"; long arrows) and sarcomeric thin filament bundles (B, B', inset). (Scale bars: 5 μm) |
PMC1779783_F6_8773.jpg | What can you see in this picture? | Expression of the NEM-linked G268R and D286G-actin mutants. Expression of the EGFP-tagged G268R-actin in either undifferentiated myoblasts (A) or differentiated myotubes (B) lead to good integration of the actin mutant into endogenous actin structures. In contrast, the D286G-isoform stayed delocalized in the majority of transfected myoblasts (C). After differentiation, EGFP fluorescence revealed the formation of giant rods in the cytoplasm of D286G-transfected myotubes (D, E; long arrows) that did not co-stain with phalloidin or alpha-actinin (D', D", E', E"; long arrows). In some myotubes, mutant actin integrated into stress fibres, but their structures were abnormally wavy (E, E"; short arrows). |
PMC1779783_F6_8778.jpg | What is the core subject represented in this visual? | Expression of the NEM-linked G268R and D286G-actin mutants. Expression of the EGFP-tagged G268R-actin in either undifferentiated myoblasts (A) or differentiated myotubes (B) lead to good integration of the actin mutant into endogenous actin structures. In contrast, the D286G-isoform stayed delocalized in the majority of transfected myoblasts (C). After differentiation, EGFP fluorescence revealed the formation of giant rods in the cytoplasm of D286G-transfected myotubes (D, E; long arrows) that did not co-stain with phalloidin or alpha-actinin (D', D", E', E"; long arrows). In some myotubes, mutant actin integrated into stress fibres, but their structures were abnormally wavy (E, E"; short arrows). |
PMC1779783_F6_8781.jpg | What is the focal point of this photograph? | Expression of the NEM-linked G268R and D286G-actin mutants. Expression of the EGFP-tagged G268R-actin in either undifferentiated myoblasts (A) or differentiated myotubes (B) lead to good integration of the actin mutant into endogenous actin structures. In contrast, the D286G-isoform stayed delocalized in the majority of transfected myoblasts (C). After differentiation, EGFP fluorescence revealed the formation of giant rods in the cytoplasm of D286G-transfected myotubes (D, E; long arrows) that did not co-stain with phalloidin or alpha-actinin (D', D", E', E"; long arrows). In some myotubes, mutant actin integrated into stress fibres, but their structures were abnormally wavy (E, E"; short arrows). |
PMC1779783_F6_8783.jpg | What is the main focus of this visual representation? | Expression of the NEM-linked G268R and D286G-actin mutants. Expression of the EGFP-tagged G268R-actin in either undifferentiated myoblasts (A) or differentiated myotubes (B) lead to good integration of the actin mutant into endogenous actin structures. In contrast, the D286G-isoform stayed delocalized in the majority of transfected myoblasts (C). After differentiation, EGFP fluorescence revealed the formation of giant rods in the cytoplasm of D286G-transfected myotubes (D, E; long arrows) that did not co-stain with phalloidin or alpha-actinin (D', D", E', E"; long arrows). In some myotubes, mutant actin integrated into stress fibres, but their structures were abnormally wavy (E, E"; short arrows). |
PMC1779783_F6_8771.jpg | What is the main focus of this visual representation? | Expression of the NEM-linked G268R and D286G-actin mutants. Expression of the EGFP-tagged G268R-actin in either undifferentiated myoblasts (A) or differentiated myotubes (B) lead to good integration of the actin mutant into endogenous actin structures. In contrast, the D286G-isoform stayed delocalized in the majority of transfected myoblasts (C). After differentiation, EGFP fluorescence revealed the formation of giant rods in the cytoplasm of D286G-transfected myotubes (D, E; long arrows) that did not co-stain with phalloidin or alpha-actinin (D', D", E', E"; long arrows). In some myotubes, mutant actin integrated into stress fibres, but their structures were abnormally wavy (E, E"; short arrows). |
PMC1779783_F6_8777.jpg | What is the focal point of this photograph? | Expression of the NEM-linked G268R and D286G-actin mutants. Expression of the EGFP-tagged G268R-actin in either undifferentiated myoblasts (A) or differentiated myotubes (B) lead to good integration of the actin mutant into endogenous actin structures. In contrast, the D286G-isoform stayed delocalized in the majority of transfected myoblasts (C). After differentiation, EGFP fluorescence revealed the formation of giant rods in the cytoplasm of D286G-transfected myotubes (D, E; long arrows) that did not co-stain with phalloidin or alpha-actinin (D', D", E', E"; long arrows). In some myotubes, mutant actin integrated into stress fibres, but their structures were abnormally wavy (E, E"; short arrows). |
PMC1779783_F6_8776.jpg | What is shown in this image? | Expression of the NEM-linked G268R and D286G-actin mutants. Expression of the EGFP-tagged G268R-actin in either undifferentiated myoblasts (A) or differentiated myotubes (B) lead to good integration of the actin mutant into endogenous actin structures. In contrast, the D286G-isoform stayed delocalized in the majority of transfected myoblasts (C). After differentiation, EGFP fluorescence revealed the formation of giant rods in the cytoplasm of D286G-transfected myotubes (D, E; long arrows) that did not co-stain with phalloidin or alpha-actinin (D', D", E', E"; long arrows). In some myotubes, mutant actin integrated into stress fibres, but their structures were abnormally wavy (E, E"; short arrows). |
PMC1779783_F6_8782.jpg | What is the core subject represented in this visual? | Expression of the NEM-linked G268R and D286G-actin mutants. Expression of the EGFP-tagged G268R-actin in either undifferentiated myoblasts (A) or differentiated myotubes (B) lead to good integration of the actin mutant into endogenous actin structures. In contrast, the D286G-isoform stayed delocalized in the majority of transfected myoblasts (C). After differentiation, EGFP fluorescence revealed the formation of giant rods in the cytoplasm of D286G-transfected myotubes (D, E; long arrows) that did not co-stain with phalloidin or alpha-actinin (D', D", E', E"; long arrows). In some myotubes, mutant actin integrated into stress fibres, but their structures were abnormally wavy (E, E"; short arrows). |
