fig_num,sub_section_headings,images-src,image_caption
Figure 19.1,Proteoglycans,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.1-e1635972748210.png,Figure 19.1: Overview of the extracellular matrix.
Figure 19.2,Integrins,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.2-e1635972764472.png,Figure 19.2: Schematic of integrin structure. The protein spans the plasma membrane and is an extracellular domain that can bind other matrix proteins.
Figure 19.3,Cell adhesion to the substratum,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.3.png,Figure 19.3: Summary of cell adhesion mechanisms.
Figure 19.1,There are four kinds of connections between cells:,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.1-e1635972748210.png,Figure 19.1: Overview of the extracellular matrix.
Figure 19.2,There are four kinds of connections between cells:,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.2-e1635972764472.png,Figure 19.2: Schematic of integrin structure. The protein spans the plasma membrane and is an extracellular domain that can bind other matrix proteins.
Figure 19.3,There are four kinds of connections between cells:,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/19.3.png,Figure 19.3: Summary of cell adhesion mechanisms.
Figure 18.2,There are four kinds of connections between cells:,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.2-e1635972595863.png,"Figure 18.2: Spatial organization of the three types of fibers. Microfilaments thicken the cortex around the cell’s inner edge. Intermediate filaments have no role in cell movement. Their function is purely structural. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell."
Figure 18.3,Microfilaments,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.3-e1635972610753.png,"Figure 18.3: Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments."
Figure 18.4,Intermediate filaments,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.4-e1635972627658.png,Figure 18.4: Several strands of fibrous proteins that are wound together comprise intermediate filaments.
Figure 18.1,Intermediate filaments,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.1-1.png,Figure 18.1: Summary of the three major types of structural filaments.
Figure 18.5,Microtubules,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.5-e1635972644512.png,Figure 18.5: Microtubules are hollow. Their walls consist of thirteen polymerized dimers of α-tubulin and β-tubulin. The left image shows the tube’s molecular structure.
Figure 18.6,Flagella and cilia,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.6.jpeg,Figure 18.6: This transmission electron micrograph of two flagella shows the microtubules’ 9 + 2 array: nine microtubule doublets surround a single microtubule doublet.
Figure 18.1,Flagella and cilia,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.1-1.png,Figure 18.1: Summary of the three major types of structural filaments.
Figure 18.2,Flagella and cilia,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.2-e1635972595863.png,"Figure 18.2: Spatial organization of the three types of fibers. Microfilaments thicken the cortex around the cell’s inner edge. Intermediate filaments have no role in cell movement. Their function is purely structural. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell."
Figure 18.3,Flagella and cilia,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.3-e1635972610753.png,"Figure 18.3: Microfilaments are comprised of two globular protein intertwined strands, which we call actin. For this reason, we also call microfilaments actin filaments."
Figure 18.4,Flagella and cilia,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.4-e1635972627658.png,Figure 18.4: Several strands of fibrous proteins that are wound together comprise intermediate filaments.
Figure 18.5,Flagella and cilia,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.5-e1635972644512.png,Figure 18.5: Microtubules are hollow. Their walls consist of thirteen polymerized dimers of α-tubulin and β-tubulin. The left image shows the tube’s molecular structure.
Figure 18.7,Flagella and cilia,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.7-e1635972668710.png,Figure 18.7: Comparison of the three different motor proteins.
Figure 18.8,Kinesin,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.8-e1635972686879.png,Figure 18.8: Summary of the roles and movement of the motor proteins along various cytoskeletal elements.
Figure 18.7,Kinesin,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.7-e1635972668710.png,Figure 18.7: Comparison of the three different motor proteins.
Figure 18.2,Kinesin,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/18.2-e1635972595863.png,"Figure 18.2: Spatial organization of the three types of fibers. Microfilaments thicken the cortex around the cell’s inner edge. Intermediate filaments have no role in cell movement. Their function is purely structural. They help the cell resist compression, provide a track along which vesicles move through the cell, and pull replicated chromosomes to opposite ends of a dividing cell."
Figure 17.1,Organization of the nucleus,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.1.jpeg,Figure 17.1: EM of the nucleus and nucleolus.
Figure 17.2,Endomembrane system,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
Figure 17.2,The endoplasmic reticulum (ER),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
Figure 17.3,Protein degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.3-scaled.jpg,Figure 17.3: Unfolded protein response in the RER.
Figure 17.2,Lysosomes and peroxisomes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.2-e1635972577198.png,Figure 17.2: Interaction of the endomembrane systems.
Figure 17.3,Lysosomes and peroxisomes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.3-scaled.jpg,Figure 17.3: Unfolded protein response in the RER.
Figure 17.1,Lysosomes and peroxisomes,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.1.jpeg,Figure 17.1: EM of the nucleus and nucleolus.
Figure 17.4,Phagocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.4-scaled.jpg,"Figure 17.4: General process of phagocytosis. In phagocytosis, the cell membrane surrounds the particle and engulfs it."
Figure 17.5,Receptor-mediated endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.5-scaled.jpg,Figure 17.5: Receptor-mediated endocytosis; LDL receptor is a classic example of this process.
Figure 17.6,Exocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.6-scaled.jpg,Figure 17.6: Exocytosis: vesicles containing substances fuse with the plasma membrane. The contents then release to the cell’s exterior.
