Ubiquitination-Induced Conformational Change within the Deiodinase Dimer Is a Switch Regulating Enzyme Activity

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Veröffentlicht in:	Molecular and Cellular Biology 2007-07, Vol.27 (13), p.4774-4783
Hauptverfasser:	Sagar, G. D. Vivek, Gereben, Balázs, Callebaut, Isabelle, Mornon, Jean-Paul, Zeöld, Anikó, da Silva, Wagner S., Luongo, Cristina, Dentice, Monica, Tente, Susana M., Freitas, Beatriz C. G., Harney, John W., Zavacki, Ann Marie, Bianco, Antonio C.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Biochemistry, Molecular Biology Catalysis Catalytic Domain Cell Line Dimerization Holoenzymes - chemistry Holoenzymes - metabolism Humans Iodide Peroxidase - chemistry Iodide Peroxidase - metabolism Life Sciences Mice Models, Molecular Molecular Sequence Data Protein Binding Protein Structure, Quaternary Protein Structure, Secondary Protein Structure, Tertiary Structural Biology Structure-Activity Relationship Ubiquitin - metabolism
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Zusammenfassung:	Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology. For an alternate route to MCB .asm.org, visit: MCB
ISSN:	0270-7306 1098-5549 1098-5549 1939-4586
DOI:	10.1128/MCB.00283-07