![]() Small heat shock proteins (sHSPs)Īre low molar mass heat shock proteins that are involved in many functions. Refers to the binding of two or more proteins to form a multisubunit protein. Molecular chaperonesĪre proteins that act as agents that guide the folding of other proteins. Chaperones in addition to folding of proteins are involved in proteolysis. Chaperonins is a special category of chaperones that primarily help in the folding of proteins. HSPs are characterized under the heading of molecular chaperones. Refers to the “pulling” of HSPs to unfold a target protein Heat shock proteins (HSPs)Īre proteins that are expressed in cells when the cell is distressed by temperature, ultraviolet light, toxic metals, and wound healing. Client proteins are also called target, nascent, and substrate proteins. Is the protein that chaperones help fold. Aggregation is diminished by chaperones/chaperonins. Is a family of ATPases associated with a multitude of cellular activities. Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase. ClpB/Hsp100 proteins and heat stress tolerance in plants. The dynamic dimer structure of the chaperone Trigger Factor. Structural basis for protein antiaggregation activity of the Trigger Factor chaperone. (2010) Structure and function of the molecular chaperone Trigger Factor. (2002) Molecular chaperones in the cytosol: Science: 295:1852. (2014) Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumption. (2010) Gymnastics of molecular chaperones. ![]() A chaperone-assisted degradation pathway targets kinetochore proteins to ensure genome stability. Kriegenburg F, Jakopec V, Poulsen EG, et al. Hsp70 and Hsp90- a relay team for protein folding. (2017) Editorial: The HSP70 molecular chaperone machines. (2013) Structural and functional aspects of hetero-oligomers formed by the small heat shock proteins αB-crystallin and HSP27. Biochim Biophys Acta: 1854:291.Īquilina JA, Shrestha S, Morris AM, et. FEBS Letters:587: 1959.īakthisaran R, Tangirala R, Rao CM (2015) Small heat shock proteins: Role in cellular functions and pathology. Nature:341: 125.Īrrigo A-P (2013) Human small heat shock proteins: Protein interactomes of homo- and hetero-oligomeric complexes: an update. (1989) Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Ostermann J, Horwich AL, Neupert W, et al. Nature: 328:378.Įllis RJ (1996) Discovery of molecular chaperones. Science: 353:6294.Įllis RJ (1987) Proteins as molecular chaperones. In vivo aspects of protein folding and quality control. Science: 181:223.īalchin D, Hayer-Hartl M, Hartl FU. Anfinsen CB (2011) Principles that govern the folding of protein chains.
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