Figure 17.4,Exocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.4-scaled.jpg,"Figure 17.4: General process of phagocytosis. In phagocytosis, the cell membrane surrounds the particle and engulfs it."
Figure 17.5,Exocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/17.5-scaled.jpg,Figure 17.5: Receptor-mediated endocytosis; LDL receptor is a classic example of this process.
Figure 16.1,Fluid mosaic model,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
Figure 16.2,Lipids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
Figure 16.2,phosphatecontaining,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
Figure 16.3,phosphatecontaining,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
Figure 16.1,Membrane fluidity,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.1-scaled.jpg,Figure 16.1: Schematic of the cell membrane. Plasma membranes range from 5 to 10 nm in thickness.
Figure 16.2,Membrane fluidity,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.2-scaled.jpg,Figure 16.2: Structure of a phospholipid.
Figure 16.3,Membrane fluidity,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.3-1024x472.png,Figure 16.3: Important membrane lipids.
Figure 16.4,Diffusion,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
Figure 16.5,Osmosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
Figure 16.6,Isotonic solutions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
Figure 16.7,Ion channels,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
Figure 16.8,Carrier proteins,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.8-scaled.jpg,"Figure 16.8: Carrier proteins. This aptly named protein binds a substance and thus triggers a change of its own shape, moving the bound molecule from the cell’s outside to its interior."
Figure 16.4,Carrier proteins,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.4-scaled.jpg,Figure 16.4: Diffusion across the plasma membrane.
Figure 16.5,Carrier proteins,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.5-e1635971760807.png,"Figure 16.5: Illustration of osmosis. In the diagram, the solute cannot pass through the selectively permeable membrane, but the water can."
Figure 16.6,Carrier proteins,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.6-e1635971779949.png,"Figure 16.6: Comparison of red blood cell morphology in isotonic, hypertonic, and hypotonic solutions."
Figure 16.7,Carrier proteins,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.7-scaled.jpg,Figure 16.7: Protein channel.
Figure 16.9,Electrochemical gradient,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
Figure 16.10,Carrier proteins for active transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
Figure 16.11,Primary active transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
Figure 16.9,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.9-scaled.jpg,Figure 16.9: Electrochemical gradients.
Figure 16.10,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.10-scaled.jpg,Figure 16.10: Different types of carrier proteins for active transport.
Figure 16.11,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/16.11-scaled.jpg,Figure 16.11: Primary active transport.
Figure 15.1,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
Figure 15.3,General G-protein-coupled receptor cascade,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
Figure 15.4,Phosphatidylinositol-derived second messengers,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
Figure 15.1,NO as a messenger,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.1-scaled.jpg,Figure 15.1: Summary of types of cell signaling.
Figure 15.2,NO as a messenger,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.2-scaled.jpg,Figure 15.2: Examples of steroid hormones.
Figure 15.3,NO as a messenger,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.3-scaled.jpg,Figure 15.3: Common G-protein-coupled receptor signaling cascade.
Figure 15.4,NO as a messenger,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.4-scaled.jpg,Figure 15.4: Signaling cascade initiated by DAG and IP3.
Figure 15.5,NO as a messenger,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.5-scaled.jpg,Figure 15.5: Receptor tyrosine kinase signaling.
Figure 15.6,NO as a messenger,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
Figure 15.6,caspases,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.6-scaled.jpg,Figure 15.6: Comparison of intrinsic and extrinsic apoptosis pathways.
Figure 15.7,caspases,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
Figure 15.7,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.7-scaled.jpg,Figure 15.7: Neurotransmission by acetylcholine.
Figure 15.9,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.9-scaled.jpg,Figure 15.9: Summary of the action potential as it relates to change in ion concentration across the membrane.
Figure 15.8,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/15.8-scaled.jpg,Figure 15.8: Summary of the action potential to membrane potential.
Figure 14.1,Frequency of the dominant allele:,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.1-scaled.jpg,Figure 14.1: Punnett square illustrating allelic distribution of recessive traits.
Figure 14.2,Frequency of the dominant allele:,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.2-scaled.jpg,Figure 14.2: Allelic distributions in dominant traits.
Figure 14.3,Additional resources,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
Figure 14.4,Extranuclear inheritance,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
Figure 14.5,Trinucleotide repeat disorders,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
Figure 14.3,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.3-scaled.jpg,Figure 14.3: Graphic representation of penetrance and expressivity.
Figure 14.4,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.4.png,Figure 14.4: Mitochondrial inheritance pattern.
Figure 14.5,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.5-scaled.jpg,Figure 14.5: Trinucleotide repeat expansion characteristic of Huntington’s disease.
Figure 14.6,"For linkage to occur, two conditions must be met:",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
Figure 14.7,Genome-wide association studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.7-scaled.jpg,Figure 14.7: Schematic of GWAS.
Figure 14.6,Genome-wide association studies (GWAS),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/14.6-scaled-e1636024890871.jpg,Figure 14.6: Relationship between centimorgans and recombination frequency.
Figure 13.1,Genetics methodology,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.1.jpg,Figure 13.1: Representative karyotype illustrating twenty-two pairs of autosomes and one pair of sex chromosomes.
Figure 13.2,Chromosome structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.2-scaled.jpg,Figure 13.2: Basics of chromosome structure.
