Zobrazeno 1 - 10
of 41
pro vyhledávání: '"Jon B. Cooper"'
Autor:
David R. Lisgarten, Rex A. Palmer, Jon B. Cooper, Claire E. Naylor, Rosemary C. Talbert, Brendan J. Howlin, John N. Lisgarten, Janez Konc, Shabir Najmudin, Carina M. C. Lobley
Publikováno v:
BMC Chemistry, Vol 17, Iss 1, Pp 1-30 (2023)
Abstract The crystal structure of orthorhombic Bovine Pancreatic Ribonuclease A has been determined to 0.85 Å resolution using low temperature, 100 K, synchrotron X-ray data collected at 16000 keV (λ = 0.77 Å). This is the first ultra-high-resolut
Externí odkaz:
https://doaj.org/article/c3e000059a4646ef998bd30012666b7f
Autor:
Melina Haupt, Matthew P. Blakeley, Stuart J. Fisher, Sax A. Mason, Jon B. Cooper, Edward P. Mitchell, V. Trevor Forsyth
Publikováno v:
IUCrJ, Vol 1, Iss 6, Pp 429-438 (2014)
Human transthyretin has an intrinsic tendency to form amyloid fibrils and is heavily implicated in senile systemic amyloidosis. Here, detailed neutron structural studies of perdeuterated transthyretin are described. The analyses, which fully exploit
Externí odkaz:
https://doaj.org/article/1b8281a5213e489194993e77fbdcee08
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 63:1080-1083
Endothiapepsin has been cocrystallized with the gem-diol inhibitor PD-135,040 in a low solvent-content (39%) unit cell, which is unprecedented for this enzyme-inhibitor complex and enables ultrahigh-resolution (1.0 A) X-ray diffraction data to be col
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1936b9927dda6c467ac0197a4b8f4875
https://doi.org/10.1107/s1744309107061283
https://doi.org/10.1107/s1744309107061283
Publikováno v:
FEBS Journal. 273:2594-2606
The pcd1 mutant of pea lacks heme oxygenase (HO) activity required for the synthesis of the phytochrome chromophore and is consequently severely deficient in all responses mediated by the phytochrome family of plant photoreceptors. Here we describe t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::331b1a0bd4a687c4f1d7eb8c35be01fb
https://doi.org/10.1111/j.1742-4658.2006.05264.x
https://doi.org/10.1111/j.1742-4658.2006.05264.x
Autor:
Steve P. Wood, Leighton Coates, Jon B. Cooper, R. Gill, Dean A. A. Myles, Peter T. Erskine, S. Mall
Publikováno v:
Protein Science. 12:1741-1749
The X-ray structures of native endothiapepsin and a complex with a hydroxyethylene transition state analog inhibitor (H261) have been determined at atomic resolution. Unrestrained refinement of the carboxyl groups of the enzyme by using the atomic re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d20f443a88e6a69357efaeaac4893d73
https://doi.org/10.1110/ps.0305203
https://doi.org/10.1110/ps.0305203
Autor:
Richard Lambert, Steve P. Wood, Peter M. Shoolingin-jordan, Alun R. Coker, Ed Norton, G. Lewis, Martin J. Warren, Mohammed Sarwar, Jon B. Cooper, Peter T. Erskine, Paul Spencer
Publikováno v:
Biochemistry. 38:4266-4276
5-Aminolevulinic acid dehydratase (ALAD), an early enzyme of the tetrapyrrole biosynthesis pathway, catalyzes the dimerization of 5-aminolevulinic acid to form the pyrrole, porphobilinogen. ALAD from Escherichia coli is shown to form a homo-octameric
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e1ef1e373cc95bd19cce6ca8b496c0d
https://doi.org/10.1021/bi982137w
https://doi.org/10.1021/bi982137w
Autor:
Natalie M. Senior, Peter M. Shoolingin-Jordan, Paul Spencer, Paul G. Thomas, M. Sarwar, G. Lewis, Richard Lambert, Steve P. Wood, Ian J. Tickle, Sarah J. Awan, Jon B. Cooper, Peter T. Erskine, Martin J. Warren
Publikováno v:
Nature Structural Biology. 4:1025-1031
5-Aminolaevulinate dehydratase (ALAD) is a homo-octameric metallo-enzyme that catalyses the formation of porphobilinogen from 5-aminolaevulinic acid. The structure of the yeast enzyme has been solved to 2.3 A resolution, revealing that each subunit a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ae59a8c3267f8064178528a3b5b3295
https://doi.org/10.1038/nsb1297-1025
https://doi.org/10.1038/nsb1297-1025
Autor:
P. T. Erskine, S.P. Wood, Paul G. Thomas, Keith Brocklehurst, Martin J. Warren, Peter M. Shoolingin-Jordan, Natalie M. Senior, Jon B. Cooper
Publikováno v:
Biochemical Journal. 320:401-412
5-Aminolaevulinic acid dehydratase (ALAD) is an essential enzyme in most organisms, catalysing an inaugural step in the tetrapyrrole biosynthetic pathway, the Knorr-type condensation reaction of two molecules of 5-aminolaevulinic acid (ALA) to form t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7a9f4e2a574f5b365bc9ba3edce85aec
https://doi.org/10.1042/bj3200401
https://doi.org/10.1042/bj3200401
Autor:
H. Driessen, M. Szelke, Javier Sueiras-Diaz, M. Badasso, C.G. Dealwis, D. M. Jones, Tom L. Blundell, Kazuo Murakami, Carlos Frazão, Jon B. Cooper, I.J. Tickle, H. Miyazaki
Publikováno v:
Journal of Molecular Biology. 236:342-360
The structure of mouse submaxillary renin complexed with a decapeptide inhibitor, CH-66 (Piv-His-Pro-Phe-His-Leu-OH-Leu-Tyr-Tyr-Ser-NH2), where Piv denotes a pivaloyl blocking group, and -OH- denotes a hydroxyethylene (-(S)CHOH-CH2-) transition state
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afa7c7ef7d580997e43c7dbabedffdaf
https://doi.org/10.1006/jmbi.1994.1139
https://doi.org/10.1006/jmbi.1994.1139
Autor:
Jon B. Cooper
Publikováno v:
Aspartic Acid Proteases as Therapeutic Targets
In this ground-breaking practical reference, the family of aspartic acid proteases is described from a drug developer's perspective.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0dbd5cf4f7c2480bf05507baea014bac
https://doi.org/10.1002/9783527630943.ch4
https://doi.org/10.1002/9783527630943.ch4
