Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Gerson H. Cohen"'
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 52:315-326
The crystal structure of the complex of the antibody Fab, HyHEL-5, with its antigen, hen egg-white lysozyme, has been refined at 2.65 A resolution to an R value of 0.196. The resulting model has significantly better stereochemistry than the previousl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d2e62efabc66da53940a97460af5eb5
https://doi.org/10.1107/s0907444995014855
https://doi.org/10.1107/s0907444995014855
Autor:
Tamio Fujiwara, Toshio Fujishita, Takeshi Endo, David R. Davies, Yehuda Goldgur, Hirohiko Sugimoto, Hitoshi Murai, Tomokazu Yoshinaga, Gerson H. Cohen, Robert Craigie
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 96(23)
HIV integrase, the enzyme that inserts the viral DNA into the host chromosome, has no mammalian counterpart, making it an attractive target for antiviral drug design. As one of the three enzymes produced by HIV, it can be expected that inhibitors of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f42bd47a4b4c75eb11ef1a19223c7c6
https://pubmed.ncbi.nlm.nih.gov/10557269
https://pubmed.ncbi.nlm.nih.gov/10557269
Autor:
Gerson H. Cohen, David R. Davies
There are now several crystal structures of antibody Fab fragments complexed to their protein antigens. These include Fab complexes with lysozyme, two Fab complexes with influenza virus neuraminidase, and three Fab complexes with their anti-idiotype
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3ac7ae1102bee1c3ab7d73516c66694
https://europepmc.org/articles/PMC40169/
https://europepmc.org/articles/PMC40169/
Publikováno v:
Science. 258:1161-1162
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6520ba6add536358b091deb74a4245a1
https://doi.org/10.1126/science.258.5085.1161
https://doi.org/10.1126/science.258.5085.1161
Autor:
Talapady N. Bhat, Gerson H. Cohen
Publikováno v:
Journal of Applied Crystallography. 17:244-248
A single-stage computer procedure to calculate an electron density map suitable to detect errors in a tentative macromolecular model has been developed. In this procedure, an atom of the tentative model does not contribute to the phases used to calcu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::110157cda1afc9a97c01981ffec95156
https://doi.org/10.1107/s0021889884011456
https://doi.org/10.1107/s0021889884011456
Publikováno v:
Molecular Immunology. 23:951-960
The effective assembly of an antibody molecule requires the proper association of the light and heavy chains, namely the tight, canonical association of VH with VL, and of CH1 with CL. In this paper the interaction of CH1 is examined by looking at th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bc0baca719b01678f50f8ad54d62237
https://doi.org/10.1016/0161-5890(86)90125-2
https://doi.org/10.1016/0161-5890(86)90125-2
Autor:
Se Won Suh, Gerson H. Cohen, Manuel A. Navia, Stuart Rudikoff, Talapady N. Bhat, D. N. Rao, David R. Davies
Publikováno v:
Proteins: Structure, Function, and Genetics. 1:74-80
The crystal structure of the Fab of the galactan-binding immunoglobulin J539 (a mouse IgA,kappa) has been determined at a resolution of approximately 2.6 A by X-ray diffraction. The starting model was that obtained from the real space search describe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c46843f3db9d6e59d0bdf598e45539db
https://doi.org/10.1002/prot.340010112
https://doi.org/10.1002/prot.340010112
Publikováno v:
Molecular Immunology. 23:475-488
The amino acid sequences of the constant regions of rabbit kappa light chains (C kappa) are remarkably divergent. The K1 allotypes differ at 47 of 106 positions; the K1 and K2 isotypes differ at three additional positions. Variability and structural
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f510b4a928da3430fcf75c3b43c27496
https://doi.org/10.1016/0161-5890(86)90111-2
https://doi.org/10.1016/0161-5890(86)90111-2
Publikováno v:
Journal of Molecular Biology. 190:593-604
The crystal structure of the Fab of McPC603, a phosphocholine-binding mouse myeloma protein, has been refined at 2.7 A resolution by a combination of restrained least-squares refinement and molecular modeling. The overall structure remains as previou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3bb435d436d32915ddc5b9577e0bc6a0
https://doi.org/10.1016/0022-2836(86)90245-7
https://doi.org/10.1016/0022-2836(86)90245-7
Autor:
David R. Davies, Sandra J. Smith-Gill, Gerson H. Cohen, Enid W. Silverton, Steven Sheriff, Eduardo A. Padlan
Publikováno v:
Proceedings of the National Academy of Sciences. 86:5938-5942
The crystal structure of the complex of the anti-lysozyme HyHEL-10 Fab and hen egg white lysozyme has been determined to a nominal resolution of 3.0 A. The antigenic determinant (epitope) on the lysozyme is discontinuous, consisting of residues from
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2eac979adee3d3fde06ff20011b09cf4
https://doi.org/10.1073/pnas.86.15.5938
https://doi.org/10.1073/pnas.86.15.5938