S. Stahl

发表

Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy

P. Wingfield, S. Stahl, J. Conway, 1997, Nature.

Hexon-only binding of VP26 reflects differences between the hexon and penton conformations of VP5, the major capsid protein of herpes simplex virus

B. Trus, P. Wingfield, S. Stahl, 1997, Journal of virology.

A theoretical model successfully identifies features of hepatitis B virus capsid assembly.

S. Stahl, A. Zlotnick, S. Stahl, 1999, Biochemistry.

Epitope diversity of hepatitis B virus capsids: quasi-equivalent variations in spike epitopes and binding of different antibodies to the same epitope.

P. Wingfield, S. Stahl, J. Conway, 2006, Journal of molecular biology.

Computational Methods for High Resolution Analysis of Cryo-Electron Micrographs of Hepatitis B Virus Capsids

J. Conway, A. Zlotnick, P. Wingfield, 1997, Microscopy and Microanalysis.

Three-dimensional structure of HIV-1 Rev protein filaments.

B. Trus, P. Wingfield, S. Stahl, 1998, Journal of structural biology.

Hepatitis core antigen produced in Escherichia coli: subunit composition, conformational analysis, and in vitro capsid assembly.

P. Wingfield, S. Stahl, A. Steven, 1995, Biochemistry.

Comparative immunogenicity of hepatitis B virus core and E antigens.

P. Wingfield, S. Stahl, G. B. Thornton, 1988, Journal of immunology.

Hepatitis B virus capsid: localization of the putative immunodominant loop (residues 78 to 83) on the capsid surface, and implications for the distinction between c and e-antigens.

P. Wingfield, S. Stahl, J. Conway, 1998, Journal of molecular biology.

Diversity of core antigen epitopes of hepatitis B virus

P. Wingfield, S. Stahl, J. Conway, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Characterization of a Conformational Epitope on Hepatitis B Virus Core Antigen and Quasiequivalent Variations in Antibody Binding

P. Wingfield, S. Stahl, J. Conway, 2003, Journal of Virology.

Dimorphism of hepatitis B virus capsids is strongly influenced by the C-terminus of the capsid protein.

P. Wingfield, S. Stahl, N. Cheng, 1996, Biochemistry.

HIV-1 Rev expressed in recombinant Escherichia coli: purification, polymerization, and conformational properties.

P. Wingfield, S. Stahl, A. Steven, 1991, Biochemistry.

Separation and crystallization of T = 3 and T = 4 icosahedral complexes of the hepatitis B virus core protein.

J. Kaufman, A. Zlotnick, P. Wingfield, 1999, Acta crystallographica. Section D, Biological crystallography.

Localization of the C terminus of the assembly domain of hepatitis B virus capsid protein: implications for morphogenesis and organization of encapsidated RNA.

P. Wingfield, S. Stahl, J. Conway, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Localization of the N terminus of hepatitis B virus capsid protein by peptide-based difference mapping from cryoelectron microscopy.

P. Wingfield, S. Stahl, J. Conway, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Tetrairidium, a four-atom cluster, is readily visible as a density label in three-dimensional cryo-EM maps of proteins at 10-25 A resolution.

S. Stahl, J. Hainfeld, J. Conway, 1999, Journal of structural biology.