Figure 13.3,Nondisjunction,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.3-e1635968565417.png,Figure 13.3: Summary of meiotic and mitotic cell divisions.
Figure 13.4,Meiotic nondisjunction,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.4-scaled.jpg,Figure 13.4: Comparison of nondisjunction in meiosis I versus meiosis II.
Figure 13.5,Mitotic nondisjunction,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.5-scaled-e1635968989259.jpg,Figure 13.5: Mosaicism resulting in cells with differing genetics across the body.
Figure 13.6,Deletions and duplications,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.6-scaled.jpg,Figure 13.6: Genetic basis of Prader-Willi syndrome (PWS) and Angelman syndrome (AS). UPD: Uniparental disomy; Square: imprinting on the maternal allele.
Figure 13.7,Inversion,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
Figure 13.7,Translocations,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
Figure 13.1,Translocations can be classified as either reciprocal or Robertsonian.,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.1.jpg,Figure 13.1: Representative karyotype illustrating twenty-two pairs of autosomes and one pair of sex chromosomes.
Figure 13.6,Translocations can be classified as either reciprocal or Robertsonian.,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.6-scaled.jpg,Figure 13.6: Genetic basis of Prader-Willi syndrome (PWS) and Angelman syndrome (AS). UPD: Uniparental disomy; Square: imprinting on the maternal allele.
Figure 13.2,Translocations can be classified as either reciprocal or Robertsonian.,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.2-scaled.jpg,Figure 13.2: Basics of chromosome structure.
Figure 13.3,Translocations can be classified as either reciprocal or Robertsonian.,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.3-e1635968565417.png,Figure 13.3: Summary of meiotic and mitotic cell divisions.
Figure 13.4,Translocations can be classified as either reciprocal or Robertsonian.,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.4-scaled.jpg,Figure 13.4: Comparison of nondisjunction in meiosis I versus meiosis II.
Figure 13.5,Translocations can be classified as either reciprocal or Robertsonian.,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.5-scaled-e1635968989259.jpg,Figure 13.5: Mosaicism resulting in cells with differing genetics across the body.
Figure 13.7,Translocations can be classified as either reciprocal or Robertsonian.,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.7-scaled.jpg,Figure 13.7: Example of a chromosome inversion and translocation.
Figure 13.8,DNA and RNA extraction,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.8-e1635968879155.png,Figure 13.8: Basic process for DNA extraction.
Figure 13.9,Karoytype and high-resolution banding,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.9-scaled.jpg,Figure 13.9: Male karyotype with G-banding patterns.
Figure 13.10,DNA sequencing techniques,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.10-scaled.jpg,Figure 13.10: Schematic of Sanger sequencing technique.
Figure 13.11,Nucleic acid fragment amplification by polymerase chain reaction (PCR),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.11-scaled.jpg,Figure 13.11: Overview of polymerase chain reaction.
Figure 13.12,"Hybridization, southern blotting, and northern blotting",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.12-scaled.jpg,Figure 13.12: Schematic of southern blotting technique.
Figure 13.8,"Hybridization, southern blotting, and northern blotting",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.8-e1635968879155.png,Figure 13.8: Basic process for DNA extraction.
Figure 13.10,"Hybridization, southern blotting, and northern blotting",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.10-scaled.jpg,Figure 13.10: Schematic of Sanger sequencing technique.
Figure 13.11,"Hybridization, southern blotting, and northern blotting",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.11-scaled.jpg,Figure 13.11: Overview of polymerase chain reaction.
Figure 13.9,"Hybridization, southern blotting, and northern blotting",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/13.9-scaled.jpg,Figure 13.9: Male karyotype with G-banding patterns.
Figure 12.1,Transcription factors: Enhancers,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
Figure 12.2,Transcription factors: Repressors,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
Figure 12.2,Transcription factors: Structure and function,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
Figure 12.3,Alternative RNA splicing,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
Figure 12.4,Translational initiation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
Figure 12.5,RNA-binding proteins,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
Figure 12.6,Protein degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.6-scaled.jpg,Figure 12.6: Proteasome-mediated degradation.
Figure 12.1,Protein degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.1-scaled.jpg,Figure 12.1: Example of transcriptional complex involving two separate genes.
Figure 12.2,Protein degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.2-scaled.jpg,Figure 12.2: Modification of DNA and histones can alter DNA accessibility and therefore transcription.
Figure 12.3,Protein degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.3-scaled.jpg,Figure 12.3: Five common modes of alternative splicing.
Figure 12.4,Protein degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.4-scaled.jpg,Figure 12.4: Regulation of translational initiation.
Figure 12.5,Protein degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.5-scaled.jpg,Figure 12.5: RNA-Binding proteins can increase stability of the transcript.
Figure 12.7,Protein degradation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
Figure 12.8,The mitotic phase,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
Figure 12.8,Mitosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
Figure 12.9,DNA damage,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
Figure 12.7,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.7-scaled.jpg,Figure 12.7: Overview of the cell cycle.
Figure 12.8,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.8-scaled.jpg,Figure 12.8: Summary of the mitotic phase.
Figure 12.9,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.9-scaled.jpg,Figure 12.9: Summary of cell cycle checkpoints and the role of CDK inhibitors in halting cell cycle progress.
