Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Ambrish Roy"'
Autor:
Peter M. Eimon, Mostafa Ghannad-Rezaie, Gianluca De Rienzo, Amin Allalou, Yuelong Wu, Mu Gao, Ambrish Roy, Jeffrey Skolnick, Mehmet Fatih Yanik
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
One challenge in drug screening for neurological disorders is how to accurately capture disease pathology and side effects. Here, the authors developed a multi-channel recording platform based on a zebrafish genetic model of epilepsy to screen for an
Externí odkaz:
https://doaj.org/article/ca48ead3c4314e8da4bd2a2868831cfd
Publikováno v:
PLoS ONE, Vol 4, Iss 8, p e6701 (2009)
Hydrogen constitutes nearly half of all atoms in proteins and their positions are essential for analyzing hydrogen-bonding interactions and refining atomic-level structures. However, most protein structures determined by experiments or computer predi
Externí odkaz:
https://doaj.org/article/8cd356f40990489d947c9118ac50d5a1
Publikováno v:
Medicinal Research Reviews. 39:684-705
Given the alarming rise in instances of antibiotic resistance displayed by disease-causing microorganisms, it is necessary to accelerate efforts to find new antibiotic agents. One prominent approach is to identify potent inhibitors of receptors that
Autor:
Fatima Zohra Smaili, Xin Gao, Ambrish Roy, P. Scott Hefty, Meshari Alazmi, Shuye Tian, Stefan T. Arold, Wei Chen, Srayanta Mukherjee
Publikováno v:
Genomics, proteomicsbioinformatics. 19(6)
The number of available protein sequences in public databases is increasing exponentially. However, a significant percentage of these sequences lack functional annotation, which is essential for the understanding of how biological systems operate. We
Autor:
Mehmet Fatih Yanik, Ambrish Roy, Mu Gao, Peter M. Eimon, Amin Allalou, Mostafa Ghannad-Rezaie, Yuelong Wu, Jeffrey Skolnick, Gianluca De Rienzo
Publikováno v:
Nature Communications, 9 (1)
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
Nature Communications
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
Nature Communications
Neurological drugs are often associated with serious side effects, yet drug screens typically focus only on efficacy. We demonstrate a novel paradigm utilizing high-throughput in vivo electrophysiology and brain activity patterns (BAPs). A platform w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8dd14828ffadb3bceee0fff779a5ab37
https://hdl.handle.net/20.500.11850/229893
https://hdl.handle.net/20.500.11850/229893
Publikováno v:
Journal of Chemical Information and Modeling. 55:1757-1770
Often in pharmaceutical research the goal is to identify small molecules that can interact with and appropriately modify the biological behavior of a new protein target. Unfortunately, most proteins lack both known structures and small molecule binde
Autor:
Kaushik Hatti, Gaurav Chopra, Ambrish Roy, George W. N. White, Jeremy A. Horst, Ram Samudrala, Geetika Sethi, Mark Minie
Publikováno v:
Drug Discovery Today
The Computational Analysis of Novel Drug Opportunities (CANDO) platform (http://protinfo.org/cando) uses similarity of compound-proteome interaction signatures to infer homology of compound/drug behavior. We constructed interaction signatures for 373
Publikováno v:
Bioinformatics. 29:2588-2595
Motivation: Identification of protein–ligand binding sites is critical to protein function annotation and drug discovery. However, there is no method that could generate optimal binding site prediction for different protein types. Combination of co
Publikováno v:
Nucleic Acids Research
BioLiP (http://zhanglab.ccmb.med.umich.edu/BioLiP/) is a semi-manually curated database for biologically relevant ligand-protein interactions. Establishing interactions between protein and biologically relevant ligands is an important step toward und
Autor:
Yang Zhang, Ambrish Roy
Publikováno v:
Structure. 20:987-997
Summary Proteins perform functions through interacting with other molecules. However, structural details for most of the protein-ligand interactions are unknown. We present a comparative approach (COFACTOR) to recognize functional sites of protein-li