Zobrazeno 1 - 10
of 70
pro vyhledávání: '"Adam D. Linstedt"'
Autor:
Tineke Veenendaal, Tim Jarvela, Adam G. Grieve, Johan H. van Es, Adam D. Linstedt, Catherine Rabouille
Publikováno v:
Biology Open, Vol 3, Iss 6, Pp 431-443 (2014)
GRASP65 and GRASP55 are peripheral Golgi proteins localized to cis and medial/trans cisternae, respectively. They are implicated in diverse aspects of protein transport and structure related to the Golgi complex, including the stacking of the Golgi s
Externí odkaz:
https://doaj.org/article/b6907d3d39f5408eb68c11a63fe0b61c
Autor:
Lina Song, Adam D Linstedt
Publikováno v:
eLife, Vol 6 (2017)
Small molecule inhibitors of site-specific O-glycosylation by the polypeptide N-acetylgalactosaminyltransferase (ppGalNAc-T) family are currently unavailable but hold promise as therapeutics, especially if selective against individual ppGalNAc-T isoz
Externí odkaz:
https://doaj.org/article/ffb0661ea53b424e96b02bf8103656c7
Autor:
Thomas Daugbjerg Madsen, Adam D. Linstedt, Collin Bachert, Hiren J. Joshi, John Hintze, Christoffer K. Goth, Ulla Mandel, Eric P. Bennett, Sergey Y. Vakhrushev, Zilu Ye, Katrine T. Schjoldager, Yoshiki Narimatsu
Publikováno v:
Journal of Biological Chemistry. 293:19064-19077
The GalNAc-type O-glycoproteome is orchestrated by a large family of polypeptide GalNAc-transferase isoenzymes (GalNAc-Ts) with partially overlapping contributions to the O-glycoproteome besides distinct nonredundant functions. Increasing evidence in
Autor:
Emily J. Simon, Adam D. Linstedt
Publikováno v:
Journal of Biological Chemistry. 293:19866-19873
The surface glycoprotein (GP) of Ebola virus causes many of the virus's pathogenic effects, including a dramatic loss of endothelial cell adhesion associated with widespread hemorrhaging during infection. Although the GP-mediated deadhesion depends o
Autor:
Raphaël Sierocki, Julien Barbier, Adam D. Linstedt, Ludger Johannes, Alison Forrester, Stefan J. Rathjen, Mathilde Munier, Sylvain Pichard, Daniel Gillet, Henri-François Renard, Christophe Lamaze, Damarys Loew, Maria Daniela Garcia-Castillo, Jennifer Martinez, Livia Tepshi, Jean-Christophe Cintrat, Collin Bachert, Audrey Couhert, Florent Dingli, Cesar Augusto Valades-Cruz
Publikováno v:
Nature Chemical Biology
Nature Chemical Biology, 2020, 16 (3), pp.327-336. ⟨10.1038/s41589-020-0474-4⟩
Nature Chemical Biology, Nature Publishing Group, 2020, 16 (3), pp.327-336. ⟨10.1038/s41589-020-0474-4⟩
Nature Chemical Biology, 2020, 16 (3), pp.327-336. ⟨10.1038/s41589-020-0474-4⟩
Nature Chemical Biology, Nature Publishing Group, 2020, 16 (3), pp.327-336. ⟨10.1038/s41589-020-0474-4⟩
International audience; The retrograde transport inhibitor Retro-2 has a protective effect on cells and in mice against Shiga-like toxins and ricin. Retro-2 causes toxin accumulation in early endosomes and relocalization of the Golgi SNARE protein sy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31f0c3f57a783df4459e09cb7a9dde00
https://hal.science/hal-04003230
https://hal.science/hal-04003230
Autor:
Swati Venkat, Adam D. Linstedt
Publikováno v:
Molecular Biology of the Cell
By binding and directing the cycling Golgi protein GPP130 to lysosomes, the sorting receptor sortilin mediates the manganese-induced GPP130 down-regulation that protects against Shiga toxicosis.
Elevated, nontoxic doses of manganese (Mn) protect
Elevated, nontoxic doses of manganese (Mn) protect
Publikováno v:
Molecular Biology of the Cell
Oligomerization or homotypic clustering diverts Golgi membrane proteins into the canonical GGA1/clathrin-dependent Golgi-to-lysosome pathway revealing the presence of cellular quality control that could be useful for therapies designed to down-regula
Publikováno v:
Journal of Biological Chemistry. 289:9683-9691
The mammalian Golgi reassembly stacking protein (GRASP) proteins are Golgi-localized homotypic membrane tethers that organize Golgi stacks into a long, contiguous ribbon-like structure. It is unknown how GRASPs undergo trans pairing given that cis in
Autor:
Adam D. Linstedt, Timothy S. Jarvela
Publikováno v:
Molecular Biology of the Cell
Use of photoinactivation, cisternae-specific fluorescence recovery, and high-resolution microscopy shows that the membrane tethers GRASP65 and GRASP55 on early and late Golgi membranes, respectively, are critical to the specific, homotypic fusion of