Zobrazeno 1 - 10 of 12 pro vyhledávání: '"R W, Janes"'
1
The Novel GABAA Receptor Ligand NNC 14-0764: 5-(3-Cyclopropyl-1,2,4-oxadiazol-5-yl)-2,3-dihydrodiimidazo[1,5-a:1',2'-c]quinazoline
Autor: A.L. Corper, Rex A. Palmer, R. W. Janes, J. N. Lisgarten, H.C. Hansen
Publikováno v: Acta Crystallographica Section C Crystal Structure Communications. 51:318-322
The structure was solved by direct methods and refined by full-matrix least squares using SHELX76 (Sheldrick, 1976). A difference map after anisotropic refinement of the TTT molecule revealed the peaks for all H atoms of TTT and additional prominent
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d3049efc5f961ed0f10f780977f303aa
https://doi.org/10.1107/s0108270194004166
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2
Structures of chromium(III) cyclam complexes. 2. Structure of trans-dibromo(1,4,8,11-tetraazacyclotetradecane)chromium(III) bromide
Autor: Colin D. Flint, Dominique Maes, Rex A. Palmer, R. W. Janes, J. N. Lisgarten, D. M. Gazi, C. G. Dealwis
Publikováno v: Acta Crystallographica Section C Crystal Structure Communications. 46:396-399
The crystal and molecular structure of trans-dichloro(1,4,8,11-tetraazacyclotetradecaneN,N',N'',N'')chromium(III) isothiocyanate has been determined. The cyclam (1,4,8,11-tetraazacyclotetradecane) moiety exists in a chair conformation located on a cr
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5d13f4efe92b61b8bbd0ff188648374d
https://doi.org/10.1107/s0108270189011248
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3
Resistance-associated point mutations of organophosphate insensitive acetylcholinesterase, in the olive fruit fly Bactrocera oleae
Autor: J G, Vontas, M J, Hejazi, N J, Hawkes, N, Cosmidis, M, Loukas, R W, Janes, J, Hemingway
Publikováno v: Insect molecular biology. 11(4)
A 2.2-kb full length cDNA containing an ORF encoding a putative acetylcholinesterase (AChE) precursor of 673 amino acid residues was obtained by a combined degenerate PCR and RACE strategy from an organophosphate-susceptible Bactrocera oleae strain.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd5b3a75551c3e96b1dbf7228446aadf
https://pubmed.ncbi.nlm.nih.gov/12144698
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5
Tryptophans in membrane proteins. X-ray crystallographic analyses
Autor: B A, Wallace, R W, Janes
Publikováno v: Advances in experimental medicine and biology. 467
While tryptophans are generally found in low abundance in soluble proteins, in many integral membrane proteins they comprise a significantly higher proportion of the amino acid composition. Now that crystal structures are available for a number of me
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e1bb6dac32741b2b1b65e812e0d2f28c
https://pubmed.ncbi.nlm.nih.gov/10721132
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6
Screening of a library of phage-displayed peptides identifies human bcl-2 as a taxol-binding protein
Autor: D J, Rodi, R W, Janes, H J, Sanganee, R A, Holton, B A, Wallace, L, Makowski
Publikováno v: Journal of molecular biology. 285(1)
A random library of phage displayed peptides was screened for binding to a biotinylated derivative of paclitaxel (Taxol). Affinity-selected peptides were analyzed for similarity to human proteins. There was no significant similarity between the pacli
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7700db236952ba812f2d3e9e40cf5c00
https://pubmed.ncbi.nlm.nih.gov/9878399
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7
The crystal structure of human endothelin-1 and how it relates to receptor binding
Autor: B A, Wallace, R W, Janes
Publikováno v: Journal of cardiovascular pharmacology. 26
Several different three-dimensional structures have recently been proposed for human endothelin-1 (ET-1) based on x-ray crystallographic, NMR spectroscopic, and modeling studies. All differ considerably in the regions that are critical for receptor b
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b6571927b0c2eb2889e3264731697196
https://pubmed.ncbi.nlm.nih.gov/8587379
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8
A comparison of X-ray and NMR structures for human endothelin-1
Autor: B A, Wallace, R W, Janes, D A, Bassolino, S R, Krystek
Publikováno v: Protein science : a publication of the Protein Society. 4(1)
Direct comparisons between the recently solved X-ray and NMR structures of human endothelin-1 with respect to secondary structure, RMS deviations, surface accessibilities, and side-chain conformers indicate important differences in conformation, espe
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5335369f8f3d694b4b6e6a091ca4801a
https://pubmed.ncbi.nlm.nih.gov/7773179
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9
Co-crystals of gramicidin A and phospholipid. A system for studying the structure of a transmembrane channel
Autor: B A, Wallace, R W, Janes
Publikováno v: Journal of molecular biology. 217(4)
Single crystals of a complex of gramicidin A, a transmembrane channel-forming polypeptide, and dipalmitoyl phosphatidylcholine, a phospholipid, have been prepared and characterized by X-ray diffraction. They belong to space group P222(1), with unit c
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c58827a6d2db18023c1d3d0878779459
https://pubmed.ncbi.nlm.nih.gov/1706436
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