PMC1779783_F6_8775.jpg | What object or scene is depicted here? | Expression of the NEM-linked G268R and D286G-actin mutants. Expression of the EGFP-tagged G268R-actin in either undifferentiated myoblasts (A) or differentiated myotubes (B) lead to good integration of the actin mutant into endogenous actin structures. In contrast, the D286G-isoform stayed delocalized in the majority of transfected myoblasts (C). After differentiation, EGFP fluorescence revealed the formation of giant rods in the cytoplasm of D286G-transfected myotubes (D, E; long arrows) that did not co-stain with phalloidin or alpha-actinin (D', D", E', E"; long arrows). In some myotubes, mutant actin integrated into stress fibres, but their structures were abnormally wavy (E, E"; short arrows). |
PMC1779783_F6_8774.jpg | What is the principal component of this image? | Expression of the NEM-linked G268R and D286G-actin mutants. Expression of the EGFP-tagged G268R-actin in either undifferentiated myoblasts (A) or differentiated myotubes (B) lead to good integration of the actin mutant into endogenous actin structures. In contrast, the D286G-isoform stayed delocalized in the majority of transfected myoblasts (C). After differentiation, EGFP fluorescence revealed the formation of giant rods in the cytoplasm of D286G-transfected myotubes (D, E; long arrows) that did not co-stain with phalloidin or alpha-actinin (D', D", E', E"; long arrows). In some myotubes, mutant actin integrated into stress fibres, but their structures were abnormally wavy (E, E"; short arrows). |
PMC1779787_F1_8811.jpg | What does this image primarily show? | Computed tomography scan showing retroperitoneal residual mass after systemic chemotherapy in 1989. |
PMC1779787_F2_8812.jpg | What is shown in this image? | Computed tomography scan showing cervical mass with extension to anterior mediastinum in 2005. |
PMC1779794_F1_8818.jpg | What is the focal point of this photograph? | Confocal laser scanning microscopy (CLSM) images of 5-HT-LIR (5-HT) in taste buds of rat and mouse circumvallate papillae. Longitudinal sections show a small subset of taste cells displaying 5-HT-LIR in rat (A) and mouse taste buds (B). Both cytoplasm and nuclei of taste cells display 5-HT-LIR. Transverse sections show 5-HT-LIR in rat (C-E) and mouse taste buds (F-H). The red cells are immunoreactive taste cells (C and F). Sytox-stained nuclei are shown in green (D and G), which stain all cells. Merges of red and green images are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F1_8816.jpg | What is the dominant medical problem in this image? | Confocal laser scanning microscopy (CLSM) images of 5-HT-LIR (5-HT) in taste buds of rat and mouse circumvallate papillae. Longitudinal sections show a small subset of taste cells displaying 5-HT-LIR in rat (A) and mouse taste buds (B). Both cytoplasm and nuclei of taste cells display 5-HT-LIR. Transverse sections show 5-HT-LIR in rat (C-E) and mouse taste buds (F-H). The red cells are immunoreactive taste cells (C and F). Sytox-stained nuclei are shown in green (D and G), which stain all cells. Merges of red and green images are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F1_8814.jpg | What is being portrayed in this visual content? | Confocal laser scanning microscopy (CLSM) images of 5-HT-LIR (5-HT) in taste buds of rat and mouse circumvallate papillae. Longitudinal sections show a small subset of taste cells displaying 5-HT-LIR in rat (A) and mouse taste buds (B). Both cytoplasm and nuclei of taste cells display 5-HT-LIR. Transverse sections show 5-HT-LIR in rat (C-E) and mouse taste buds (F-H). The red cells are immunoreactive taste cells (C and F). Sytox-stained nuclei are shown in green (D and G), which stain all cells. Merges of red and green images are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F1_8819.jpg | What is the central feature of this picture? | Confocal laser scanning microscopy (CLSM) images of 5-HT-LIR (5-HT) in taste buds of rat and mouse circumvallate papillae. Longitudinal sections show a small subset of taste cells displaying 5-HT-LIR in rat (A) and mouse taste buds (B). Both cytoplasm and nuclei of taste cells display 5-HT-LIR. Transverse sections show 5-HT-LIR in rat (C-E) and mouse taste buds (F-H). The red cells are immunoreactive taste cells (C and F). Sytox-stained nuclei are shown in green (D and G), which stain all cells. Merges of red and green images are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F1_8813.jpg | What does this image primarily show? | Confocal laser scanning microscopy (CLSM) images of 5-HT-LIR (5-HT) in taste buds of rat and mouse circumvallate papillae. Longitudinal sections show a small subset of taste cells displaying 5-HT-LIR in rat (A) and mouse taste buds (B). Both cytoplasm and nuclei of taste cells display 5-HT-LIR. Transverse sections show 5-HT-LIR in rat (C-E) and mouse taste buds (F-H). The red cells are immunoreactive taste cells (C and F). Sytox-stained nuclei are shown in green (D and G), which stain all cells. Merges of red and green images are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F1_8817.jpg | What does this image primarily show? | Confocal laser scanning microscopy (CLSM) images of 5-HT-LIR (5-HT) in taste buds of rat and mouse circumvallate papillae. Longitudinal sections show a small subset of taste cells displaying 5-HT-LIR in rat (A) and mouse taste buds (B). Both cytoplasm and nuclei of taste cells display 5-HT-LIR. Transverse sections show 5-HT-LIR in rat (C-E) and mouse taste buds (F-H). The red cells are immunoreactive taste cells (C