83-kilodalton heat shock proteins of trypanosomes are potent peptide-stimulated ATPases.
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Review: The HSP90 molecular chaperone-an enigmatic ATPaseATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo.Trypanosomatid protein phosphatasesMolecular cloning and characterization of the 78-kilodalton glucose-regulated protein of Trypanosoma cruzi.Stability of the Hsp90 inhibitor 17AAG hydroquinone and prevention of metal-catalyzed oxidation.Potent antitrypanosomal activities of heat shock protein 90 inhibitors in vitro and in vivo.The chaperone toolbox at the single-molecule level: From clamping to confining.S100A6 mediates nuclear translocation of Sgt1: a heat shock-regulated protein.ATP-binding properties of human Hsp90.Tumour rejection antigens of the hsp90 family (gp96) closely resemble tumour-associated heparanase enzymes.Assessment of the ATP binding properties of Hsp90.
P2860
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P2860
83-kilodalton heat shock proteins of trypanosomes are potent peptide-stimulated ATPases.
description
1992 nî lūn-bûn
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1992年の論文
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1992年学术文章
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1992年学术文章
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1992年学术文章
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1992年学术文章
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1992年學術文章
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name
83-kilodalton heat shock proteins of trypanosomes are potent peptide-stimulated ATPases.
@ast
83-kilodalton heat shock proteins of trypanosomes are potent peptide-stimulated ATPases.
@en
type
label
83-kilodalton heat shock proteins of trypanosomes are potent peptide-stimulated ATPases.
@ast
83-kilodalton heat shock proteins of trypanosomes are potent peptide-stimulated ATPases.
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prefLabel
83-kilodalton heat shock proteins of trypanosomes are potent peptide-stimulated ATPases.
@ast
83-kilodalton heat shock proteins of trypanosomes are potent peptide-stimulated ATPases.
@en
P2093
P2860
P356
P1433
P1476
83-kilodalton heat shock proteins of trypanosomes are potent peptide-stimulated ATPases.
@en
P2093
P2860
P304
P356
10.1002/PRO.5560010802
P577
1992-08-01T00:00:00Z