The p38β Mitogen-activated Protein Kinase Possesses an Intrinsic Autophosphorylation Activity, Generated by a Short Region Composed of the α-G Helix and MAPK Insert
Journal Article
Overview
publication date
- August 22, 2014
has subject area
- Biochemical Phenomena - Amino Acid Sequence
- Biochemical Phenomena - Biocatalysis
- Biochemical Phenomena - Phosphorylation
- Biochemical Phenomena - Sequence Homology, Amino Acid
- Catalysis - Biocatalysis
- Cell Line, Transformed - HEK293 Cells
- Enzymes - Isoenzymes
- Epithelial Cells - HEK293 Cells
- Genetic Phenomena - Sequence Homology, Amino Acid
- Humans
- Metabolism - Biocatalysis
- Metabolism - Phosphorylation
- Molecular Sequence Data
- Molecular Sequence Data - Amino Acid Sequence
- Organic Chemistry Phenomena - Phosphorylation
- Peptides - Mitogen-Activated Protein Kinases
- Peptides - p38 Mitogen-Activated Protein Kinases
- Protein Isoforms - Isoenzymes
- Protein-Serine-Threonine Kinases - Mitogen-Activated Protein Kinases
- Protein-Serine-Threonine Kinases - p38 Mitogen-Activated Protein Kinases
- Proteins - Mitogen-Activated Protein Kinases
- Proteins - p38 Mitogen-Activated Protein Kinases
has restriction
- green
Date in CU Experts
- October 9, 2014 10:40 AM
Full Author List
- Beenstock J; Ben-Yehuda S; Melamed D; Admon A; Livnah O; Ahn NG; Engelberg D
author count
- 7
citation count
- 35
published in
- Journal of Biological Chemistry Journal
Other Profiles
Electronic International Standard Serial Number (EISSN)
- 1083-351X
Digital Object Identifier (DOI)
Additional Document Info
start page
- 23546
end page
- 23556
volume
- 289
issue
- 34