Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Alexandra Vardi Kilshtain"'
Publikováno v:
Current Pharmaceutical Design. 26:5713-5719
Background: As not all target proteins can be easily screened in vitro, advanced virtual screening is becoming critical. Objective: In this study, we demonstrate the application of reinforcement learning guided virtual screening for γ-aminobutyric a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8258cc734bdc67c18db7032467a50803
https://doi.org/10.2174/1381612826666201113104150
https://doi.org/10.2174/1381612826666201113104150
Publikováno v:
Journal of Biological Chemistry. 292:14229-14239
A key question concerning the catalytic cycle of Escherichia coli dihydrofolate reductase (ecDHFR) is whether the Met20 loop is dynamically coupled to the chemical step during catalysis. A more basic, yet unanswered question is whether the Met20 loop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::38cc23040b97fcd6daf44dbf0169fde1
https://doi.org/10.1074/jbc.m117.777136
https://doi.org/10.1074/jbc.m117.777136
Autor:
Bilha Fischer, Alexandra Vardi-Kilshtain, Eliav Blum, Dan Thomas Major, Alon Haim Sayer, Bosmat Levi Hevroni
Publikováno v:
Dalton Transactions. 44:7305-7317
Although involved in various physiological functions, nucleoside bis-phosphate analogues and their metal-ion complexes have been scarcely studied. Hence, here, we explored the solution conformation of 2′-deoxyadenosine- and 2′-deoxyguanosine-3′
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df4db7e3634934163b55e5a18463b316
https://doi.org/10.1039/c5dt00080g
https://doi.org/10.1039/c5dt00080g
Publikováno v:
The Journal of biological chemistry. 292(34)
A key question concerning the catalytic cycle of Escherichia coli dihydrofolate reductase (ecDHFR) is whether the Met20 loop is dynamically coupled to the chemical step during catalysis. A more basic, yet unanswered question is whether the Met20 loop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fa797fba01b7413e7518882499c79c70
https://pubmed.ncbi.nlm.nih.gov/28620051
https://pubmed.ncbi.nlm.nih.gov/28620051
Autor:
Lokesh Gakhar, Alexandra Vardi-Kilshtain, Dvir Doron, Dan Thomas Major, Vanja Stojković, Amnon Kohen
Publikováno v:
The Journal of Physical Chemistry B. 119:906-916
This study employs hybrid quantum mechanics-molecular mechanics (QM/MM) simulations to investigate the effect of mutations of the active-site residue I14 of E. coli dihydrofolate reductase (DHFR) on the hydride transfer. Recent kinetic measurements o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d1730d0f42c302a507da9d6d52f7900
https://doi.org/10.1021/jp5059963
https://doi.org/10.1021/jp5059963
Autor:
Shina Caroline Lynn Kamerlin, Alexandra Vardi Kilshtain, Dvir Doron, Dan Thomas Major, Alexandra T. P. Carvalho, Alexandre Barrozo
Publikováno v:
Journal of Molecular Graphics and Modelling. 54:62-79
In this review we give an overview of the field of Computational enzymology. We start by describing the birth of the field, with emphasis on the work of the 2013 chemistry Nobel Laureates. We then present key features of the state-of-the-art in the f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29117dcd1f3045f80a8bf4acade2467c
Publikováno v:
Protein Science. 23:1102-1112
Thioredoxin superfamily proteins introduce disulfide bonds into substrates, catalyze the removal of disulfides, and operate in electron relays. These functions rely on one or more dithiol/disulfide exchange reactions. The flavoenzyme quiescin sulfhyd
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8213221a643965609d850f861a709ca7
https://doi.org/10.1002/pro.2496
https://doi.org/10.1002/pro.2496
Autor:
Alexandra Vardi-Kilshtain, Michal Weitman, Dvir Doron, Hamutal Engel, Dan Thomas Major, Asaf Azuri
Publikováno v:
Israel Journal of Chemistry. 54:1108-1117
Enzymes are remarkably efficient catalysts evolved to perform well-defined and highly specific chemical transformations. Studying the nature of enzymatic rate enhancements is highly important from several aspects, including the rational design of syn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::07813d2bfa9fb98e2d8890d3f7b642d1
https://doi.org/10.1002/ijch.201400026
https://doi.org/10.1002/ijch.201400026
Publikováno v:
Biochemistry. 52:4382-4390
Orotidine 5'-monophosphate (OMP) decarboxylase (ODCase) catalyzes the decarboxylation of OMP to uridine 5'-monophosphate (UMP). Numerous studies of this reaction have suggested a plethora of mechanisms including covalent addition, ylide or carbene fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::021b3ed3306eed7e3c2ca4cc48944137
https://doi.org/10.1021/bi400190v
https://doi.org/10.1021/bi400190v
Autor:
Christopher M. Cheatum, Dan Thomas Major, Amnon Kohen, Kevin Francis, Qi Guo, Alexandra Vardi-Kilshtain, Kyle Wickersham, Lokesh Gakhar
The structure of formate dehydrogenase from Candida boidinii (CbFDH) is of both academic and practical interests. First, this enzyme represents a unique model system for studies on the role of protein dynamics in catalysis, but so far these studies h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::681a0e4d3baddb34b284750eb2159f7f
https://europepmc.org/articles/PMC4917879/
https://europepmc.org/articles/PMC4917879/
