Zobrazeno 1 - 10
of 17
pro vyhledávání: '"J. Chris Culberson"'
Publikováno v:
Pure and Applied Chemistry. 94:737-744
We present a simple, biochemistry data model (BioChemUDM) to represent compounds and assays for the purpose of capturing, reporting, and sharing data, both biological and chemical. We describe an approach to register a compound based solely on a ster
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f58c0e9ce505d942b6ae67e2172e05b7
https://doi.org/10.1515/pac-2021-1004
https://doi.org/10.1515/pac-2021-1004
Publikováno v:
Journal of chemical information and modeling. 62(14)
As with many other institutions, our company maintains many quantitative structure-activity relationship (QSAR) models of absorption, distribution, metabolism, excretion, and toxicity (ADMET) end points and updates the models regularly. We recently e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::701037575d8f7662625114930b4af51e
https://pubmed.ncbi.nlm.nih.gov/35796226
https://pubmed.ncbi.nlm.nih.gov/35796226
Autor:
Jinchu Liu, John Kong, Tiffany M. Jarrell, Edward C. Sherer, Leo A. Joyce, J. Chris Culberson
Publikováno v:
Chirality. 29(12)
The absolute configurations of the separated enantiomers of fluralaner, a racemic animal health product used to prevent fleas and ticks, have been assigned using vibrational circular dichroism (VCD). The crystallographic structure of the active enant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a97e70d93a81ab2ae1e891eed7e06c32
https://pubmed.ncbi.nlm.nih.gov/28981965
https://pubmed.ncbi.nlm.nih.gov/28981965
Autor:
Kelly-Ann S. Schlegel, Peter S. Kutchukian, Lee Warren, Sophie Parmentier-Batteur, Jason Cassaday, Victor N. Uebele, Brian C. Magliaro, Brian Squadroni, Danielle M. Hurzy, Eric N. Johnson, J. Chris Culberson, Gregory O'Donnell, Adam Amoss, Fiona Thomson, Michael F.A. Finley, Paul Zuck, Andrew J. Cooke, Danette Pascarella, Jeffrey D. Hermes
N-methyl-d-aspartate receptors (NMDARs) mediate glutamatergic signaling that is critical to cognitive processes in the central nervous system, and NMDAR hypofunction is thought to contribute to cognitive impairment observed in both schizophrenia and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83ee89032dec0bd4c1bf64d0fea584c0
https://eprints.gla.ac.uk/146530/1/146530.pdf
https://eprints.gla.ac.uk/146530/1/146530.pdf
Autor:
Wendy D. Cornell, Vladimir N. Maiorov, Stacey R. Lindsley, Constantine Kreatsoulas, Georgia B. McGaughey, Christopher I. Bayly, J. Chris Culberson, Jean‐Francois Truchon, Robert P. Sheridan
Publikováno v:
Journal of Chemical Information and Modeling. 47:1504-1519
Virtual screening benchmarking studies were carried out on 11 targets to evaluate the performance of three commonly used approaches: 2D ligand similarity (Daylight, TOPOSIM), 3D ligand similarity (SQW, ROCS), and protein structure-based docking (FLOG
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6f0cd2b918b79dd1b726830dcf27f77
https://doi.org/10.1021/ci700052x
https://doi.org/10.1021/ci700052x
Autor:
Georgia B. McGaughey, Joseph Shpungin, Constantine Kreatsoulas, Bradley P. Feuston, J. Chris Culberson, Vladimir N. Maiorov
Publikováno v:
Molecular Diversity. 10:341-347
Within a congeneric series of ATP-competitive KDR kinase inhibitors, we determined that the IC(50) values, which span four orders of magnitude, correlated best with the calculated ligand-protein interaction energy using the Merck Molecular Force Fiel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc4bf094251b3d2401e96da82330ea8b
https://doi.org/10.1007/s11030-006-9037-1
https://doi.org/10.1007/s11030-006-9037-1
Autor:
Mark E. Duggan, J. Chris Culberson, Chih-Tai Leu, Bradley P. Feuston, George D. Hartman, Sevgi B. Rodan
Publikováno v:
Journal of Medicinal Chemistry. 45:5640-5648
A binding model for nonpeptide antagonists of integrin αvβ3 has been developed through docking analyses utilizing the MMFFs force field and the recently published crystal structure, 1JV2. Results of this docking study have led to the identification
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::55926dcb21a807fced503d448aeac484
https://doi.org/10.1021/jm0203130
https://doi.org/10.1021/jm0203130
Autor:
Bradley V. Clineschmidt, Richard G. Ball, Douglas J. Pettibone, Daniel F. Veber, Joseph M. Pawluczyk, J. Chris Culberson, Roger M. Freidinger, Jill M. Erb, Peter D. Williams, Debra S. Perlow
Publikováno v:
Bioorganic & Medicinal Chemistry. 2:971-985
A series of new o-tolylpiperazine camphorsulfonamide OT antagonists is described. Analogs containing conformationally constrained 1-acylamino-2-propyl substituents at the camphor C2 endo position exhibit high affinity for OT and AVP-V1a receptors or
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47c18cfacbda565886989135864d1510
https://doi.org/10.1016/s0968-0896(00)82046-5
https://doi.org/10.1016/s0968-0896(00)82046-5
Publikováno v:
ChemInform. 37
The idea of a "transformation", making a small change to a chemical structure, for instance removing or replacing a substituent, is familiar to chemists. We suggest two ways of representing a transformation in silico, as a substructure descriptor dif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3455f7cc49f70199b2778853e7e2868
https://doi.org/10.1002/chin.200617219
https://doi.org/10.1002/chin.200617219
Autor:
Bradley P, Feuston, J Chris, Culberson, Mark E, Duggan, George D, Hartman, Chih-Tai, Leu, Sevgi B, Rodan
Publikováno v:
Journal of medicinal chemistry. 45(26)
A binding model for nonpeptide antagonists of integrin alpha(v)beta(3) has been developed through docking analyses utilizing the MMFFs force field and the recently published crystal structure, 1JV2. Results of this docking study have led to the ident
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::090e135a860b3252630b00bdcf2febf8
https://pubmed.ncbi.nlm.nih.gov/12477347
https://pubmed.ncbi.nlm.nih.gov/12477347