Zobrazeno 1 - 10
of 78
pro vyhledávání: '"Steve W. Homans"'
Autor:
Steve W. Homans, Kazumi Hiruma-Shimizu, Simon G. Patching, Arnout P. Kalverda, Peter J. F. Henderson
Publikováno v:
Journal of Labelled Compounds and Radiopharmaceuticals. 57:737-743
This work reports the first synthesis of uniformly deuterated n-dodecyl-β-D-maltoside (d39-DDM). DDM is a mild non-ionic detergent often used in the extraction and purification of membrane proteins and for solubilizing them in experimental studies o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4406dfe99de0c1d6d5a049bd87641f91
https://doi.org/10.1002/jlcr.3249
https://doi.org/10.1002/jlcr.3249
Autor:
Georgina Cox, Andreas Savelsbergh, Gary S. Thompson, Thomas A. Edwards, Frank Peske, Wolfgang Wintermeyer, Huw T. Jenkins, Steve W. Homans, Alex J. O'Neill, Marina V. Rodnina
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Resistance to the antibiotic fusidic acid (FA) in the human pathogen Staphylococcus aureus usually results from expression of FusB-type proteins (FusB or FusC). These proteins bind to elongation factor G (EF-G), the target of FA, and rescue translati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71cac9411f5b312e127ae0867efe4d4f
https://doi.org/10.1073/pnas.1117275109
https://doi.org/10.1073/pnas.1117275109
Publikováno v:
Molecular Cell
Summary Numerous studies of amyloid assembly have indicated that partially folded protein species are responsible for initiating aggregation. Despite their importance, the structural and dynamic features of amyloidogenic intermediates and the molecul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d1cb0d6dcb3c5c391478d5c443112ef
https://doi.org/10.1016/j.molcel.2010.11.028
https://doi.org/10.1016/j.molcel.2010.11.028
Autor:
Sheena E. Radford, Walraj S. Gosal, Andrew L. Hellewell, Eric W. Hewitt, Wei-Feng Xue, Steve W. Homans
Publikováno v:
The Journal of Biological Chemistry
Fibrils associated with amyloid disease are molecular assemblies of key biological importance, yet how cells respond to the presence of amyloid remains unclear. Cellular responses may not only depend on the chemical composition or molecular propertie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ccc1ff03f2f42a3db64e17fe06bc765e
http://europepmc.org/articles/PMC2797196
http://europepmc.org/articles/PMC2797196
Publikováno v:
Protein Engineering, Design and Selection
Amyloid fibrils are proteinaceous nano-scale linear aggregates. They are of key interest not only because of their association with numerous disorders, such as type II diabetes mellitus, Alzheimer's and Parkinson's diseases, but also because of their
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4c0ff7ca6346b67994826fdae7188fd
http://europepmc.org/articles/PMC2719499
http://europepmc.org/articles/PMC2719499
Autor:
Wolfgang Jahnke, Gregg Siegal, Thomas L. James, Jeff Peng, Steve W. Homans, Claudio Dalvit, Ernest Giralt, Claudio Luchinat, Ivano Bertini, Maurizio Pellecchia, David Cowburn, Horst Kessler, Harald Schwalbe, Hartmut Oschkinat, Bernd Meyer
Publikováno v:
Nature reviews, 7: 738–745
In the past decade, the potential of harnessing the ability of nuclear magnetic resonance (NMR) spectroscopy to monitor intermolecular interactions as a tool for drug discovery has been increasingly appreciated in academia and industry. In this Persp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66e72586c4b550fc2eae5c33ab506aca
https://doi.org/10.1038/nrd2606
https://doi.org/10.1038/nrd2606
Autor:
Arnout P. Kalverda, Stuart L. Warriner, Henning Stöckmann, Agnieszka K. Bronowska, Neil R. Syme, Steve W. Homans, Gary S. Thompson
Publikováno v:
Journal of the American Chemical Society. 130:12420-12426
In studies on the thermodynamics of ligand-protein interactions, it is often assumed that the configurational and conformational entropy of the ligand is zero in the bound state (i.e., the ligand is rigidly fixed in the binding pocket). However, ther
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d161b7cb8ee08f8523097c4e7e1d4e8
https://doi.org/10.1021/ja803755m
https://doi.org/10.1021/ja803755m
Publikováno v:
Journal of Molecular Biology
Amyloid is a highly ordered form of aggregate comprising long, straight and unbranched proteinaceous fibrils that are formed with characteristic nucleation-dependent kinetics in vitro. Currently, the structural molecular mechanism of fibril nucleatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b112cefb5b6979041ca50ab3e7c3c69
https://doi.org/10.1016/j.jmb.2008.01.092
https://doi.org/10.1016/j.jmb.2008.01.092
Publikováno v:
Journal of Biomolecular NMR. 39:239-245
Here we present a suite of pulse sequences for the measurement of (15)N T(1), T(1rho) and NOE data that combine traditional TROSY-based pulse sequences with band-selective Hadamard frequency encoding. The additive nature of the Hadamard matrix produc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d251bc9029423140f4eb5e6e3c5b801
https://doi.org/10.1007/s10858-007-9192-4
https://doi.org/10.1007/s10858-007-9192-4
Autor:
Steve W. Homans
Publikováno v:
Drug Discovery Today. 12:534-539
Biological processes depend on specific recognition between molecules with carefully tuned affinities. Because of the complexity of the problem, binding affinities cannot reliably be computed from molecular structures. Modern biophysical techniques c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6177db3471226e29e2bb30ea5d3be5bf
https://doi.org/10.1016/j.drudis.2007.05.004
https://doi.org/10.1016/j.drudis.2007.05.004