about
Comparative genomics and evolution of the HSP90 family of genes across all kingdoms of organismsInteraction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradationTheileria-induced constitutive IKK activation is independent of functional Hsp90Identification and characterization of SSTK, a serine/threonine protein kinase essential for male fertilitySuppression of the mTOR-raptor signaling pathway by the inhibitor of heat shock protein 90 geldanamycinGCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasomeThe expression of HSP83 genes in Leishmania infantum is affected by temperature and by stage-differentiation and is regulated at the levels of mRNA stability and translationThe heat shock protein 90 of Plasmodium falciparum and antimalarial activity of its inhibitor, geldanamycinAnalysis and characterization of differential gene expression during rapid trophoblastic elongation in the pig using suppression subtractive hybridizationGanetespib: research and clinical developmentTargeting JAK2 in the therapy of myeloproliferative neoplasmsRole of heat shock proteins in stem cell behaviorHsp90 selectively modulates phenotype in vertebrate developmentElectrostatic Interactions of Hsp-organizing Protein Tetratricopeptide Domains with Hsp70 and Hsp90: COMPUTATIONAL ANALYSIS AND PROTEIN ENGINEERINGCrystallographic structure of the tetratricopeptide repeat domain ofPlasmodium falciparumFKBP35 and its molecular interaction with Hsp90 C-terminal pentapeptideNovel targeted therapies for Bcr-Abl positive acute leukemias: beyond STI571.Sti1 is a novel activator of the Ssa proteins.Functional interactions between Hsp90 and the co-chaperones Cns1 and Cpr7 in Saccharomyces cerevisiae.Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast.Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologiesA truncated form of p23 down-regulates telomerase activity via disruption of Hsp90 functionComparative analysis of the ATP-binding sites of Hsp90 by nucleotide affinity cleavage: a distinct nucleotide specificity of the C-terminal ATP-binding siteRegulation of telomerase activity and anti-apoptotic function by protein-protein interaction and phosphorylationEvidence that peroxisome proliferator-activated receptor alpha is complexed with the 90-kDa heat shock protein and the hepatitis virus B X-associated protein 2Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasivenessThe regulatory mechanism of Hsp90alpha secretion and its function in tumor malignancyInhibition of heat-shock protein 90 reduces Ebola virus replicationHeat shock protein 90 positively regulates Chikungunya virus replication by stabilizing viral non-structural protein nsP2 during infectionRab-alphaGDI activity is regulated by a Hsp90 chaperone complexDifferential modulation of functional dynamics and allosteric interactions in the Hsp90-cochaperone complexes with p23 and Aha1: a computational study.Dynamic Interaction of Hsp90 with Its Client Protein p53.Clathrin-independent endocytosis of ErbB2 in geldanamycin-treated human breast cancer cells.The 90-kDa heat shock protein Hsp90 protects tubulin against thermal denaturationDynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle.Stress response in tardigrades: differential gene expression of molecular chaperonesEvidence that hsp90 is involved in the altered interactions of Acanthamoeba castellanii variants with bacteria.Nrf2 is an inhibitor of the Fas pathway as identified by Achilles' Heel Method, a new function-based approach to gene identification in human cells.Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37.Control of canalization and evolvability by Hsp90
P2860
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P2860
description
2001 nî lūn-bûn
@nan
2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Hsp90: chaperoning signal transduction.
@ast
Hsp90: chaperoning signal transduction.
@en
Hsp90: chaperoning signal transduction.
@nl
type
label
Hsp90: chaperoning signal transduction.
@ast
Hsp90: chaperoning signal transduction.
@en
Hsp90: chaperoning signal transduction.
@nl
prefLabel
Hsp90: chaperoning signal transduction.
@ast
Hsp90: chaperoning signal transduction.
@en
Hsp90: chaperoning signal transduction.
@nl
P2860
P356
P1476
Hsp90: chaperoning signal transduction.
@en
P2093
P2860
P304
P356
10.1002/JCP.1131
P577
2001-09-01T00:00:00Z