Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Keith G. Inman"'
Autor:
Andrea A Berry, Yi Yang, Natalia Pakharukova, James A Garnett, Wei-chao Lee, Ernesto Cota, Jan Marchant, Saumendra Roy, Minna Tuittila, Bing Liu, Keith G Inman, Fernando Ruiz-Perez, Inacio Mandomando, James P Nataro, Anton V Zavialov, Steve Matthews
Publikováno v:
PLoS Pathogens, Vol 10, Iss 9, p e1004404 (2014)
Enteroaggregative Escherichia coli (EAEC) is a leading cause of acute and persistent diarrhea worldwide. A recently emerged Shiga-toxin-producing strain of EAEC resulted in significant mortality and morbidity due to progressive development of hemolyt
Externí odkaz:
https://doaj.org/article/2fd6baa77f094eb08a903919a04007e9
Autor:
Jan Marchant, Sarah A. Fogel, Yi Yang, Steven J. Matthews, Wei-chao Lee, James A. Garnett, Andrea A. Berry, Peter Simpson, James P. Nataro, Keith G. Inman, Kristen M. Varney, Jonathan A. Levine
Publikováno v:
Biomolecular NMR Assignments. 5:1-5
Aggregative adherence fimbriae (AAF) are the primary adhesive factors of enteroaggregative Escherichia coli (EAEC) and are required for intestinal colonization. They mediate binding to extracellular matrix proteins of the enteric mucosa and display p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff55b53981a923fcda600a9c41c5892b
https://doi.org/10.1007/s12104-010-9252-7
https://doi.org/10.1007/s12104-010-9252-7
Publikováno v:
Infection and Immunity. 76:4378-4384
Enteroaggregative Escherichia coli (EAEC) adherence to human intestinal tissue is mediated by aggregative adherence fimbriae (AAF); however, the receptors involved in EAEC adherence remain uncharacterized. Adhesion to extracellular matrix proteins is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10cd9e74145cf32aebda081d8c6497ac
https://doi.org/10.1128/iai.00439-08
https://doi.org/10.1128/iai.00439-08
Autor:
James P. Nataro, Jorge J. Velarde, Keith G. Inman, Jonathan N. Fletcher, Mauricio J. Farfan, Kristen M. Varney, David J. Weber, Edward G. Dudley
Publikováno v:
Molecular Microbiology. 66:1123-1135
Enteroaggregative Escherichia coli (EAEC), increasingly recognized as an important cause of infant and travelers' diarrhoea, exhibits an aggregative, stacked-brick pattern of adherence to epithelial cells. Adherence is mediated by aggregative adheren
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8f6537acea5e0a0d04a1c3fba091e2a
https://doi.org/10.1111/j.1365-2958.2007.05985.x
https://doi.org/10.1111/j.1365-2958.2007.05985.x
Autor:
Keith G. Inman, Richard R. Rustandi, Ruiqing Yang, Donna M. Baldisseri, David J. Weber, Kristine E. Miller
Publikováno v:
Journal of Molecular Biology. 324:1003-1014
The solution NMR structure is reported for Ca(2+)-loaded S100B bound to a 12-residue peptide, TRTK-12, from the actin capping protein CapZ (alpha1 or alpha2 subunit, residues 265-276: TRTKIDWNKILS). This peptide was discovered by Dimlich and co-worke
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce7c9c5df017c4603b93e91e208229b9
https://doi.org/10.1016/s0022-2836(02)01152-x
https://doi.org/10.1016/s0022-2836(02)01152-x
Autor:
Donna M. Baldisseri, Aimee Landar, Alexander Landar, Shannon M Hamilton, Peter Nizner, David J. Weber, Keith G. Inman, Danna B. Zimmer, Richard R. Rustandi
Publikováno v:
Biochemistry. 41:788-796
S100A1, a member of the S100 protein family, is an EF-hand containing Ca(2+)-binding protein (93 residues per subunit) with noncovalent interactions at its dimer interface. Each subunit of S100A1 has four alpha-helices and a small antiparallel beta-s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bdbb82f72bf0c84f7a367be068bfb32
https://doi.org/10.1021/bi0118308
https://doi.org/10.1021/bi0118308
Publikováno v:
Biochemistry. 40:3439-3448
Backbone dynamics of homodimeric apo-S100B were studied by (15)N nuclear magnetic resonance relaxation at 9.4 and 14.1 T. Longitudinal relaxation (T(1)), transverse relaxation (T(2)), and the (15)N-[(1)H] NOE were measured for 80 of 91 backbone amide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d91a2f72ec845cd7ea06cf18b61e8fb5
https://doi.org/10.1021/bi0027478
https://doi.org/10.1021/bi0027478
Autor:
Brian R. Cannon, Keith G. Inman, Jonathan A. Levine, Nathan T. Wright, David J. Weber, Kristen M. Varney
Biological context The small (~10.5 kDa) acidic Ca2+-binding protein S100B belongs to the S100 protein family, a group of over 20 members that share significant sequence homology and undergo a large conformational change upon the addition of calcium.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7791bf571fd869b6096bcdf13afd29c6
https://europepmc.org/articles/PMC2804984/
https://europepmc.org/articles/PMC2804984/
Publikováno v:
Journal of magnetic resonance (San Diego, Calif. : 1997). 146(1)
It has recently become more widely appreciated that the presence of rotational diffusional anisotropy in proteins and other macromolecules can have a significant affect on the interpretation of NMR relaxation data in terms of molecular motion. In thi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0bc2b7a6c241903bf0792328b84ef08
https://pubmed.ncbi.nlm.nih.gov/10968959
https://pubmed.ncbi.nlm.nih.gov/10968959