about
Molecular Chaperones as Targets to Circumvent the CFTR Defect in Cystic FibrosisComparative genomics and evolution of the HSP90 family of genes across all kingdoms of organismsA proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting proteinHeat shock protein 90: role in enterovirus 71 entry and assembly and potential target for therapyCHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substratesHsp90-Tau complex reveals molecular basis for specificity in chaperone actionMultifunctional Microtubule-Associated Proteins in PlantsInsights into the molecular mechanism of allostery in Hsp70s.Targeting Plasmodium falciparum Hsp90: Towards Reversing Antimalarial ResistanceProtein homeostasis at the plasma membraneHeat-shock Protein 90 Is Essential for Stabilization of the Hepatitis C Virus Nonstructural Protein NS3Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining ConformationStructure of Minimal Tetratricopeptide Repeat Domain Protein Tah1 Reveals Mechanism of Its Interaction with Pih1 and Hsp90The hsp90 molecular chaperone modulates multiple telomerase activities.The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90The p23 molecular chaperone promotes functional telomerase complexes through DNA dissociationCns1 is an activator of the Ssa1 ATPase activity.Drugging the cancer kinome: progress and challenges in developing personalized molecular cancer therapeuticsA proteomic snapshot of the human heat shock protein 90 interactomeHold me tight: Role of the heat shock protein family of chaperones in cardiac diseasePhenotypic diversity and altered environmental plasticity in Arabidopsis thaliana with reduced Hsp90 levelsHuman mitochondrial Hsp70 (mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organizationProtein targeting and transport as a necessary consequence of increased cellular complexityThe impact of long-term exposure to space environment on adult mammalian organisms: a study on mouse thyroid and testisMerging traditional Chinese medicine with modern drug discovery technologies to find novel drugs and functional foodsATPase activity and ATP-dependent conformational change in the co-chaperone HSP70/HSP90-organizing protein (HOP)Dynamic Interaction of Hsp90 with Its Client Protein p53.The 90-kDa heat shock protein Hsp90 protects tubulin against thermal denaturationCrystallization and X-ray data analysis of the 10 kDa C-terminal lid subdomain from Caenorhabditis elegans Hsp70Regulation of Nod1 by Hsp90 chaperone complex.Systems analysis of chaperone networks in the malarial parasite Plasmodium falciparum.Pharmacokinetics and transcriptional effects of the anti-salmon lice drug emamectin benzoate in Atlantic salmon (Salmo salar L.).Hsp70 chaperones and type I PRMTs are sequestered at intranuclear inclusions caused by polyalanine expansions in PABPN1Synthesis of reblastatin, autolytimycin, and non-benzoquinone analogues: potent inhibitors of heat shock protein 90.Hsp90 and co-chaperones twist the functions of diverse client proteins.Targeting PI3K/Akt/HSP90 signaling sensitizes gastric cancer cells to deoxycholate-induced apoptosis.Fine mapping and expression of candidate genes within the chromosome 10 QTL region of the high and low alcohol-drinking ratsEvidence of a Cell Surface Role for Hsp90 Complex Proteins Mediating Neuroblast Migration in the Subventricular Zone.Hsp90 cochaperone Aha1 is a negative regulator of the Saccharomyces MAL activator and acts early in the chaperone activation pathway.Immunotherapy of radioresistant mammary tumors with early metastasis using molecular chaperone vaccines combined with ionizing radiation.
P2860
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P2860
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Hsp70 and Hsp90--a relay team for protein folding.
@ast
Hsp70 and Hsp90--a relay team for protein folding.
@en
Hsp70 and Hsp90--a relay team for protein folding.
@nl
type
label
Hsp70 and Hsp90--a relay team for protein folding.
@ast
Hsp70 and Hsp90--a relay team for protein folding.
@en
Hsp70 and Hsp90--a relay team for protein folding.
@nl
prefLabel
Hsp70 and Hsp90--a relay team for protein folding.
@ast
Hsp70 and Hsp90--a relay team for protein folding.
@en
Hsp70 and Hsp90--a relay team for protein folding.
@nl
P2093
P1476
Hsp70 and Hsp90--a relay team for protein folding.
@en
P2093
P2888
P356
10.1007/S10254-003-0021-1
P577
2004-01-23T00:00:00Z