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Lawrence Stern, Ph.D.
Academic Role: Professor
Faculty Appointment(s) In:
Pathology
Joint Faculty In:
Biochemistry and Molecular Pharmacology
Other Affiliation(s):
Center for AIDS Research
Program in Immunology and Virology
Representative Publications
T.O. Cameron, B.D. Walker, L.J. Stern, and G.B.Cohen.
Towards TCR proteomics: Examination of a highly diverse repertoire of CD4+ T cells specific for an influenza peptide bound to HLA-DR1.
Immunogenetics (2002) in press.
J. Stone, J.R. Cochran, and L.J. Stern.
T cell activation by soluble MHC oligomers can be described by a two-parameter binding model.
Biophys. J. (2001) 81, 2547-255.
J.A. Zarutskie, R.Busch, Z. Zavala-Ruiz, Mia Rushe, E.D. Mellins, L.J. Stern.
The kinetic basis of peptide exchange catalysis by HLA-DM.
Proc. Natl. Acad. Sci (2001) 98, 12450-12455.
J.R. Cochran, T.O. Cameron, J. Stone, J. D. Lubetsky, and, L.J. Stern.
Receptor proximity, not intermolecular orientation, is critical for triggering T-cell activation.
J. Biol. Chem. (2001) 276, 28068-28074.
R. Riese, S.L. Belyanskaya, F.R. Fischer, B. Cipriani, C. Brosnan, P. Riccardi-Castognoli, L.J. Stern, J.L. Strominger, L. Santambrogio.
Developmental plasticity of central nervous system microglia.
Proc. Natl. Acad. Sci. (2001) 98, 6295-6300.
J.R. Cochran, T.O. Cameron, D. Aivazian, L.J. Stern.
Receptor clustering and transmembrane signaling in CD4+ T cells (review).
Trends in Biochem. Sci. (2001) 26, 304-310.
T.O. Cameron, J.R. Cochran, Y. Bader, R.-P. Sekaly, L.J. Stern.
Detection of antigen-specific CD4+ T cells by HLA-DR1 oligomers is dependent on the T cell activation state.
J. Immunol. (2001) 166, 741-745.
D. Aivazian and L.J. Stern.
T cell receptor zeta phosphorylation is regulated by a lipid-dependent folding transition.
Nature Struct. Biol. (2000) 7, 1023-1026.
J.R. Cochran, T.O. Cameron, L.J. Stern
The relationship between MHC-peptide binding and T-cell activation probed using chemically defined MHC class II oligomers.
Immunity (2000) 12, 241-250.
R.V. Joshi, J.A. Zarutskie, L.J. Stern
A three-step kinetic mechanism for peptide binding to class II MHC proteins
Biochemistry (2000) 39, 3752-3761.
A.K. Sato, J.A. Zarutskie, M.M. Rushe, A. Lomakin, S.K.Natarajan, S. Sadegh-Nasseri, G.B. Benedek, L.J. Stern.
Determinants of the peptide-induced conformational change in the class II MHC protein HLA-DR1
J. Biol Chem. (2000), 275, 2165-2173.
L. Santambrogio, A.K. Sato, G. Carven, S.L. Belyanskaya, J. Strominger, L.J. Stern.
Extracellular antigen processing and presentation by immature dendritic cells.
Proc. Natl. Acad. Sci. (1999), 96, 15050-15055.
L. Santambrogio, A.K. Sato, F.K. Fischer, M. Dorf, L.J. Stern.
Abundant empty class II MHC molecules on the surface of immature dendritic cells.
Proc. Natl. Acad. Sci. (1999), 96, 15050-15055.
J.A. Zarutskie, A.K. Sato, M. Rushe, I.C. Chan, A. Lomakin, G.B. Benedek, L.J. Stern.
A conformational change in the human class II MHC protein HLA-DR1 induced by
peptide binding.
Biochemistry (1999), 38, 5878-5887.
A.B. Sigalov and L.J. Stern.
Enzymatic repair of oxidative damage to human apolipoprotein A-I.
FEBS Lett. (1998), 433, 196-200.
V. Murthy and L.J. Stern.
The class II MHC protein HLA-DR1 in complex with an endogenous peptide: Implications for the structural basis of the specificity of peptide binding.
Structure (1997), 5, 1385-1396.
H. Kropshofer, A.B. Vogt, L.J. Stern, G.J. Hammerling.
Self-release of CLIP in peptide loading of HLA-DR1 molecules.
Science (1995) 270, 1357-1359.
P.J. Booth, S.L. Flitsch, L.J. Stern, D.A. Greenhalgh, P.S. Kim, H.G. Khorana.
Intermediates in the folding of the membrane protein bacteriorhodopsin.
Nature Structural Biology (1995), 2, 139-143.
L.J. Stern and D.C. Wiley.
Antigenic peptide binding by class I and class II histocompatibility proteins (review).
Structure (1994), 2, 245-251.
A.H. Seth, L.J. Stern, T.H.M. Ottonhoff, I. Engel, M.J. Owen, J.R. Lamb, R.D. Klausner, D.C. Wiley.
Binary and tertiary complexes among soluble T-cell receptor, soluble class II MHC,
and superantigen.
Nature (1994), 369, 324-327.
S. Sadegh-Nasseri, L.J. Stern, D.C. Wiley, R.N. Germain.
MHC class II function preserved by low-affinity peptide interactions preceding stable binding.
Nature (1994), 370, 647-670.
L.J. Stern, J.H. Brown, T.S. Jardetzky, J.C. Gorga, R.G. Urban, J.L. Strominger, D.C. Wiley.
Crystal structure of the human class II MHC protein HLA-DR1 complexed with an antigenic peptide from influenza virus.
Nature (1994), 368, 215-221.
L.J. Stern and D.C. Wiley.
The human class II MHC protein HLA-DR1 assembles as empty aß heterodimers in the absence of antigenic peptide.
Cell (1992), 68, 465-477.
R.M. Chicz, R.G. Urban, W.S. Lane, J.G. Gorga, L.J. Stern, D.D.A. Vignali, J.L. Strominger.
Predominant naturally processed peptides bound to HLA-DR1 are derived from MHC-related molecules and are heterogenous in size.
Nature (1992), 358, 764-768.
Office: S2-127
Phone: 508-856-1831
E-mail: Lawrence.Stern@umassmed.edu
Keywords:
Immunology,
Structural Biology,
Biochemistry
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