Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Rod E. Hubbard"'
Autor:
F. Javier Luque, Natalia Matassova, Xavier Barril, James Murray, Rod E. Hubbard, Peter Schmidtke, Ben Davis, Stephen D. Roughley, Sergio Ruiz-Carmona, Lisa Baker
Publikováno v:
Nature chemistry. 9(3)
There is a pressing need for new technologies that improve the efficacy and efficiency of drug discovery. Structure-based methods have contributed towards this goal but they focus on predicting the binding affinity of protein-ligand complexes, which
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8061d6d1e0af12622c47d078ec631b21
https://pubmed.ncbi.nlm.nih.gov/28221352
https://pubmed.ncbi.nlm.nih.gov/28221352
Autor:
John Gary Montana, Paul V. Murphy, Ruth Elizabeth Wills, Rod E. Hubbard, Richard J. K. Taylor, David T. Manallack
Publikováno v:
Bioorganic & Medicinal Chemistry. 6:2421-2439
The design and synthesis of a series of analogues of sialyl Lewisx (1) which incorporate conformationally rigid tetralin and naphthalene ring systems (2–4) has led to novel compounds which have similar potency to 1 as inhibitors of cell adhesion.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17a6cd5b7b4a61917d0d5c4090a5562e
https://doi.org/10.1016/s0968-0896(98)80017-5
https://doi.org/10.1016/s0968-0896(98)80017-5
Publikováno v:
Tetrahedron Letters. 39:3273-3276
The synthesis of conformationally rigid tetralin-based mimics of the tetrasaccharide sialyl Lewisx are described. Palladium catalysed coupling reactions are employed in the key synthetic steps.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::700cdce9e3ddd33e91896341b7c82e42
https://doi.org/10.1016/s0040-4039(98)00468-7
https://doi.org/10.1016/s0040-4039(98)00468-7
Publikováno v:
Carbohydrate Research. 287:247-253
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::385cca790ecdf2b6a8ba3555c8371300
https://doi.org/10.1016/0008-6215(96)00077-8
https://doi.org/10.1016/0008-6215(96)00077-8
Autor:
Anthony J. Wilkinson, Eleanor J. Dodson, Guy Dodson, Jeremy R. H. Tame, Robert C. Liddington, Massimo Paoli, Rod E. Hubbard
Publikováno v:
Proceedings of the Royal Society of London. Series A: Mathematical and Physical Sciences. 442:193-205
The reconstruction of the electron density of molecules in crystals from X-ray diffraction measurements depends on the exactness of the packing of the molecules in the unit cell and the crystal lattice. Crystals of T-state haemoglobin, the low affini
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6f0e45c2ce2bdc1142dbb00c2e440762
https://doi.org/10.1098/rspa.1993.0099
https://doi.org/10.1098/rspa.1993.0099
Publikováno v:
Journal of Molecular Biology. 228:551-579
The origin of co-operativity in haemoglobin (Hb) resides in the reduced affinity of the T-state. T-state Hb crystals grown from polyethyleneglycol can be liganded without the molecule switching to the R high affinity state. X-ray analysis of T-state
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3669541baaeae0db7d965b19d1cfe699
https://doi.org/10.1016/0022-2836(92)90842-8
https://doi.org/10.1016/0022-2836(92)90842-8
Publikováno v:
ImmunoMethods. 1:71-79
The antigen combining site of antibody molecules consists of six separate loops supported by a conserved β-sheet framework. The specificity of the antibody is conferred by the structure of these loops, which in turn is related to their length and se
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::944cfbabf417c1d6f94a54d12bfa649c
https://doi.org/10.1016/s1058-6687(05)80030-0
https://doi.org/10.1016/s1058-6687(05)80030-0
Autor:
Carl Dudley Jarman, Chris Holt, Rod E. Hubbard, Andrew G. McArthur, Peter J. Lillford, Sarah Twigg, Dawn Worrall, Paul D. A. Pudney, Chris Sidebottom, Sarah L. Buckley, J. H. Telford
Publikováno v:
Nature. 406(6793)
We have discovered an antifreeze protein1 in an overwintering perennial ryegrass, Lolium perenne. The protein is stable at 100 °C and although it is a less effective antifreeze than proteins found in antarctic fish and insects, it is better at preve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a168fb51bf12dcbff8338775c3b01509
https://pubmed.ncbi.nlm.nih.gov/10917514
https://pubmed.ncbi.nlm.nih.gov/10917514
Publikováno v:
Molecular Modeling and Prediction of Bioactivity ISBN: 9781461368571
The Selectin family of proteins comprises three carbohydrate binding proteins (E, P and L) involved in cell adhesion events1. In response to inflammatory stimuli, these proteins play a crucial role in the recognition of sialyl Lewis X (sLeX) and rela
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bea2e21b69062dd872d86876e031ddeb
https://doi.org/10.1007/978-1-4615-4141-7_82
https://doi.org/10.1007/978-1-4615-4141-7_82
Autor:
Christine A. Power, Arlene J. Hoogewerf, Gabriele S. V. Kuschert, Rod E. Hubbard, Timothy N. C. Wells
Publisher Summary This chapter develops a solid-phase binding assay for chemokine-glycosaminoglycan interactions. Optimization and validation studies were performed to recognize and avoid significant ligand depletion, retain a significant signal-to-n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c92d21ca8227e033163ef213d27bc7e9
https://doi.org/10.1016/s0076-6879(97)87025-5
https://doi.org/10.1016/s0076-6879(97)87025-5