A new look at the molecular mechanism of thymidylate synthase and its interaction with nucleotide analogues

T. I. Kalman; D. A. Matthews

doi:10.1080/15257779908041576

A new look at the molecular mechanism of thymidylate synthase and its interaction with nucleotide analogues

T. I. Kalman
, D. A. Matthews

Chemistry

Pfizer

Research output: Contribution to journal › Article › peer-review

Abstract

The increasing availability of the crystal structures of a variety of complexes of thymidylate synthase (TS) and its mutants with nucleotide and folate analogues, has greatly advanced our understanding of the mechanism of catalysis, and the detailed interaction of the enzyme with inhibitors.

Original language	English
Pages (from-to)	843-844
Number of pages	2
Journal	Nucleosides and Nucleotides
Volume	18
Issue number	4-5
DOIs	https://doi.org/10.1080/15257779908041576
State	Published - 1999

Access to Document

10.1080/15257779908041576

Cite this

@article{df8fb254f7d74c06aa7c4fc473273234,

title = "A new look at the molecular mechanism of thymidylate synthase and its interaction with nucleotide analogues",

abstract = "The increasing availability of the crystal structures of a variety of complexes of thymidylate synthase (TS) and its mutants with nucleotide and folate analogues, has greatly advanced our understanding of the mechanism of catalysis, and the detailed interaction of the enzyme with inhibitors.",

author = "Kalman, \{T. I.\} and Matthews, \{D. A.\}",

year = "1999",

doi = "10.1080/15257779908041576",

language = "English",

volume = "18",

pages = "843--844",

journal = "Nucleosides and Nucleotides",

issn = "0732-8311",

publisher = "Marcel Dekker Inc.",

number = "4-5",

}

TY - JOUR

T1 - A new look at the molecular mechanism of thymidylate synthase and its interaction with nucleotide analogues

AU - Kalman, T. I.

AU - Matthews, D. A.

PY - 1999

Y1 - 1999

N2 - The increasing availability of the crystal structures of a variety of complexes of thymidylate synthase (TS) and its mutants with nucleotide and folate analogues, has greatly advanced our understanding of the mechanism of catalysis, and the detailed interaction of the enzyme with inhibitors.

AB - The increasing availability of the crystal structures of a variety of complexes of thymidylate synthase (TS) and its mutants with nucleotide and folate analogues, has greatly advanced our understanding of the mechanism of catalysis, and the detailed interaction of the enzyme with inhibitors.

UR - https://www.scopus.com/pages/publications/0033062975

U2 - 10.1080/15257779908041576

DO - 10.1080/15257779908041576

M3 - Article

AN - SCOPUS:0033062975

SN - 0732-8311

VL - 18

SP - 843

EP - 844

JO - Nucleosides and Nucleotides

JF - Nucleosides and Nucleotides

IS - 4-5

ER -

A new look at the molecular mechanism of thymidylate synthase and its interaction with nucleotide analogues

Abstract

Access to Document

Other files and links

Fingerprint

Cite this