Position available

lsklar@medusa.unm.edu
Mon, 15 Jan 1996 07:17:04 -0700 (MST)

Research Associate Position

To investigate the relationship of formyl peptide ligand-receptor-G
protein dynamics to cell activation and cell physiology. We are interested
in the implications of receptor-G protein precoupling for signal
transduction.

PhD, MD with research experience or related degree and related
experience required. Desirable qualifications include experience in
signal transduction, fluorescence, and a record of publications.

For best consideration, apply by March 1,1996. Position will remain
open until filled.

Opportunities include: 1) real-time subsecond analysis of ligand-receptor
interactions with stopped flow flow cytometry and spectroscopy; 2)
analysis of a family of fluorescent ligands with variable kinetic
characteristics; 3) analysis of mutant receptors; 4) biochemical analysis
of transduction assemblies including phosphorylation; 5) computer
modeling; 6) access to the Los Alamos National Flow Cytometry Resource

Contact or send CV to: Larry A. Sklar, PhD
Professor of Pathology, UNM Health Sciences Center
Co-Director National Flow Cytometry Resource, Los Alamos Nat. Lab

Phone 505-277-7249; Fax 505-255-7790
Address: Cancer Center Rm 325
900 Camino de Salud
University of New Mexico Health Sciences Center
Albuquerque, NM 87131

Representative recent publications

1. Neubig, R. and Sklar, L.A., Subsecond modulation of formyl peptide
linked guanine nucleotide-binding proteins by guanosine 5'-0-(3-thio)
triphosphate in permeabilized neutrophils, Mol. Pharm, 43:734-740, 1993.

2. Posner, R.G., Fay, S.P., Domalewski, M. and Sklar, L.A., Continuous
spectrofluorometric analysis of formyl peptide receptor ternary complex
interactions. Mol. Pharm., 45:65-73, 1994.

3. Nolan, J.P., Posner, R.G., Martin, J.C., Habbersett, R., and Sklar,
L.A. A Rapid Mix Flow Cytometer With Subsecond Kinetic Resolution,
Cytometry, 21:223-229,1995.

4. Domalewski, M.D., Guyer, D.A., Freer, R.J., Muthukumaraswamy, N. and
Sklar,L.A. Fixation traps receptors in high and low affinity forms that
can be regulated by GTP[S] in the absence of ligand, In Press, J. Rec. Res.
1996


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