Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Hannes Simader"'
Publikováno v:
Nucleic Acids Research
Nucleic acids symposium series 41(1), 667-676 (2013). doi:10.1093/nar/gks1072
Nucleic acids symposium series 41(1), 667-676 (2013). doi:10.1093/nar/gks1072
In the yeast Saccharomyces cerevisiae, the aminoacyl-tRNA synthetases (aaRS) GluRS and MetRS form a complex with the auxiliary protein cofactor Arc1p. The latter binds the N-terminal domains of both synthetases increasing their affinity for the trans
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8654452d329a088f9adb13c05a8c131f
https://doi.org/10.1093/nar/gks1072
https://doi.org/10.1093/nar/gks1072
Autor:
Stefan Gerhardt, Andrew David Morley, Peter W. Kenny, Hannes Simader, Emma V. Jones, Galith Karoutchi, Stephan Krapp, Neil Rankine, Keith Oldham, Paul A. Bethel, Stefan Steinbacher, Martin Augustin
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 19:4622-4625
A number of molecular recognition features have been exploited in structure-based design of selective Cathepsin inhibitors.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b5e987a8e0f4a810fd0d5bfae2d2508
https://doi.org/10.1016/j.bmcl.2009.06.090
https://doi.org/10.1016/j.bmcl.2009.06.090
Autor:
Neil Rankine, Linda J. Wood, Galith Karoutchi, Michelle Coulson, Keith Oldham, Emma V. Jones, Paul A. Bethel, Stephan Krapp, Susannah J. Ford, Stefan Gerhardt, David Ryan, Matthew Grist, Peter W. Kenny, Hannes Simader, Andrew David Morley, Stuart L. Wells, Gordon A. Hamlin, Stefan Steinbacher, Jack E. Dawson, Nabil Asaad, Martin Augustin, Michael James
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 19:4280-4283
A series of potent Cathepsin L inhibitors with good selectivity with respect to other cysteine Cathepsins is described and SAR is discussed with reference to the crystal structure of a protein-ligand complex.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca39a993160acd7584b90a963ada1ade
https://doi.org/10.1016/j.bmcl.2009.05.071
https://doi.org/10.1016/j.bmcl.2009.05.071
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 62:1510-1519
Eukaryotic aminoacyl-tRNA synthetases (aaRS) frequently contain additional appended domains that are absent from their prokaryotic counterparts which mediate complex formation between eukaryotic aaRS and cofactors of aminoacylation and translation. H
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ea6f242801533bfb180a476adbcbe07
https://doi.org/10.1107/s0907444906039850
https://doi.org/10.1107/s0907444906039850
Autor:
Dietrich Suck, Michael Hothorn, Hannes Simader, Jérôme Basquin, George Simos, Christine Köhler
Publikováno v:
Nucleic Acids Research
The yeast aminoacyl-tRNA synthetase (aaRS) complex is formed by the methionyl- and glutamyl-tRNA synthetases (MetRS and GluRS, respectively) and the tRNA aminoacylation cofactor Arc1p. It is considered an evolutionary intermediate between prokaryotic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2316012356a92830270d5176a9be01e
https://doi.org/10.1093/nar/gkl560
https://doi.org/10.1093/nar/gkl560
Autor:
Hannes Simader, Dietrich Suck
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62:346-349
Eukaryotic aminoacyl-tRNA synthetases (aaRSs) must be integrated into an efficient tRNA-export and shuttling machinery. This is reflected by the presence of additional protein-protein interaction domains and a correspondingly higher degree of complex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dadefc993c558360059e119ecfee01ec
https://doi.org/10.1107/s1744309106005823
https://doi.org/10.1107/s1744309106005823
Publikováno v:
Journal of molecular biology. 374(4)
Eukaryotic aminoacyl-tRNA synthetases are usually organized into high-molecular-weight complexes, the structure and function of which are poorly understood. We have previously described a yeast complex containing two aminoacyl-tRNA synthetases, methi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb9d332c18e5060e4db58b2d997b4cb6
https://pubmed.ncbi.nlm.nih.gov/17976650
https://pubmed.ncbi.nlm.nih.gov/17976650
Publikováno v:
Acta Crystallographica Section A Foundations of Crystallography. 62:s23-s23
Bcl-2 family proteins play a central role in regulating the intrinsic apoptotic pathway. Pro-survival family members such as Bcl-2, Bcl-xL, Bcl-w,Mcl-1 andA1 protect cells from apoptosis. Pro-apoptotic BH3-only proteins such as Bim, Puma, Noxa, Bad,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::53202815959a7b592c9fcd37a1e70cec
https://doi.org/10.1107/s0108767306099533
https://doi.org/10.1107/s0108767306099533