The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone
about
Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradationA structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activitiesCrystal structures of Escherichia coli topoisomerase IV ParE subunit (24 and 43 kilodaltons): a single residue dictates differences in novobiocin potency against topoisomerase IV and DNA gyraseThe heat shock protein 90 of Plasmodium falciparum and antimalarial activity of its inhibitor, geldanamycinHsp90 Inhibitors for the Treatment of Chronic Myeloid LeukemiaThe 'active life' of Hsp90 complexesGRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulumSmall Molecule Inhibitors to Disrupt Protein-protein Interactions of Heat Shock Protein 90 Chaperone MachineryTargeting Hsp90 in urothelial carcinomaHeat shock transcription factor 1 as a therapeutic target in neurodegenerative diseasesModeling signal propagation mechanisms and ligand-based conformational dynamics of the Hsp90 molecular chaperone full-length dimerComparative analysis of the ATP-binding sites of Hsp90 by nucleotide affinity cleavage: a distinct nucleotide specificity of the C-terminal ATP-binding siteNucleotide binding states of hsp70 and hsp90 during sequential steps in the process of glucocorticoid receptor.hsp90 heterocomplex assemblyBinding of ATP to heat shock protein 90: evidence for an ATP-binding site in the C-terminal domainElucidation of the Hsp90 C-terminal inhibitor binding siteEnzymatic methods for glyco(diversification/randomization) of drugs and small moleculesDrugging the cancer chaperone HSP90: combinatorial therapeutic exploitation of oncogene addiction and tumor stressHigh throughput screen identifies small molecule inhibitors specific for Mycobacterium tuberculosis phosphoserine phosphataseMarine sediment-derived Streptomyces bacteria from British Columbia, Canada are a promising microbiota resource for the discovery of antimicrobial natural productsRegulation and function of the human HSP90AA1 geneEvidence that hsp90 is involved in the altered interactions of Acanthamoeba castellanii variants with bacteria.Synthesis and evaluation of Hsp90 inhibitors that contain the 1,4-naphthoquinone scaffold.Optimizing glycosyltransferase specificity via "hot spot" saturation mutagenesis presents a catalyst for novobiocin glycorandomization.A high-throughput TNP-ATP displacement assay for screening inhibitors of ATP-binding in bacterial histidine kinasesHsp90 directly modulates the spatial distribution of AF9/MLLT3 and affects target gene expression.Novobiocin analogues with second-generation noviose surrogates.Inhibiting heat-shock protein 90 reverses sensory hypoalgesia in diabetic mice.A Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocket.Probing molecular mechanisms of the Hsp90 chaperone: biophysical modeling identifies key regulators of functional dynamics.Gyrase B inhibitor impairs HIV-1 replication by targeting Hsp90 and the capsid protein.HSP90 as a new therapeutic target for cancer therapy: the story unfolds.The discovery of potential acetylcholinesterase inhibitors: a combination of pharmacophore modeling, virtual screening, and molecular docking studies.Hsp90 functions in the targeting and outer membrane translocation steps of Tom70-mediated mitochondrial import.Structural basis for depletion of heat shock protein 90 client proteins by deguelin.3D-QSAR Assisted Design, Synthesis and Evaluation of Novobiocin Analogues.A novel function of novobiocin: disrupting the interaction of HIF 1α and p300/CBP through direct binding to the HIF1α C-terminal activation domain.Bioactive metabolites from Chaetomium aureum: structure elucidation and inhibition of the Hsp90 machine chaperoning activity.Inhibition of FLT3 expression by green tea catechins in FLT3 mutated-AML cellsTargeting heat-shock-protein 90 (Hsp90) by natural products: geldanamycin, a show case in cancer therapy.
P2860
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P2860
The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone
description
2000 nî lūn-bûn
@nan
2000 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
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2000年论文
@wuu
name
The heat shock protein 90 anta ...... oxyl terminus of the chaperone
@ast
The heat shock protein 90 anta ...... oxyl terminus of the chaperone
@en
The heat shock protein 90 anta ...... oxyl terminus of the chaperone
@nl
type
label
The heat shock protein 90 anta ...... oxyl terminus of the chaperone
@ast
The heat shock protein 90 anta ...... oxyl terminus of the chaperone
@en
The heat shock protein 90 anta ...... oxyl terminus of the chaperone
@nl
prefLabel
The heat shock protein 90 anta ...... oxyl terminus of the chaperone
@ast
The heat shock protein 90 anta ...... oxyl terminus of the chaperone
@en
The heat shock protein 90 anta ...... oxyl terminus of the chaperone
@nl
P2093
P2860
P3181
P356
P1476
The heat shock protein 90 anta ...... oxyl terminus of the chaperone
@en
P2093
P2860
P304
P3181
P356
10.1074/JBC.M003701200
P407
P577
2000-11-24T00:00:00Z