The effect of bisphosphonate acidity on the activity of a thymidylyltransferase.

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On the observation of discrete fluorine NMR spectra for uridine 5'-β,γ-fluoromethylenetriphosphate diastereomers at basic pH.5'-β,γ-CHF-ATP diastereomers: synthesis and fluorine-mediated selective binding by c-Src protein kinase.

P2860

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P2860

The effect of bisphosphonate acidity on the activity of a thymidylyltransferase.

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http://www.wikidata.org/entity/Q48001390

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2013 nî lūn-bûn

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2013年学术文章

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The effect of bisphosphonate acidity on the activity of a thymidylyltransferase.

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The effect of bisphosphonate acidity on the activity of a thymidylyltransferase.

@nl

type

Item

label

The effect of bisphosphonate acidity on the activity of a thymidylyltransferase.

@en

The effect of bisphosphonate acidity on the activity of a thymidylyltransferase.

@nl

prefLabel

The effect of bisphosphonate acidity on the activity of a thymidylyltransferase.

@en

The effect of bisphosphonate acidity on the activity of a thymidylyltransferase.

@nl

P1476

The effect of bisphosphonate acidity on the activity of a thymidylyltransferase.

@en

P2093

David L Jakeman

http://www.w3.org/2001/XMLSchema#string

Jonathan C Melong

http://www.w3.org/2001/XMLSchema#string

Matthew W Loranger

http://www.w3.org/2001/XMLSchema#string

Patricia M Jiang

http://www.w3.org/2001/XMLSchema#string

Samy Mohamady

http://www.w3.org/2001/XMLSchema#string

Stephen A Beaton

http://www.w3.org/2001/XMLSchema#string

Thomas I Veinot

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal structures of Escherichia coli glycerol kinase variant S58-->W in complex with nonhydrolyzable ATP analogues reveal a putative active conformation of the enzyme as a result of domain motion

The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA)

Crystal structures of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, in apo form at 2.33 A resolution and in complex with UDP-N-acetylglucosamine and Mg(2+) at 1.96 A resolution

Structure, mechanism and engineering of a nucleotidylyltransferase as a first step toward glycorandomization

Kinetic and crystallographic analyses support a sequential-ordered bi bi catalytic mechanism for Escherichia coli glucose-1-phosphate thymidylyltransferase

Crystal structure of Escherichia coli glucose-1-phosphate thymidylyltransferase (RffH) complexed with dTTP and Mg2+

Expanding pyrimidine diphosphosugar libraries via structure-based nucleotidylyltransferase engineering

The molecular architecture of glucose-1-phosphate uridylyltransferase

( R )-β,γ-Fluoromethylene-dGTP-DNA Ternary Complex with DNA Polymerase β

Halogenated β,γ-Methylene- and Ethylidene-dGTP-DNA Ternary Complexes with DNA Polymerase β: Structural Evidence for Stereospecific Binding of the Fluoromethylene Analogues

P304

5473-5480

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scholarly article

P356

10.1039/C3OB41017J

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P433

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P478

http://www.w3.org/2001/XMLSchema#string

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2013-09-01T00:00:00Z

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P698

23857455

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The effect of bisphosphonate acidity on the activity of a thymidylyltransferase.

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P2860

P2860

The effect of bisphosphonate acidity on the activity of a thymidylyltransferase.

description

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type

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prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698