Figure 12.10,Meiosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
Figure 12.10,Meiotic pairing,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/12.10-scaled.jpg,Figure 12.10: Overview of meiosis.
Figure 11.2,Gene structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.2-1.png,Figure 11.2: Schematic view of a eukaryotic gene structure.
Figure 11.3,Initiation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.3-scaled.jpg,Figure 11.3: Transcription initiation.
Figure 11.4,mRNA,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.4-scaled.jpg,Figure 11.4: Overview of mRNA processing involving the removal of introns (splicing) and the addition of a 5’ cap and 3’ tail.
Figure 11.5,mRNA,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.5-scaled.jpg,Figure 11.5: Summary of mRNA splicing.
Figure 11.3,rRNA,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.3-scaled.jpg,Figure 11.3: Transcription initiation.
Figure 11.4,rRNA,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.4-scaled.jpg,Figure 11.4: Overview of mRNA processing involving the removal of introns (splicing) and the addition of a 5’ cap and 3’ tail.
Figure 11.5,rRNA,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.5-scaled.jpg,Figure 11.5: Summary of mRNA splicing.
Figure 11.1,rRNA,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.1-scaled.jpg,Figure 11.1: Colinearity of DNA and RNA.
Figure 11.2,rRNA,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.2-1.png,Figure 11.2: Schematic view of a eukaryotic gene structure.
Figure 11.8,Translational initiation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
Figure 11.8,Translation elongation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
Figure 11.6,Translational termination,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.6-scaled.jpg,"Figure 11.6: Genetic code; each codons is three nucleotides corresponding to a specific amino acid. The code is degenerate, meaning several codes are present for the same amino acid and the codes for similar amino acids are clustered."
Figure 11.7,Translational termination,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.7-scaled.jpg,"Figure 11.7: Summary of translational initiation. eIF4 recruits the small ribosomal subunit and other initiation factors to the mRNA. The charge Met-tRNA also binds the complex, and the large ribosomal subunit is recruited to the initiation complex. Once the large ribosomal subunit binds, the initiation factors can be released, and translation can proceed to elongation of the polypeptide chain."
Figure 11.8,Translational termination,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/11.8-scaled.jpg,Figure 11.8: Summary of translational elongation.
Figure 10.3,Nucleotides and basic DNA structure,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
Figure 10.4,DNA packaging and organization,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.4.png,Figure 10.4: Organizational structure of DNA illustrating condensation and supercoiling into chromosomes.
Figure 10.1,DNA packaging and organization,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.1-scaled.jpg,"Figure 10.1: Basic structure of nucleotides including the sugar (ribose or deoxyribose), base (pyrimidine or purine), and phosphate groups."
Figure 10.2,DNA packaging and organization,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.2-scaled.jpg,Figure 10.2: Structure of pyrimidine and purine bases.
Figure 10.3,DNA packaging and organization,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.3-scaled.jpg,Figure 10.3: General structure and hydrogen bonding pattern of DNA.
Figure 10.5,DNA packaging and organization,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
Figure 10.5,Mismatch repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
Figure 10.5,Nucleotide excision repair (NER),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
Figure 10.6,Base excision repair (BER),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
Figure 10.5,Double-stranded break repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.5-scaled.jpg,"Figure 10.5: Comparison on three types of repair: (A) proofreading, (B) mismatch, and (C) nucleotide excision repair."
Figure 10.6,Double-stranded break repair,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.6-scaled.jpg,Figure 10.6: Summary of base excision repair. This is a similar process to NER but requires a glycosylase.
Figure 10.8,Telomere replication,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
Figure 10.7,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.7-scaled.jpg,Figure 10.7: Summary of DNA replication.
Figure 10.8,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/10.8-scaled.jpg,Figure 10.8: Summary of telomerase activity to fill the overhang on the lagging strand.
Figure 9.2,Galactose metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.2-scaled.jpg,"Figure 9.2: Fructose metabolism and reaction by aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance, while deficiencies in frutokinase can result in essential fructosuria."
Figure 9.1,Deficiencies in galactose metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.1-scaled.jpg,Figure 9.1: Convergence of fructose and glucose metabolism.
Figure 9.2,Deficiencies in galactose metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.2-scaled.jpg,"Figure 9.2: Fructose metabolism and reaction by aldolase B. Deficiencies in aldolase B can result in hereditary fructose intolerance, while deficiencies in frutokinase can result in essential fructosuria."
Figure 9.3,Deficiencies in galactose metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.3-scaled.jpg,"Figure 9.3: Galactose metabolism; glucose 6-phosphate is converted to glucose 1-phosphate, which enters the pathway."
Figure 9.4,Deficiencies in galactose metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.4-scaled.jpg,Figure 9.4: Comparison of classical and nonclassical galatosemia.
Figure 9.5,Deficiencies in galactose metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
Figure 9.5,Consequences of ethanol metabolism in the liver,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
Figure 9.7,Excessive alcohol consumption,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.7-scaled.jpg,Figure 9.7: Clinical consequences of alcoholism.
Figure 9.5,P450,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.5-scaled.jpg,"Figure 9.5: Overview of ethanol metabolism. The pathway spans the cytosol and the mitochondria, and NADH is produced in both steps of the pathway."
