Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural and Kinetic Characterization of Human Deoxycytidine Kinase Variants Able To Phosphorylate 5-Substituted Deoxycytidine and Thymidine Analogues,

8 Jul 2010

Abstract excerpt

The physiological role of human deoxycytidine kinase (dCK) is to phosphorylate deoxynucleosides required for DNA synthesis, with the exception of thymidine. Previous structural analysis of dCK implicated steric factors, specifically the thymine methyl group at the 5-position, that prevent thymidine phosphorylation by dCK. This hypothesis is supported by the observation that mutations that enlarge the active site...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Biochemical and Molecular Research
Share to Cancer-related Molecular Pathways
Share to Chronic Lymphocytic Leukemia Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 20614893
DOI: 10.1021/bi100839e

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and Kinetic Characterization of Human Deoxycytidine Kinase Variants Able To Phosphorylate 5-Substituted Deoxycytidine and Thymidine Analogues,PMID 20614893Read ↗

Extending thymidine kinase activity to the catalytic repertoire of human deoxycytidine kinase.Semantic proximity Read ↗

Systematic exploration of active site mutations on human deoxycytidine kinase substrate specificity.Semantic proximity Read ↗

Post-translational phosphorylation of serine 74 of human deoxycytidine kinase favors the enzyme adopting the open conformation making it competent for nucleoside binding and release.Semantic proximity Read ↗

Identification of phosphorylation sites on human deoxycytidine kinase after overexpression in eucaryotic cells.Semantic proximity Read ↗

Four Deoxynucleoside Kinase Activities from Drosophila melanogaster Are Contained within a Single Monomeric Enzyme, a New Multifunctional Deoxynucleoside KinaseSemantic proximity Read ↗

Mimicking phosphorylation of Ser‐74 on human deoxycytidine kinase selectively increases catalytic activity for dC and dC analoguesSemantic proximity Read ↗

Dynamic behavior and ligand binding properties of the wild type dCK and its characterized gemcitabine-resistant variant: a bioinformatics and computational studySemantic proximity Read ↗

Identification of in vivo phosphorylation sites on human deoxycytidine kinase. Role of Ser-74 in the control of enzyme activity.Semantic proximity Read ↗

Structural basis for the changed substrate specificity of Drosophila melanogaster deoxyribonucleoside kinase mutant N64D.Semantic proximity Read ↗

Modifying Human Thymidylate Kinase to Potentiate Azidothymidine ActivationSemantic proximity Read ↗

Comparative active-site mutation study of human and Caenorhabditis elegans thymidine kinase 1.Semantic proximity Read ↗

Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificitySemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.