(Q28204780)

2

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G Leone

3

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M C Coffey

4

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B Weber

5

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P W Lee

Journal of Biological Chemistry

6

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language of work or name

English

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publication date

31 August 2001

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published in

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volume

276

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issue

35

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page(s)

32822-7

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cites work

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Getting newly synthesized proteins into shape.

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Protein folding in vivo: the importance of molecular chaperones

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Hsp90 & Co. - a holding for folding

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Hsp90's secrets unfold: new insights from structural and functional studies

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Molecular chaperones: the busy life of Hsp90.

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Structure and in vivo function of Hsp90.

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Chaperones in progesterone receptor complexes

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Hsp90 as a capacitor for morphological evolution

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Stepwise assembly of a glucocorticoid receptor.hsp90 heterocomplex resolves two sequential ATP-dependent events involving first hsp70 and then hsp90 in opening of the steroid binding pocket

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The phosphorylation state of the reticulocyte 90-kDa heat shock protein affects its ability to increase phosphorylation of peptide initiation factor 2 alpha subunit by the heme-sensitive kinase.

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Possible role for serine/threonine phosphorylation in the regulation of the heteroprotein complex between the hsp90 stress protein and the pp60v-src tyrosine kinase

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Hsp90 is obligatory for the heme-regulated eIF-2alpha kinase to acquire and maintain an activable conformation.

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The reovirus cell attachment protein possesses two independently active trimerization domains: basis of dominant negative effects

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Active participation of Hsp90 in the biogenesis of the trimeric reovirus cell attachment protein sigma1.

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The cell attachment proteins of type 1 and type 3 reovirus are differentially susceptible to trypsin and chymotrypsin

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The N-terminal quarter of reovirus cell attachment protein sigma 1 possesses intrinsic virion-anchoring function

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Conformational and functional analysis of the C-terminal globular head of the reovirus cell attachment protein

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Characterization of purified avian 90,000-Da heat shock protein

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Identifiers

DOI

10.1074/JBC.M105562200

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

11438552

1 reference

Consolidated OpenCitations Corpus – April 2017