scholarly journals Human cyclophilin 40 unravels neurotoxic amyloids

PLoS Biology ◽  
2017 ◽  
Vol 15 (6) ◽  
pp. e2001336 ◽  
Author(s):  
Jeremy D. Baker ◽  
Lindsey B. Shelton ◽  
Dali Zheng ◽  
Filippo Favretto ◽  
Bryce A. Nordhues ◽  
...  
Keyword(s):  
2001 ◽  
Vol 6 (1) ◽  
pp. 59 ◽  
Author(s):  
Peter J. Mark ◽  
Bryan K. Ward ◽  
Premlata Kumar ◽  
Hooshang Lahooti ◽  
Rodney F. Minchin ◽  
...  

Genomics ◽  
1996 ◽  
Vol 35 (3) ◽  
pp. 448-455 ◽  
Author(s):  
Haruhiko Yokoi ◽  
Yukiko Shimizu ◽  
Hideharu Anazawa ◽  
Charles A. Lefebvre ◽  
Robert G. Korneluk ◽  
...  

2001 ◽  
Vol 284 (1) ◽  
pp. 219-225 ◽  
Author(s):  
Premlata Kumar ◽  
Peter J. Mark ◽  
Bryan K. Ward ◽  
Rodney F. Minchin ◽  
Thomas Ratajczak

2011 ◽  
Vol 31 (2) ◽  
pp. 267-278 ◽  
Author(s):  
Taichiro Iki ◽  
Manabu Yoshikawa ◽  
Tetsuo Meshi ◽  
Masayuki Ishikawa
Keyword(s):  

1998 ◽  
Vol 18 (12) ◽  
pp. 7353-7359 ◽  
Author(s):  
James A. Marsh ◽  
Helen M. Kalton ◽  
Richard F. Gaber

ABSTRACT Saccharomyces cerevisiae harbors two cyclophilin 40-type enzymes, Cpr6 and Cpr7, which are components of the Hsp90 molecular chaperone machinery. Cpr7 is required for normal growth and is required for maximal activity of heterologous Hsp90-dependent substrates, including glucocorticoid receptor (GR) and the oncogenic tyrosine kinase pp60v-src . In addition, it has recently been shown that Cpr7 plays a major role in negative regulation of the S. cerevisiae heat shock transcription factor (HSF). To better understand functions associated with Cpr7, a search was undertaken for multicopy suppressors of the cpr7Δ slow-growth phenotype. The screen identified a single gene, designatedCNS1 (for cyclophilin seven suppressor), capable of suppressing the cpr7Δ growth defect. Overexpression ofCNS1 in cpr7Δ cells also largely restored GR activity and negative regulation of HSF. In vitro protein retention experiments in which Hsp90 heterocomplexes were precipitated resulted in coprecipitation of Cns1. Interaction between Cns1 and the carboxy terminus of Hsp90 was also shown by two-hybrid analysis. The functional consequences of CNS1 overexpression and its physical association with the Hsp90 machinery indicate that Cns1 is a previously unidentified component of molecular chaperone complexes. Thus far, Cns1 is the only tetratricopeptide repeat-containing component of Hsp90 heterocomplexes found to be essential for cell viability under all conditions tested.


1995 ◽  
Vol 307 (1) ◽  
pp. 5-8 ◽  
Author(s):  
K Hoffmann ◽  
R E Handschumacher

The expression of human cyclophilin 40 (CyP-40) as a glutathione S-transferase fusion protein has provided a means to identify cellular components that are in association with this ubiquitous protein. When the fusion protein was coupled to a GSH affinity matrix, heat-shock protein 90 (hsp90) was found to be the predominant associated protein in all tissue extracts examined. The relatively high concentration of each of these proteins in various tissues indicates that the dimeric complex exists in concentrations that exceed those of the inactive steroid receptors of which each protein is a component. Association does not occur with heat-shock protein 70 and is not affected by cyclosporin A (CsA). Independent expression of two domains of CyP-40 permitted dissociation of N-terminal isomerase and CsA binding activity from the hsp90 binding site, which is located at the FKBP-59-like C-terminal region. The biological association of CyP-40 with hsp90 in many tissues may reflect a conjoint role in protein folding and trafficking.


1999 ◽  
Vol 55 (5) ◽  
pp. 1079-1082 ◽  
Author(s):  
Jacqueline Dornan ◽  
Paul Taylor ◽  
Amerigo Carrello ◽  
Rodney F. Minchin ◽  
Thomas Ratajczak ◽  
...  
Keyword(s):  

2001 ◽  
Vol 127 (2) ◽  
pp. 109-115 ◽  
Author(s):  
Bryan K. Ward ◽  
Premlata Kumar ◽  
Gavin R. Turbett ◽  
Joanne E. Edmondston ◽  
John M. Papadimitriou ◽  
...  

2009 ◽  
Vol 41 (8-9) ◽  
pp. 1652-1655 ◽  
Author(s):  
Thomas Ratajczak ◽  
Bryan K. Ward ◽  
Carmel Cluning ◽  
Rudi K. Allan

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