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The additivity of substrate fragments in enzyme-ligand binding
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scholarly article
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title
The additivity of substrate fragments in enzyme-ligand binding
(English)
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main subject
ligand binding
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inferred from title
author name string
T J Stout
series ordinal
1
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C R Sage
series ordinal
2
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R M Stroud
series ordinal
3
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language of work or name
English
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publication date
15 July 1998
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published in
Structure
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volume
6
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issue
7
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page(s)
839-48
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cites work
The catalytic mechanism and structure of thymidylate synthase
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Atomic structure of thymidylate synthase: target for rational drug design
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Pairwise specificity and sequential binding in enzyme catalysis: thymidylate synthase
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Cofactor triggers the conformational change in thymidylate synthase: implications for an ordered binding mechanism
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Refined structures of substrate-bound and phosphate-bound thymidylate synthase from Lactobacillus casei
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Plastic adaptation toward mutations in proteins: structural comparison of thymidylate synthases
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Structure, multiple site binding, and segmental accommodation in thymidylate synthase on binding dUMP and an anti-folate
1 reference
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reference URL
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A C-terminal conformational equilibrium in thymidylate synthase observed by electron paramagnetic resonance spectroscopy
1 reference
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An essential role for water in an enzyme reaction mechanism: the crystal structure of the thymidylate synthase mutant E58Q
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Biochemical effects of a quinazoline inhibitor of thymidylate synthetase, N-(4-(N-(( 2-amino-4-hydroxy-6-quinazolinyl)methyl)prop-2-ynylamino) benzoyl)-L-glutamic acid (CB3717), on human lymphoblastoid cells
1 reference
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The clinical pharmacokinetics of the novel antifolate N10-propargyl-5,8-dideazafolic acid (CB 3717)
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The measurement of polyglutamate metabolites of the thymidylate synthase inhibitor, ICI D1694, in mouse and human cultured cells
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The pharmacokinetics of the quinazoline antifolate ICI D 1694 in mice and rats
1 reference
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Kinetic characteristics of ICI D1694: a quinazoline antifolate which inhibits thymidylate synthase
1 reference
stated in
Crossref
reference URL
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7 January 2021
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inferred from DOI database lookup
Kinetics and mechanism of interaction of 10-propargyl-5,8-dideazafolate with thymidylate synthase
1 reference
stated in
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Biochemical factors affecting the tightness of 5-fluorodeoxyuridylate binding to human thymidylate synthetase
1 reference
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Mutation of asparagine 229 to aspartate in thymidylate synthase converts the enzyme to a deoxycytidylate methylase
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A novel dCMP methylase by engineering thymidylate synthase
1 reference
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Where freedom is given, liberties are taken
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Phi/psi-chology: Ramachandran revisited
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PROCHECK: a program to check the stereochemical quality of protein structures
1 reference
stated in
Crossref
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Identifiers
DOI
10.1016/S0969-2126(98)00086-0
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4501953
OpenCitations bibliographic resource ID
4501953
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4501953
PubMed publication ID
9687366
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4501953
ResearchGate publication ID
13598575
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