Zobrazeno 1 - 10
of 102
pro vyhledávání: '"Jonathan B, Cooper"'
Autor:
Jingxu Guo, Alice Douangamath, Weixiao Song, Alun R. Coker, A.W. Edith Chan, Steve P. Wood, Jonathan B. Cooper, Efrat Resnick, Nir London, Frank von Delft
Publikováno v:
Journal of Structural Biology: X, Vol 4, Iss , Pp 100031- (2020)
Outbreaks of human epidemic nonbacterial gastroenteritis are mainly caused by noroviruses. Viral replication requires a 3C-like cysteine protease (3CLpro) which processes the 200 kDa viral polyprotein into six functional proteins. The 3CLpro has attr
Externí odkaz:
https://doaj.org/article/f7ec49afe3444088a8e5ae5ef622317b
Autor:
Patricia S. Langan, Venu Gopal Vandavasi, Kevin L. Weiss, Jonathan B. Cooper, Stephan L. Ginell, Leighton Coates
Publikováno v:
FEBS Open Bio, Vol 6, Iss 12, Pp 1170-1177 (2016)
The role of the conserved residue Tyr105 in class A β‐lactamases has been the subject of investigation using both structural studies and saturation mutagenesis. Both have shown that while it does not need to be strictly conserved for activity, it
Externí odkaz:
https://doaj.org/article/6286bd10149741c0898537416d718fab
Autor:
Steve P. Wood, Jonathan B. Cooper, Daniel J. Rigden, Jingxu Guo, Ronan M. Keegan, Peter T. Erskine, Sheng Li
Publikováno v:
Acta Crystallogr F Struct Biol Commun
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Insect juvenile hormones (JHs) are a family of sesquiterpenoid molecules that are secreted into the haemolymph. JHs have multiple roles in insect development, metamorphosis and sexual maturation. A number of pesticides work by chemically mimicking JH
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e20217a843010a5a06ee02818d0444dc
https://europepmc.org/articles/PMC8647211/
https://europepmc.org/articles/PMC8647211/
Autor:
Josh Bennett, Jonathan B. Cooper, Steve P. Wood, Eyram Adjogatse, Peter T. Erskine, Jingxu Guo, Brendan W. Wren
Publikováno v:
Acta Crystallogr F Struct Biol Commun
In many prokaryotes, the first step of threonine metabolism is catalysed by the enzyme threonine dehydrogenase (TDH), which uses NAD+ to oxidize its substrate to 2-amino-3-ketobutyrate. The absence of a functional TDH gene in humans suggests that inh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c1e79538289072d9a3090eb7ae4e78b
https://pubmed.ncbi.nlm.nih.gov/34341193
https://pubmed.ncbi.nlm.nih.gov/34341193
Autor:
Steve P. Wood, Jonathan B. Cooper, Jingxu Guo, M. Akhtar, Alun R. Coker, Nasir Ahmad, Ronan M. Keegan, Majida Atta Muhammad, Naeem Rashid
Publikováno v:
Acta Crystallographica Section D Structural Biology. 74:305-314
Pullulan-hydrolysing enzymes, more commonly known as debranching enzymes for starch and other polysaccharides, are of great interest and have been widely used in the starch-saccharification industry. Type III pullulan hydrolase fromThermococcus kodak
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::443dfe00fa52fa5b52274cc0bc9a951d
https://doi.org/10.1107/s2059798318001754
https://doi.org/10.1107/s2059798318001754
Publikováno v:
Acta Crystallographica Section F Structural Biology Communications. 73:612-620
The enzyme porphobilinogen deaminase (PBGD) is one of the key enzymes in tetrapyrrole biosynthesis. It catalyses the formation of a linear tetrapyrrole from four molecules of the substrate porphobilinogen (PBG). It has a dipyrromethane cofactor (DPM)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d9d267d07d7263bbdf0c17ed8290585
https://doi.org/10.1107/s2053230x17015436
https://doi.org/10.1107/s2053230x17015436
Structure of the family B DNA polymerase from the hyperthermophilic archaeonPyrobaculum calidifontis
Autor:
Jingxu Guo, M. Akhtar, Alun R. Coker, Wenling Zhang, Shazeel Ahmad, Syed Shahid Ali, Naeem Rashid, Steve P. Wood, Jonathan B. Cooper
Publikováno v:
Acta Crystallographica Section D Structural Biology. 73:420-427
The family B DNA polymerase fromPyrobaculum calidifontis(Pc-polymerase) consists of 783 amino acids and is magnesium-ion dependent. It has an optimal pH of 8.5, an optimal temperature of 75°C and a half-life of 4.5 h at 95°C, giving it greater ther
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b822b69b90f8213d1a23e043f3a5e02d
https://doi.org/10.1107/s2059798317004090
https://doi.org/10.1107/s2059798317004090
Autor:
Steve P. Wood, Alun R. Coker, Alice Douangamath, Nir London, A. W. Edith Chan, Frank von Delft, Weixiao Song, Efrat Resnick, Jonathan B. Cooper, Jingxu Guo
Publikováno v:
Journal of Structural Biology: X, Vol 4, Iss, Pp 100031-(2020)
Journal of Structural Biology: X
Journal of Structural Biology: X
Graphical abstract
Highlights • Noroviruses responsible for 99% of viral foodborne illness. • Norovirus 3C-like protease is excellent drug target. • X-ray fragment-screening gave a total of 19 fragment hits. • Two located at the active s
Highlights • Noroviruses responsible for 99% of viral foodborne illness. • Norovirus 3C-like protease is excellent drug target. • X-ray fragment-screening gave a total of 19 fragment hits. • Two located at the active s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce8b757740ea34d20ac76937b369f57a
https://www.repository.cam.ac.uk/handle/1810/310735
https://www.repository.cam.ac.uk/handle/1810/310735
Autor:
Jonathan B. Cooper, Venu Gopal Vandavasi, Patricia S. Langan, Leighton Coates, Kevin L. Weiss, Stephan L. Ginell
Publikováno v:
FEBS Open Bio
The role of the conserved residue Tyr105 in class A β‐lactamases has been the subject of investigation using both structural studies and saturation mutagenesis. Both have shown that while it does not need to be strictly conserved for activity, it
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d878f1772f368a02283b05d5b8e165e
https://doi.org/10.1002/2211-5463.12132
https://doi.org/10.1002/2211-5463.12132
Autor:
David G. Waterman, Steve P. Wood, Jonathan B. Cooper, Peter T. Erskine, Ronan M. Keegan, Graham Taylor, Leighton Coates, Alun R. Coker, Jingxu Guo, David J. Hopper
Publikováno v:
Acta Crystallographica Section D Structural Biology. 72:933-943
During efforts to crystallize the enzyme 2,4-dihydroxyacetophenone dioxygenase (DAD) fromAlcaligenessp. 4HAP, a small number of strongly diffracting protein crystals were obtained after two years of crystal growth in one condition. The crystals diffr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::efb4d531b163f49539756dd88b6afc90
https://doi.org/10.1107/s2059798316010433
https://doi.org/10.1107/s2059798316010433