Zobrazeno 1 - 10 of 22 pro vyhledávání: '"S J, Remington"'
1
‘Collagen Vitrigel Sheet’ as a Novel Drug Delivery Bio-material
Autor: Michitaka Ozaki, Toshiaki Takezawa, Takeaki Ozawa, S. J. Remington, Naoki Morita, Sanae Haga
Publikováno v: IFMBE Proceedings ISBN: 9783642235078
Background/Aims. Ischemia/reperfusion (I/R)- induced injury is an acute injury mainly caused by surgical procedures. And HGF (hepatocyte growth factor) is known to protect against I/R-injury effectively. The sufficient dose of HGF must be topically d
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::198653a86c22f97c9bc536ee7225f601
https://doi.org/10.1007/978-3-642-23508-5_349
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3
Crystallographic and energetic analysis of binding of selected anions to the yellow variants of green fluorescent protein
Autor: R M, Wachter, D, Yarbrough, K, Kallio, S J, Remington
Publikováno v: Journal of molecular biology. 301(1)
The fluorescence emission of yellow fluorescent proteins (YFPs) has been shown to respond rapidly and reversibly to changes in the concentration of some small anions such as halides; this allows for the use of YFPs as genetically encodable Cl(-) sens
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d81794b8121e2f2507f15df81e85b484
https://pubmed.ncbi.nlm.nih.gov/10926499
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5
Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability
Autor: K C, Usher, A F, de la Cruz, F W, Dahlquist, R V, Swanson, M I, Simon, S J, Remington
Publikováno v: Protein science : a publication of the Protein Society. 7(2)
The crystal structure of CheY protein from Thermotoga maritima has been determined in four crystal forms with and without Mg++ bound, at up to 1.9 A resolution. Structural comparisons with CheY from Escherichia coli shows substantial similarity in th
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::fa409f985efb8c919a8b028f54d06b51
https://pubmed.ncbi.nlm.nih.gov/9521117
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6
Crystal structure and photodynamic behavior of the blue emission variant Y66H/Y145F of green fluorescent protein
Autor: Roger Heim, S. J. Remington, Roger Y. Tsien, K. Kallio, Rebekka M. Wachter, B A King, Steven G. Boxer
Publikováno v: Biochemistry. 36(32)
The crystal structure of a blue emission variant (Y66H/Y145F) of the Aequorea victoria green fluorescent protein has been determined by molecular replacement and the model refined. The crystallographic R-factor is 18.1% for all data from 20 to 2.1 A,
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a1ba4872b1a23f53239f7fbdb4aae44
https://pubmed.ncbi.nlm.nih.gov/9245407
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7
Structures of active site histidine mutants of IIIGlc, a major signal-transducing protein in Escherichia coli. Effects on the mechanisms of regulation and phosphoryl transfer
Autor: J G, Pelton, D A, Torchia, S J, Remington, K P, Murphy, N D, Meadow, S, Roseman
Publikováno v: The Journal of biological chemistry. 271(52)
IIIGlc (also called IIAGlc), a major signal-transducing protein in Escherichia coli, is also a phosphorylcarrier in glucose uptake. The crystal and NMR structures of IIIGlc show that His90, the phosphoryl acceptor, adjoins His75 in the active site. G
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bb81c27bd6e2203087a3d13e50c16171
https://pubmed.ncbi.nlm.nih.gov/8969208
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8
Effects of introduced aspartic and glutamic acid residues on the P'1 substrate specificity, pH dependence and stability of carboxypeptidase Y
Autor: H R, Stennicke, U H, Mortensen, U, Christensen, S J, Remington, K, Breddam
Publikováno v: Protein engineering. 7(7)
Carboxypeptidase Y is a serine carboxypeptidase isolated from Saccharomyces cerevisiae with a preference for C-terminal hydrophobic amino acid residues. In order to alter the inherent substrate specificity of CPD-Y into one for basic amino acid resid
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f54421975fd46258d1fd9bff8880887b
https://pubmed.ncbi.nlm.nih.gov/7971953
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10
Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase
Autor: J H, Hurley, H R, Faber, D, Worthylake, N D, Meadow, S, Roseman, D W, Pettigrew, S J, Remington
Publikováno v: Science (New York, N.Y.). 259(5095)
The phosphocarrier protein IIIGlc is an integral component of the bacterial phosphotransferase (PTS) system. Unphosphorylated IIIGlc inhibits non-PTS carbohydrate transport systems by binding to diverse target proteins. The crystal structure at 2.6 A
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::90357f3d501f73ee3f222d2a698f3ae5
https://pubmed.ncbi.nlm.nih.gov/8430315
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