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Ambrish Roy
Researcher at University of Michigan
Publications - 25
Citations - 13107
Ambrish Roy is an academic researcher from University of Michigan. The author has contributed to research in topics: Threading (protein sequence) & Protein structure. The author has an hindex of 16, co-authored 25 publications receiving 10931 citations. Previous affiliations of Ambrish Roy include University of Kansas & Georgia Institute of Technology.
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I-TASSER: a unified platform for automated protein structure and function prediction
TL;DR: The iterative threading assembly refinement (I-TASSER) server is an integrated platform for automated protein structure and function prediction based on the sequence- to-structure-to-function paradigm.
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The I-TASSER Suite: protein structure and function prediction
TL;DR: A stand-alone I-TASSER Suite that can be used for off-line protein structure and function prediction and three complementary algorithms to enhance function inferences are developed, the consensus of which is derived by COACH4 using support vector machines.
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Protein–ligand binding site recognition using complementary binding-specific substructure comparison and sequence profile alignment
TL;DR: Two new methods, one based on binding-specific substructure comparison (TM-Site) and another on sequence profile alignment (S-SITE), for complementary binding site predictions are developed, which demonstrate a new robust approach to protein-ligand binding site recognition, ready for genome-wide structure-based function annotations.
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COFACTOR: an accurate comparative algorithm for structure-based protein function annotation
TL;DR: A new COFACTOR webserver for automated structure-based protein function annotation and was ranked as the best method for protein–ligand binding site predictions in the recent community-wide CASP9 experiment.
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BioLiP: a semi-manually curated database for biologically relevant ligand–protein interactions
TL;DR: To facilitate template-based ligand–protein docking, virtual ligand screening and protein function annotations, a hierarchical procedure for assessing the biological relevance of ligands present in the PDB structures is developed which involves a four-step biological feature filtering followed by careful manual verifications.