Dynamic cycling with Hsp90 stabilizes neuronal nitric oxide synthase through calmodulin-dependent inhibition of ubiquitination.
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Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseasesCalmodulin promotes matrix metalloproteinase 9 production and cell migration by inhibiting the ubiquitination and degradation of TBC1D3 oncoprotein in human breast cancer cells.Inhibition of hsp70 by methylene blue affects signaling protein function and ubiquitination and modulates polyglutamine protein degradationC331A mutant of neuronal nitric-oxide synthase is labilized for Hsp70/CHIP (C terminus of HSC70-interacting protein)-dependent ubiquitination.Liver cytochrome P450 3A ubiquitination in vivo by gp78/autocrine motility factor receptor and C terminus of Hsp70-interacting protein (CHIP) E3 ubiquitin ligases: physiological and pharmacological relevance.Proposal for a role of the Hsp90/Hsp70-based chaperone machinery in making triage decisions when proteins undergo oxidative and toxic damage.A model in which heat shock protein 90 targets protein-folding clefts: rationale for a new approach to neuroprotective treatment of protein folding diseasesHeme-dependent activation of neuronal nitric oxide synthase by cytosol is due to an Hsp70-dependent, thioredoxin-mediated thiol-disulfide interchange in the heme/substrate binding cleftModulation of heme/substrate binding cleft of neuronal nitric-oxide synthase (nNOS) regulates binding of Hsp90 and Hsp70 proteins and nNOS ubiquitinationSoluble guanylyl cyclase requires heat shock protein 90 for heme insertion during maturation of the NO-active enzyme.Ubiquitination of neuronal nitric-oxide synthase in the calmodulin-binding site triggers proteasomal degradation of the protein.Stromal cell-derived factor 2 is critical for Hsp90-dependent eNOS activation.Heat shock proteins regulate activation-induced proteasomal degradation of the mature phosphorylated form of protein kinase C.Just say NO: nitric oxide regulation of Hsp90.The Ubiquitination, Disaggregation and Proteasomal Degradation Machineries in Polyglutamine DiseaseResearch progress on neurobiology of neuronal nitric oxide synthase.No-dependent signaling pathways in unloaded skeletal muscle.Centrosomes at M phase act as a scaffold for the accumulation of intracellular ubiquitinated proteins.ATP binding to Hsp90 is sufficient for effective chaperoning of p53 protein.Counteracting neuronal nitric oxide synthase proteasomal degradation improves glucose transport in insulin-resistant skeletal muscle from Zucker fa/fa rats.
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Dynamic cycling with Hsp90 stabilizes neuronal nitric oxide synthase through calmodulin-dependent inhibition of ubiquitination.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on September 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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Dynamic cycling with Hsp90 sta ...... inhibition of ubiquitination.
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Dynamic cycling with Hsp90 sta ...... inhibition of ubiquitination.
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Dynamic cycling with Hsp90 sta ...... inhibition of ubiquitination.
@en
Dynamic cycling with Hsp90 sta ...... inhibition of ubiquitination.
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prefLabel
Dynamic cycling with Hsp90 sta ...... inhibition of ubiquitination.
@en
Dynamic cycling with Hsp90 sta ...... inhibition of ubiquitination.
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P2093
P2860
P356
P1433
P1476
Dynamic cycling with Hsp90 sta ...... inhibition of ubiquitination.
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P2093
Hwei-Ming Peng
Kelly M Clapp
Miranda Lau
William B Pratt
Yoichi Osawa
Yoshihiro Morishima
P2860
P304
P356
10.1021/BI901058G
P407
P577
2009-09-01T00:00:00Z