Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Christopher J, Marklew"'
Publikováno v:
iScience, Vol 15, Iss , Pp 173-184 (2019)
Summary: Artificial cells can shed new light on the molecular basis for life and hold potential for new chemical technologies. Inspired by how nature dynamically regulates its membrane compartments, we aim to repurpose the endosomal sorting complex r
Externí odkaz:
https://doaj.org/article/e264cc031f0d49cb8cde9be9055b535b
Autor:
Laila Moustaq, Iwona I. Smaczynska-de Rooij, Sarah E. Palmer, Christopher J. Marklew, Kathryn R. Ayscough
Publikováno v:
Microbial Cell, Vol 3, Iss 4, Pp 147-158 (2016)
The dynamins represent a superfamily of proteins that have been shown to function in a wide range of membrane fusion and fission events. An increasing number of mutations in the human classical dynamins, Dyn-1 and Dyn-2 has been reported, with diseas
Externí odkaz:
https://doaj.org/article/f8c0e1bb87b046d48a51e00b11427e5a
Autor:
Iwona I Smaczynska-de Rooij, Christopher J Marklew, Sarah E Palmer, Ellen G Allwood, Kathryn R Ayscough
Publikováno v:
PLoS ONE, Vol 14, Iss 4, p e0215102 (2019)
The yeast dynamin-like protein Vps1 has roles at multiple stages of membrane trafficking including Golgi to vacuole transport, endosomal recycling, endocytosis and in peroxisomal fission. While the majority of the Vps1 amino acid sequence shows a hig
Externí odkaz:
https://doaj.org/article/a72d29a976a94208aab5e5914b6ec298
Publikováno v:
iScience, Vol 15, Iss, Pp 173-184 (2019)
iScience
iScience
Summary Artificial cells can shed new light on the molecular basis for life and hold potential for new chemical technologies. Inspired by how nature dynamically regulates its membrane compartments, we aim to repurpose the endosomal sorting complex re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::186319df9330754a71f44effcdae25f1
http://www.sciencedirect.com/science/article/pii/S258900421930118X
http://www.sciencedirect.com/science/article/pii/S258900421930118X
Autor:
Danqing Tong, David J Thaller, Nicholas R. Ader, Philip J. Mannino, Megan C. King, Sapan Borah, Barbara Ciani, C. Patrick Lusk, Christopher J. Marklew
Publikováno v:
The Journal of Cell Biology
Thaller et al. demonstrate that direct binding between phosphatidic acid (PA) and the ESCRT Chm7 is required for nuclear envelope surveillance; PA also accumulates at nuclear envelope herniations. Thus, tight control of PA metabolism is required for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::338c89afde91f8f4018847f226d4495d
http://europepmc.org/articles/PMC7816628
http://europepmc.org/articles/PMC7816628
Autor:
Sapan Borah, Christopher J. Marklew, Danqing Tong, C. Patrick Lusk, Barbara Ciani, David J Thaller
Mechanisms that control nuclear membrane remodeling are essential to maintain the integrity of the nucleus but remain to be fully defined. Here, we identify a phosphatidic acid (PA)-binding activity in the nuclear envelope-specific ESCRT, Chm7, in bu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::316d094edbdffad96966df3dde8546f7
Publikováno v:
bioRxiv
The endosomal sorting complex required for transport (ESCRT) organises in supramolecular structures on the surface of lipid bilayers to drive membrane invagination and scission of intraluminal vesicles (ILVs), a process also controlled by membrane me
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cea8ff31b238fbc77113f8deac6394df
https://doi.org/10.1101/2020.04.21.053389
https://doi.org/10.1101/2020.04.21.053389
Autor:
Iwona I. Smaczynska-de Rooij, Christopher J. Marklew, Kathryn R. Ayscough, Laila Moustaq, Sarah E. Palmer
Publikováno v:
Microbial Cell
The dynamins represent a superfamily of proteins that have been shown to function in a wide range of membrane fusion and fission events. An increasing number of mutations in the human classical dynamins, Dyn-1 and Dyn-2 has been reported, with diseas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9af568af965c05290ba7617017b78720
https://doi.org/10.15698/mic2016.04.490
https://doi.org/10.15698/mic2016.04.490
Autor:
Kathryn R. Ayscough, Ellen G. Allwood, Christopher J. Marklew, Iwona I. Smaczynska-de Rooij, Sarah E. Palmer
Publikováno v:
PLoS ONE
PLoS ONE, Vol 14, Iss 4, p e0215102 (2019)
PLoS ONE, Vol 14, Iss 4, p e0215102 (2019)
The yeast dynamin-like protein Vps1 has roles at multiple stages of membrane trafficking including Golgi to vacuole transport, endosomal recycling, endocytosis and in peroxisomal fission. While the majority of the Vps1 amino acid sequence shows a hig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32ed8e2497977e070b40b3e7cbd6df0b
https://pubmed.ncbi.nlm.nih.gov/31009484
https://pubmed.ncbi.nlm.nih.gov/31009484
Artificial cells can shed new light on the molecular basis for life and hold potential for new chemical technologies. Inspired by how nature dynamically regulates its membrane compartments, we aim to repurpose the endosomal sorting complex required f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d05e86c35f6a99ab1f17eb3017e5d27