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Chaperone protein


In molecular biology, chaperones are proteins that assist the non-covalent folding disassembly of other macromolecular structures, but do not occur in these structures when the latter are performing their normal biological...
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Chaperone ( protein), a protein that assists the non-covalent folding/unfolding ... chaperone, a small molecule which stabilizes the correct folding of a protein ...
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Protein-folding Diseases and Chaperone Biology ... length of the polyglutamine expansion and the expression of chaperone proteins. ...
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... cell to survive such stress is the production of "molecular chaperone" proteins. ... amplify molecular chaperone proteins specifically in diseased ...
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Muscles Need Chaperone' Proteins, But More Not Always Better ... Dysregulation of this chaperone protein may underlie the type of wasting seen in ...
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Yeast chaperone protein and mad cow disease. Article highlights or off-site fulltexts 1, 2 ... Chaperone-supervised conversion of prion protein to its protease ...
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Chaperone Proteins, a Brief Overview. Manipulating HSP Levels—Chaperone Proteins as ... Chaperone proteins are most notable for the proteo- and cyotoprotective ...
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Interaction of intracellular β amyloid peptide with chaperone proteins ... Previous studies have suggested the involvement of chaperone proteins in AD pathology. ...
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... chaperone actually covers up these hydrophobic residues, preventing protein aggregation. Then, when the chaperone moves off, the protein has a chance to fold ...
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The European Bioinformatics Institute ... IPR001623 Heat shock protein DnaJ, N-terminal. IPR002939 Chaperone DnaJ, C-terminal ...
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The European ... Proteins are produced in the cytoplasm as precursors, and ... of the bacterial protein export chaperone secB. Nat. Struct. Biol. ...
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Proper formation of the proteins that power heart and skeletal muscle seems to rely on a precise concentration of a "chaperone" protein known as UNC-45, according to ...
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Copper chaperone proteins have consequently evolved as part of a complex network ... ATPase to have the same CXXC Cu-binding motif as the chaperone protein (Figure 2) ...
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"Pilus biogenesis via the chaperone/usher pathway: an integration of structure ... "Crystal structure of chaperone protein PapD reveals an immunoglobulin fold. ...
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... Feb. 1, 2008) This months issue of ... methods to understand developmental processes in plants and flies. ... on the Web site for Cold Spring Harbor Protocols ... use of RNAi to investigate gene function in fruit flies. ...
... the role of a gene important to the embryonic ... coordination of differentiation of immature neural cells with the ... now, the mechanisms regulating these distinct cellular activities have ... published in the Feb. 15 issue of Development. ...
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Cached Biology News:RNA-based methods for developmental studies are featured in Cold Spring Harbor Protocols 2Trainor Lab characterizes gene essential for prenatal development of nervous system 2Poxvirus potency uncovered in new atomic map 2
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