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An interaction network predicted from public data as a discovery tool: application to the Hsp90 molecular chaperone machineThe p23 molecular chaperone and GCN5 acetylase jointly modulate protein-DNA dynamics and open chromatin statusHSP90 controls SIR2 mediated gene silencingCombined protein- and nucleic acid-level effects of rs1143679 (R77H), a lupus-predisposing variant within ITGAMManagement of cytoskeleton architecture by molecular chaperones and immunophilins.Single-stranded DNA repeat synthesis by telomeraseA Chemical Biology Study of Human Pluripotent Stem Cells Unveils HSPA8 as a Key Regulator of PluripotencyDsHsp90 is involved in the early response of Dunaliella salina to environmental stress.Telomere dysfunction in human bone marrow failure syndromes.Diversity in the origins of proteostasis networks--a driver for protein function in evolutionHuman telomerase domain interactions capture DNA for TEN domain-dependent processive elongation.Hsp90-binding immunophilin FKBP51 forms complexes with hTERT enhancing telomerase activity.Both the charged linker region and ATPase domain of Hsp90 are essential for Rad51-dependent DNA repair.
P2860
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P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 16 March 2010
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
HSP90 manages the ends.
@en
HSP90 manages the ends.
@nl
type
label
HSP90 manages the ends.
@en
HSP90 manages the ends.
@nl
prefLabel
HSP90 manages the ends.
@en
HSP90 manages the ends.
@nl
P2860
P1476
HSP90 manages the ends.
@en
P2093
Brian C Freeman
Diane C DeZwaan
P2860
P304
P356
10.1016/J.TIBS.2010.02.005
P577
2010-03-16T00:00:00Z