Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Dorothea Kominos"'
Publikováno v:
International Journal of Quantum Chemistry. 75:187-195
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::934d81f84f65c309438991ebdd4aab98
https://doi.org/10.1002/(sici)1097-461x(1999)75:3<187::aid-qua8>3.0.co
https://doi.org/10.1002/(sici)1097-461x(1999)75:3<187::aid-qua8>3.0.co
Autor:
Mei S. Duguid, Jurcak John G, Ram Dharanipragada, Rachel Wang, Matthew A. Smicker, Kwon Yon Musick, Xiping Bi, Ashfaq Parkar, Jane Peppard, Ying Zhang, Zhicheng Zhao, Nisha Zaidi, Choi Yong-Mi, Jeremy Fordham, Gillespy Timothy Alan, Dorothea Kominos, Matthieu Barrague, Larry R. McLean
Publikováno v:
Bioorganicmedicinal chemistry letters. 22(9)
Beginning with a screening hit, unique thienopyrazole-indole inhibitors of Itk (interleukin-2-inducible tyrosine kinase) were designed, synthesized, and crystallized in the target kinase. Although initial compounds were highly active in Itk, they wer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7571214176f5282eafced780512a7d95
https://pubmed.ncbi.nlm.nih.gov/22464456
https://pubmed.ncbi.nlm.nih.gov/22464456
Autor:
Steven E. Shoelson, Joseph Schlessinger, Steven Jacques, Dorothea Kominos, Chi-Hon Lee, Ben Margolis, John Kuriyan
Publikováno v:
Structure. 2:423-438
Background Src homology 2 (SH2) domains bind to phosphotyrosine residues in a sequence-specific manner, and thereby couple tyrosine phosphorylation to changes in the localization or catalytic activity of signal transducing molecules. Current understa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ea8f7c3a36d684d75269e693c1c70e1
https://doi.org/10.1016/s0969-2126(00)00044-7
https://doi.org/10.1016/s0969-2126(00)00044-7
Autor:
David Cowburn, Bruce J. Mayer, Nalin Pant, Marilyn D. Resh, Carlos B. Rios, Lauren Silverman, David Baltimore, John Kuriyan, Raymond B. Birge, Hidesaburo Hanafusa, Scott C. Robertson, Michael Overduin, Gabriel Waksman, Dorothea Kominos
Publikováno v:
Nature. 358:646-653
Three-dimensional structures of complexes of the SH2 domain of the v-src oncogene product with two phosphotyrosyl peptides have been determined by X-ray crystallography at resolutions of 1.5 and 2.0 A, respectively. A central antiparallel beta-sheet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcc9b0e8c9e72bfaa3c9f671e71042c3
https://doi.org/10.1038/358646a0
https://doi.org/10.1038/358646a0
Publikováno v:
Journal of Magnetic Resonance (1969). 97:398-410
The use of structural information derived from NMR data, when combined with computer modeling techniques, has enabled the structures of many proteins to be determined ( 1-6). Among the most useful structural information is interproton distances which
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::23cda973397db84189c35ceb0710d1ba
https://doi.org/10.1016/0022-2364(92)90325-2
https://doi.org/10.1016/0022-2364(92)90325-2
Publikováno v:
Chemical Physics. 158:295-301
Molecular-dynamics simulations of the partial unfolding of α-lactalbumin are described. The effects of introducing various intramolecular constraints on the unfolding are compared. In one set of simulations, intrahelical constraints designed to forc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e823152a635099022ab2b8ae86e0a6b6
https://doi.org/10.1016/0301-0104(91)87073-5
https://doi.org/10.1016/0301-0104(91)87073-5
Autor:
Nigel S. Scrutton, John Kuriyan, Alan Berry, Dorothea Kominos, Anthony Cerami, Nicholas J. Murgolo, Graeme B. Henderson, Richard N. Perham, Klara Osapay, Nigel W. Hinchliffe
Publikováno v:
Proceedings of the National Academy of Sciences. 88:8769-8773
Glutathione reductase (EC 1.6.4.2; CAS registry number 9001-48-3) and trypanothione reductase (CAS registry number 102210-35-5), which are related flavoprotein disulfide oxidoreductases, have marked specificities for glutathione and trypanothione, re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::874dc4194adb30170020077e6217ceb7
https://doi.org/10.1073/pnas.88.19.8769
https://doi.org/10.1073/pnas.88.19.8769
Autor:
Dorothea Kominos, Ronald M. Levy, Jean Baum, Yuan Chen, Victor M. Garsky, Steven M. Pitzenberger, Gautam Sanyal, Asif K. Suri, Adel M. Naylor
Publikováno v:
Journal of Biomolecular NMR. 4
The snake venom protein echistatin contains the cell recognition sequence Arg-Gly-Asp and is a potent inhibitor of platelet aggregation. The three-dimensional structure of echistatin and the dynamics of the active RGD site are presented. A set of str
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d231eb103cb4e34e895ca11815c4d353
https://doi.org/10.1007/bf00179342
https://doi.org/10.1007/bf00179342
Publikováno v:
Protein engineering. 6(6)
A Monte Carlo method is presented which can obtain the correct tertiary fold of a protein given the secondary structure and as few as three interactions between each secondary structure unit. This method was used to fold hemerythrin, flavodoxin, bovi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14c8e590471fd83ec99a462bffa1fc9e
https://pubmed.ncbi.nlm.nih.gov/7694274
https://pubmed.ncbi.nlm.nih.gov/7694274
Publikováno v:
Biopolymers. 29(14)
The side-chain conformations have been analyzed in the antimicrobial peptide, Neutrophil Peptide-5 (NP-5), whose structure was independently generated from nmr-derived distance constraints using a distance geometry algorithm. The side-chain and pepti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90f62ea67a4de4b2e940804d9eb3e9fe
https://pubmed.ncbi.nlm.nih.gov/2207287
https://pubmed.ncbi.nlm.nih.gov/2207287