and F). Sytox-stained nuclei are shown in green (D and G), which stain all cells. Merges of red and green images are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F1_8820.jpg | What object or scene is depicted here? | Confocal laser scanning microscopy (CLSM) images of 5-HT-LIR (5-HT) in taste buds of rat and mouse circumvallate papillae. Longitudinal sections show a small subset of taste cells displaying 5-HT-LIR in rat (A) and mouse taste buds (B). Both cytoplasm and nuclei of taste cells display 5-HT-LIR. Transverse sections show 5-HT-LIR in rat (C-E) and mouse taste buds (F-H). The red cells are immunoreactive taste cells (C and F). Sytox-stained nuclei are shown in green (D and G), which stain all cells. Merges of red and green images are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F3_8824.jpg | What key item or scene is captured in this photo? | Confocal laser scanning microscopy (CLSM) images of PGP 9.5-LIR (PGP 9.5) in taste buds of rat and mouse circumvallate papillae. Longitudinal sections show a small subset of taste cells and nerve processes expressing PGP 9.5 in rat (A) and mouse taste buds (B). Both cytoplasm and nuclei of taste cells display PGP 9.5-LIR. Transverse sections show PGP 9.5-LIR in rat (C-E) and mouse taste buds (F-H). Immunoreactive taste cells and nerve processes are shown in C and F. Sytox-stained nuclei are shown in D and G and merges are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F3_8827.jpg | What is being portrayed in this visual content? | Confocal laser scanning microscopy (CLSM) images of PGP 9.5-LIR (PGP 9.5) in taste buds of rat and mouse circumvallate papillae. Longitudinal sections show a small subset of taste cells and nerve processes expressing PGP 9.5 in rat (A) and mouse taste buds (B). Both cytoplasm and nuclei of taste cells display PGP 9.5-LIR. Transverse sections show PGP 9.5-LIR in rat (C-E) and mouse taste buds (F-H). Immunoreactive taste cells and nerve processes are shown in C and F. Sytox-stained nuclei are shown in D and G and merges are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F3_8825.jpg | What is the principal component of this image? | Confocal laser scanning microscopy (CLSM) images of PGP 9.5-LIR (PGP 9.5) in taste buds of rat and mouse circumvallate papillae. Longitudinal sections show a small subset of taste cells and nerve processes expressing PGP 9.5 in rat (A) and mouse taste buds (B). Both cytoplasm and nuclei of taste cells display PGP 9.5-LIR. Transverse sections show PGP 9.5-LIR in rat (C-E) and mouse taste buds (F-H). Immunoreactive taste cells and nerve processes are shown in C and F. Sytox-stained nuclei are shown in D and G and merges are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F3_8826.jpg | What is the principal component of this image? | Confocal laser scanning microscopy (CLSM) images of PGP 9.5-LIR (PGP 9.5) in taste buds of rat and mouse circumvallate papillae. Longitudinal sections show a small subset of taste cells and nerve processes expressing PGP 9.5 in rat (A) and mouse taste buds (B). Both cytoplasm and nuclei of taste cells display PGP 9.5-LIR. Transverse sections show PGP 9.5-LIR in rat (C-E) and mouse taste buds (F-H). Immunoreactive taste cells and nerve processes are shown in C and F. Sytox-stained nuclei are shown in D and G and merges are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F3_8828.jpg | What can you see in this picture? | Confocal laser scanning microscopy (CLSM) images of PGP 9.5-LIR (PGP 9.5) in taste buds of rat and mouse circumvallate papillae. Longitudinal sections show a small subset of taste cells and nerve processes expressing PGP 9.5 in rat (A) and mouse taste buds (B). Both cytoplasm and nuclei of taste cells display PGP 9.5-LIR. Transverse sections show PGP 9.5-LIR in rat (C-E) and mouse taste buds (F-H). Immunoreactive taste cells and nerve processes are shown in C and F. Sytox-stained nuclei are shown in D and G and merges are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F4_8836.jpg | What's the most prominent thing you notice in this picture? | Confocal laser scanning microscopy (CLSM) images of α-gustducin-LIR (α-gustducin) in taste buds of rat and mouse circumvallate papillae. Longitudinal sections show a subset of taste cells displaying α-gustducin-LIR in rat (A) and mouse taste buds (B). The α-gustducin-LIR taste cells are spindle-shaped with large, round nuclei. Transverse sections show α-gustducin-LIR in rat (C-E) and mouse taste buds (F-H). The immunoreactivity is only cytoplasmic in both transverse and longitudinal sections. Immunoreactive taste cells (red) are shown in C and F. Sytox-stained nuclei (green) are shown in D and G and merges are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F4_8834.jpg | What can you see in this picture? | Confocal laser scanning microscopy (CLSM) images of α-gustducin-LIR (α-gustducin) in taste buds of rat and mouse circumvallate papillae. Longitudinal sections show a subset of taste cells displaying α-gustducin-LIR in rat (A) and mouse taste buds (B). The α-gustducin-LIR taste cells are spindle-shaped with large, round nuclei. Transverse sections show α-gustducin-LIR in rat (C-E) and mouse taste buds (F-H). The immunoreactivity is only cytoplasmic in both transverse and longitudinal sections. Immunoreactive taste cells (red) are shown in C and F. Sytox-stained nuclei (green) are shown in D and G and merges are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F4_8829.jpg | What is the core subject represented in this visual? | Confocal laser scanning microscopy (CLSM) images of α-gustducin-LIR (α-gustducin) in taste buds of rat and mouse circumvallate papillae. Longitudinal sections show a subset of taste cells displaying α-gustducin-LIR in rat (A) and mouse taste buds (B). The α-gustducin-LIR taste cells are spindle-shaped with large, round nuclei. Transverse sections show α-gustducin-LIR in rat (C-E) and mouse taste buds (F-H). The