The dual role of ubiquitin-like protein Urm1 as a protein modifier and sulfur carrier
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Title
The dual role of ubiquitin-like protein Urm1 as a protein modifier and sulfur carrier
Authors
Keywords
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Journal
Protein & Cell
Volume 2, Issue 8, Pages 612-619
Publisher
Springer Nature
Online
2011-09-08
DOI
10.1007/s13238-011-1074-6
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Note: Only part of the references are listed.- Urm1 couples sulfur transfer to ubiquitin-like protein function in oxidative stress: Fig. 1.
- (2011) Matthew D. Petroski et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-directed protein modifier
- (2011) Annemarthe G. Van der Veen et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- E1- and ubiquitin-like proteins provide a direct link between protein conjugation and sulfur transfer in archaea
- (2011) H. V. Miranda et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax volcanii
- (2010) Matthew A. Humbard et al. NATURE
- Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site
- (2010) J. Ling et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Ubiquitin-related modifier Urm1 acts as a sulphur carrier in thiolation of eukaryotic transfer RNA
- (2009) Sebastian Leidel et al. NATURE
- Innate immune and chemically triggered oxidative stress modifies translational fidelity
- (2009) Nir Netzer et al. NATURE
- Origin and function of ubiquitin-like proteins
- (2009) Mark Hochstrasser NATURE
- Mechanistic characterization of the sulfur-relay system for eukaryotic 2-thiouridine biogenesis at tRNA wobble positions
- (2009) Akiko Noma et al. NUCLEIC ACIDS RESEARCH
- The Sulfurtransferase Activity of Uba4 Presents a Link between Ubiquitin-like Protein Conjugation and Activation of Sulfur Carrier Proteins†
- (2008) Jennifer Schmitz et al. BIOCHEMISTRY
- Urm1 at the crossroad of modifications. ‘Protein Modifications: Beyond the Usual Suspects’ Review Series
- (2008) Patrick G A Pedrioli et al. EMBO REPORTS
- Bringing order to translation: the contributions of transfer RNA anticodon-domain modifications
- (2008) Paul F Agris EMBO REPORTS
- Thio-modification of Yeast Cytosolic tRNA Requires a Ubiquitin-related System That Resembles Bacterial Sulfur Transfer Systems
- (2008) Yumi Nakai et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- A Novel Role for Human Nfs1 in the Cytoplasm
- (2008) Zvonimir Marelja et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Eukaryotic Wobble Uridine Modifications Promote a Functionally Redundant Decoding System
- (2008) M. J. O. Johansson et al. MOLECULAR AND CELLULAR BIOLOGY
- The conserved Wobble uridine tRNA thiolase Ctu1-Ctu2 is required to maintain genome integrity
- (2008) M. Dewez et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- A functional proteomics approach links the ubiquitin-related modifier Urm1 to a tRNA modification pathway
- (2008) C. D. Schlieker et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Crystal structure of the dimeric Urm1 from the yeastSaccharomyces cerevisiae
- (2008) Jiang Yu et al. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
- A genome-wide screen identifies genes required for formation of the wobble nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces cerevisiae
- (2008) B. Huang et al. RNA
- HIV-1 reverse transcription initiation: A potential target for novel antivirals?
- (2008) Truus E.M. Abbink et al. VIRUS RESEARCH
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