Vanderpool Darin Louis
General Atomics
3 Papers
57 Citations
Vanderpool Darin Louis is an academic researcher from General Atomics. The author has contributed to research in topics: Subtilase & Catalytic triad. The author has an hindex of 3, co-authored 3 publications.
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Papers
Single-chain Recombinant Human Cytomegalovirus Protease ACTIVITY AGAINST ITS NATURAL PROTEIN SUBSTRATE AND FLUOROGENIC PEPTIDE SUBSTRATES
Christopher Pinko,Stephen Margosiak,Vanderpool Darin Louis,Jeanine C. Gutowski,Brad Condon,Chen-Chen Kan +5 more
TL;DR: The production of active recombinant single-chain human cytomegalovirus protease in Escherichia coli and development of a continuous assay for this protease are reported, which can detect nM HCMV protease activity.
50
Patent
Peptide mutant of human ERAB/HADH2, its X-ray crystal structure, and materials and method for identification of inhibitors thereof
Melwyn A. Abreo,Charles S. Agree,Robert M. Aust,Charles R. Kissinger,Stephen Margosiak,Jerry J. Meng,Laura A. Pelletier,Paul A. Rejto,Richard E. Showalter,Anna Tempczyk-Russel,Jim Thomson,Vanderpool Darin Louis,Jesus Ernesto Villafranca +12 more
- 17 Aug 2001
TL;DR: In this article, the identification, isolation and modification of human ERAB or HADH2 is described, which may be used in the discovery, identification and characterization of inhibitors or modulators for Alzheimer's disease.
8
Structure of the Human Cytomegalovirus Protease Catalytic Domain Reveals a Novel Serine Protease Fold and Catalytic Triad
Ping Chen,Hideaki Tsuge,Robert Almassy,Cindy L. Gribskov,Susumu Katoh,Vanderpool Darin Louis,Stephen Margosiak,Christopher Pinko,David A. Matthews,Chen-Chen Kan +9 more
TL;DR: A crystal structure of the human cytomegalovirus protease catalytic domain has been determined by X-ray diffraction and defines a new class of serine protease with respect to global-fold topology and has a catalytic triad consisting of Ser-132, His-63, and His-157 in contrast with the Ser-His-Asp triads found in otherserine proteases.