Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Christine A Oellig"'
Autor:
My-Hang Huynh, Marijo S. Roiko, Angelica O. Gomes, Ellyn N. Schinke, Aric J. Schultz, Swati Agrawal, Christine A. Oellig, Travis R. Sexton, Jessica M. Beauchamp, Julie Laliberté, Komagal Kannan Sivaraman, Louis B. Hersh, Sheena McGowan, Vern B. Carruthers
Publikováno v:
mSphere, Vol 6, Iss 3 (2021)
After replicating within infected host cells, the single-celled parasite Toxoplasma gondiiT. gondii
Externí odkaz:
https://doaj.org/article/edd43c30582d46ed92946c373690f57b
Autor:
James C. Whisstock, Jamie Seymour, Andrew M. Ellisdon, Rodney K. Tweten, Cyril F. Reboul, Kelly Lee Winter, Santosh Panjikar, Wayne C. Hodgson, Michelle A. Dunstone, Sheena McGowan, Peter K. Dearden, Kitmun Huynh, Christine A Oellig
Publikováno v:
Proceedings of the National Academy of Sciences. 112:15360-15365
The lethal factor in stonefish venom is stonustoxin (SNTX), a heterodimeric cytolytic protein that induces cardiovascular collapse in humans and native predators. Here, using X-ray crystallography, we make the unexpected finding that SNTX is a pore-f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e0597256171ecf4d85cc2ae08ff1559
https://doi.org/10.1073/pnas.1507622112
https://doi.org/10.1073/pnas.1507622112
Autor:
Adrian Zander, Sabine Schneider, Ronan M. Keegan, Sarah Willkomm, Dina Grohmann, Tobias Restle, Christine A. Oellig
Publikováno v:
Nature Microbiology. 2
Argonaute (Ago) proteins in eukaryotes are known as key players in post-transcriptional gene silencing1, while recent studies on prokaryotic Agos hint at their role in the protection against invading DNA2,3. Here, we present crystal structures of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ad6cda5ac5b69fdf981c958725bbbd34
https://doi.org/10.1038/nmicrobiol.2017.35
https://doi.org/10.1038/nmicrobiol.2017.35
Autor:
Michael Klemba, Geetha Velmourougane, Seema Dalal, Doron C. Greenbaum, Nataline Meinhardt, Michael B. Harbut, Sheena McGowan, James C. Whisstock, Christine A Oellig
Publikováno v:
Journal of Medicinal Chemistry. 54:1655-1666
The malarial PfA-M1 metallo-aminopeptidase is considered a putative drug target. The natural product dipeptide mimetic, bestatin, is a potent inhibitor of PfA-M1. Herein we present a new, efficient, and high-yielding protocol for the synthesis of bes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de4cd1f54ccf6faec17095997b56f2e9
https://doi.org/10.1021/jm101227t
https://doi.org/10.1021/jm101227t
Autor:
Marcin Drag, Marcin Sieńczyk, Chiara Ruggeri, John P. Dalton, Peter J. Scammells, Alessandro Paiardini, Sheena McGowan, Christine A Oellig, Komagal Kannan Sivaraman
The malaria parasite Plasmodium falciparum employs two metallo- aminopeptidases, PfA-M1 and PfA-M17, which are essential for parasite survival. Compounds that inhibit the activity of either enzyme represent leads for the development of new antimalari
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9762f0a391ad899e4cfba88232282287
https://hdl.handle.net/10453/23944
https://hdl.handle.net/10453/23944
Autor:
James C. Whisstock, Christine A Oellig, Ashley M. Buckle, Woldeamanuel A. Birru, Jonathan Lowther, Tom T. Caradoc-Davies, Colin M. Stack, Donald L. Gardiner, Jolanta Grembecka, Katharine R. Trenholme, Paweł Kafarski, Artur Mucha, Tina S. Skinner-Adams, John P. Dalton, Sheena McGowan
Publikováno v:
McGowan, S, Oellig, C A, Birru, W A, Caradoc-Davies, T T, Stack, C M, Lowther, J, Skinner-Adams, T, Mucha, A, Kafarski, P, Grembecka, J, Trenholme, K R, Buckle, A M, Gardiner, D L, Dalton, J P & Whisstock, J C 2010, ' Structure of the Plasmodium falciparum M17 aminopeptidase and significance for the design of drugs targeting the neutral exopeptidases ', Proceedings of the National Academy of Sciences, vol. 107, no. 6, pp. 2449-2454 . https://doi.org/10.1073/pnas.0911813107
Current therapeutics and prophylactics for malaria are under severe challenge as a result of the rapid emergence of drug-resistant parasites. The human malaria parasite Plasmodium falciparum expresses two neutral aminopeptidases, Pf A-M1 and Pf A-M17
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac84073dcc34444463ca679b0c1f6e6b
https://hdl.handle.net/10453/14605
https://hdl.handle.net/10453/14605
Autor:
Geetha Velmourougane, Michael B. Harbut, Seema Dalal, Sheena McGowan, Christine A. Oellig, Nataline Meinhardt, James C. Whisstock, Michael Klemba, Doron C. Greenbaum
Publikováno v:
Journal of Medicinal Chemistry; Mar2011, Vol. 54 Issue 6, p1655-1666, 12p
X-ray Crystal Structure and Specificity of the Plasmodium falciparum Malaria Aminopeptidase PfM18AAP
Autor:
Marcin Drag, Sarah C. Atkinson, John P. Dalton, Matthew A. Perugini, Donald L. Gardiner, Marcin Poreba, James C. Whisstock, Kitmun Huynh, Sheena McGowan, Katharine R. Trenholme, Komagal Kannan Sivaraman, Christine A Oellig, Guy S. Salvesen
Publikováno v:
Journal of Molecular Biology. (4):495-507
The malarial aminopeptidases have emerged as promising new drug targets for the development of novel antimalarial drugs. The M18AAP of Plasmodium falciparum malaria is a metallo-aminopeptidase that we show demonstrates a highly restricted specificity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::525a2f8804f034713d75ffba76e96b0e