S
Stephen C. Harrison
Researcher at Howard Hughes Medical Institute
Publications - 483
Citations - 63813
Stephen C. Harrison is an academic researcher from Howard Hughes Medical Institute. The author has contributed to research in topics: Protein structure & Kinetochore. The author has an hindex of 123, co-authored 420 publications receiving 59495 citations. Previous affiliations of Stephen C. Harrison include Boston Children's Hospital & National Institute for Medical Research.
Papers
More filters
Journal ArticleDOI
Structure of SARS Coronavirus Spike Receptor-Binding Domain Complexed with Receptor
Fang Li,Wenhui Li,Wenhui Li,Michael Farzan,Michael Farzan,Stephen C. Harrison,Stephen C. Harrison +6 more
TL;DR: The structure of the RBD suggests ways to make truncated disulfide-stabilized RBD variants for use in the design of coronavirus vaccines.
Journal ArticleDOI
Atomic structure of the ectodomain from HIV-1 gp41
Winfried Weissenhorn,Andréa Dessen,Stephen C. Harrison,Stephen C. Harrison,John J. Skehel,Don C. Wiley,Don C. Wiley +6 more
TL;DR: X-ray crystallography determines the structure of the protease-resistant part of a gp41 ectodomain solubilized with a trimeric GCN4 coiled coil in place of the amino-terminal fusion peptide, and suggests a common mechanism for initiating fusion.
Journal ArticleDOI
Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance.
TL;DR: A combinatorial disulfide cross-linking strategy was used to prepare a stalled complex of human immunodeficiency virus-type 1 (HIV-1) reverse transcriptase with a DNA template:primer and a deoxynucleoside triphosphate (dNTP), and the crystal structure of the complex was determined at a resolution of 3.2 angstroms.
Journal ArticleDOI
The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution
Félix A. Rey,Franz X. Heinz,Christian W. Mandl,Christian Kunz,Stephen C. Harrison,Stephen C. Harrison +5 more
TL;DR: The clustering of mutations that affect virulence in various flaviviruses indicates a possible receptor binding site and, together with other mutational and biochemical data, suggests a picture for the fusion-activating, conformational change triggered by low pH.
Journal ArticleDOI
Three-dimensional structure of the tyrosine kinase c-Src
TL;DR: The structure of a large fragment of the c-SRC tyrosine kinase, comprising the regulatory and kinase domains and the carboxy-terminal tail, has been determined and shows how appropriate cellular signals, or transforming mutations in v-Src, could break these interactions to produce an open, active kinase.