Sequence composition of disordered regions fine-tunes protein half-life.
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Intracellular Dynamics of the Ubiquitin-Proteasome-SystemThe contribution of intrinsically disordered regions to protein function, cellular complexity, and human diseaseAn Inducible System for Rapid Degradation of Specific Cellular Proteins Using Proteasome AdaptorsVariation in auxin sensing guides AUX/IAA transcriptional repressor ubiquitylation and destruction.Pri sORF peptides induce selective proteasome-mediated protein processing.Gates, Channels, and Switches: Elements of the Proteasome MachineSubstrate Ubiquitination Controls the Unfolding Ability of the Proteasome.Site-specific proteasome phosphorylation controls cell proliferation and tumorigenesis.Rapidly Translated Polypeptides Are Preferred Substrates for Cotranslational Protein Degradation.The Proteasome Ubiquitin Receptor hRpn13 and Its Interacting Deubiquitinating Enzyme Uch37 Are Required for Proper Cell Cycle ProgressionUbiquitin-like domains can target to the proteasome but proteolysis requires a disordered region.Phosphorylation of the C-terminal tail of proteasome subunit α7 is required for binding of the proteasome quality control factor Ecm29.Regulation of Proteasomal Degradation by Modulating Proteasomal Initiation RegionsConserved Sequence Preferences Contribute to Substrate Recognition by the Proteasome.Mouse Mammary Tumor Virus Signal Peptide Uses a Novel p97-Dependent and Derlin-Independent Retrotranslocation Mechanism To Escape Proteasomal Degradation.How do disordered regions achieve comparable functions to structured domains?Structural disorder and its role in proteasomal degradation.Reciprocal proteasome-mediated degradation of PIFs and HFR1 underlies photomorphogenic development in Arabidopsis.Ubiquitin recognition by the proteasome.AAA-ATPases in Protein Degradation.An assay for 26S proteasome activity based on fluorescence anisotropy measurements of dye-labeled protein substratesAltered Co-Translational Processing Plays a Role in Huntington's Pathogenesis-A Hypothesis.Incomplete proteasomal degradation of green fluorescent proteins in the context of tandem fluorescent protein timers.A conserved degron containing an amphipathic helix regulates the cholesterol-mediated turnover of human squalene monooxygenase, a rate-limiting enzyme in cholesterol synthesis.In Vivo Reporters for Protein Half-Life.Constraints and consequences of the emergence of amino acid repeats in eukaryotic proteins.Predicting proteome dynamics using gene expression data
P2860
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P2860
Sequence composition of disordered regions fine-tunes protein half-life.
description
2015 nî lūn-bûn
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2015年の論文
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2015年学术文章
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2015年学术文章
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2015年学术文章
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2015年学术文章
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2015年学术文章
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2015年學術文章
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2015年學術文章
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name
Sequence composition of disordered regions fine-tunes protein half-life.
@en
Sequence composition of disordered regions fine-tunes protein half-life.
@nl
type
label
Sequence composition of disordered regions fine-tunes protein half-life.
@en
Sequence composition of disordered regions fine-tunes protein half-life.
@nl
prefLabel
Sequence composition of disordered regions fine-tunes protein half-life.
@en
Sequence composition of disordered regions fine-tunes protein half-life.
@nl
P2093
P2860
P50
P356
P1476
Sequence composition of disordered regions fine-tunes protein half-life.
@en
P2093
Eitan Israeli
Grace Kago
Houqing Yu
Sreenivas Chavali
Susan Fishbain
P2860
P2888
P304
P356
10.1038/NSMB.2958
P577
2015-02-02T00:00:00Z