Hsp90: a chaperone for protein folding and gene regulation.
about
Protein Hit1, a novel box C/D snoRNP assembly factor, controls cellular concentration of the scaffolding protein Rsa1 by direct interactionA dynamic scaffold of pre-snoRNP factors facilitates human box C/D snoRNP assemblyHsp90 selectively modulates phenotype in vertebrate developmentCharacterization of the interaction between protein Snu13p/15.5K and the Rsa1p/NUFIP factor and demonstration of its functional importance for snoRNP assemblyNop17 is a key R2TP factor for the assembly and maturation of box C/D snoRNP complex.HDAC6 controls major cell response pathways to cytotoxic accumulation of protein aggregatesPhase I evaluation of STA-1474, a prodrug of the novel HSP90 inhibitor ganetespib, in dogs with spontaneous cancerMarine sediment-derived Streptomyces bacteria from British Columbia, Canada are a promising microbiota resource for the discovery of antimicrobial natural productsHeat shock proteins: cellular and molecular mechanisms in the central nervous system.A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering.A class of extracellular vesicles from breast cancer cells activates VEGF receptors and tumour angiogenesis.Transcriptomic response of the mycoparasitic fungus Trichoderma atroviride to the presence of a fungal prey.Shotgun glycopeptide capture approach coupled with mass spectrometry for comprehensive glycoproteomics.A purine scaffold Hsp90 inhibitor destabilizes BCL-6 and has specific antitumor activity in BCL-6-dependent B cell lymphomas.The synthesis and evaluation of flavone and isoflavone chimeras of novobiocin and derruboneAlternative oligomeric states of the yeast Rvb1/Rvb2 complex induced by histidine tags.Gyrase B inhibitor impairs HIV-1 replication by targeting Hsp90 and the capsid protein.In Vitro Activity of Geldanamycin Derivatives against Schistosoma japonicum and Brugia malayiTargeting heat-shock-protein 90 (Hsp90) by natural products: geldanamycin, a show case in cancer therapy.HSP90 supports tumor growth and angiogenesis through PRKD2 protein stabilization.Dealing with misfolded proteins: examining the neuroprotective role of molecular chaperones in neurodegeneration.Engineering an antibiotic to fight cancer: optimization of the novobiocin scaffold to produce anti-proliferative agents.Interactions between Hsp90 and oncogenic viruses: implications for viral cancer therapeuticsHeat shock proteins in association with heat tolerance in grasses.Regulation of proto-oncogenic dbl by chaperone-controlled, ubiquitin-mediated degradation.Hsp90 Is a Novel Target Molecule of CDDO-Me in Inhibiting Proliferation of Ovarian Cancer CellsThe Hsp40 molecular chaperone Ydj1p, along with the protein kinase C pathway, affects cell-wall integrity in the yeast Saccharomyces cerevisiae.Characterizing the role of Hsp90 in production of heat shock proteins in motor neurons reveals a suppressive effect of wild-type Hsf1.Expression of heat shock protein 70 in the thermally stressed antarctic clam Laternula elliptica.Cisplatin resistance: a cellular self-defense mechanism resulting from multiple epigenetic and genetic changes.Functioning of the Hsp90 machine in chaperoning checkpoint kinase I (Chk1) and the progesterone receptor (PR).Control of estradiol-directed gene transactivation by an intracellular estrogen-binding protein and an estrogen response element-binding protein.Shuttling of the chaperones Unc45b and Hsp90a between the A band and the Z line of the myofibrilHsp90 at the crossroads of genetics and epigenetics.The activities and function of molecular chaperones in the endoplasmic reticulum.Association of hsp90 to the hTERT promoter is necessary for hTERT expression in human oral cancer cellsStress, drugs, and evolution: the role of cellular signaling in fungal drug resistanceEstradiol and tamoxifen mediate rescue of the dominant-negative effects of estrogen response element-binding protein in vivo and in vitroNovobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket.Pharmacokinetics and dose escalation of the heat shock protein inhibitor 17-allyamino-17-demethoxygeldanamycin in combination with bortezomib in relapsed or refractory acute myeloid leukemia.
P2860
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P2860
Hsp90: a chaperone for protein folding and gene regulation.
description
2005 nî lūn-bûn
@nan
2005 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Hsp90: a chaperone for protein folding and gene regulation.
@ast
Hsp90: a chaperone for protein folding and gene regulation.
@en
Hsp90: a chaperone for protein folding and gene regulation.
@nl
type
label
Hsp90: a chaperone for protein folding and gene regulation.
@ast
Hsp90: a chaperone for protein folding and gene regulation.
@en
Hsp90: a chaperone for protein folding and gene regulation.
@nl
prefLabel
Hsp90: a chaperone for protein folding and gene regulation.
@ast
Hsp90: a chaperone for protein folding and gene regulation.
@en
Hsp90: a chaperone for protein folding and gene regulation.
@nl
P2860
P356
P1476
Hsp90: a chaperone for protein folding and gene regulation.
@en
P2093
Rongmin Zhao
Walid A Houry
P2860
P304
P356
10.1139/O05-158
P577
2005-12-01T00:00:00Z