Compulsory order of substrate binding to herpes simplex virus type 1 thymidine kinase. A calorimetric study. (Q45743431)

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5 November 2019

title

Compulsory order of substrate binding to herpes simplex virus type 1 thymidine kinase. A calorimetric study (English)

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Herpes simplex virus type 1

5 November 2019

main subject

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4

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5 November 2019

author name string

Perozzo R

1

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5 November 2019

Jelesarov I

2

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5 November 2019

Bosshard HR

3

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5 November 2019

Scapozza L

5

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5 November 2019

language of work or name

English

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publication date

1 May 2000

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Journal of Biological Chemistry

5 November 2019

number of pages

7

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based on heuristic

inferred from page(s)

published in

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5 November 2019

volume

275

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issue

21

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page(s)

16139-16145

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The three-dimensional structure of thymidine kinase from herpes simplex virus type 1.

5 November 2019

cites work

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The structures of thymidine kinase from herpes simplex virus type 1 in complex with substrates and a substrate analogue

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Exploring the active site of herpes simplex virus type-1 thymidine kinase by X-ray crystallography of complexes with aciclovir and other ligands

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Crystal structures of the thymidine kinase from herpes simplex virus type-1 in complex with deoxythymidine and ganciclovir

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Structure to 1.9 A resolution of a complex with herpes simplex virus type-1 thymidine kinase of a novel, non-substrate inhibitor: X-ray crystallographic comparison with binding of aciclovir

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Anti-herpesvirus activity of the acyclic nucleoside 9-(1,3-dihydroxy-2-propoxymethyl)guanine

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Characterization of Abnormal Thymidine Kinases Induced by Drug-resistant Strains of Herpes Simplex Virus Type 1

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L-thymidine is phosphorylated by herpes simplex virus type 1 thymidine kinase and inhibits viral growth.

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Refined structure of porcine cytosolic adenylate kinase at 2.1 A resolution

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The structure of bovine mitochondrial adenylate kinase: comparison with isoenzymes in other compartments

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The structure of uridylate kinase with its substrates, showing the transition state geometry.

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Structure of thymidylate kinase reveals the cause behind the limiting step in AZT activation

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Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases

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Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding

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A fast method for obtaining highly pure recombinant herpes simplex virus type 1 thymidine kinase

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Rapid measurement of binding constants and heats of binding using a new titration calorimeter

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Substrate diversity of herpes simplex virus thymidine kinase. Impact Of the kinematics of the enzyme.

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21 January 2018

Identifiers

DOI

10.1074/JBC.M000509200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10747922%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

1 reference