Figure 9.6,P450,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.6-scaled.jpg,Figure 9.6: Overview of alcohol metabolism.
Figure 9.7,P450,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.7-scaled.jpg,Figure 9.7: Clinical consequences of alcoholism.
Figure 9.8,P450,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/9.8-scaled.jpg,Figure 9.8: Ethanol detoxification by MEOS.
Figure 8.1,Phenylalanine and tyrosine,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.1-scaled.jpg,Figure 8.1: Metabolism of phenylalanine requires BH4 and also produces tyrosine. Deficiencies in cofactor or phenylalanine hydroxylase can result in phenylketonuria.
Figure 8.2,Phenylalanine and tyrosine,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.2-scaled.jpg,"Figure 8.2: Tyrosine can be produced from phenylalanine metabolism and is required for the production of melanin and the catecholamines. Deficiencies can occur at several different locations in the pathway and result in albinism, alkaptonuria, or tyrosinemia."
Figure 8.3,Tryptophan,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.3-scaled.jpg,Figure 8.3: Metabolism of tryptophan to melatonin.
Figure 8.4,Glutamate,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.4-scaled.jpg,Figure 8.4: Glutamate metabolism as it interfaces with nitrogen transport and synthesis of GABA.
Figure 8.6,Methionine,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.6-scaled.jpg,Figure 8.6: Metabolism of methionine. Remethylation and transsulfuration of homocysteine are illustrated. Cofactor or enzymatic deficiencies can result in an elevation of homocysteine.
Figure 8.6,Transsulfuration pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.6-scaled.jpg,Figure 8.6: Metabolism of methionine. Remethylation and transsulfuration of homocysteine are illustrated. Cofactor or enzymatic deficiencies can result in an elevation of homocysteine.
Figure 8.1,Consequences of elevated homocysteine,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.1-scaled.jpg,Figure 8.1: Metabolism of phenylalanine requires BH4 and also produces tyrosine. Deficiencies in cofactor or phenylalanine hydroxylase can result in phenylketonuria.
Figure 8.2,Consequences of elevated homocysteine,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.2-scaled.jpg,"Figure 8.2: Tyrosine can be produced from phenylalanine metabolism and is required for the production of melanin and the catecholamines. Deficiencies can occur at several different locations in the pathway and result in albinism, alkaptonuria, or tyrosinemia."
Figure 8.3,Consequences of elevated homocysteine,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.3-scaled.jpg,Figure 8.3: Metabolism of tryptophan to melatonin.
Figure 8.4,Consequences of elevated homocysteine,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.4-scaled.jpg,Figure 8.4: Glutamate metabolism as it interfaces with nitrogen transport and synthesis of GABA.
Figure 8.5,Consequences of elevated homocysteine,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.5-scaled.jpg,Figure 8.5: Metabolism of branched-chain amino acids. Deficiencies in branched-chain keto acid dehydrogenase (BCKAD) can result in the presentation of maple syrup urine disease.
Figure 8.6,Consequences of elevated homocysteine,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/8.6-scaled.jpg,Figure 8.6: Metabolism of methionine. Remethylation and transsulfuration of homocysteine are illustrated. Cofactor or enzymatic deficiencies can result in an elevation of homocysteine.
Figure 7.1,Oxidative and nonoxidative functions,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.1-scaled.jpg,Figure 7.1: Overview of the pentose phosphate pathway and its interface with glycolysis.
Figure 7.2,Regulation of the pentose phosphate pathway,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.2-scaled.jpg,Figure 7.2: Pentose phosphate pathway and its connection to glycolysis and glutathione synthesis.
Figure 7.3,Requirement of the pentose phosphate pathway in RBCs,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
Figure 7.3,RBCs,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
Figure 7.2,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.2-scaled.jpg,Figure 7.2: Pentose phosphate pathway and its connection to glycolysis and glutathione synthesis.
Figure 7.1,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.1-scaled.jpg,Figure 7.1: Overview of the pentose phosphate pathway and its interface with glycolysis.
Figure 7.3,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.3-scaled.jpg,Figure 7.3: NADPH in the red blood cell as a means of reducing glutathione.
Figure 7.4,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.4-scaled.jpg,Figure 7.4: Basic structure of nucleotides.
Figure 7.5,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.5-scaled.jpg,Figure 7.5: Overview of purine and pyrimidine bases.
Figure 7.6,Generation of 5-phosphoribosyl-1-phosphate (PRPP),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.6-scaled.jpg,Figure 7.6: Synthesis of PRPP and regulation of PRPP synthetase.
Figure 7.7,Synthesis of purines,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.7-1-scaled.jpg,Figure 7.7: Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway.
Figure 7.9,Degradation of purines,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.9-scaled.jpg,Figure 7.9: Breakdown of nucleotides.
Figure 7.10,Degradation of purines,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
Figure 7.10,Salvage of purines,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
Figure 7.12,Synthesis of pyrimidines,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.12-scaled.jpg,Figure 7.12: Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway.
Figure 7.13,Synthesis of pyrimidines,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
Figure 7.13,Clinical importance of folate cycle inhibitors and synthesis of dTMP,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.13-scaled.jpg,Figure 7.13: Interaction of thymidylate synthesis with the folate cycle. SHMT: serine hydroxymethyltransferase; DHFR: dihydrofolate reductase.
