Abstract

This project is comprised of research into the structure and functioning of ion transport systems. Major current studies are 1) research into the basis of the kinetic heterogeneity exhibited by the Na,K-ATPase as manifest in several different rapid-quenching experiments, 2) research into the basis of the structural heterogeneity manifest in the electrophoretic mobility of the catalytic subunit of the Na,K-ATPase from Electrophorus electric organ, and 3) development and characterization of antibodies to synthetic peptides corresponding to selected portions of transport ATPase primary structure.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Neurological Disorders and Stroke (NINDS)
Type
Intramural Research (Z01)
Project #
1Z01NS000813-25
Application #
3968877
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
25
Fiscal Year
1986
Total Cost
Indirect Cost

  Institution

Name
National Institute of Neurological Disorders and Stroke
Department
Type
DUNS #
City
State
Country
United States
Zip Code

  Publications

Rudrabhatla, Parvathi; Zheng, Ya-Li; Amin, Niranjana D et al. (2008) Pin1-dependent prolyl isomerization modulates the stress-induced phosphorylation of high molecular weight neurofilament protein. J Biol Chem 283:26737-47
Amin, Niranjana D; Zheng, Ya-Li; Kesavapany, Sashi et al. (2008) Cyclin-dependent kinase 5 phosphorylation of human septin SEPT5 (hCDCrel-1) modulates exocytosis. J Neurosci 28:3631-43
Kesavapany, Sashi; Patel, Vyomesh; Zheng, Ya-Li et al. (2007) Inhibition of Pin1 reduces glutamate-induced perikaryal accumulation of phosphorylated neurofilament-H in neurons. Mol Biol Cell 18:3645-55
Mahaney, James E; Albers, R Wayne; Waggoner, Jason R et al. (2005) Intermolecular conformational coupling and free energy exchange enhance the catalytic efficiency of cardiac muscle SERCA2a following the relief of phospholamban inhibition. Biochemistry 44:7713-24
Mahaney, James E; Albers, R Wayne; Kutchai, Howard et al. (2003) Phospholamban inhibits Ca2+ pump oligomerization and intersubunit free energy exchange leading to activation of cardiac muscle SERCA2a. Ann N Y Acad Sci 986:338-40
Amin, Niranjana D; Albers, Wayne; Pant, Harish C (2002) Cyclin-dependent kinase 5 (cdk5) activation requires interaction with three domains of p35. J Neurosci Res 67:354-62
Zheng, Ya-Li; Li, Bing-Sheng; Amin, Niranjana D et al. (2002) A peptide derived from cyclin-dependent kinase activator (p35) specifically inhibits Cdk5 activity and phosphorylation of tau protein in transfected cells. Eur J Biochem 269:4427-34