immunoreactivity is only cytoplasmic in both transverse and longitudinal sections. Immunoreactive taste cells (red) are shown in C and F. Sytox-stained nuclei (green) are shown in D and G and merges are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F4_8830.jpg | Can you identify the primary element in this image? | Confocal laser scanning microscopy (CLSM) images of α-gustducin-LIR (α-gustducin) in taste buds of rat and mouse circumvallate papillae. Longitudinal sections show a subset of taste cells displaying α-gustducin-LIR in rat (A) and mouse taste buds (B). The α-gustducin-LIR taste cells are spindle-shaped with large, round nuclei. Transverse sections show α-gustducin-LIR in rat (C-E) and mouse taste buds (F-H). The immunoreactivity is only cytoplasmic in both transverse and longitudinal sections. Immunoreactive taste cells (red) are shown in C and F. Sytox-stained nuclei (green) are shown in D and G and merges are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F4_8831.jpg | What is the focal point of this photograph? | Confocal laser scanning microscopy (CLSM) images of α-gustducin-LIR (α-gustducin) in taste buds of rat and mouse circumvallate papillae. Longitudinal sections show a subset of taste cells displaying α-gustducin-LIR in rat (A) and mouse taste buds (B). The α-gustducin-LIR taste cells are spindle-shaped with large, round nuclei. Transverse sections show α-gustducin-LIR in rat (C-E) and mouse taste buds (F-H). The immunoreactivity is only cytoplasmic in both transverse and longitudinal sections. Immunoreactive taste cells (red) are shown in C and F. Sytox-stained nuclei (green) are shown in D and G and merges are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F4_8832.jpg | What object or scene is depicted here? | Confocal laser scanning microscopy (CLSM) images of α-gustducin-LIR (α-gustducin) in taste buds of rat and mouse circumvallate papillae. Longitudinal sections show a subset of taste cells displaying α-gustducin-LIR in rat (A) and mouse taste buds (B). The α-gustducin-LIR taste cells are spindle-shaped with large, round nuclei. Transverse sections show α-gustducin-LIR in rat (C-E) and mouse taste buds (F-H). The immunoreactivity is only cytoplasmic in both transverse and longitudinal sections. Immunoreactive taste cells (red) are shown in C and F. Sytox-stained nuclei (green) are shown in D and G and merges are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F5_8837.jpg | What key item or scene is captured in this photo? | Confocal laser scanning microscopy (CLSM) images of PLCβ2-LIR (PLCβ2) in taste buds of rat or mouse circumvallate papillae. Longitudinal sections show a large subset of taste cells expressing PLCβ2 in rat (A) and mouse taste buds (B). The PLCβ2-LIR taste cells are spindle-shaped with large, round nuclei. Transverse sections show PLCβ2-LIR in rat (C-E) and mouse taste buds (F-H). The immunoreactivity is restricted to the cytoplasm in both transverse and longitudinal sections. Immunoreactive taste cells (red) are shown in C and F. Sytox-stained nuclei (green) are shown in D and G and merges are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F5_8842.jpg | What stands out most in this visual? | Confocal laser scanning microscopy (CLSM) images of PLCβ2-LIR (PLCβ2) in taste buds of rat or mouse circumvallate papillae. Longitudinal sections show a large subset of taste cells expressing PLCβ2 in rat (A) and mouse taste buds (B). The PLCβ2-LIR taste cells are spindle-shaped with large, round nuclei. Transverse sections show PLCβ2-LIR in rat (C-E) and mouse taste buds (F-H). The immunoreactivity is restricted to the cytoplasm in both transverse and longitudinal sections. Immunoreactive taste cells (red) are shown in C and F. Sytox-stained nuclei (green) are shown in D and G and merges are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F5_8844.jpg | What is being portrayed in this visual content? | Confocal laser scanning microscopy (CLSM) images of PLCβ2-LIR (PLCβ2) in taste buds of rat or mouse circumvallate papillae. Longitudinal sections show a large subset of taste cells expressing PLCβ2 in rat (A) and mouse taste buds (B). The PLCβ2-LIR taste cells are spindle-shaped with large, round nuclei. Transverse sections show PLCβ2-LIR in rat (C-E) and mouse taste buds (F-H). The immunoreactivity is restricted to the cytoplasm in both transverse and longitudinal sections. Immunoreactive taste cells (red) are shown in C and F. Sytox-stained nuclei (green) are shown in D and G and merges are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F5_8839.jpg | What is the central feature of this picture? | Confocal laser scanning microscopy (CLSM) images of PLCβ2-LIR (PLCβ2) in taste buds of rat or mouse circumvallate papillae. Longitudinal sections show a large subset of taste cells expressing PLCβ2 in rat (A) and mouse taste buds (B). The PLCβ2-LIR taste cells are spindle-shaped with large, round nuclei. Transverse sections show PLCβ2-LIR in rat (C-E) and mouse taste buds (F-H). The immunoreactivity is restricted to the cytoplasm in both transverse and longitudinal sections. Immunoreactive taste cells (red) are shown in C and F. Sytox-stained nuclei (green) are shown in D and G and merges are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F6_8846.jpg | Describe the main subject of this image. | Confocal laser scanning microscopy (CLSM) images of synaptobrevin-2-LIR (VAMP-2) in taste buds of rat or mouse circumvallate papillae. Longitudinal sections show a large subset of taste cells and nerve processes displaying synaptobrevin-2-LIR in rat (A) and mouse taste buds (B). Transverse sections show synaptobrevin-2-LIR in rat (C-E) and mouse taste buds (F-H). The red are immunoreactive taste cells and nerve processes (C and F). Immunoreactivity is restricted to the cytoplasm (red) in both transverse and longitudinal sections. Sytox-stained nuclei (green) are shown in D and G and merges