|Molecular cloning of cDNA encoding a human heat-shock protein whose expression is induced by adenovirus type 12 E1A in HeLa cells.
|Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related genes encode formerly identified tumour-specific transplantation antigens.
|Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II.
|The human double-stranded DNA-activated protein kinase phosphorylates the 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal threonine residues.
|Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein.
|Cloning and analysis of a human 86-kDa heat-shock-protein-encoding gene.
|Nucleotide sequence of a full-length cDNA for 90 kDa heat-shock protein from human peripheral blood lymphocytes.
|Mechanism of dimer formation of the 90-kDa heat-shock protein.
|The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo.
|Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent.
|Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin.
|Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90.
|In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis.
|Kinase suppressor of Ras forms a multiprotein signaling complex and modulates MEK localization.
|Antigens recognized by autologous antibody in patients with renal-cell carcinoma.
|Stable association of hsp90 and p23, but Not hsp70, with active human telomerase.
|A CD14-independent LPS receptor cluster.
|Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex.
|The DNA sequence and analysis of human chromosome 14.
|Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone.
|Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system.
|Complete sequencing and characterization of 21,243 full-length human cDNAs.
|SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells.
|Human protein phosphatase 5 dissociates from heat-shock proteins and is proteolytically activated in response to arachidonic acid and the microtubule-depolymerizing drug nocodazole.
|The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
|Molecular basis for TPR domain-mediated regulation of protein phosphatase 5.
|Small glutamine-rich tetratricopeptide repeat-containing protein is composed of three structural units with distinct functions.
|S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities.
|Proteomic identification of proteins conjugated to ISG15 in mouse and human cells.
|The HSP90 family of genes in the human genome: insights into their divergence and evolution.
|Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.
|Conformational diversity in the TPR domain-mediated interaction of protein phosphatase 5 with Hsp90.
|Phosphoproteomic analysis of the human pituitary.
|Folliculin encoded by the BHD gene interacts with a binding protein, FNIP1, and AMPK, and is involved in AMPK and mTOR signaling.
|Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.
|Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
|Phosphoproteome of resting human platelets.
|The ATPase-dependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis.
|Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.
|Conserved conformational changes in the ATPase cycle of human Hsp90.
|A quantitative atlas of mitotic phosphorylation.
|Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
|Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.
|Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
|Lysine acetylation targets protein complexes and co-regulates major cellular functions.
|Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
|Hsp90 is regulated by a switch point in the C-terminal domain.
|A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein.
|Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
|Stat1 mediates an auto-regulation of hsp90beta gene in heat shock response.
|Initial characterization of the human central proteome.
|System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
|Toward a comprehensive characterization of a human cancer cell phosphoproteome.
|Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites.
|An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
|Hsp70 and Hsp90 oppositely regulate TGF-beta signaling through CHIP/Stub1.
|The NLR-related protein NWD1 is associated with prostate cancer and modulates androgen receptor signaling.
|C-terminal domain of SMYD3 serves as a unique HSP90-regulated motif in oncogenesis.
|N-terminome analysis of the human mitochondrial proteome.
|Hsp90, the concertmaster: tuning transcription.
|Client proteins and small molecule inhibitors display distinct binding preferences for constitutive and stress-induced HSP90 isoforms and their conformationally restricted mutants.
|IER5 generates a novel hypo-phosphorylated active form of HSF1 and contributes to tumorigenesis.
|Review: The HSP90 molecular chaperone-an enigmatic ATPase.
|Hsp90: Friends, clients and natural foes.
|The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding.