about
Near-atomic resolution analysis of BipD, a component of the type III secretion system ofBurkholderia pseudomalleiStructural Basis for Phosphorylation-Dependent Recruitment of Tel2 to Hsp90 by Pih1The Structure of the R2TP Complex Defines a Platform for Recruiting Diverse Client Proteins to the HSP90 Molecular Chaperone System.The structure of FKBP38 in complex with the MEEVD tetratricopeptide binding-motif of Hsp90Tah1 helix-swap dimerization prevents mixed Hsp90 co-chaperone complexes.RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex.Structural mechanism for regulation of the AAA-ATPases RUVBL1-RUVBL2 in the R2TP co-chaperone revealed by cryo-EM
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Q27664318-290262E4-391F-4C97-8DC7-42DC88F8BDBAQ27683635-28B9B95F-3A14-4EA3-B1EA-42FAA7D3EF43Q33884673-5CD28844-A101-4633-90B4-F0A09F48357BQ36302519-156366BB-80D6-4F20-8C40-592A51E1AD18Q40530080-9BCA3174-1970-4C7C-8C0C-19C9A255D85CQ52319714-8D3ACE78-29B7-4234-B61B-2B9D1B57A180Q64076979-65C50C14-3735-4A69-B4EC-ABEADB4BE2F9
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description
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Mohinder Pal
@ast
Mohinder Pal
@en
Mohinder Pal
@es
Mohinder Pal
@nl
Mohinder Pal
@sl
type
label
Mohinder Pal
@ast
Mohinder Pal
@en
Mohinder Pal
@es
Mohinder Pal
@nl
Mohinder Pal
@sl
prefLabel
Mohinder Pal
@ast
Mohinder Pal
@en
Mohinder Pal
@es
Mohinder Pal
@nl
Mohinder Pal
@sl
P106
P31
P496
0000-0002-8025-0119