are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F6_8851.jpg | What is the central feature of this picture? | Confocal laser scanning microscopy (CLSM) images of synaptobrevin-2-LIR (VAMP-2) in taste buds of rat or mouse circumvallate papillae. Longitudinal sections show a large subset of taste cells and nerve processes displaying synaptobrevin-2-LIR in rat (A) and mouse taste buds (B). Transverse sections show synaptobrevin-2-LIR in rat (C-E) and mouse taste buds (F-H). The red are immunoreactive taste cells and nerve processes (C and F). Immunoreactivity is restricted to the cytoplasm (red) in both transverse and longitudinal sections. Sytox-stained nuclei (green) are shown in D and G and merges are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F6_8852.jpg | Can you identify the primary element in this image? | Confocal laser scanning microscopy (CLSM) images of synaptobrevin-2-LIR (VAMP-2) in taste buds of rat or mouse circumvallate papillae. Longitudinal sections show a large subset of taste cells and nerve processes displaying synaptobrevin-2-LIR in rat (A) and mouse taste buds (B). Transverse sections show synaptobrevin-2-LIR in rat (C-E) and mouse taste buds (F-H). The red are immunoreactive taste cells and nerve processes (C and F). Immunoreactivity is restricted to the cytoplasm (red) in both transverse and longitudinal sections. Sytox-stained nuclei (green) are shown in D and G and merges are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F6_8848.jpg | What is the focal point of this photograph? | Confocal laser scanning microscopy (CLSM) images of synaptobrevin-2-LIR (VAMP-2) in taste buds of rat or mouse circumvallate papillae. Longitudinal sections show a large subset of taste cells and nerve processes displaying synaptobrevin-2-LIR in rat (A) and mouse taste buds (B). Transverse sections show synaptobrevin-2-LIR in rat (C-E) and mouse taste buds (F-H). The red are immunoreactive taste cells and nerve processes (C and F). Immunoreactivity is restricted to the cytoplasm (red) in both transverse and longitudinal sections. Sytox-stained nuclei (green) are shown in D and G and merges are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F6_8845.jpg | What is the central feature of this picture? | Confocal laser scanning microscopy (CLSM) images of synaptobrevin-2-LIR (VAMP-2) in taste buds of rat or mouse circumvallate papillae. Longitudinal sections show a large subset of taste cells and nerve processes displaying synaptobrevin-2-LIR in rat (A) and mouse taste buds (B). Transverse sections show synaptobrevin-2-LIR in rat (C-E) and mouse taste buds (F-H). The red are immunoreactive taste cells and nerve processes (C and F). Immunoreactivity is restricted to the cytoplasm (red) in both transverse and longitudinal sections. Sytox-stained nuclei (green) are shown in D and G and merges are shown in E and H. Scale bars = 20 μm. |
PMC1779794_F6_8849.jpg | What is the principal component of this image? | Confocal laser scanning microscopy (CLSM) images of synaptobrevin-2-LIR (VAMP-2) in taste buds of rat or mouse circumvallate papillae. Longitudinal sections show a large subset of taste cells and nerve processes displaying synaptobrevin-2-LIR in rat (A) and mouse taste buds (B). Transverse sections show synaptobrevin-2-LIR in rat (C-E) and mouse taste buds (F-H). The red are immunoreactive taste cells and nerve processes (C and F). Immunoreactivity is restricted to the cytoplasm (red) in both transverse and longitudinal sections. Sytox-stained nuclei (green) are shown in D and G and merges are shown in E and H. Scale bars = 20 μm. |
PMC1779795_F7_8853.jpg | What is the core subject represented in this visual? | Sagittal transperineal sonography showing the recurrent mass in the same patient occupying the rectovaginal septum. The vagina has been filled with acoustic contrast. |
PMC1779809_pone-0000179-g002_8858.jpg | What is the central feature of this picture? | Clustered podosomes.Intact osteoclast (A,B) or ventral membranes (C–E) fixed and stained for actin (A) or paxillin (B) or prepared for HR-SEM (C–E). (A) Actin pillars emanate from an “actin-cloud”. (B) Paxillin is largely shared by the cluster and overlaps with the “actin-cloud”. The insert in (A) shows a merged image of actin/paxillin staining. (C) SEM over-view of a cluster. The radial podosome actin fibers appear to correspond to the “actin-cloud”. (D) Higher magnification view of two clustered podosomes showing interactions between radial peripheral cables. There are no cables directly connecting between cores. (E) The same organization as in (D) is detected on bone. |
PMC1779809_pone-0000179-g002_8857.jpg | What is the main focus of this visual representation? | Clustered podosomes.Intact osteoclast (A,B) or ventral membranes (C–E) fixed and stained for actin (A) or paxillin (B) or prepared for HR-SEM (C–E). (A) Actin pillars emanate from an “actin-cloud”. (B) Paxillin is largely shared by the cluster and overlaps with the “actin-cloud”. The insert in (A) shows a merged image of actin/paxillin staining. (C) SEM over-view of a cluster. The radial podosome actin fibers appear to correspond to the “actin-cloud”. (D) Higher magnification view of two clustered podosomes showing interactions between radial peripheral cables. There are no cables directly connecting between cores. (E) The same organization as in (D) is detected on bone. |
PMC1779809_pone-0000179-g002_8855.jpg | What does this image primarily show? | Clustered podosomes.Intact osteoclast (A,B) or ventral membranes (C–E) fixed and stained for actin (A) or paxillin (B) or prepared for HR-SEM (C–E). (A) Actin pillars emanate from an “actin-cloud”. (B) Paxillin is largely shared by the cluster and overlaps with the “actin-cloud”. The insert in (A) shows a merged image of actin/paxillin staining. (C) SEM over-view of a cluster. The radial podosome actin fibers appear to correspond to the “actin-cloud”. (D) Higher magnification view of two clustered podosomes showing interactions between radial peripheral cables. There are no cables directly connecting between cores. (E) The same organization as in (D) is detected on bone. |
