about
Nucleophilic activation by positioning in phosphoryl transfer catalyzed by nucleoside diphosphate kinaseThe Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)NADH oxidase activity of Bacillus subtilis nitroreductase NfrA1: insight into its biological roleStructure/Function Analysis of Protein-Protein Interactions Developed by the Yeast Pih1 Platform Protein and Its Partners in Box C/D snoRNP AssemblyCrystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complexRegulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.Drosophila Spag is the homolog of RNA polymerase II-associated protein 3 (RPAP3) and recruits the heat shock proteins 70 and 90 (Hsp70 and Hsp90) during the assembly of cellular machineriesHuman and viral nucleoside/nucleotide kinases involved in antiviral drug activation: structural and catalytic properties.The Pih1-Tah1 cochaperone complex inhibits Hsp90 molecular chaperone ATPase activity.Molecular chaperone complexes with antagonizing activities regulate stability and activity of the tumor suppressor LKB1.Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery.Deep Structural Analysis of RPAP3 and PIH1D1, Two Components of the HSP90 Co-chaperone R2TP ComplexStructural analysis of B. subtilis CcpA effector binding siteRemodeling of the Binding Site of Nucleoside Diphosphate Kinase Revealed by X-ray Structure and H/D Exchange
P50
Q27617881-1894AB65-B700-4838-871C-1BF1C238C92CQ27642926-277F2097-0026-4974-A4B4-7EA5A99D4741Q27664111-46DB2DD4-ED34-4DCE-B5B3-885FF77A651AQ27701645-9BF80183-DFAF-426E-981E-A50406A19724Q29617515-789F1BE2-851E-41DF-B0A4-268C2EA0AA3EQ34120745-91EC920E-8AA4-4C4B-B648-D34537A36BBEQ37608575-0698F433-61C4-441A-825A-2BB1065EE370Q37736819-F0AB2256-31F3-4E89-9693-54C41D7750E6Q42005667-3E581CC1-2F46-494C-B795-E11E1A28A1F8Q51546346-202848F8-D2E8-4B61-81AA-3CE14CC31762Q55220174-5E379F6A-33C7-4B54-82E3-F7553669EE81Q58216548-CE958333-65E9-40E5-8E0E-995DBCB9A8FFQ83932046-5C136D6F-6200-4C05-A916-D526BDF326F6Q91746741-C0C8649A-5FD1-4DCF-9D13-C0C8E4E239E9
P50
description
researcher
@en
wetenschapper
@nl
name
Philippe Meyer
@en
Philippe Meyer
@nl
type
label
Philippe Meyer
@en
Philippe Meyer
@nl
prefLabel
Philippe Meyer
@en
Philippe Meyer
@nl
P106
P31
P496
0000-0002-6220-0679