Zobrazeno 1 - 10
of 98
pro vyhledávání: '"Ethan D Goddard-Borger"'
Autor:
Cristina Giogha, Nichollas E Scott, Tania Wong Fok Lung, Georgina L Pollock, Marina Harper, Ethan D Goddard-Borger, Jaclyn S Pearson, Elizabeth L Hartland
Publikováno v:
PLoS Pathogens, Vol 17, Iss 6, p e1009658 (2021)
During infection, enteropathogenic Escherichia coli (EPEC) and enterohaemorrhagic E. coli (EHEC) directly manipulate various aspects of host cell function through the translocation of type III secretion system (T3SS) effector proteins directly into t
Externí odkaz:
https://doaj.org/article/2006b1e2b92648679cfa2dc62a009493
Autor:
Lin Chen, Yibin Xu, Wilson Wong, Jennifer K Thompson, Julie Healer, Ethan D Goddard-Borger, Michael C Lawrence, Alan F Cowman
Publikováno v:
eLife, Vol 6 (2017)
Plasmodium falciparum causes malaria in humans with over 450,000 deaths annually. The asexual blood stage involves invasion of erythrocytes by merozoites, in which they grow and divide to release daughter merozoites, which in turn invade new erythroc
Externí odkaz:
https://doaj.org/article/1713c79e917b4c25b466cdbbb54f5a40
Autor:
Alexander J.D. Snow, Mahima Sharma, James P. Lingford, Yunyang Zhang, Janice W.-Y. Mui, Ruwan Epa, Ethan D. Goddard-Borger, Spencer J. Williams, Gideon J. Davies
Publikováno v:
Current Research in Structural Biology, Vol 4, Iss , Pp 51-58 (2022)
Sulfoquinovose (SQ) is the anionic headgroup of the ubiquitous plant sulfolipid, sulfoquinovosyl diacylglycerol (SQDG). SQDG can undergo delipidation to give sulfoquinovosyl glycerol (SQGro) and further glycoside cleavage to give SQ, which can be met
Externí odkaz:
https://doaj.org/article/b2d19574ebb74217b20dddd19cfcbe18
Autor:
Mahima Sharma, Palika Abayakoon, Ruwan Epa, Yi Jin, James P. Lingford, Tomohiro Shimada, Masahiro Nakano, Janice W.-Y. Mui, Akira Ishihama, Ethan D. Goddard-Borger, Gideon J. Davies, Spencer J. Williams
Publikováno v:
ACS Central Science, Vol 7, Iss 3, Pp 476-487 (2021)
Externí odkaz:
https://doaj.org/article/2f2ce95f6e74441092b676f9ffdc734f
Autor:
Michael A. Järvå, James P. Lingford, Alan John, Niccolay Madiedo Soler, Nichollas E. Scott, Ethan D. Goddard-Borger
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
Trefoil factors (TFFs) protect the mucosa and have various reported binding activities, but whether they share a common interaction mechanism has remained unclear. Here, the authors provide structural and biochemical evidence that all three human TFF
Externí odkaz:
https://doaj.org/article/cf2cbf05a6394844b850bf051a2a3963
Autor:
Palika Abayakoon, Yi Jin, James P. Lingford, Marija Petricevic, Alan John, Eileen Ryan, Janice Wai-Ying Mui, Douglas E.V. Pires, David B. Ascher, Gideon J. Davies, Ethan D. Goddard-Borger, Spencer J. Williams
Publikováno v:
ACS Central Science, Vol 4, Iss 9, Pp 1266-1273 (2018)
Externí odkaz:
https://doaj.org/article/26a26980956f4b03b45d9c4d2d4581a1
Autor:
Sash Lopaticki, Annie S. P. Yang, Alan John, Nichollas E. Scott, James P. Lingford, Matthew T. O’Neill, Sara M. Erickson, Nicole C. McKenzie, Charlie Jennison, Lachlan W. Whitehead, Donna N. Douglas, Norman M. Kneteman, Ethan D. Goddard-Borger, Justin A. Boddey
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
The role of O-glycosylation in the malaria life cycle is largely unknown. Here, the authors identify a Plasmodium protein O-fucosyltransferase and show that it is important for normal trafficking of a subset of surface proteins, particularly CSP and
Externí odkaz:
https://doaj.org/article/09e0a0fb76224df8a67b76f39e4a21ef
Autor:
Abdulrahman M. Shathili, Esther Bandala-Sanchez, Alan John, Ethan D. Goddard-Borger, Morten Thaysen-Andersen, Arun V. Everest-Dass, Timothy E. Adams, Leonard C. Harrison, Nicolle H. Packer
Publikováno v:
Frontiers in Immunology, Vol 10 (2019)
Human CD52 is a small glycopeptide (12 amino acid residues) with one N-linked glycosylation site at asparagine 3 (Asn3) and several potential O-glycosylation serine/threonine sites. Soluble CD52 is released from the surface of activated T cells and m
Externí odkaz:
https://doaj.org/article/ed7fb9f56edd4e41b632ff8207663306
Autor:
Thimali Arumapperuma, Jinling Li, Bastian Hornung, Niccolay Madiedo Soler, Ethan D. Goddard-Borger, Nicolas Terrapon, Spencer J. Williams
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, 2023, 299 (4), pp.103038. ⟨10.1016/j.jbc.2023.103038⟩
J Biol Chem
Journal of Biological Chemistry, 2023, 299 (4), pp.103038. ⟨10.1016/j.jbc.2023.103038⟩
J Biol Chem
International audience; The Carbohydrate-Active Enzyme classification groups enzymes that breakdown, assemble, or decorate glycans into protein families based on sequence similarity. The glycoside hydrolases (GH) are arranged into over 170 enzyme fam
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e3873697d20c2d596e8dd4c9fd6cadd
https://cnrs.hal.science/hal-04070174
https://cnrs.hal.science/hal-04070174
Autor:
Jinling Li, Janice Mui, Bruna M. da Silva, Douglas E.V. Pires, David B. Ascher, Niccolay Madiedo Soler, Ethan D. Goddard-Borger, Spencer J. Williams
Glycoside hydrolases (GHs) are a diverse group of enzymes that catalyze the hydrolysis of glycosidic bonds. The Carbohydrate-Active enZymes (CAZy) database organizes GHs into families based on sequence data and function, with fewer than 1% of the pre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ca15f324747daae4351896b4e5d2ee99
https://doi.org/10.1101/2023.03.31.535182
https://doi.org/10.1101/2023.03.31.535182