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Titlebook: Cell Stress Proteins; Stuart K. Calderwood Book 2007 Springer-Verlag New York 2007 Antigen.Cell Stress.Chaperone.Immunity.Nucleotide.Prote

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CaTiSiO5, CaSnSiO3 and related silicates,ck elements (abbreviated HSEs) (.; .). HSEs are arrays of three or more modules of the sequence element NGAAN (or AGAAN) or variations thereof (.; .). Heat shock factors (HSFs) are defined as proteins that are capable of specifically binding HSE sequences. The first attempts at identifying and/or pu
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M2SiO4 orthosilicates and related compounds,members between species (e.g., ,10 in mammals, ,20 in plants) (.; .). Their common feature is a central α-crystallin domain. The core structure of the α-crystallin domain, rather than its amino acid sequence, is conserved between species. This ,90 amino acid domain presents a well-preserved double β
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Humite and leucophoenicite groups,the expression of specific sets of protective proteins that have been commonly referred to for more than 30 years as heat shock proteins (hsps). Most, if not all, of these proteins are also expressed in the absence of stress. Many of these highly conserved proteins function as molecular chaperones t
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CaTiSiO5, CaSnSiO3 and related silicates, acid sequence (.). However, Afinsen’s experiments were performed in vitro with dilute solutions of a small globular protein (ribonuclease A), and these conditions are distinct from the highly crowded environment inside a cell where protein conformations vary and protein concentrations may be as hig
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Humite and leucophoenicite groups,sp70 actively unfolds proteins during translocation across membranes (.), whether it fragments aggregates or extracts polypeptides (.), and whether it acts a “holdase” or a “foldase” (.,.). These are related questions because they ask whether Hsp70 exerts a force on its clients during these processe
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List of symbols and abbreviations,f misfolded proteins, translocation of proteins into organelles, assembly of proteins, and their degradation (.; .; .; .). HSP70 chaperone proteins catalyze these biological processes with the aid of HSP40/DnaJ proteins and co-chaperones (Fig. 1A). HSP40/DnaJ proteins initially recognize substrate p
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