Hsp90 phosphorylation is linked to its chaperoning function. Assembly of the reovirus cell attachment protein (Q28204780)

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G Leone

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M C Coffey

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B Weber

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P W Lee

Journal of Biological Chemistry

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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

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page(s)

32822-7

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cites work

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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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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

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