Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Ben Spiller"'
Autor:
Roman A. Melnyk, Ramyavardhanee Chandrasekaran, D.B. Lacy, Xiaofang Jin, Zhifen Zhang, Godfrey Rainey, Andrew C. Nyborg, Ben Spiller, Heather K. Kroh, Paul Warrener, Kim Rosenthal, Robert M. Woods
Publikováno v:
Journal of Biological Chemistry. 293:941-952
Clostridium difficile infection is the leading cause of hospital-acquired diarrhea and is mediated by the actions of two toxins, TcdA and TcdB. The toxins perturb host cell function through a multistep process of receptor binding, endocytosis, low pH
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bf822b7b7856be7d7def3a46ef4e5a71
https://doi.org/10.1074/jbc.m117.813428
https://doi.org/10.1074/jbc.m117.813428
Autor:
John J. Ramirez-Avila, Sandra L. Ortega-Achury, Nathan Forbes, Ben Spiller, Harley M. Wilkinson
Publikováno v:
World Environmental and Water Resources Congress 2018.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0a8794d586eff476be75f564b9594a79
https://doi.org/10.1061/9780784481424.033
https://doi.org/10.1061/9780784481424.033
Autor:
Melissa A. Farrow, Rory N. Pruitt, David B. Friedman, D. Borden Lacy, Stacey A. Rutherford, Nicole M. Chumbler, Ben Spiller
Publikováno v:
Journal of Biological Chemistry. 287:8013-8020
The principle virulence factors in Clostridium difficile pathogenesis are TcdA and TcdB, homologous glucosyltransferases capable of inactivating small GTPases within the host cell. We present crystal structures of the TcdA glucosyltransferase domain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab6b768c9b699afbec4d702c178c758f
https://doi.org/10.1074/jbc.m111.298414
https://doi.org/10.1074/jbc.m111.298414
Publikováno v:
Science. 279:1929-1933
The three-dimensional structure of an antibody (39-A11) that catalyzes a Diels-Alder reaction has been determined. The structure suggests that the antibody catalyzes this pericyclic reaction through a combination of packing and hydrogen-bonding inter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::764be7983603fc06e9c5fa8cac495128
https://doi.org/10.1126/science.279.5358.1929
https://doi.org/10.1126/science.279.5358.1929
Autor:
Helle D. Ulrich, Linda C. Hsieh-Wilson, Ben Spiller, Leo H. Wang, Dwight Barnes, Phillip A. Patten, Floyd E. Romesberg, Bernard D. Santarsiero, Gary J. Wedemayer, Raymond C. Stevens, Peter G. Schultz
Publikováno v:
Israel Journal of Chemistry. 36:121-132
A panel of catalytic antibodies which catalyze ester hydrolysis, transesterification, porphyrin metallation, Diels-Alder, and redox reactions has been selected for crystallographic study. While these examples are only a handful of the catalytic antib
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d77bc41d9d3d2d1e8883d84e286d2056
https://doi.org/10.1002/ijch.199600018
https://doi.org/10.1002/ijch.199600018
Autor:
Benjamin Chagot, Ben Spiller, Michael Cover, Rory N. Pruitt, D. Borden Lacy, Walter J. Chazin
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2009, 284 (33), pp.21934-21940. ⟨10.1074/jbc.M109.018929⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2009, 284 (33), pp.21934-21940. ⟨10.1074/jbc.M109.018929⟩
The action of Clostridium difficile toxins A and B depends on inactivation of host small G-proteins by glucosylation. Cellular inositol hexakisphosphate (InsP6) induces an autocatalytic cleavage of the toxins, releasing an N-terminal glucosyltransfer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1877b008526cb29a6e9866f5b7eff1b4
https://hal.archives-ouvertes.fr/hal-01637796
https://hal.archives-ouvertes.fr/hal-01637796
Autor:
Ben Spiller, Darren J. Mushrush, Mark S. McClain, Timothy L. Cover, Kelly A. Gangwer, Devin L. Stauff, D. Borden Lacy
Helicobacter pylori VacA, a pore-forming toxin secreted by an autotransporter pathway, causes multiple alterations in human cells, contributes to the pathogenesis of peptic ulcer disease and gastric cancer, and is a candidate antigen for inclusion in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b1d9611e419ef26121719f05b8b0544
https://europepmc.org/articles/PMC2042200/
https://europepmc.org/articles/PMC2042200/
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 96(22)
Two directed evolution experiments on p -nitrobenzyl esterase yielded one enzyme with a 100-fold increased activity in aqueous-organic solvents and another with a 17°C increase in thermostability. Structures of the wild type and its organophilic and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ca5868a5ba41d5dda41fe87b9c1a151
https://pubmed.ncbi.nlm.nih.gov/10535917
https://pubmed.ncbi.nlm.nih.gov/10535917
Autor:
Floyd E. Romesberg, Peter G. Schultz, Ben Spiller, Dwight Barnes, Raymond C. Stevens, Jun Yin, Bernard D. Santarsiero
Publikováno v:
Biochemistry. 37(41)
A classic hypothesis for enzyme catalysis is the induction of strain in the substrate. This notion was first expressed by Haldane with the lock and key analogy-"the key does not fit the lock perfectly but exercises a certain strain on it" (1). This m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::097f113b11c658a03de1c4feadd17ef7
https://pubmed.ncbi.nlm.nih.gov/9772166
https://pubmed.ncbi.nlm.nih.gov/9772166