PMC1779809_pone-0000179-g002_8854.jpg | What is shown in this image? | Clustered podosomes.Intact osteoclast (A,B) or ventral membranes (C–E) fixed and stained for actin (A) or paxillin (B) or prepared for HR-SEM (C–E). (A) Actin pillars emanate from an “actin-cloud”. (B) Paxillin is largely shared by the cluster and overlaps with the “actin-cloud”. The insert in (A) shows a merged image of actin/paxillin staining. (C) SEM over-view of a cluster. The radial podosome actin fibers appear to correspond to the “actin-cloud”. (D) Higher magnification view of two clustered podosomes showing interactions between radial peripheral cables. There are no cables directly connecting between cores. (E) The same organization as in (D) is detected on bone. |
PMC1779809_pone-0000179-g003_8861.jpg | What does this image primarily show? | Sealing zone-like structure.Intact osteoclast (A,B) or ventral membrane (C, D) on glass cover-slips were fixed and stained for actin (A) or paxillin (B) or prepared for HR-SEM (C–D). (A) A dense actin belt is surrounded by inner and outer paxillin belts (B). The insert in (A) shows a merged image of actin/paxillin staining. (C) SEM over-view of a sealing zone-like structure on glass: note the continuous, robust actin organization. (D) Higher magnification view of two neighboring pillars showing numerous inter-pillar cables. |
PMC1779809_pone-0000179-g003_8860.jpg | What is the central feature of this picture? | Sealing zone-like structure.Intact osteoclast (A,B) or ventral membrane (C, D) on glass cover-slips were fixed and stained for actin (A) or paxillin (B) or prepared for HR-SEM (C–D). (A) A dense actin belt is surrounded by inner and outer paxillin belts (B). The insert in (A) shows a merged image of actin/paxillin staining. (C) SEM over-view of a sealing zone-like structure on glass: note the continuous, robust actin organization. (D) Higher magnification view of two neighboring pillars showing numerous inter-pillar cables. |
PMC1779809_pone-0000179-g003_8859.jpg | What is the central feature of this picture? | Sealing zone-like structure.Intact osteoclast (A,B) or ventral membrane (C, D) on glass cover-slips were fixed and stained for actin (A) or paxillin (B) or prepared for HR-SEM (C–D). (A) A dense actin belt is surrounded by inner and outer paxillin belts (B). The insert in (A) shows a merged image of actin/paxillin staining. (C) SEM over-view of a sealing zone-like structure on glass: note the continuous, robust actin organization. (D) Higher magnification view of two neighboring pillars showing numerous inter-pillar cables. |
PMC1779809_pone-0000179-g004_8869.jpg | What is the central feature of this picture? | Sealing zone.(A, B) Frames from a movie taken by time-lapse microscopy from live GFP-actin osteoclasts plated on bone. (A) Four frames taken at 10 minutes intervals showing dynamic reorganization of actin belts. (B)One minute temporal ratio figure. Blue pixels represent new structures and red pixels faded structures. Note the high rate of dynamic reorganization. (C–E)Osteoclast ventral membrane on bone. (C) SEM overview of the ventral membrane of a cell plated on bone. The central area (arrow head) presumably corresponds to the ruffled border. The sealing zone (double arrow) is thicker than on glass. (D, E) Higher magnification views (from yellow box in (E)) of the podosomes forming the sealing zone. (F) Osteoclasts were plated on bone slices and removed three days later, leaving numerous resorption pits on the surface. |
PMC1779809_pone-0000179-g004_8866.jpg | What is shown in this image? | Sealing zone.(A, B) Frames from a movie taken by time-lapse microscopy from live GFP-actin osteoclasts plated on bone. (A) Four frames taken at 10 minutes intervals showing dynamic reorganization of actin belts. (B)One minute temporal ratio figure. Blue pixels represent new structures and red pixels faded structures. Note the high rate of dynamic reorganization. (C–E)Osteoclast ventral membrane on bone. (C) SEM overview of the ventral membrane of a cell plated on bone. The central area (arrow head) presumably corresponds to the ruffled border. The sealing zone (double arrow) is thicker than on glass. (D, E) Higher magnification views (from yellow box in (E)) of the podosomes forming the sealing zone. (F) Osteoclasts were plated on bone slices and removed three days later, leaving numerous resorption pits on the surface. |
PMC1779809_pone-0000179-g004_8865.jpg | What is shown in this image? | Sealing zone.(A, B) Frames from a movie taken by time-lapse microscopy from live GFP-actin osteoclasts plated on bone. (A) Four frames taken at 10 minutes intervals showing dynamic reorganization of actin belts. (B)One minute temporal ratio figure. Blue pixels represent new structures and red pixels faded structures. Note the high rate of dynamic reorganization. (C–E)Osteoclast ventral membrane on bone. (C) SEM overview of the ventral membrane of a cell plated on bone. The central area (arrow head) presumably corresponds to the ruffled border. The sealing zone (double arrow) is thicker than on glass. (D, E) Higher magnification views (from yellow box in (E)) of the podosomes forming the sealing zone. (F) Osteoclasts were plated on bone slices and removed three days later, leaving numerous resorption pits on the surface. |
PMC1779809_pone-0000179-g004_8867.jpg | Describe the main subject of this image. | Sealing zone.(A, B) Frames from a movie taken by time-lapse microscopy from live GFP-actin osteoclasts plated on bone. (A) Four frames taken at 10 minutes intervals showing dynamic reorganization of actin belts. (B)One minute temporal ratio figure. Blue pixels represent new structures and red pixels faded structures. Note the high rate of dynamic reorganization. (C–E)Osteoclast ventral membrane on bone. (C) SEM overview of the ventral membrane of a cell plated on bone. The central area (arrow head) presumably corresponds to the ruffled border. The sealing zone (double arrow) is thicker than on glass. (D, E) Higher magnification views (from yellow box in (E)) of the podosomes forming the sealing zone. (F) Osteoclasts were plated on bone slices and removed three days later, leaving numerous resorption pits on the surface. |
