Garland R. Marshall
Washington University in St. Louis
330 Papers
5.5K Citations
Garland R. Marshall is an academic researcher from Washington University in St. Louis. The author has contributed to research in topics: Angiotensin II & Chemistry. The author has an hindex of 57, co-authored 330 publications. Previous affiliations of Garland R. Marshall include Sapienza University of Rome & University of Washington.
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Papers
Validation of Active-Site Mapping of Enzymes
Daniel J. Kuster,Garland R. Marshall +1 more
- 01 Jan 2006
Cyclopentapeptides as Rigidified Templates for Probing Interactions with the AT-1 Receptors
Gregory V. Nikiforovich,Gunnar Lindeberg,Katalin E. Kövér,Yunpeng Ye,Per-Anders Frändberg,Fred Nyberg,Anders Karlén,Anders Hallberg,Garland R. Marshall +8 more
- 01 Jan 2001
TL;DR: In this article, a 3D model of the receptor-bound conformation of angiotensin II has been proposed, where the side chains that are crucial for ligand binding and signal transduction are represented by the corresponding cyclopentapeptides.
Cavity search: An algorithm for the isolation and display of cavity-like binding regions
TL;DR: In this paper, a set of algorithms designed to enhance the display of protein binding cavities is presented, collectively entitled CAVITY SEARCH, which allow the user to isolate and fully define the extent of a particular cavity.
SPLICE: A program to assemble partial query solutions from three-dimensional database searches into novel ligands
TL;DR: SPLICE is a program that processes partial query solutions retrieved from 3D, structural databases to generate novel, aggregate ligands to ensure receptor complementarity, and is designed to interface with the database searching program FOUNDATION, which retrieves fragments containing any combination of a user-specified minimum number of matching query elements.
Novel cyclic analogs of angiotensin II with cyclization between positions 5 and 7: conformational and biological implications.
Wei-Jun Zhang,Gregory V. Nikiforovich,Jacqueline Pérodin,Darren E. Richard,Emanuel Escher,Garland R. Marshall +5 more
TL;DR: Molecular modeling suggested a possible explanation for the relatively strong binding and the weak partial agonistic activity of compound 9 are due to interaction with AT-1 receptor of only two functionally important groups, namely, the side chains of the His6 and Phe8 residues.