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Origin and function of ubiquitin-like proteins
scientific article
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scholarly article
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review article
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Europe PubMed Central
title
Origin and function of ubiquitin-like proteins
(English)
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author
Mark Hochstrasser
series ordinal
1
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language of work or name
English
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publication date
26 March 2009
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published in
Nature
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volume
458
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page(s)
422-9
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issue
7237
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cites work
ISG15 inhibits Ebola VP40 VLP budding in an L-domain-dependent manner by blocking Nedd4 ligase activity
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ISG15 inhibits Nedd4 ubiquitin E3 activity and enhances the innate antiviral response
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Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3
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Interferon-inducible ubiquitin E2, Ubc8, is a conjugating enzyme for protein ISGylation
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The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an IFN-alpha/beta-induced ubiquitin-like protein
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Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein
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A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
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Structural insights into E1-catalyzed ubiquitin activation and transfer to conjugating enzymes
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Proteasome subunit Rpn13 is a novel ubiquitin receptor
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The sulfurtransferase activity of Uba4 presents a link between ubiquitin-like protein conjugation and activation of sulfur carrier proteins
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Solution structure of ThiS and implications for the evolutionary roots of ubiquitin
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Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation
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Mechanisms underlying ubiquitination
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A genome-wide screen identifies genes required for formation of the wobble nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces cerevisiae
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Thio-modification of yeast cytosolic tRNA requires a ubiquitin-related system that resembles bacterial sulfur transfer systems
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Multiple interactions of rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis
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Attachment of the ubiquitin-related protein Urm1p to the antioxidant protein Ahp1p
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Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome
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A protein conjugation system in yeast with homology to biosynthetic enzyme reaction of prokaryotes
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Ubiquitin-dependent protein degradation
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UBA 1: an essential yeast gene encoding ubiquitin-activating enzyme
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Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis
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IFN-stimulated gene 15 functions as a critical antiviral molecule against influenza, herpes, and Sindbis viruses
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Proteasome-independent functions of ubiquitin in endocytosis and signaling
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Modification of proteins by ubiquitin and ubiquitin-like proteins
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Reconstitution of a new cysteine biosynthetic pathway in Mycobacterium tuberculosis
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Molecular dissection of autophagy: two ubiquitin-like systems
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Ubiquitin-binding domains
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The ubiquitin system for protein degradation
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Evolution and function of ubiquitin-like protein-conjugation systems
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Unraveling the biochemistry and provenance of pupylation: a prokaryotic analog of ubiquitination
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Targeting proteins for destruction by the ubiquitin system: implications for human pathobiology
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7 January 2021
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Identifiers
DOI
10.1038/NATURE07958
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
427125
Dimensions Publication ID
1028692773
0 references
OpenCitations bibliographic resource ID
427125
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
427125
PMCID
2819001
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
427125
PubMed ID
19325621
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
427125
ResearchGate publication ID
24238216
0 references
Springer Nature article ID
10.1038/nature07958
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