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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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