Ubiquitin depletion as a key mediator of toxicity by translational inhibitors. - Wikidata - awgldk - TriplyDB

Ubiquitin depletion as a key mediator of toxicity by translational inhibitors.

Ubiquitin depletion as a key mediator of toxicity by translational inhibitors.

http://www.wikidata.org/entity/Q34986792

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Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14 Protein degradation and the stress response The Not4 RING E3 Ligase: A Relevant Player in Cotranslational Quality Control Conformational dynamics control ubiquitin-deubiquitinase interactions and influence in vivo signaling The predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradation The 26S proteasome drives trinucleotide repeat expansions Interaction of the deubiquitinating enzyme Ubp2 and the e3 ligase Rsp5 is required for transporter/receptor sorting in the multivesicular body pathway.DOA1/UFD3 plays a role in sorting ubiquitinated membrane proteins into multivesicular bodies The deubiquitinating enzyme Ubp1 affects sorting of the ATP-binding cassette-transporter Ste6 in the endocytic pathway.Disassembly of Lys11 and mixed linkage polyubiquitin conjugates provides insights into function of proteasomal deubiquitinases Rpn11 and Ubp6.Accumulation of ubiquitin and sequestosome-1 implicate protein damage in diacetyl-induced cytotoxicity Regulatory mechanisms involved in the control of ubiquitin homeostasis Identification of aneuploidy-tolerating mutations The mouse polyubiquitin gene UbC is essential for fetal liver development, cell-cycle progression and stress tolerance Regulation of proteasome activity in health and disease Hypothalamic neurodegeneration and adult-onset obesity in mice lacking the Ubb polyubiquitin gene Determination of ubiquitin fitness landscapes under different chemical stresses in a classroom setting Recognition and processing of ubiquitin-protein conjugates by the proteasome Enhancement of proteasome activity by a small-molecule inhibitor of USP14 Characterizing ubiquitination sites by peptide-based immunoaffinity enrichment.Cell periphery-related proteins as major genomic targets behind the adaptive evolution of an industrial Saccharomyces cerevisiae strain to combined heat and hydrolysate stress N-linked glycosylation does not impair proteasomal degradation but affects class I major histocompatibility complex presentation.Proteasome-mediated degradation of cotranslationally damaged proteins involves translation elongation factor 1A.Signaling from the adherens junction.Ubiquitin C-terminal hydrolase-L1 protects cystic fibrosis transmembrane conductance regulator from early stages of proteasomal degradation.Proteomic Analysis of the EWS-Fli-1 Interactome Reveals the Role of the Lysosome in EWS-Fli-1 Turnover.FOXO3a mediates signaling crosstalk that coordinates ubiquitin and atrogin-1/MAFbx expression during glucocorticoid-induced skeletal muscle atrophy Identification of mammalian protein quality control factors by high-throughput cellular imaging A deubiquitylating complex required for neosynthesis of a yeast mitochondrial ATP synthase subunit The eukaryotic translation elongation Factor 1Bgamma has a non-guanine nucleotide exchange factor role in protein metabolism Rsp5 ubiquitin ligase modulates translation accuracy in yeast Saccharomyces cerevisiae Muscle wasting in aged, sarcopenic rats is associated with enhanced activity of the ubiquitin proteasome pathway.Loss of polyubiquitin gene Ubb leads to metabolic and sleep abnormalities in mice Saccharomyces cerevisiae Ub-conjugating enzyme Ubc4 binds the proteasome in the presence of translationally damaged proteins Proteasomal degradation of Sfp1 contributes to the repression of ribosome biogenesis during starvation and is mediated by the proteasome activator Blm10.In vivo and in silico analysis of PCNA ubiquitylation in the activation of the Post Replication Repair pathway in S. cerevisiae.Werner helicase-interacting protein 1 binds polyubiquitin via its zinc finger domain.Polyubiquitin linkage profiles in three models of proteolytic stress suggest the etiology of Alzheimer disease.Improved quantitative mass spectrometry methods for characterizing complex ubiquitin signals.Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes.

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Ubiquitin depletion as a key mediator of toxicity by translational inhibitors.

http://www.wikidata.org/entity/Q34986792

description

2003 nî lūn-bûn

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2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

Ubiquitin depletion as a key mediator of toxicity by translational inhibitors.

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Ubiquitin depletion as a key mediator of toxicity by translational inhibitors.

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Ubiquitin depletion as a key mediator of toxicity by translational inhibitors.

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type

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Ubiquitin depletion as a key mediator of toxicity by translational inhibitors.

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Ubiquitin depletion as a key mediator of toxicity by translational inhibitors.

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Ubiquitin depletion as a key mediator of toxicity by translational inhibitors.

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Ubiquitin depletion as a key mediator of toxicity by translational inhibitors.

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Ubiquitin depletion as a key mediator of toxicity by translational inhibitors.

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Ubiquitin depletion as a key mediator of toxicity by translational inhibitors.

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MCB.23.24.9251-9261.2003

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Molecular and Cellular Biology

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Ubiquitin depletion as a key mediator of toxicity by translational inhibitors.

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P2093

Daniel Finley

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David S Leggett

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John Hanna

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P2860

Multiple associated proteins regulate proteasome structure and function.

Yeast gene YRR1, which is required for resistance to 4-nitroquinoline N-oxide, mediates transcriptional activation of the multidrug resistance transporter gene SNQ2.

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

Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome.

Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome.

A cryptic protease couples deubiquitination and degradation by the proteasome.

Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins.

The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis.

New roles for ubiquitin in the assembly and function of neuronal circuits

Synaptic defects in ataxia mice result from a mutation in Usp14, encoding a ubiquitin-specific protease

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9251-9261

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10.1128/MCB.23.24.9251-9261.2003

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