"Protein Structure, Quaternary" - Books

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Select item 14152801.

Madame Curie Bioscience Database [Internet].

Austin (TX): Landes Bioscience; 2000-2013.

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Select item 44036682.

StatPearls [Internet].

Treasure Island (FL): StatPearls Publishing; 2026 Jan-.

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Select item 23580523.

Probe Reports from the NIH Molecular Libraries Program [Internet].

Bethesda (MD): National Center for Biotechnology Information (US); 2010-.

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Select item 53216724.

Essentials of Glycobiology [Internet]. 4th edition.

Varki A, Cummings RD, Esko JD, et al., editors.

Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2022.

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Select item 14109445.

TRP Ion Channel Function in Sensory Transduction and Cellular Signaling Cascades.

Liedtke WB, Heller S, editors.

Boca Raton (FL): CRC Press/Taylor & Francis; 2007.

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Select item 23639746.

Human Herpesviruses: Biology, Therapy, and Immunoprophylaxis.

Arvin A, Campadelli-Fiume G, Mocarski E, et al., editors.

Cambridge: Cambridge University Press; 2007.

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Select item 19111647.

Genomes. 2nd edition.

Brown TA.

Oxford: Wiley-Liss; 2002.

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Select item 13969108.

Biology of the NMDA Receptor.

Van Dongen AM, editor.

Boca Raton (FL): CRC Press/Taylor & Francis; 2009.

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Select item 15995249.

The Cell: A Molecular Approach. 2nd edition.

Cooper GM.

Sunderland (MA): Sinauer Associates; 2000.

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Select item 555888410.

Systems Biology: Functional Strategies of Living Organisms [Internet]. 2nd edition.

Konieczny L, Roterman-Konieczna I, Spólnik P.

Cham (CH): Springer; 2023.

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Select item 188138211.

Basic Neurochemistry: Molecular, Cellular and Medical Aspects. 6th edition.

Siegel GJ, Agranoff BW, Albers RW, et al., editors.

Philadelphia: Lippincott-Raven; 1999.

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Select item 144161812.

Helicobacter pylori: Physiology and Genetics.

Mobley HLT, Mendz GL, Hazell SL, editors.

Washington (DC): ASM Press; 2001.

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Select item 318983413.

Self-Perpetuating Structural States in Biology, Disease, and Genetics.

National Academy of Sciences (US); Lindquist S, Henikoff S, editors.

Washington (DC): National Academies Press (US); 2002.

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Select item 540176814.

Streptococcus pyogenes: Basic Biology to Clinical Manifestations [Internet]. 2nd edition.

Ferretti JJ, Stevens DL, Fischetti VA, editors.

Oklahoma City (OK): University of Oklahoma Health Sciences Center; 2022 Oct 8.

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Select item 189578815.

Molecular Biology of the Cell. 4th edition.

Alberts B, Johnson A, Lewis J, et al.

New York: Garland Science; 2002.

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Select item 557352416.

Toxicological Profile for Ethylbenzene.

Atlanta (GA): Agency for Toxic Substances and Disease Registry (US); 2010 Nov.

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Select item 327826817.

Frontiers in the Nutrition Sciences: Proceedings of a Symposium.

Institute of Medicine (US) Food and Nutrition Board.

Washington (DC): National Academies Press (US); 1989.

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Select item 420372018.

Streptococcus pyogenes : Basic Biology to Clinical Manifestations [Internet].

Ferretti JJ, Stevens DL, Fischetti VA, editors.

Oklahoma City (OK): University of Oklahoma Health Sciences Center; 2016-.

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Select item 333880019.

A systematic review of the clinical effectiveness and cost-effectiveness of sensory, psychological and behavioural interventions for managing agitation in older adults with dementia.

Livingston G, Kelly L, Lewis-Holmes E, et al.

Southampton (UK): NIHR Journals Library; 2014 Jun. (Health Technology Assessment, No. 18.39.)

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Select item 145898420.

GeneReviews® [Internet].

Adam MP, Bick S, Mirzaa GM, et al., editors.

Seattle (WA): University of Washington, Seattle; 1993-2026.

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Fig. 3.28

Self-organization example: (a) polypeptide chain folding, (b) formation of quaternary protein structure, and (c) integration of proteins in the cellular membrane

Information: Its Role and Meaning in Organisms.

Konieczny L, Roterman-Konieczna I, Spólnik P. Systems Biology: Functional Strategies of Living Organisms [Internet]. 2nd edition. Cham (CH): Springer; 2023.
Figure 3-35Three levels of organization of a protein

The three-dimensional structure of a protein can be described in terms of different levels of folding, each of which is constructed from the preceding one in hierarchical fashion. These levels are illustrated here using the catabolite activator protein (CAP), a bacterial gene regulatory protein with two domains. When the large domain binds cyclic AMP, it causes a conformational change in the protein that enables the small domain to bind to a specific DNA sequence. The amino acid sequence is termed the primary structure and the first folding level the secondary structure. As indicated under the brackets at the bottom of this figure, the combination of the second and third folding levels shown here is commonly termed the tertiary structure, and the fourth level (the assembly of subunits) the quaternary structure of a protein. (Modified from a drawing by Jane Richardson.)

Protein Structure .

Alberts B, Bray D, Lewis J, et al. Molecular Biology of the Cell. 3rd edition. New York: Garland Science; 1994.
Figure 5.

Model for differential ingestion of S. pyogenes mediated by Sfb1 and M1 proteins. Interactions of fibronectin bound to Sfb1 and M1 protein with epithelial cells lead to different ingestion pathways. Sfb1-Fn complexes promote uptake of streptococci via caveolae, while M1-Fn complexes foster receptor-mediated endocytosis. The model proposes that these two different streptococcal fibronectin binding proteins direct distinct changes in the quaternary structure of fibronectin, which in turn generate divergent signals when fibronectin engages α5β1 receptors at the surface of epithelial cells. In the end, streptococci are either deposited into relatively safe caveosomes or into bactericidal phagolysosomes. Common components of the signal cascade include PI3K, ILK, and Paxillin; however, data suggest that the signals diverge at the point of Paxillin phosphorylation.

Adhesion and invasion of Streptococcus pyogenes into host cells and clinical relevance of intracellular streptococci.

Ferretti JJ, Stevens DL, Fischetti VA, editors. Streptococcus pyogenes: Basic Biology to Clinical Manifestations [Internet]. 2nd edition. Oklahoma City (OK): University of Oklahoma Health Sciences Center; 2022 Oct 8.
Figure 5.

Model for differential ingestion of S. pyogenes mediated by Sfb1 and M1 proteins. Interactions of fibronectin bound to Sfb1 and M1 protein with epithelial cells lead to different ingestion pathways. Sfb1-Fn complexes promote uptake of streptococci via caveolae, while M1-Fn complexes foster receptor-mediated endocytosis. The model proposes that these two different streptococcal fibronectin binding proteins direct distinct changes in the quaternary structure of fibronectin, which in turn generate divergent signals when fibronectin engages α5β1 receptors at the surface of epithelial cells. In the end, streptococci are either deposited into relatively safe caveosomes or into bactericidal phagolysosomes. Common components of the signal cascade include PI3K, ILK, and Paxillin; however, data suggest that the signals diverge at the point of Paxillin phosphorylation.

Adhesion and invasion of Streptococcus pyogenes into host cells and clinical relevance of intracellular streptococci.

Ferretti JJ, Stevens DL, Fischetti VA, editors. Streptococcus pyogenes : Basic Biology to Clinical Manifestations [Internet]. Oklahoma City (OK): University of Oklahoma Health Sciences Center; 2016-.