S
Stephen J. Stahl
Researcher at National Institutes of Health
Publications - 95
Citations - 8506
Stephen J. Stahl is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Protein structure & Capsid. The author has an hindex of 51, co-authored 95 publications receiving 8241 citations. Previous affiliations of Stephen J. Stahl include University of Central Oklahoma.
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Journal ArticleDOI
Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
TL;DR: Density maps calculated from cryo-electron micrographs show that the assembly domain dimer is T-shaped: its stem constitutes the dimer interface and the tips of its arms make the polymerization contacts, and major elements of secondary structure are revealed.
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NMR structure of a specific DNA complex of Zn-containing DNA binding domain of GATA-1.
James G. Omichinski,G M Clore,O Schaad,Gary Felsenfeld,Cecelia D. Trainor,Ettore Appella,Stephen J. Stahl,Angela M. Gronenborn +7 more
TL;DR: The three-dimensional solution structure of a complex between the DNA binding domain of the chicken erythroid transcription factor GATA-1 and its cognate DNA site has been determined with multidimensional heteronuclear magnetic resonance spectroscopy.
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Three‐dimensional solution structure of the 44 kDa ectodomain of SIV gp41
Michael Caffrey,Mengli Cai,Joshua Kaufman,Stephen J. Stahl,Paul T. Wingfield,David G. Covell,Angela M. Gronenborn,G. Marius Clore +7 more
TL;DR: The solution structure of the SIV e‐gp41 ectodomain provides insight into the binding site of gp120 and the mechanism of cell fusion and the present structure represents one of the largest protein structures determined by NMR to date.
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The CD4 Determinant for Downregulation by HIV-1 Nef Directly Binds to Nef. Mapping of the Nef Binding Surface by NMR†
TL;DR: Using heteronuclear NMR spectroscopy, it is demonstrated that a 13-residue peptide from the cytoplasmic tail of CD4 binds to Nef protein, indicating that the binding ofCD4 and Hck SH3 to Naf are two compatible and slightly cooperative events.
Journal ArticleDOI
The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase.
Stephan Grzesiek,Ad Bax,G M Clore,Angela M. Gronenborn,Jin-Shan Hu,Joshua D. Kaufman,Ira Palmer,Stephen J. Stahl,Paul T. Wingfield +8 more
TL;DR: The binding surface of Nef for the SH3 domain of Hck tyrosine protein kinase has been mapped and reveals a non-contiguous amino-acid sequence interaction surface, which may suggest possible avenues for drug design aimed at inhibiting the interaction between Nef and SH3 domains.