Zobrazeno 1 - 10
of 46
pro vyhledávání: '"Nicholas G. Rutherford"'
NMR methods have been adopted to observe directly the characteristics of substrate binding to the galactose-H+ symport protein GalP, in its native environment, the inner membranes of Escherichia coli. Sedimented inner-membrane vesicles containing the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f848d043a31fb198c512f2329041182
https://doi.org/10.1073/pnas.91.9.3877
https://doi.org/10.1073/pnas.91.9.3877
Autor:
S. W. Homans, W. J. O'reilly, Peter J. F. Henderson, Paul J. R. Spooner, Anthony Watts, Nicholas G. Rutherford
The weak binding of sugar substrates fails to induce any quantifiable physical changes in the L-fucose-H+ symport protein, FucP, from Escherichia coli, and this protein lacks any strongly binding ligands for competitive binding assays. Access to subs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be5fd14b9c5eef31635b041eae62d657
https://ora.ox.ac.uk/objects/uuid:172676df-e815-473e-acc9-2ba1415bd02f
https://ora.ox.ac.uk/objects/uuid:172676df-e815-473e-acc9-2ba1415bd02f
Autor:
Mark S.P. Sansom, Nicholas G. Rutherford, Simone Weyand, Jonathan M. Hadden, So Iwata, Peter J. F. Henderson, Oliver Beckstein, David Sharples, Alexander D. Cameron, Tatsuro Shimamura
Publikováno v:
Science; Vol 328
Triangulating to Mechanism Cellular uptake and release of a variety of substrates are mediated by secondary transporters, but no crystal structures are known for all three fundamental states of the transport cycle, which has limited explanations for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a83b7fd5d34d47aab61ca4f3241a9fb
https://ora.ox.ac.uk/objects/uuid:7f6ce3af-858e-489a-8b07-d447c1d388a0
https://ora.ox.ac.uk/objects/uuid:7f6ce3af-858e-489a-8b07-d447c1d388a0
Autor:
Nicholas G. Rutherford, Yoshichika Arakawa, Jun-ichi Wachino, Keigo Shibayama, Peter J. F. Henderson, Massoud Saidijam
Publikováno v:
Molecular Microbiology. 64:396-406
gamma-Glutamyltranspeptidase (GGT) is a periplasmic enzyme of Helicobacter pylori implicated in its pathogenesis towards mammalian cells. We have cloned and expressed the H. pylori strain 26695 recombinant GGT protein in Escherichia coli and purified
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::218f1c8faab2ea95fe2298c037f98000
https://doi.org/10.1111/j.1365-2958.2007.05661.x
https://doi.org/10.1111/j.1365-2958.2007.05661.x
Autor:
Hao Xie, Wei-Jun Liang, Peter J. F. Henderson, Kate J. Wilson, Shunichi Suzuki, Nicholas G. Rutherford, Jan Knol, Richard A. Jefferson
Publikováno v:
Journal of Bacteriology, 187(7), 2377-2385. AMER SOC MICROBIOLOGY
Journal of Bacteriology
Journal of Bacteriology
Two genes, gusB and gusC , from a natural fecal isolate of Escherichia coli are shown to encode proteins responsible for transport of β-glucuronides with synthetic [ 14 C]phenyl-1-thio-β- d -glucuronide as the substrate. These genes are located in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30640fa4e3378d17bd721bca921aa979
https://doi.org/10.1128/jb.187.7.2377-2385.2005
https://doi.org/10.1128/jb.187.7.2377-2385.2005
Autor:
Qinghu Ren, Dong Leng, Nicholas G. Rutherford, Pikyee Ma, Zhiqiang Xu, Gerda Szakonyi, Ian T. Paulsen, Jeffrey N. Keen, Anne-Brit Kolstø, Massoud Saidijam, Ingerid Nes, Jasmin K. Kroeger, Kim E. Bettaney, Peter J. F. Henderson, Alison Ward
Publikováno v:
Advances in Enzymology and Related Areas of Molecular Biology
Macquarie University
Macquarie University
By MASSOUD SAIDIJAM, Department of Molecular Medicine and Genetics, School of Medicine, Hamedan University of Medical Sciences, Hamedan, Iran, KIM E. BETTANEY, DONG LENG, PIKYEE MA, ZHIQIANG XU, JEFFREY G. KEEN, NICHOLAS G. RUTHERFORD, ALISON WARD AN
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d21386fd581a4682af7ebc0adf32eaf
https://doi.org/10.1002/9780470920541.ch4
https://doi.org/10.1002/9780470920541.ch4
Autor:
Nicholas G. Rutherford, Jeffrey Griffith, Adrian R. Walmsley, Giles E. M. Martin, Manuel F. Varela, Kenneth B. Seamon, Peter J. F. Henderson, Paul E. Roberts
Publikováno v:
Biochemical Society Transactions. 21:1002-1006
Homologous sugar-transport proteins in microbes and man Peter J. F. Henderson,* Paul E. Roberts,t Giles E. M. Martin,* Kenneth 6. Seamon,$ Adrian R. Walmsley,§ Nicholas G. Rutherford,* Manuel F. Varelall and Jeffrey K. Griffithll *Department of Bioc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db3e784e1774221aa6e7317a11c8cf58
https://doi.org/10.1042/bst0211002
https://doi.org/10.1042/bst0211002
Autor:
Christopher J. Hoyle, S.L. Palmer, Alison Ward, Martin K Pos, Simon Baumberg, Johan Meuller, Richard C. Essenberg, Nicholas G. Rutherford, Mary K. Phillips-Jones, Alex A Neyfakh, Jeffrey K Griffith, Scott Morrison, Atif A.W. Abu‐Bakr, Martin C. J. Maiden, Shunichi Suzuki, Joanne Clough, Peter J. F. Henderson, Massoud Saidijam, John O'Reilly, Michael J. R. Stark, Georgios Psakis
Publikováno v:
FEBS Letters. 555:170-175
A general strategy for the amplified expression in Escherichia coli of membrane transport and receptor proteins from other bacteria is described. As an illustration we report the cloning of the putative α-ketoglutarate membrane transport gene from t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a458718367dc1076d1f7bf1180d38775
https://doi.org/10.1016/s0014-5793(03)01148-7
https://doi.org/10.1016/s0014-5793(03)01148-7
Autor:
Massoud, Saidijam, Kim E, Bettaney, Dong, Leng, Pikyee, Ma, Zhiqiang, Xu, Jeffrey N, Keen, Nicholas G, Rutherford, Alison, Ward, Peter J F, Henderson, Gerda, Szakonyi, Qinghu, Ren, Ian T, Paulsen, Ingerid, Nes, Jasmin K, Kroeger, Anne-Brit, Kolsto
Publikováno v:
Advances in enzymology and related areas of molecular biology. 77
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e351d281a5f59e853b01891a9c0438b1
https://pubmed.ncbi.nlm.nih.gov/21692369
https://pubmed.ncbi.nlm.nih.gov/21692369
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 107(43)
Understanding how an amino acid sequence folds into a functional, three-dimensional structure has proved to be a formidable challenge in biological research, especially for transmembrane proteins with multiple alpha helical domains. Mechanistic foldi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d095e6adeb4267115ea545c66d2e7080
https://pubmed.ncbi.nlm.nih.gov/20937906
https://pubmed.ncbi.nlm.nih.gov/20937906