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rdf:type |
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|
lifeskim:mentions |
|
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pubmed:issue |
8
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pubmed:dateCreated |
2009-5-25
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pubmed:abstractText |
Less than 6 feet under: Serum proteins C3, C4, and alpha(2)M each contain a thioester domain buried within a hydrophobic pocket, which is thought to shield the labile thioester from hydrolysis. Herein, we make use of the inherent reactivity of the hydrazide for thioester moieties to chemoselectively label these crucial serum regulators in their native conformation; this demonstrates that access to the thioester site is much greater than previously supposed.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
|
|
pubmed:citationSubset |
IM
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|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
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pubmed:month |
May
|
|
pubmed:issn |
1439-7633
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|
pubmed:author |
|
|
pubmed:issnType |
Electronic
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pubmed:day |
25
|
|
pubmed:volume |
10
|
|
pubmed:owner |
NLM
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|
pubmed:authorsComplete |
Y
|
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pubmed:pagination |
1340-3
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|
pubmed:meshHeading |
|
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pubmed:year |
2009
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|
pubmed:articleTitle |
A chemical approach to immunoprotein engineering: chemoselective functionalization of thioester proteins in their native state.
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|
pubmed:affiliation |
The Scripps-Oxford Laboratory, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
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|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|