PMC1779809_pone-0000179-g004_8863.jpg | What is the main focus of this visual representation? | Sealing zone.(A, B) Frames from a movie taken by time-lapse microscopy from live GFP-actin osteoclasts plated on bone. (A) Four frames taken at 10 minutes intervals showing dynamic reorganization of actin belts. (B)One minute temporal ratio figure. Blue pixels represent new structures and red pixels faded structures. Note the high rate of dynamic reorganization. (C–E)Osteoclast ventral membrane on bone. (C) SEM overview of the ventral membrane of a cell plated on bone. The central area (arrow head) presumably corresponds to the ruffled border. The sealing zone (double arrow) is thicker than on glass. (D, E) Higher magnification views (from yellow box in (E)) of the podosomes forming the sealing zone. (F) Osteoclasts were plated on bone slices and removed three days later, leaving numerous resorption pits on the surface. |
PMC1779809_pone-0000179-g004_8868.jpg | What key item or scene is captured in this photo? | Sealing zone.(A, B) Frames from a movie taken by time-lapse microscopy from live GFP-actin osteoclasts plated on bone. (A) Four frames taken at 10 minutes intervals showing dynamic reorganization of actin belts. (B)One minute temporal ratio figure. Blue pixels represent new structures and red pixels faded structures. Note the high rate of dynamic reorganization. (C–E)Osteoclast ventral membrane on bone. (C) SEM overview of the ventral membrane of a cell plated on bone. The central area (arrow head) presumably corresponds to the ruffled border. The sealing zone (double arrow) is thicker than on glass. (D, E) Higher magnification views (from yellow box in (E)) of the podosomes forming the sealing zone. (F) Osteoclasts were plated on bone slices and removed three days later, leaving numerous resorption pits on the surface. |
PMC1779809_pone-0000179-g005_8872.jpg | Can you identify the primary element in this image? | Structural relations between podosome ring and core domains.(A) Osteoclast ventral membranes were labeled for paxillin and actin, and simultaneously prepared for HR-SEM. On the left is the actin labeling, followed by paxillin labeling and by their merged picture. On the right is the corresponding SEM micrograph. (B) Higher magnification view of the area in the yellow rectangle in (A). (C) Higher magnification view of the area in the yellow rectangle in (B). (D) Merged actin/paxillin labeling from the same area as in (C). (E) Merged image between (C) and (D). The correlation between SEM and immunofluorescence shows paxillin association with podosome radial actin fibers, reaching up to but not co-localizing with the central bundle. (F, G, H) Osteoclast ventral membranes were labeled for paxillin with 15nm colloidal gold particles and visualized by back scattering signal (F) or secondary electron detector (G, H). (F) and (G) show the same area. The colloidal gold particles in (G, H) are marked with brownish dots, showing paxillin in association with actin fibers in close proximity with the ventral membrane. |
PMC1779809_pone-0000179-g005_8877.jpg | What is the core subject represented in this visual? | Structural relations between podosome ring and core domains.(A) Osteoclast ventral membranes were labeled for paxillin and actin, and simultaneously prepared for HR-SEM. On the left is the actin labeling, followed by paxillin labeling and by their merged picture. On the right is the corresponding SEM micrograph. (B) Higher magnification view of the area in the yellow rectangle in (A). (C) Higher magnification view of the area in the yellow rectangle in (B). (D) Merged actin/paxillin labeling from the same area as in (C). (E) Merged image between (C) and (D). The correlation between SEM and immunofluorescence shows paxillin association with podosome radial actin fibers, reaching up to but not co-localizing with the central bundle. (F, G, H) Osteoclast ventral membranes were labeled for paxillin with 15nm colloidal gold particles and visualized by back scattering signal (F) or secondary electron detector (G, H). (F) and (G) show the same area. The colloidal gold particles in (G, H) are marked with brownish dots, showing paxillin in association with actin fibers in close proximity with the ventral membrane. |
PMC1779809_pone-0000179-g005_8874.jpg | What is the dominant medical problem in this image? | Structural relations between podosome ring and core domains.(A) Osteoclast ventral membranes were labeled for paxillin and actin, and simultaneously prepared for HR-SEM. On the left is the actin labeling, followed by paxillin labeling and by their merged picture. On the right is the corresponding SEM micrograph. (B) Higher magnification view of the area in the yellow rectangle in (A). (C) Higher magnification view of the area in the yellow rectangle in (B). (D) Merged actin/paxillin labeling from the same area as in (C). (E) Merged image between (C) and (D). The correlation between SEM and immunofluorescence shows paxillin association with podosome radial actin fibers, reaching up to but not co-localizing with the central bundle. (F, G, H) Osteoclast ventral membranes were labeled for paxillin with 15nm colloidal gold particles and visualized by back scattering signal (F) or secondary electron detector (G, H). (F) and (G) show the same area. The colloidal gold particles in (G, H) are marked with brownish dots, showing paxillin in association with actin fibers in close proximity with the ventral membrane. |
