Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties (Q27938998)

Peptidylprolyl isomerase CPR7 YJR032W

GOA release 2020-03-11

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GOA release 2020-03-11

author name string

C Mayr

1

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K Richter

2

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H Lilie

3

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J Buchner

Journal of Biological Chemistry

4

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language of work or name

English

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publication date

3 November 2000

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published in

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1 December 2016

275

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page(s)

34140-6

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issue

44

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cites work

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A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase

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A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin

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Steroid receptor interactions with heat shock protein and immunophilin chaperones

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Hsp90 & Co. - a holding for folding

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The ability of the immunophilin FKBP59-HBI to interact with the 90-kDa heat shock protein is encoded by its tetratricopeptide repeat domain

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Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay

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Kinetic analysis of the unfolding and refolding of ribonuclease T1 by a stopped-flow double-mixing technique

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SOPM: a self-optimized method for protein secondary structure prediction

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CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with Hsp90.

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An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function

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Different regions of the immunophilin FKBP52 determine its association with the glucocorticoid receptor, hsp90, and cytoplasmic dynein

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A Protease-Free Assay for Peptidyl Prolylcis/transIsomerases Using Standard Peptide Substrates

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