Oncoprotein protein kinase
Abstract
An isolated polypeptide (JNK) characterized by having a molecular weight of 46 kD as determined by reducing SDS-PAGE is disclosed. The polypeptide has serine and threonine kinase activity, phosphorylating the c-Jun N-terminal activation domain and polynucleotide sequences. The method of detection of JNK is also provided. JNK phosphorylates c-Jun N-terminal activation domain which affects gene expression from AP-1 sites. 44 figs.
- Inventors:
- Issue Date:
- Research Org.:
- Univ. of California (United States)
- OSTI Identifier:
- 441865
- Patent Number(s):
- 5605808
- Application Number:
- PAN: 8-444,393; CNN: Grant CA-50528;Grant CA-58396
- Assignee:
- Univ. of California, Oakland, CA (United States)
- DOE Contract Number:
- FG03-86ER60429
- Resource Type:
- Patent
- Resource Relation:
- Other Information: PBD: 25 Feb 1997
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 55 BIOLOGY AND MEDICINE, BASIC STUDIES; POLYPEPTIDES; PHOSPHOTRANSFERASES; ENZYME ACTIVITY; AMINO ACID SEQUENCE; PHOSPHORYLATION; GENE REGULATION; CHEMICAL COMPOSITION
Citation Formats
Karin, M, Hibi, M, and Lin, A. Oncoprotein protein kinase. United States: N. p., 1997.
Web.
Karin, M, Hibi, M, & Lin, A. Oncoprotein protein kinase. United States.
Karin, M, Hibi, M, and Lin, A. Tue .
"Oncoprotein protein kinase". United States.
@article{osti_441865,
title = {Oncoprotein protein kinase},
author = {Karin, M and Hibi, M and Lin, A},
abstractNote = {An isolated polypeptide (JNK) characterized by having a molecular weight of 46 kD as determined by reducing SDS-PAGE is disclosed. The polypeptide has serine and threonine kinase activity, phosphorylating the c-Jun N-terminal activation domain and polynucleotide sequences. The method of detection of JNK is also provided. JNK phosphorylates c-Jun N-terminal activation domain which affects gene expression from AP-1 sites. 44 figs.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {1997},
month = {2}
}
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