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Christopher P. Hill
Researcher at University of Utah
Publications - 167
Citations - 16466
Christopher P. Hill is an academic researcher from University of Utah. The author has contributed to research in topics: Protein structure & Proteasome. The author has an hindex of 66, co-authored 165 publications receiving 15371 citations. Previous affiliations of Christopher P. Hill include Harvard University & Brookhaven National Laboratory.
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Journal ArticleDOI
Ubiquitin-binding domains
TL;DR: This work has shown how binding specificity is determined, how ubiquitin binding is regulated, and the function of UBDs in the context of full-length proteins is controlled by studying their mechanism of action.
Journal ArticleDOI
Crystal Structure of Human Cyclophilin A Bound to the Amino-Terminal Domain of HIV-1 Capsid
T.R. Gamble,Felix Vajdos,Sanghee Yoo,David K. Worthylake,Megan Houseweart,Wesley I. Sundquist,Christopher P. Hill +6 more
TL;DR: The structure suggests how cyclophilin A can act as a sequence-specific binding protein and a nonspecific prolyl isomerase, and in the crystal lattice, capsid molecules assemble into continuous planar strips.
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Structure of the Carboxyl-Terminal Dimerization Domain of the HIV-1 Capsid Protein
T.R. Gamble,Sanghee Yoo,Felix Vajdos,Uta K. von Schwedler,David K. Worthylake,Hui Wang,John P. McCutcheon,Wesley I. Sundquist,Christopher P. Hill +8 more
TL;DR: Alignment of the CA(146-231) dimer with the crystal structure of the capsid amino-terminal domain provides a model for the intact protein and extends models for assembly of the central conical core of HIV-1.
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Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization.
TL;DR: The high-resolution crystal structure of defensin HNP-3 reveals a dimeric beta sheet that has an architecture very different from other lytic peptides, and suggests mechanisms by which defensins might bind to and permeabilize the lipid bilayer.
Journal ArticleDOI
X-Ray Structures of the Hexameric Building Block of the HIV Capsid
Owen Pornillos,Barbie K. Ganser-Pornillos,Barbie K. Ganser-Pornillos,Brian N. Kelly,Yuanzi Hua,Frank G. Whitby,C. David Stout,Wesley I. Sundquist,Christopher P. Hill,Mark Yeager,Mark Yeager,Mark Yeager +11 more
TL;DR: Methods for isolating soluble, assembly-competent CA hexamers are devised and derived four crystallographically independent models that define the structure of this capsid assembly unit at atomic resolution, which clarify the molecular basis for Capsid assembly inhibition and should facilitate structure-based drug design strategies.