Figure 7.5,Clinical importance of folate cycle inhibitors and synthesis of dTMP,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.5-scaled.jpg,Figure 7.5: Overview of purine and pyrimidine bases.
Figure 7.6,Clinical importance of folate cycle inhibitors and synthesis of dTMP,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.6-scaled.jpg,Figure 7.6: Synthesis of PRPP and regulation of PRPP synthetase.
Figure 7.7,Clinical importance of folate cycle inhibitors and synthesis of dTMP,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.7-1-scaled.jpg,Figure 7.7: Overview of purine synthesis. The reaction catalyzed by GPAT is the regulatory enzyme of the pathway.
Figure 7.8,Clinical importance of folate cycle inhibitors and synthesis of dTMP,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.8-662x1024.jpg,Figure 7.8: Purine synthesis and regulation of glutamine: phosphoribosylpyrophosphate amidotransferase.
Figure 7.9,Clinical importance of folate cycle inhibitors and synthesis of dTMP,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.9-scaled.jpg,Figure 7.9: Breakdown of nucleotides.
Figure 7.10,Clinical importance of folate cycle inhibitors and synthesis of dTMP,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.10-scaled.jpg,Figure 7.10: Nucleotide base salvage. Reaction catalyzed by HGPRT is clinically relevant as deficiencies can cause accumulation of uric acid.
Figure 7.11,Clinical importance of folate cycle inhibitors and synthesis of dTMP,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.11-1024x799.jpg,Figure 7.11: Nucleotide specific pathways for base salvage.
Figure 7.12,Clinical importance of folate cycle inhibitors and synthesis of dTMP,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.12-scaled.jpg,Figure 7.12: Overview of pyrimidine synthesis. The reaction catalyzed by carbamoyl phosphate synthetase I is the regulatory enzyme of the pathway.
Figure 7.4,Clinical importance of folate cycle inhibitors and synthesis of dTMP,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/7.4-scaled.jpg,Figure 7.4: Basic structure of nucleotides.
Figure 6.2,Clinical importance of folate cycle inhibitors and synthesis of dTMP,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.2-scaled.jpg,Figure 6.2: Cholesterol synthetic pathway.
Figure 6.3,Synthesis of mevalonate from acetyl-CoA,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.3-1-scaled.jpg,Figure 6.3: Regulatory step catalyzed by HMG-CoA reductase.
Figure 6.4,Regulation of cholesterol synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
Figure 6.4,Transcriptional control,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
Figure 6.5,Cholesterol esterification and transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.5-1.png,Figure 6.5: Esterification of cholesterol by LCAT.
Figure 6.1,Synthesis of specialized products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.1-scaled.jpg,Figure 6.1: Structure of cholesterol.
Figure 6.2,Synthesis of specialized products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.2-scaled.jpg,Figure 6.2: Cholesterol synthetic pathway.
Figure 6.3,Synthesis of specialized products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.3-1-scaled.jpg,Figure 6.3: Regulatory step catalyzed by HMG-CoA reductase.
Figure 6.5,Synthesis of specialized products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.5-1.png,Figure 6.5: Esterification of cholesterol by LCAT.
Figure 6.4,Synthesis of specialized products,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.4-scaled.jpg,Figure 6.4: Regulation of cholesterol synthesis.
Figure 6.6,TAGs,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.6-e1635884201180.png,Figure 6.6: Overview of lipoprotein size and structure.
Figure 6.7,Chylomicrons: Transport of dietary lipids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.7-scaled.jpg,Figure 6.7: Transport of dietary lipids via chylomicrons.
Figure 6.8,VLDL: Transport of TAGs and cholesterol synthesized in the liver,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.8-scaled.jpg,Figure 6.8: Transport of TAGs from de novo synthesis using VLDL.
Figure 6.9,VLDL: Transport of TAGs and cholesterol synthesized in the liver,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.9-scaled.jpg,Figure 6.9: Comparison of the role of chylomicrons and VLDLs in lipid transport.
Figure 6.11,Fate of VLDL,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
Figure 6.10,HDL: Reverse cholesterol transport,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
Figure 6.10,Fate of HDL,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
Figure 6.10,HDL interactions with other particles,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
Figure 6.11,Lipoprotein receptor-mediated endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.11-scaled.jpg,Figure 6.11: Uptake of LDL and regulation of cholesterol synthesis.
Figure 6.6,Lipoprotein receptor-mediated endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.6-e1635884201180.png,Figure 6.6: Overview of lipoprotein size and structure.
Figure 6.7,Lipoprotein receptor-mediated endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.7-scaled.jpg,Figure 6.7: Transport of dietary lipids via chylomicrons.
Figure 6.8,Lipoprotein receptor-mediated endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.8-scaled.jpg,Figure 6.8: Transport of TAGs from de novo synthesis using VLDL.
Figure 6.10,Lipoprotein receptor-mediated endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.10-scaled.jpg,Figure 6.10: Interaction of chylomicrons and VLDL with HDL in circulation.
Figure 6.9,Lipoprotein receptor-mediated endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.9-scaled.jpg,Figure 6.9: Comparison of the role of chylomicrons and VLDLs in lipid transport.
