Global functional map of the p23 molecular chaperone reveals an extensive cellular network.
about
A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathwaysHsp90: A New Player in DNA Repair?The p23 molecular chaperone and GCN5 acetylase jointly modulate protein-DNA dynamics and open chromatin statusThe Hsp90 cochaperones Cpr6, Cpr7, and Cns1 interact with the intact ribosomeApproaches for defining the Hsp90-dependent proteome.A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering.GIGANTEA is a co-chaperone which facilitates maturation of ZEITLUPE in the Arabidopsis circadian clockControl of steroid receptor dynamics and function by genomic actions of the cochaperones p23 and Bag-1LHSP90 regulates DNA repair via the interaction between XRCC1 and DNA polymerase βA network of its own: the unique interactome of the Hsp90 cochaperone, Sba1/p23Co-chaperone p23 regulates C. elegans Lifespan in Response to Temperature.Research resource: enhanced genome-wide occupancy of estrogen receptor α by the cochaperone p23 in breast cancer cellsdaf-41/p23: A Small Protein Heating Up Lifespan RegulationLeishmania donovani P23 protects parasites against HSP90 inhibitor-mediated growth arrest.The co-chaperone p23 promotes prostate cancer motility and metastasisCaspase-7: a critical mediator of optic nerve injury-induced retinal ganglion cell deathBiology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Gedunin inactivates the co-chaperone p23 protein causing cancer cell death by apoptosis.Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors.Emerging roles of NudC family: from molecular regulation to clinical implications.Lysine deacetylases regulate the heat shock response including the age-associated impairment of HSF1.Both the charged linker region and ATPase domain of Hsp90 are essential for Rad51-dependent DNA repair.The Aryl-Hydrocarbon Receptor Protein Interaction Network (AHR-PIN) as Identified by Tandem Affinity Purification (TAP) and Mass Spectrometry.Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding.Characterization of an Hsp90-Independent Interaction between Co-Chaperone p23 and Transcription Factor p53.Importance of cycle timing for the function of the molecular chaperone Hsp90.The HSP90 chaperone machinery.Adapting to stress - chaperome networks in cancer.
P2860
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P2860
Global functional map of the p23 molecular chaperone reveals an extensive cellular network.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Global functional map of the p ...... an extensive cellular network.
@en
type
label
Global functional map of the p ...... an extensive cellular network.
@en
prefLabel
Global functional map of the p ...... an extensive cellular network.
@en
P2093
P2860
P1433
P1476
Global functional map of the p ...... an extensive cellular network.
@en
P2093
Brenda J Andrews
Brian C Freeman
Elena Zelin
Ellinor Oxelmark
Frank J Echtenkamp
Joyce I Woo
Michael Garabedian
P2860
P304
P356
10.1016/J.MOLCEL.2011.05.029
P577
2011-07-01T00:00:00Z