Identification of residues involved in the substrate specificity of human and murine dCK (Q28620109)

3 February 2017

title

Identification of residues involved in the substrate specificity of human and murine dCK (English)

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3 February 2017

Elena V. Usova

1

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3 February 2017

Staffan Eriksson

series ordinal

2

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3 February 2017

language of work or name

English

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publication date

1 December 2002

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3 February 2017

published in

Biochemical Pharmacology

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3 February 2017

volume

64

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3 February 2017

issue

11

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3 February 2017

page(s)

1559–1567

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Mammalian deoxyribonucleoside kinases

3 February 2017

cites work

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Identification of purine deoxyribonucleoside kinases from human leukemia cells: substrate activation by purine and pyrimidine deoxyribonucleosides

7 January 2021

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Comparison of the substrate specificities of human thymidine kinase 1 and 2 and deoxycytidine kinase toward antiviral and cytostatic nucleoside analogs

7 January 2021

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Properties and levels of deoxynucleoside kinases in normal and tumor cells; implications for chemotherapy

7 January 2021

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Deoxynucleoside phosphorylating enzymes in monkey and human tissues show great similarities, while mouse deoxycytidine kinase has a different substrate specificity

7 January 2021

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The in vitro and in vivo anti-retrovirus activity, and intracellular metabolism of 3'-azido-2',3'-dideoxythymidine and 2',3'-dideoxycytidine are highly dependent on the cell species

7 January 2021

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Cloning and expression of human deoxycytidine kinase cDNA

7 January 2021

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Differences in kinetic properties of pure recombinant human and mouse deoxycytidine kinase.

7 January 2021

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Site-directed mutagenesis by overlap extension using the polymerase chain reaction

7 January 2021

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The effects of high salt concentrations on the regulation of the substrate specificity of human recombinant deoxycytidine kinase

7 January 2021

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Structural basis for substrate specificities of cellular deoxyribonucleoside kinases

7 January 2021

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10.1016/S0006-2952(02)01389-8

7 January 2021

Identifiers

DOI

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