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Bioorganic & Medicinal Chemistry Letters
Article . 2011 . Peer-reviewed
License: Elsevier TDM
Data sources: Crossref
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Specific biotinylation of IMP dehydrogenase

Authors: B Christopher, Hoefler; Deviprasad R, Gollapalli; Lizbeth, Hedstrom;

Specific biotinylation of IMP dehydrogenase

Abstract

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.

Related Organizations
Keywords

Models, Molecular, Dithiothreitol, IMP Dehydrogenase, Molecular Structure, Humans, Biotinylation

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    popularity
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    influence
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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
2
Average
Average
Average
bronze