Zobrazeno 1 - 10
of 55
pro vyhledávání: '"Benjamin D. Bax"'
Autor:
Chloe R. Koulouris, Sian E. Gardiner, Tessa K. Harris, Karen T. Elvers, S. Mark Roe, Jason A. Gillespie, Simon E. Ward, Olivera Grubisha, Robert A. Nicholls, John R. Atack, Benjamin D. Bax
Publikováno v:
Communications Biology, Vol 5, Iss 1, Pp 1-15 (2022)
The catalytic mechanisms of human serine racemase reveal a ligandable pocket near Tyr121 that could be targeted for the development of novel inhibitors.
Externí odkaz:
https://doaj.org/article/08d2829bfb8f4f288b7fb5de272a4d80
Publikováno v:
Acta Crystallographica. Section F, Structural Biology Communications
A 1.47 Å resolution crystal structure of human inositol monophosphatase bound to the inhibitor ebselen is presented. In the structure, ebselen forms a selenosulfide bond to Cys141 and ebselen-mediated contacts between two dimers give a tetramer with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::876bc2bbd358c03443c35c6b3e1da589
http://europepmc.org/articles/PMC7531247
http://europepmc.org/articles/PMC7531247
Publikováno v:
Acta Crystallogr F Struct Biol Commun
Serine racemase (SR) is a pyridoxal 5′-phosphate (PLP)-containing enzyme that converts L-serine to D-serine, an endogenous co-agonist for the N-methyl-D-aspartate receptor (NMDAR) subtype of glutamate ion channels. SR regulates D-serine levels by t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8799b6b32ce7af72e9c69668a20a354b
https://doi.org/10.1107/s2053230x20001193
https://doi.org/10.1107/s2053230x20001193
Publikováno v:
Journal of Molecular Biology
Type II topoisomerases regulate DNA topology by making a double-stranded break in one DNA duplex, transporting another DNA segment through this break and then resealing it. Bacterial type IIA topoisomerase inhibitors, such as fluoroquinolones and nov
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81fa9545cfa9a6268a7132365ad0a567
https://doi.org/10.1016/j.jmb.2019.07.008
https://doi.org/10.1016/j.jmb.2019.07.008
Autor:
Pan F. Chan, Kaushik Raha, Shruti Jain, Geoffrey Quinque, Margarete Neu, Daniele Andreotti, Roberto Profeta, Reema K. Thalji, Brian Donovan, Simona Tommasi, Lynn McCloskey, Christopher J. Nixon, Giovanni Meneghelli, Tania Bakshi, Anna Checchia, Robert A. Stavenger, Benjamin D. Bax, Alison Howells, Federica Tonelli, Haifeng Cui
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 29:1407-1412
A series of DNA gyrase inhibitors were designed based on the X-ray structure of a parent thiophene scaffold with the objective to improve biochemical and whole-cell antibacterial activity, while reducing cardiac ion channel activity. The binding mode
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f63ff5d1f9eeb44a22b39b1dba435047
https://doi.org/10.1016/j.bmcl.2019.03.029
https://doi.org/10.1016/j.bmcl.2019.03.029
Autor:
Chloe R, Koulouris, Sian E, Gardiner, Tessa K, Harris, Karen T, Elvers, S, Mark Roe, Jason A, Gillespie, Simon E, Ward, Olivera, Grubisha, Robert A, Nicholls, John R, Atack, Benjamin D, Bax
Publikováno v:
Communications biology. 5(1)
Human serine racemase (hSR) catalyses racemisation of L-serine to D-serine, the latter of which is a co-agonist of the NMDA subtype of glutamate receptors that are important in synaptic plasticity, learning and memory. In a 'closed' hSR structure con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::82c5a0696958e8707974e024cedc3442
https://pubmed.ncbi.nlm.nih.gov/35410329
https://pubmed.ncbi.nlm.nih.gov/35410329
Autor:
Gardiner Se, Benjamin D. Bax, Harris Tk, Robert Na, Gillespie Ja, Grubisha Od, Koulouris Cr, Karen T Elvers, Roe Ms, Simon E. Ward, Atack
Human serine racemase (hSR) catalyses racemisation of L-serine to D-serine, the latter of which is a co-agonist of the NMDA subtype of glutamate receptors that are important in synaptic plasticity, learning and memory. In a ‘closed’ hSR structure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::59b1000f7c1b63ae060c6b6ca8992aba
https://doi.org/10.1101/2021.02.12.430960
https://doi.org/10.1101/2021.02.12.430960
Inositol monophosphatase (IMPase) is inhibited by lithium, the most efficacious treatment for bipolar disorder. Several therapies have been approved, or are going through clinical trials, aimed at the replacement of lithium in the treatment of bipola
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2fd395b58c40d33473bceae5140b2b4a
https://orca.cardiff.ac.uk/id/eprint/134752/3/uf5002.pdf
https://orca.cardiff.ac.uk/id/eprint/134752/3/uf5002.pdf
Autor:
Thomas Germe, Judit Vörös, Frederic Jeannot, Thomas Taillier, Robert A Stavenger, Eric Bacqué, Anthony Maxwell, Benjamin D Bax
Publikováno v:
'Nucleic Acids Research ', vol: 46, pages: 4114-4128 (2018)
Nucleic Acids Research
Nucleic Acids Research
Imidazopyrazinones (IPYs) are a new class of compounds that target bacterial topoisomerases as a basis for their antibacterial activity. We have characterized the mechanism of these compounds through structural/mechanistic studies showing they bind a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78b2261fc0c457dde126409167bcaa7d
https://doi.org/10.1093/nar/gky181
https://doi.org/10.1093/nar/gky181