Protein modification by SUMO

Trends in Biochemical Sciences

Volumn 26, Issue 5, 2001, Pages 332-333

  Hay, R T ^a  

^a UNIVERSITY OF ST ANDREWS   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMINO ACID; CAMPTOTHECIN; DNA TOPOISOMERASE; HYDROLASE; LIGASE; PROTEIN; PROTEINASE; SMALL UBIQUITIN LIKE MODIFIER; SUMO 1 PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CELL FUNCTION; EUKARYOTE; GENE DELETION; GENE MUTATION; GENETIC CODE; HUMAN; NONHUMAN; NOTE; PRIORITY JOURNAL; PROTEIN MODIFICATION; PROTEIN STRUCTURE; PROTEIN TARGETING; SACCHAROMYCES; SURFACE CHARGE;

EUKARYOTA; SACCHAROMYCES;

EID: 0035336677     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(01)01849-7     Document Type: Note

References (7)

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3. Y. Mao SUMO-1 conjugation totopoisomerase I: a possible repair responsetotopoisomerase-mediated DNA damage Proc.Natl. Acad. Sci. USA 97 2000 4046 4051
4. F. Melchior SUMO – nonclassical ubiquitin Annu. Rev. Cell Dev. Biol. 16 2000 591 626
5. Rodriguez, M.S. et al . (2000) SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting. J. Biol. Chem. [ http://www.jbc.org/cgi/reprint/M009476200v1 ]
6. E.T. Yeh Ubiquitin-like proteins: new wines in new bottles Gene 248 2000 1 14
7. S. Zhong Role of SUMO-1-modified PML in nuclear body formation Blood 95 2000 2748 2752