Biochemical and functional analysis of highly phosphorylated forms of c-Jun protein.

doi:10.1016/s0014-5793(98)00618-8

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Article

Biochemical and functional analysis of highly phosphorylated forms of c-Jun protein.

FEBS letters - 16 Jun 1998

Ui M, Sonobe M H, Ito T, Murakami M, Okazaki S, Takada M, Sato T, Iba H

Abstract excerpt

We report here that, upon UV irradiation or growth stimulation, endogenous c-Jun (40 kDa) in chicken embryo fibroblasts (CEF) is converted into several forms with apparently higher molecular weights in SDS-polyacrylamide gel electrophoresis (45, 44, 42 kDa). Two of the bands (44 and 45 kDa) were...

Topics

Amino Acid Sequence
Animals
Blotting, Western
Calcium-Calmodulin-Dependent Protein Kinases
Cell Transformation, Neoplastic
Chick Embryo
Fibroblasts
JNK Mitogen-Activated Protein Kinases
Mitogen-Activated Protein Kinases
Molecular Sequence Data
Mutation
Phosphorylation
Proto-Oncogene Proteins c-jun
Serine
Species Specificity
Ultraviolet Rays

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Identifiers

PMID: 9662434
DOI: 10.1016/s0014-5793(98)00618-8

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9662434-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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