Figure 6.2,Lipoprotein receptor-mediated endocytosis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/6.2-scaled.jpg,Figure 6.2: Cholesterol synthetic pathway.
Figure 5.1,Urea cycle and nitrogen metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
Figure 5.2,Urea cycle and nitrogen metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
Figure 5.11,Amino acids,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
Figure 5.3,Lactate,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
Figure 5.4,Glycerol,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
Figure 5.2,Pyruvate carboxylase and phosphoenol carboxykinase (PEPCK),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
Figure 5.2,"Fructose 1,6-bisphosphatase (FBP1)",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
Figure 4.1,"Fructose 1,6-bisphosphatase (FBP1)",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
Figure 5.6,Hepatic glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
Figure 5.7,Skeletal muscle glycogenolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
Figure 5.1,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.1-scaled.jpg,Figure 5.1: Glucose production by glycogenolysis and gluconeogenesis.
Figure 5.2,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.2-scaled.jpg,Figure 5.2: Comparison of glycolysis and gluconeogenesis.
Figure 5.3,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
Figure 5.4,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.4-scaled.jpg,"Figure 5.4: Glycerol as a substrate for gluconeogenesis; after phosphorylation to glycerol 3-phosphate it can be converted to DHAP, which can enter directly into glycolysis."
Figure 5.5,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.5-scaled.jpg,Figure 5.5: Reaction catalyzed by pyruvate carboxylase; this allows the bypass of the irreversible step catalyzed by pyruvate kinase.
Figure 5.7,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.7-scaled.jpg,Figure 5.7: Skeletal muscle glycogenolysis.
Figure 5.6,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
Figure 5.6,Lipolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.6-scaled.jpg,Figure 5.6: Hepatic glycogenolysis by epinephrine.
Figure 5.9,β-oxidation (oxidation of free fatty acids),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
Figure 5.10,Regulation of β-oxidation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
Figure 5.11,Ketogenesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
Figure 5.8,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.8-scaled.jpg,Figure 5.8: Process of lipolysis.
Figure 5.9,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.9-scaled.jpg,Figure 5.9: Overview of LCFA transport into the mitochondria and β-oxidation.
Figure 5.10,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.10-scaled.jpg,Figure 5.10: Regulation of β-oxidation.
Figure 5.11,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.11-scaled.jpg,Figure 5.11: Overview of ketone body formation.
Figure 5.14,"Glutamate dehydrogenase, glutamine synthetase, and glutaminase",https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
Figure 5.14,GDH,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
Figure 5.16,Regulation of the urea cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.16-scaled.jpg,Figure 5.16: Key regulatory step in the urea cycle. CPS1 is activated by N-acetylglutamate.
Figure 5.3,Regulation of the urea cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.3-scaled.jpg,Figure 5.3: Locations of amino acid and lactate entering gluconeogenesis as substrates for the pathway.
Figure 5.12,Regulation of the urea cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.12-scaled.jpg,Figure 5.12: Transamination reaction.
Figure 5.13,Regulation of the urea cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.13-scaled.jpg,"Figure 5.13: Reactions catalyzed by glutamate dehydrogenase, glutaminase, and glutamine synthetase."
Figure 5.14,Regulation of the urea cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.14-scaled.jpg,Figure 5.14: Movement of ammonia from peripheral tissues to the liver.
Figure 5.15,Regulation of the urea cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.15-scaled.jpg,Figure 5.15: Overview of the urea cycle; the pathway spans both the mitochondria and cytosol.
Figure 5.17,Regulation of the urea cycle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/5.17-scaled.jpg,Figure 5.17: Entry of the second nitrogen into the urea cycle; aspartate donates the second nitrogen for the synthesis of urea.
Figure 4.1,Regulation of glycolysis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
Figure 4.2,Glucokinase: Glucose to glucose 6-phosphate,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
Figure 4.3,GLUT2,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
Figure 4.4,Regulation of glucokinase and hexokinase,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
Figure 4.5,Regulation of phosphofructokinase 1 (PFK1),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
Figure 4.6,Regulation of pyruvate kinase (PK),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
Figure 4.7,Glycerol 3-phosphate shuttle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
Figure 4.8,Malate-aspartate shuttle,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
Figure 4.9,Regulation of the pyruvate dehydrogenase complex (PDC),https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
Figure 4.1,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.1-1-598x1024.png,"Figure 4.1: Summary of glycolysis. The three regulated steps of the process will be the focus, and those are catalyzed by the enzymes glucokinase/hexokinase, phosphofructokinase 1 (PFK1), and pyruvate kinase. All other steps in glycolysis are reversible (as indicated by the arrows) and are also used in gluconeogenesis."
Figure 4.2,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.2-scaled.jpg,"Figure 4.2: Regulatory step committed by hexo or glucokinase. The first regulatory step in glycolysis is the phosphorylation of glucose by hexo or glucokinase. The reverse reaction, which is part of gluconeogensis, is catalyzed by glucose 6-phosphatase."
Figure 4.3,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.3.png,Figure 4.3: Comparison of glucokinase and hexokinase kinetics.
Figure 4.4,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.4-e1635872274208.png,Figure 4.4: Regulation of glucokinase by glucokinase regulatory protein.
Figure 4.5,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.5-scaled.jpg,"Figure 4.5: Regulation of PFK1 by fructose 2,6-bisphosphate generated by PFK2."
