Kyle G. Grant

Works (2)

Updated: July 5th, 2023 15:44

2014 article

Data‐driven modeling reconciles kinetics of ERK phosphorylation, localization, and activity states

Ahmed, S., Grant, K. G., Edwards, L. E., Rahman, A., Cirit, M., Goshe, M. B., & Haugh, J. M. (2014, January 1). Molecular Systems Biology, Vol. 10, pp. 718–718.

By: S. Ahmed n, K. Grant n, L. Edwards  n, A. Rahman n, M. Cirit n, M. Goshe n, J. Haugh n 

author keywords: growth factor receptors; mitogen-activated protein kinases; negative feedback; nucleocytoplasmic shuttling; mathematical model
MeSH headings : Active Transport, Cell Nucleus; Animals; Extracellular Signal-Regulated MAP Kinases / chemistry; Extracellular Signal-Regulated MAP Kinases / metabolism; Feedback, Physiological; Kinetics; Mice; Models, Theoretical; NIH 3T3 Cells; Phosphorylation; Protein Transport / genetics; Receptors, Growth Factor / genetics; Signal Transduction / genetics
topics (OpenAlex): Cellular Mechanics and Interactions; Melanoma and MAPK Pathways; Cell Image Analysis Techniques
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Sources: Web Of Science, ORCID, NC State University Libraries
Added: August 6, 2018

2012 article

Systemic Perturbation of the ERK Signaling Pathway by the Proteasome Inhibitor, MG132

Cirit, M., Grant, K. G., & Haugh, J. M. (2012, November 30). (L. Buday, Ed.). PLoS ONE, Vol. 7, p. e50975.

By: M. Cirit n, K. Grant n & J. Haugh n 

Ed(s): L. Buday

MeSH headings : Animals; Computer Simulation; Dual-Specificity Phosphatases / metabolism; Embryo, Mammalian / cytology; Enzyme Activation / drug effects; Fibroblast Growth Factors / pharmacology; Fibroblasts / cytology; Fibroblasts / drug effects; Fibroblasts / enzymology; Humans; Leupeptins / pharmacology; MAP Kinase Signaling System / drug effects; Mesoderm / cytology; Mice; Mitogen-Activated Protein Kinase Kinases / metabolism; NIH 3T3 Cells; Phosphorylation / drug effects; Platelet-Derived Growth Factor / pharmacology; Proteasome Inhibitors / pharmacology; Up-Regulation / drug effects
topics (OpenAlex): Ubiquitin and proteasome pathways; Protein Tyrosine Phosphatases; 14-3-3 protein interactions
TL;DR: It is shown that the effects of MG132 treatment on ERK signaling are more widespread, leading to a reduction in activation of the upstream kinase MEK, suggesting that MG132 systemically perturbs the intracellular phosphoproteome, impactingERK signaling by reducing phosphorylation status at multiple levels of the kinase cascade. (via Semantic Scholar)
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Sources: Web Of Science, ORCID, NC State University Libraries
Added: August 6, 2018

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