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

Functional regulation of TEL by p38-induced phosphorylation.

Biochemical and biophysical research communications - 22 Nov 2002

Arai Honoka, Maki Kazuhiro, Waga Kazuo, Sasaki Ko, Nakamura Yuichi, Imai Yoichi, Kurokawa Mineo, Hirai Hisamaru, Mitani Kinuko

Abstract excerpt

TEL is a nuclear phosphoprotein that belongs to a member of the ETS family transcription factors. TEL acts as a tumor suppressor and is essential for establishing hematopoiesis in neonatal bone marrow. Because TEL possesses multiple putative mitogen-activated protein (MAP) kinase phosphorylation sites, we here investigated functional regulation of TEL via stress signaling pathways. We showed that TEL becomes...

Read the complete abstract on PubMed

Topics

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

Share to COS Cells
Share to ETS Translocation Variant 6 Protein

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Luciferases

Share to Mitogen-Activated Protein Kinases

Share to p38 Mitogen-Activated Protein Kinases

Share to Precipitin Tests

Share to Proto-Oncogene Proteins c-ets

Share to Serine

Source

Identifiers

PMID: 12435397
DOI: 10.1016/s0006-291x(02)02588-3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional regulation of TEL by p38-induced phosphorylation.PMID 12435397Read ↗

Nuclear P38: Roles in Physiological and Pathological Processes and Regulation of Nuclear TranslocationSemantic proximity Read ↗

TEL/ETV6 induces apoptosis in 32D cells through p53-dependent pathways.Semantic proximity Read ↗

TEL-JAK2 constitutively activates the extracellular signal-regulated kinase (ERK), stress-activated protein/Jun kinase (SAPK/JNK), and p38 signaling pathways.Semantic proximity Read ↗

Type II Keratins Are Phosphorylated on a Unique Motif during Stress and Mitosis in Tissues and Cultured CellsSemantic proximity Read ↗

Mechanisms regulating the nuclear translocation of p38 MAP kinase.Semantic proximity Read ↗

p38alpha is active in vitro and in vivo when monophosphorylated at threonine 180.Semantic proximity Read ↗

MafA transcription factor is phosphorylated by p38 MAP kinase.Semantic proximity Read ↗

Stimulation of hTAFII68 (NTD)-mediated transactivation by v-Src.Semantic proximity Read ↗

Identification of a major phosphopeptide in human tristetraprolin by phosphopeptide mapping and mass spectrometry.Semantic proximity Read ↗

Identification of in vivo phosphorylation sites of SET, a nuclear phosphoprotein encoded by the translocation breakpoint in acute undifferentiated leukemiaSemantic proximity Read ↗

Regulation of TCF ETS-domain transcription factors by helix-loop-helix motifs.Semantic proximity Read ↗

cAMP/PKA signalling reinforces the LATS-YAP pathway to fully suppress YAP in response to actin cytoskeletal changes.Semantic proximity Read ↗

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