Figure 4.6,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.6-scaled.jpg,"Figure 4.6: Regulation of pyruvate kinase phosphorylation and fructose 1,6-bisphosphate."
Figure 4.7,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.7-scaled.jpg,Figure 4.7: Glycerol 3-phosphate shuttle.
Figure 4.8,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.8.png,Figure 4.8: Malate-aspartate shuttle.
Figure 4.9,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.9-scaled.jpg,Figure 4.9: Regulation of the pyruvate dehydrogenase complex (PDC).
Figure 4.10,Summary of pathway regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
Figure 4.11,FADH2,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
Figure 4.12,FADH2,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
Figure 4.13,Ca2,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.13-scaled.jpg,Figure 4.13: Regulation of the TCA cycle.
Figure 4.10,Ca2,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.10-scaled.jpg,Figure 4.10: Overview of the TCA cycle.
Figure 4.11,Ca2,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.11-scaled.jpg,Figure 4.11: Substrates produced by the TCA cycle.
Figure 4.12,Ca2,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.12-scaled.jpg,Figure 4.12: Anaplerotic reactions of the TCA cycle.
Figure 4.14,Ca2,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
Figure 4.14,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.14.png,Figure 4.14: Overview of the electron transport chain (ETC).
Figure 4.15,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
Figure 4.16,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
Figure 4.17,Regulation of fatty acid synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.17-scaled.jpg,Figure 4.17: Regulatory reaction of fatty acid synthesis. The synthesis of malonyl-CoA by acetyl-CoA carboxylase is highly regulated within the cytosol.
Figure 4.15,Regulation of fatty acid synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.15-scaled.jpg,Figure 4.15: Citrate shuttle reaction moves citrate from the mitochondria to the cytosol for fatty acid synthesis.
Figure 4.16,Regulation of fatty acid synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.16-scaled.jpg,"Figure 4.16: Fatty acid synthesis is an iterative process that begins with the transfer of an acetyl moiety from acetyl-CoA to fatty acid synthase; following this activation, carbons are added to the growing chain in the form of malonyl-CoA."
Figure 4.18,Regulation of fatty acid synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
Figure 4.18,Regulation of glycogen synthesis,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/4.18-scaled.jpg,Figure 4.18: Glycogen synthesis.
Figure 3.1,Fed state metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.1-scaled.jpg,Figure 3.1: Overview of the fed state.
Figure 3.1,Liver metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.1-scaled.jpg,Figure 3.1: Overview of the fed state.
Figure 3.2,Fasted state metabolism,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.2-scaled.jpg,Figure 3.2: Overview of fasted state metabolism.
Figure 3.1,.,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.1-scaled.jpg,Figure 3.1: Overview of the fed state.
Figure 3.2,.,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/3.2-scaled.jpg,Figure 3.2: Overview of fasted state metabolism.
Figure 2.1,Liver tests,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
Figure 2.2,Lactate,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.2-1024x294.jpg,Figure 2.2: Reaction catalyzed by lactate dehydrogenase.
Figure 2.1,Chemical exam,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.1--1024x145.jpg,Figure 2.1: Heme degradation.
Figure 2.2,Chemical exam,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.2-1024x294.jpg,Figure 2.2: Reaction catalyzed by lactate dehydrogenase.
Figure 2.3,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.3-869x1024.jpg,Figure 2.3: Mechanism of action of vitamin A.
Figure 2.4,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/11/2.4-scaled.jpg,Figure 2.4: Vitamin K stimulates the maturation of clotting factors.
Figure 1.2,Tables,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.2-744x1024.jpg,Figure 1.2: Chart of amino acids.
Figure 1.1,Polar residues,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.1-scaled.jpg,Figure 1.1: Basic structure of amino acids and ionization.
Figure 1.2,Polar residues,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.2-744x1024.jpg,Figure 1.2: Chart of amino acids.
Figure 1.3,Polar residues,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.3-1024x178.jpg,Figure 1.3: Basics of enzyme kinetics.
Figure 1.4,Polar residues,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
Figure 1.6,Competitive and noncompetitive inhibition,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
Figure 1.7,Allosteric regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7a-1024x454.jpg,Figure 1.7(a): Allosteric enzyme regulation.
Figure 1.7,Allosteric regulation,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7b-1024x617.jpg,Figure 1.7(b): Allosteric enzyme regulation.
Figure 1.3,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.3-1024x178.jpg,Figure 1.3: Basics of enzyme kinetics.
Figure 1.4,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.4-928x1024.jpg,Figure 1.4: Graphical representation of the Michaelis–Menten equation.
Figure 1.5,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.5-1024x918.jpg,Figure 1.5: Lineweaver–Burk plot to illustrate Km and Vmax.
Figure 1.6,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.6-1024x829.jpg,Figure 1.6: Competitive vs. noncompetitive inhibition.
Figure 1.7,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7a-1024x454.jpg,Figure 1.7(a): Allosteric enzyme regulation.
Figure 1.7,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.7b-1024x617.jpg,Figure 1.7(b): Allosteric enzyme regulation.
Figure 1.2,Text,https://pressbooks.lib.vt.edu/app/uploads/sites/66/2021/10/1.2-744x1024.jpg,Figure 1.2: Chart of amino acids.