Protein Kinase C: in Vitro Studies - Gary Nelsestuen

Abstract

Funding Agency

Agency: National Institute of Health (NIH)
Institute: National Institute of General Medical Sciences (NIGMS)
Type: Research Project (R01)
Project #: 3R01GM038819-06S1
Application #: 3295530
Study Section: Physiological Chemistry Study Section (PC)

Project Start: 1992-07-01
Project End: 1996-06-30
Budget Start: 1992-07-01
Budget End: 1993-06-30
Support Year: 6
Fiscal Year: 1993
Total Cost
Indirect Cost

Institution

Name: University of Minnesota Twin Cities
Department
Type: Schools of Arts and Sciences
DUNS #: 168559177

City: Minneapolis
State: MN
Country: United States
Zip Code: 55455

Related projects


NIH 1995 R01 GM	Protein Kinase C - IN Vitro Studies Nelsestuen, Gary L. / University of Minnesota Twin Cities
NIH 1994 R01 GM	Protein Kinase C - IN Vitro Studies Nelsestuen, Gary L. / University of Minnesota Twin Cities
NIH 1993 R01 GM	Protein Kinase C: in Vitro Studies Nelsestuen, Gary L. / University of Minnesota Twin Cities
NIH 1993 R01 GM	Protein Kinase C: in Vitro Studies Nelsestuen, Gary L. / University of Minnesota Twin Cities
NIH 1992 R01 GM	Protein Kinase C - IN Vitro Studies Nelsestuen, Gary L. / University of Minnesota Twin Cities
NIH 1991 R01 GM	Protein Kinase C - IN Vitro Studies Nelsestuen, Gary L. / University of Minnesota Twin Cities
NIH 1990 R01 GM	Protein Kinase C - IN Vitro Studies Nelsestuen, Gary L. / University of Minnesota Twin Cities
NIH 1989 R01 GM	Protein Kinase C - IN Vitro Studies Nelsestuen, Gary / University of Minnesota Twin Cities
NIH 1988 R01 GM	Protein Kinase C - IN Vitro Studies Nelsestuen, Gary / University of Minnesota Twin Cities
NIH 1987 R01 GM	Protein Kinase C - IN Vitro Studies Nelsestuen, Gary / University of Minnesota Twin Cities

Publications

Shen, L; Shah, A M; Dahlback, B et al. (1997) Enhancing the activity of protein C by mutagenesis to improve the membrane-binding site: studies related to proline-10. Biochemistry 36:16025-31

Nelsestuen, G L; Martinez, M B (1997) Steady state enzyme velocities that are independent of [enzyme]: an important behavior in many membrane and particle-bound states. Biochemistry 36:9081-6

Harvey, S B; Nelsestuen, G L (1995) Reaction of nitric oxide and its derivatives with sulfites: a possible role in sulfite toxicity. Biochim Biophys Acta 1267:41-4

Lu, Y; Bazzi, M D; Nelsestuen, G L (1995) Kinetics of annexin VI, calcium, and phospholipid association and dissociation. Biochemistry 34:10777-85

Evans Jr, T C; Nelsestuen, G L (1994) Calcium and membrane-binding properties of monomeric and multimeric annexin II. Biochemistry 33:13231-8

Plager, D A; Nelsestuen, G L (1994) Direct enthalpy measurements of the calcium-dependent interaction of annexins V and VI with phospholipid vesicles. Biochemistry 33:13239-49

Bazzi, M D; Nelsestuen, G L (1992) Interaction of annexin VI with membranes: highly restricted dissipation of clustered phospholipids in membranes containing phosphatidylethanolamine. Biochemistry 31:10406-13

Bazzi, M D; Nelsestuen, G L (1992) Autophosphorylation of protein kinase C may require a high order of protein-phospholipid aggregates. J Biol Chem 267:22891-6

Plager, D A; Nelsestuen, G L (1992) Dissociation of peripheral protein-membrane complexes by high pressure. Protein Sci 1:530-9

Xu, C J; Nelsestuen, G L (1992) Association of alpha-phosphatidylinositol-specific phospholipase C with phospholipid vesicles. Biochim Biophys Acta 1120:49-58

Showing the most recent 10 out of 21 publications

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