Zobrazeno 1 - 10
of 101
pro vyhledávání: '"Richard B. Honzatko"'
Autor:
Supreet Kaur, Nicholas S. Nieto, Peter McDonald, Josh R. Beck, Richard B. Honzatko, Anuradha Roy, Scott W. Nelson
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 37, Iss 1, Pp 1320-1326 (2022)
Malaria is caused by infection with protozoan parasites of the Plasmodium genus, which is part of the phylum Apicomplexa. Most organisms in this phylum contain a relic plastid called the apicoplast. The apicoplast genome is replicated by a single DNA
Externí odkaz:
https://doaj.org/article/b8a4728eceee430bb8cbaf513d0499d2
Autor:
Robert L. Jernigan, Richard B. Honzatko, Sayane Shome, Richard Weerts, Jacqueline J Ehrlich, Alan T. Culbertson, Olga A. Zabotina
Publikováno v:
Plantcell physiology. 62(12)
Glycosyltransferases (GTs) are a large family of enzymes that add sugars to a broad range of acceptor substrates, including polysaccharides, proteins and lipids, by utilizing a wide variety of donor substrates in the form of activated sugars. Individ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc683a13f50066ac69dc61fb276c3098
https://pubmed.ncbi.nlm.nih.gov/34265062
https://pubmed.ncbi.nlm.nih.gov/34265062
Autor:
Jun-Yong Choe, Olga A. Zabotina, Richard B. Honzatko, Jacqueline J Ehrlich, Alan T. Culbertson
Publikováno v:
Proceedings of the National Academy of Sciences. 115:6064-6069
The plant cell wall is primarily a polysaccharide mesh of the most abundant biopolymers on earth. Although one of the richest sources of biorenewable materials, the biosynthesis of the plant polysaccharides is poorly understood. Structures of many es
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a67ef5d8050d02812565c8b9e6c61f58
https://doi.org/10.1073/pnas.1801105115
https://doi.org/10.1073/pnas.1801105115
Publikováno v:
Journal of Molecular Biology. 428:3920-3934
Plasmodium falciparum , the primary cause of malaria, contains a non-photosynthetic plastid called the apicoplast. The apicoplast exists in most members of the phylum Apicomplexa and has its own genome along with organelle-specific enzymes for its re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45054cb1b273c45fa15e0f7ad6cd5bcd
https://doi.org/10.1016/j.jmb.2016.07.016
https://doi.org/10.1016/j.jmb.2016.07.016
Publikováno v:
Acta Crystallographica Section F Structural Biology Communications. 71:333-337
Infection by the parasitePlasmodium falciparumis the leading cause of malaria in humans. The parasite has a unique and essential plastid-like organelle called the apicoplast. The apicoplast contains a genome that undergoes replication and repair thro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4949f61d3a92770652cf337c8c111de
https://doi.org/10.1107/s2053230x15002423
https://doi.org/10.1107/s2053230x15002423
Publikováno v:
Journal of Biological Chemistry. 287:6840-6850
Abietadiene synthase from Abies grandis (AgAS) is a model system for diterpene synthase activity, catalyzing class I (ionization-initiated) and class II (protonation-initiated) cyclization reactions. Reported here is the crystal structure of AgAS at
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::204d635d72d9ddc8fd4425026c989126
https://doi.org/10.1074/jbc.m111.337592
https://doi.org/10.1074/jbc.m111.337592
Autor:
Nathaniel D. Ginder, Richard B. Honzatko, Jay C. Nix, Amy H. Andreotti, Raji E. Joseph, Julie A. Hoy
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67:269-273
Proline is a unique amino acid owing to the relatively small energy difference between the cis and trans conformations of its peptide bond. The X-Pro imide bond readily undergoes cis-trans isomerization in the context of short peptides as well as som
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81f110431f3b9d3a5f9f2528512de9ab
https://doi.org/10.1107/s1744309110052346
https://doi.org/10.1107/s1744309110052346
Autor:
Christopher F. Basler, Zbyszek Otwinowski, Mina Farahbakhsh, Luke A. Helgeson, Tianjiao Wang, Parameshwaran Ramanan, Daisy W. Leung, Richard B. Honzatko, Gaya K. Amarasinghe, Dominika Borek, Kathleen C. Prins, Jay C. Nix
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66:689-692
VP35 is one of seven structural proteins encoded by the Ebola viral genome and mediates viral replication, nucleocapsid formation and host immune suppression. The C-terminal interferon inhibitory domain (IID) of VP35 is critical for dsRNA binding and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a199eaf8e7ee6ea0baa55e01ff70907f
https://doi.org/10.1107/s1744309110013266
https://doi.org/10.1107/s1744309110013266
Autor:
Julie A. Hoy, Richard B. Honzatko, Nathaniel D. Ginder, Peter J. Reilly, Christopher D. Warner, Michael Linnen, Clark Ford, Taran C. Shilling
Publikováno v:
Applied and Environmental Microbiology. 76:338-346
A gene encoding a glycoside hydrolase family 44 (GH44) protein from Clostridium acetobutylicum ATCC 824 was synthesized and transformed into Escherichia coli. The previously uncharacterized protein was expressed with a C-terminal His tag and purified
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74f7e0363c19eca09b687a7865cd9e9d
https://doi.org/10.1128/aem.02026-09
https://doi.org/10.1128/aem.02026-09
Autor:
D.B Fulton, Richard B. Honzatko, Nathaniel D. Ginder, Christopher F. Basler, Gaya K. Amarasinghe, Jay C. Nix, Daisy W. Leung
Publikováno v:
Proceedings of the National Academy of Sciences. 106:411-416
Ebola viruses (EBOVs) cause rare but highly fatal outbreaks of viral hemorrhagic fever in humans, and approved treatments for these infections are currently lacking. The Ebola VP35 protein is multifunctional, acting as a component of the viral RNA po
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32d5e4ee68659d2fea4408b4298b3e0a
https://doi.org/10.1073/pnas.0807854106
https://doi.org/10.1073/pnas.0807854106