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

Carboxy-terminal phosphorylation of SIRT1 by protein kinase CK2.

Biochemical and biophysical research communications - 10 Apr 2009

Zschoernig Barbara, Mahlknecht Ulrich

Abstract excerpt

Previous analyses of the sirtuin family of histone deacetylases and its most prominent member SIRT1 have focused primarily on the identification of cellular targets exploring the underlying molecular mechanisms of its implicated function in the control of metabolic homeostasis, differentiation, apoptosis and cell survival. So far, little is known about the regulation of SIRT1 itself. In the study presented...

Read the complete abstract on PubMed

Topics

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

Share to Casein Kinase II
Share to Phosphorylation
Share to Protein Processing, Post-Translational

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Structure, Tertiary

Share to Sequence Deletion

Share to Serine

Share to Sirtuin 1

Share to Sirtuins

Source

Identifiers

PMID: 19236849
DOI: 10.1016/j.bbrc.2009.02.085

Genes

SIRT1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Carboxy-terminal phosphorylation of SIRT1 by protein kinase CK2.PMID 19236849Read ↗

Long-lived mammals contain more phosphorylation sites in the SIRT6 C-terminus that enhance PARP1 interaction and resistance to oxidative stressSemantic proximity Read ↗

CK2α/CSNK2A1 Phosphorylates SIRT6 and Is Involved in the Progression of Breast Carcinoma and Predicts Shorter Survival of Diagnosed Patients.Semantic proximity Read ↗

Mitotic regulation of SIRT2 by cyclin-dependent kinase 1-dependent phosphorylation.Semantic proximity Read ↗

Structure, regulation, and (patho-)physiological functions of the stress-induced protein kinase CK1 delta (CSNK1D)Semantic proximity Read ↗

JNK1 phosphorylates SIRT1 and promotes its enzymatic activity.Semantic proximity Read ↗

Identification of a Tissue-Restricted Isoform of SIRT1 Defines a Regulatory Domain that Encodes SpecificitySemantic proximity Read ↗

The Multifaceted Role of S6K1 in Cellular Regulation and Disease: Structural Insights, Isoform-Specific Functions, and Therapeutic PotentialSemantic proximity Read ↗

The Multifaceted Role of S6K1 in Cellular Regulation: Structural Insights, Isoform-Specific Functions, and Therapeutic PotentialSemantic proximity Read ↗

Identification of and Molecular Basis for SIRT6 Loss-of-Function Point Mutations in CancerSemantic proximity Read ↗

A c-Myc–SIRT1 feedback loop regulates cell growth and transformationSemantic proximity Read ↗

SIRT1 regulates metabolism and leukemogenic potential in CML stem cellsSemantic proximity Read ↗

Mutations in SIRT2 deacetylase which regulate enzymatic activity but not its interaction with HDAC6 and tubulin.Semantic proximity Read ↗

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