Pleiotropic effects of Ubp6 loss on drug sensitivities and yeast prion are due to depletion of the free ubiquitin pool. - Wikidata - wikimedia - TriplyDB

Pleiotropic effects of Ubp6 loss on drug sensitivities and yeast prion are due to depletion of the free ubiquitin pool.

Pleiotropic effects of Ubp6 loss on drug sensitivities and yeast prion are due to depletion of the free ubiquitin pool.

http://www.wikidata.org/entity/Q44618291

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Prion switching in response to environmental stress Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14 Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes The role of deubiquitinating enzymes in synaptic function and nervous system diseases Doa1 is a Cdc48 adapter that possesses a novel ubiquitin binding domain The deubiquitinating enzyme Ubp1 affects sorting of the ATP-binding cassette-transporter Ste6 in the endocytic pathway.The ESCRT-III adaptor protein Bro1 controls functions of regulator for free ubiquitin chains 1 (Rfu1) in ubiquitin homeostasis.Regulatory mechanisms involved in the control of ubiquitin homeostasis Identification of aneuploidy-tolerating mutations The NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotype The requirement for Cdc48/p97 in nuclear protein quality control degradation depends on the substrate and correlates with substrate insolubility Recognition and processing of ubiquitin-protein conjugates by the proteasome Enhancement of proteasome activity by a small-molecule inhibitor of USP14 Characterization of the 26S proteasome network in Plasmodium falciparum De novo [PSI +] prion formation involves multiple pathways to form infectious oligomers.Disease-associated mutant ubiquitin causes proteasomal impairment and enhances the toxicity of protein aggregates.Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104.Eukaryotic cells producing ribosomes deficient in Rpl1 are hypersensitive to defects in the ubiquitin-proteasome system Stress-dependent proteolytic processing of the actin assembly protein Lsb1 modulates a yeast prion Rsp5 ubiquitin ligase modulates translation accuracy in yeast Saccharomyces cerevisiae Severe acute respiratory syndrome coronavirus papain-like protease: structure of a viral deubiquitinating enzyme.Trans-species activity of a nonself recognition domain.Ubiquitin C-terminal hydrolase-l1 activity induces polyubiquitin accumulation in podocytes and increases proteinuria in rat membranous nephropathy.Prion induction by the short-lived, stress-induced protein Lsb2 is regulated by ubiquitination and association with the actin cytoskeleton.Role of the deubiquitylating enzyme DmUsp5 in coupling ubiquitin equilibrium to development and apoptosis in Drosophila melanogaster.Deconstructing the genetic basis of spent sulphite liquor tolerance using deep sequencing of genome-shuffled yeast.The 26S Proteasome Degrades the Soluble but Not the Fibrillar Form of the Yeast Prion Ure2p In Vitro.Ubiquitin-specific protease 14 modulates degradation of cellular prion protein A proteasome for all occasions.Prions in yeast.The ubiquitin-proteasome system of Saccharomyces cerevisiae.Proteasome-associated proteins: regulation of a proteolytic machine.The effect of acetaminophen on ubiquitin homeostasis in Saccharomyces cerevisiae Ubiquitin-specific protease 9x deubiquitinates and stabilizes the spinal muscular atrophy protein-survival motor neuron Open-gate mutants of the mammalian proteasome show enhanced ubiquitin-conjugate degradation Inhibitor recognition specificity of MERS-CoV papain-like protease may differ from that of SARS-CoV Extraproteasomal Rpn10 restricts access of the polyubiquitin-binding protein Dsk2 to proteasome.Sem1p and Ubp6p orchestrate telomeric silencing by modulating histone H2B ubiquitination and H3 acetylation.Polyubiquitin binding and disassembly by deubiquitinating enzymes.

P2860

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P2860

Pleiotropic effects of Ubp6 loss on drug sensitivities and yeast prion are due to depletion of the free ubiquitin pool.

http://www.wikidata.org/entity/Q44618291

description

2003 nî lūn-bûn

@nan

2003年の論文

@ja

2003年学术文章

@wuu

2003年学术文章

@zh

2003年学术文章

@zh-cn

2003年学术文章

@zh-hans

2003年学术文章

@zh-my

2003年学术文章

@zh-sg

2003年學術文章

@yue

2003年學術文章

@zh-hant

name

Pleiotropic effects of Ubp6 lo ...... on of the free ubiquitin pool.

@en

Pleiotropic effects of Ubp6 lo ...... on of the free ubiquitin pool.

@nl

type

label

Pleiotropic effects of Ubp6 lo ...... on of the free ubiquitin pool.

@en

Pleiotropic effects of Ubp6 lo ...... on of the free ubiquitin pool.

@nl

prefLabel

Pleiotropic effects of Ubp6 lo ...... on of the free ubiquitin pool.

@en

Pleiotropic effects of Ubp6 lo ...... on of the free ubiquitin pool.

@nl

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P1433

Journal of Biological Chemistry

P1476

Pleiotropic effects of Ubp6 lo ...... on of the free ubiquitin pool.

@en

P2093

John R Shanks

http://www.w3.org/2001/XMLSchema#string

Keith D Wilkinson

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Kim D Allen

http://www.w3.org/2001/XMLSchema#string

Lisa M Wesoloski

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Tatiana A Chernova

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P2860

Subcellular localization, stoichiometry, and protein levels of 26 S proteasome subunits in yeast

Decreased insulin binding to mononuclear leucocytes and erythrocytes from dogs after S-nitroso-N-acetypenicillamine administration

The ubiquitin system

Proteasome subunit Rpn1 binds ubiquitin-like protein domains.

Multiple associated proteins regulate proteasome structure and function.

Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes

Analysis of the deubiquitinating enzymes of the yeast Saccharomyces cerevisiae.

Interaction of the Doa4 deubiquitinating enzyme with the yeast 26S proteasome.

Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome

A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly.

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52102-52115

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scholarly article

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10.1074/JBC.M310283200

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P433

52

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P478

278

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Yury O. Chernoff

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2003-10-14T00:00:00Z

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14559899

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Prion protein family