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Chaperone (protein)
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Proteins assisting in protein folding
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BiP and multiple DNAJ molecular chaperones in the endoplasmic reticulum are required for efficient simian virus 40 infection
scientific article
Pseudomonas syringae pv. tomato DC3000 HopPtoM (CEL ORF3) is important for lesion formation but not growth in tomato and is secreted and translocated by the Hrp type III secretion system in a chaperone-dependent manner
scientific article published in September 2003
Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.
scientific article
The heat shock response and chaperones/heat shock proteins in brain tumors: surface expression, release, and possible immune consequences.
scientific article
Kinetic analysis of the interaction of the copper chaperone Atox1 with the metal binding sites of the Menkes protein
scientific article (publication date: 6 June 2003)
Expression and crystallization of the yeast Hsp82 chaperone, and preliminary x‐ray diffraction studies of the amino‐terminal domain
scholarly article by Chrisostomos Prodromou published in August 1996
The pharmacological chaperone 1-deoxygalactonojirimycin reduces tissue globotriaosylceramide levels in a mouse model of Fabry disease
scientific article
Regulated degradation of Chk1 by chaperone-mediated autophagy in response to DNA damage
scientific article
Retrotranslocation of the chaperone calreticulin from the endoplasmic reticulum lumen to the cytosol
scientific article
The pharmacological chaperone isofagomine increases the activity of the Gaucher disease L444P mutant form of beta-glucosidase
scientific article
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In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial...

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