Work

KSR1 is a functional protein kinase capable of serine autophosphorylation and direct phosphorylation of MEK1

Year: 2010

Type: article

Source: Experimental Cell Research

DOI: 10.1016/j.yexcr.2010.11.018

Authors: Jeremy A. Goettel, Dongchun Liang, Valda C. Hilliard, Karen L. Edelblum, Matthew R. Broadus, Kathleen L. Gould, Steven K. Hanks, D. Brent Polk

Institutions: Vanderbilt University, Vanderbilt University Medical Center, Howard Hughes Medical Institute

Language: English

Topic: Protein Kinase Regulation and GTPase Signaling

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green

Funders: Howard Hughes Medical Institute, National Institutes of Health, National Cancer Institute, National Institute of General Medical Sciences, National Institute of Diabetes and Digestive and Kidney Diseases

Awards: Cytokine regulation of intestinal epithelial restitution, G252522409, Mechanisms of KSR regulation in intestinal cell survival, BRCA1 and estrogen signaling during tumorigenesis, G6843006214, Regulation and function of the Clp 1p protein phosphatase, Biochemical and Chemical Training for Cancer Research

OpenAlex ID: W2011948787

FWCI: 1.172

Cites: 71

Cited by: 23

Related to: 10