J
Jack L. Strominger
Researcher at Harvard University
Publications - 826
Citations - 92603
Jack L. Strominger is an academic researcher from Harvard University. The author has contributed to research in topics: Antigen & Major histocompatibility complex. The author has an hindex of 145, co-authored 826 publications receiving 89885 citations. Previous affiliations of Jack L. Strominger include Max Planck Society & Howard Hughes Medical Institute.
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Journal ArticleDOI
Structure of the human class I histocompatibility antigen, HLA-A2.
Pamela J. Bjorkman,Mark A. Saper,Boudjéma Samraoui,W. S. Bennett,W. S. Bennett,Jack L. Strominger,Don C. Wiley +6 more
TL;DR: The class I histocompatibility antigen from human cell membranes has two structural motifs: the membrane-proximal end of the glycoprotein contains two domains with immunoglobulin-folds that are paired in a novel manner and the region distal from the membrane is a platform of eight antiparallel β-strands topped by α-helices.
Journal ArticleDOI
A modified colorimetric method for the estimation of n-acetylamino sugars
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Nomenclature for factors of the HLA system, 2010.
Steven G.E. Marsh,E. D. Albert,Walter F. Bodmer,Ronald E. Bontrop,Bo Dupont,Henry A. Erlich,Marcelo Fernandez-Vina,Daniel E. Geraghty,Rhonda Holdsworth,Carolyn Katovich Hurley,M. Lau,Keun-Seok Lee,Bernard Mach,Martin Maiers,Wolfgang R. Mayr,Carlheinz Müller,Peter Parham,Effie W. Petersdorf,Takehiko Sasazuki,Jack L. Strominger,A. Svejgaard,Paul I. Terasaki,Jean-Marie Tiercy,John Trowsdale +23 more
TL;DR: This report documents the additions and revisions to the nomenclature of HLA specificities following the principles established in previous reports.
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The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens
Pamela J. Bjorkman,Pamela J. Bjorkman,Pamela J. Bjorkman,Mark A. Saper,Boudjéma Samraoui,W. S. Bennett,W. S. Bennett,Jack L. Strominger,Don C. Wiley +8 more
TL;DR: Most of the polymorphic amino acids of the class I histocompatibility antigen, HLA-A2, are clustered on top of the molecule in a large groove identified as the recognition site for processed foreign antigens.
Journal ArticleDOI
Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1
Jerry H. Brown,Theodore S. Jardetzky,Joan C. Gorga,Joan C. Gorga,Lawrence J. Stern,Lawrence J. Stern,Robert G. Urban,Jack L. Strominger,Don C. Wiley,Don C. Wiley +9 more
TL;DR: A dimer of the class II αβ heterodimers is seen in the crystal forms of HLA-DR1, suggesting class II HLA dimerization as a mechanism for initiating the cytoplasmic signalling events in T-cell activation.