Source:http://linkedlifedata.com/resource/pubmed/id/21295473
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
2011-2-21
|
| pubmed:abstractText |
IMP dehydrogenase (IMPDH) catalyzes a critical step in guanine nucleotide biosynthesis. IMPDH also has biological roles that are distinct from its enzymatic function. We report a biotin-linked reagent that selectively labels IMPDH and is released by dithiothreitol. This reagent will be invaluable in elucidating the moonlighting functions of IMPDH.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
1464-3405
|
| pubmed:author | |
| pubmed:copyrightInfo |
Copyright © 2011 Elsevier Ltd. All rights reserved.
|
| pubmed:issnType |
Electronic
|
| pubmed:day |
1
|
| pubmed:volume |
21
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1363-5
|
| pubmed:meshHeading | |
| pubmed:year |
2011
|
| pubmed:articleTitle |
Specific biotinylation of IMP dehydrogenase.
|
| pubmed:affiliation |
Graduate Program in Biochemistry, Brandeis University, Waltham, MA 02454, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
|