PMC1779809_pone-0000179-g005_8870.jpg | What key item or scene is captured in this photo? | Structural relations between podosome ring and core domains.(A) Osteoclast ventral membranes were labeled for paxillin and actin, and simultaneously prepared for HR-SEM. On the left is the actin labeling, followed by paxillin labeling and by their merged picture. On the right is the corresponding SEM micrograph. (B) Higher magnification view of the area in the yellow rectangle in (A). (C) Higher magnification view of the area in the yellow rectangle in (B). (D) Merged actin/paxillin labeling from the same area as in (C). (E) Merged image between (C) and (D). The correlation between SEM and immunofluorescence shows paxillin association with podosome radial actin fibers, reaching up to but not co-localizing with the central bundle. (F, G, H) Osteoclast ventral membranes were labeled for paxillin with 15nm colloidal gold particles and visualized by back scattering signal (F) or secondary electron detector (G, H). (F) and (G) show the same area. The colloidal gold particles in (G, H) are marked with brownish dots, showing paxillin in association with actin fibers in close proximity with the ventral membrane. |
PMC1779809_pone-0000179-g005_8875.jpg | What can you see in this picture? | Structural relations between podosome ring and core domains.(A) Osteoclast ventral membranes were labeled for paxillin and actin, and simultaneously prepared for HR-SEM. On the left is the actin labeling, followed by paxillin labeling and by their merged picture. On the right is the corresponding SEM micrograph. (B) Higher magnification view of the area in the yellow rectangle in (A). (C) Higher magnification view of the area in the yellow rectangle in (B). (D) Merged actin/paxillin labeling from the same area as in (C). (E) Merged image between (C) and (D). The correlation between SEM and immunofluorescence shows paxillin association with podosome radial actin fibers, reaching up to but not co-localizing with the central bundle. (F, G, H) Osteoclast ventral membranes were labeled for paxillin with 15nm colloidal gold particles and visualized by back scattering signal (F) or secondary electron detector (G, H). (F) and (G) show the same area. The colloidal gold particles in (G, H) are marked with brownish dots, showing paxillin in association with actin fibers in close proximity with the ventral membrane. |
PMC1779809_pone-0000179-g005_8873.jpg | What does this image primarily show? | Structural relations between podosome ring and core domains.(A) Osteoclast ventral membranes were labeled for paxillin and actin, and simultaneously prepared for HR-SEM. On the left is the actin labeling, followed by paxillin labeling and by their merged picture. On the right is the corresponding SEM micrograph. (B) Higher magnification view of the area in the yellow rectangle in (A). (C) Higher magnification view of the area in the yellow rectangle in (B). (D) Merged actin/paxillin labeling from the same area as in (C). (E) Merged image between (C) and (D). The correlation between SEM and immunofluorescence shows paxillin association with podosome radial actin fibers, reaching up to but not co-localizing with the central bundle. (F, G, H) Osteoclast ventral membranes were labeled for paxillin with 15nm colloidal gold particles and visualized by back scattering signal (F) or secondary electron detector (G, H). (F) and (G) show the same area. The colloidal gold particles in (G, H) are marked with brownish dots, showing paxillin in association with actin fibers in close proximity with the ventral membrane. |
PMC1779809_pone-0000179-g005_8871.jpg | What is the core subject represented in this visual? | Structural relations between podosome ring and core domains.(A) Osteoclast ventral membranes were labeled for paxillin and actin, and simultaneously prepared for HR-SEM. On the left is the actin labeling, followed by paxillin labeling and by their merged picture. On the right is the corresponding SEM micrograph. (B) Higher magnification view of the area in the yellow rectangle in (A). (C) Higher magnification view of the area in the yellow rectangle in (B). (D) Merged actin/paxillin labeling from the same area as in (C). (E) Merged image between (C) and (D). The correlation between SEM and immunofluorescence shows paxillin association with podosome radial actin fibers, reaching up to but not co-localizing with the central bundle. (F, G, H) Osteoclast ventral membranes were labeled for paxillin with 15nm colloidal gold particles and visualized by back scattering signal (F) or secondary electron detector (G, H). (F) and (G) show the same area. The colloidal gold particles in (G, H) are marked with brownish dots, showing paxillin in association with actin fibers in close proximity with the ventral membrane. |
PMC1780055_F1_8885.jpg | What key item or scene is captured in this photo? | A, C Pre-Operative MRI: contrast-enhancing lesion in the left and right frontal lobe. B MRI follow-up after 6 month: no recurrence of the tumor after resection and irradiation (left frontal). D MRI follow-up after 6 month: no progression of the tumor after irradiation only (right frontal). |
PMC1780055_F1_8882.jpg | What is the core subject represented in this visual? | A, C Pre-Operative MRI: contrast-enhancing lesion in the left and right frontal lobe. B MRI follow-up after 6 month: no recurrence of the tumor after resection and irradiation (left frontal). D MRI follow-up after 6 month: no progression of the tumor after irradiation only (right frontal). |
PMC1780055_F1_8883.jpg | What stands out most in this visual? | A, C Pre-Operative MRI: contrast-enhancing lesion in the left and right frontal lobe. B MRI follow-up after 6 month: no recurrence of the tumor after resection and irradiation (left frontal). D MRI follow-up after 6 month: no progression of the tumor after irradiation only (right frontal). |
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