Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Jean L. Whittingham"'
Autor:
William T. Ferreira, Jean L. Whittingham, James A. Brannigan, Simon M. Cutting, Shumpei Hanai, Johan P. Turkenburg, Anthony J. Wilkinson, Eleanor J. Dodson, Jared Cartwright
Publikováno v:
Acta Crystallographica. Section F, Structural Biology Communications
Clostridium difficile is a spore-forming bacterium and a leading cause of hospital-acquired antibiotic-associated diarrhoea. Symptoms of disease result from secreted toxins, while disease transmission is mediated via resistant endospores. CotE is a b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06df931b3a27f466b6aa023f4b6e5b00
https://doi.org/10.1107/s2053230x20006147
https://doi.org/10.1107/s2053230x20006147
Autor:
Dolores González-Pacanowska, Ana P. G. Silva, Luis M. Ruiz-Pérez, Ian H. Gilbert, Juana Carrero-Lérida, Keith S. Wilson, Huaqing Cui, Jean L. Whittingham, Kevin D. Read, James A. Brannigan
Publikováno v:
Journal of Medicinal Chemistry
Plasmodium falciparum thymidylate kinase (PfTMPK) is a key enzyme in pyrimidine nucleotide biosynthesis. 3-Trifluoromethyl-4-chloro-phenyl-urea-α-thymidine has been reported as an inhibitor of Mycobacterium tuberculosis TMPK (MtTMPK). Starting from
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4bf3aa4a740868b7d45a0861989695f8
https://doi.org/10.1021/jm301328h
https://doi.org/10.1021/jm301328h
Autor:
James W. B. Moir, Melanie J. Thomson, Diana Quinn, Jean L. Whittingham, James Edwards, Karyn‑Anne Rowbottom
Publikováno v:
Biochemical Journal. 445:69-79
The closely related pathogenic Neisseria species N. meningitidis and N. gonorrhoeae are able to respire in the absence of oxygen, using nitrite as an alternative electron acceptor. aniA (copper-containing nitrite reductase) is tightly regulated by fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6922d83dc6210e76290ea8eeb5073b58
https://doi.org/10.1042/bj20111984
https://doi.org/10.1042/bj20111984
Autor:
Jasper B. Green, Jean L. Whittingham, A. Jamie Wood, James Edwards, Melanie J. Thomson, Lindsay J. Cole, James W. B. Moir
Publikováno v:
Journal of Biological Chemistry. 285:1105-1112
Here, we report the overexpression, purification, and characterization of the transcriptional activator fumarate and nitrate reductase regulator from the pathogenic bacterium Neisseria meningitidis (NmFNR). Like its homologue from Escherichia coli (E
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0ddb2b2aa1a29a957ad94621a732591
https://doi.org/10.1074/jbc.m109.057810
https://doi.org/10.1074/jbc.m109.057810
Autor:
Jens Brange, Johan P. Turkenburg, Zhang Youshang, Lenka Zakova, Jean L. Whittingham, Guy Dodson, Eleanor J. Dodson
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 62:505-511
Despentapeptide (des-B26-B30) insulin (DPI), an active modified insulin, has been crystallized in the presence of 20% acetic acid pH 2. A crystal structure analysis to 1.8 A spacing (space group I222) revealed that the DPI molecule, which is unable t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f009874fb48116120cd5a81c9c236edd
https://doi.org/10.1107/s0907444906006871
https://doi.org/10.1107/s0907444906006871
Publikováno v:
Journal of Biological Chemistry. 278:1744-1750
6-Oxo camphor hydrolase (OCH) is an enzyme of the crotonase superfamily that catalyzes carbon-carbon bond cleavage in bicyclic β-diketones via aretro-Claisen reaction (Grogan, G., Roberts, G. A., Bougioukou, D., Turner, N. J., and Flitsch, S. L. (20
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::539b68d3987c6a8bd5eda321c8bfc4a7
https://doi.org/10.1074/jbc.m211188200
https://doi.org/10.1074/jbc.m211188200
Autor:
John T. Finch, Ashley J. Wilson, David J. Scott, Jean L. Whittingham, Guy Dodson, Jens Brange, Karen Chance
Publikováno v:
Journal of Molecular Biology. 318:479-490
When insulin solutions are subjected to acid, heat and agitation, the normal pattern of insulin assembly (dimers-->tetramers-->hexamers) is disrupted; the molecule undergoes conformational changes allowing it to follow an alternative aggregation path
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d08ef07c31f5220fa8a404bb7c59b24c
https://doi.org/10.1016/s0022-2836(02)00021-9
https://doi.org/10.1016/s0022-2836(02)00021-9
Autor:
Haixia Luo, Ciaran E. Finn, Jean L. Whittingham, Wim G. Meijer, Elena Blagova, Raúl Miranda-CasoLuengo, Anthony J. Wilkinson, Andrew P. Leech, Alexey G. Murzin, Paul H. Walton, Johan P. Turkenburg
Publikováno v:
Acta Crystallographica Section D: Biological Crystallography
VapD is one of a set of highly homologous virulence-associated proteins from the multi-host pathogen Rhodococcus equi. The crystal structure reveals an eight-stranded β-barrel with a novel fold and a glycine rich ‘bald’ surface.
Rhodococcus
Rhodococcus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89885d7cad4c0f8df4b5ddf26e79183b
https://pubmed.ncbi.nlm.nih.gov/25084333
https://pubmed.ncbi.nlm.nih.gov/25084333
Publikováno v:
Proteins: Structure, Function, and Genetics. 27:507-516
The crystal structure of despentapeptide insulin, a monomeric insulin, has been refined at 1.3 A spacing and subsequently used to predict and model the organization in the insulin fibril. The model makes use of the contacts in the densely packed desp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bdd9e50e8737db5044f6ca58e59cda34
https://doi.org/10.1002/(sici)1097-0134(199704)27:4<507::aid-prot4>3.0.co
https://doi.org/10.1002/(sici)1097-0134(199704)27:4<507::aid-prot4>3.0.co
Publikováno v:
Biochemistry. 36:2826-2831
The fatty acid acylated insulin, Lys(B29)-tetradecanoyl, des-(B30) human insulin, has been crystallized and the structure determined by X-ray crystallography. The fatty acid substituent on residue B29 Lys binds reversibly to circulating albumin prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a87f4cb41142821d9a4b39e1df61cae
https://doi.org/10.1021/bi9625105
https://doi.org/10.1021/bi9625105