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

Perturbation of ATP-induced tetramerization of human cytosolic thymidine kinase by substitution of serine-13 with aspartic acid at the mitotic phosphorylation site.

Biochemical and biophysical research communications - 16 Jan 2004

Li Chia-Lung, Lu Ching-Yi, Ke Po-Yuan, Chang Zee-Fen

Abstract excerpt

Human cytosolic thymidine kinase (TK1) is tightly regulated in the cell cycle by multiple mechanisms. Our laboratory has previously shown that in mitotic-arrested cells human TK1 is phosphorylated at serine-13, accompanied by a decrease in catalytic efficiency. In this study we investigated wheth...

Read the complete abstract on PubMed

Topics

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

Share to Aspartic Acid
Share to Chromatography
Share to Chromatography, Gel

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytosol

Share to G2 Phase

Share to Protein Structure, Quaternary

Share to Thymidine

Share to Thymidine Kinase

Source

Identifiers

PMID: 14697231
DOI: 10.1016/j.bbrc.2003.11.147

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-14697231-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Perturbation of ATP-induced tetramerization of human cytosolic thymidine kinase by substitution of serine-13 with aspartic acid at the mitotic phosphorylation site.PMID 14697231Read ↗

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

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

Exploring a non-ATP pocket for potential allosteric modulation of PI3Kα.Semantic proximity Read ↗

Reversible ATP-dependent transition between two forms of human cytosolic thymidine kinase with different enzymatic propertiesSemantic proximity Read ↗

Effect of valine 106 on structure-function relation of cytosolic human thymidine kinase. Kinetic properties and oligomerization pattern of nine substitution mutants of V106.Semantic proximity Read ↗

The kinetic mechanism of Human Thymidine Phosphorylase – a molecular target for cancer drug developmentSemantic proximity Read ↗

Novel phosphorylation sites in the S. cerevisiae Cdc13 protein reveal new targets for telomere length regulation.Semantic proximity Read ↗

Regulation of mammalian pyruvate dehydrogenase complex by phosphorylation: complexity of multiple phosphorylation sites and kinases.Semantic proximity Read ↗

Mitotic Regulation of Ribosomal S6 Kinase 1 Involves Ser/Thr, Pro Phosphorylation of Consensus and Non-consensus Sites by Cdc2Semantic proximity Read ↗

Phosphorylation of cytosolic hPGK1 affects protein stability and ligand binding: implications for its subcellular targeting in cancer.Semantic proximity Read ↗

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