Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Sally Prouty"'
Autor:
Ameya S Walimbe, Hidehiko Okuma, Soumya Joseph, Tiandi Yang, Takahiro Yonekawa, Jeffrey M Hord, David Venzke, Mary E Anderson, Silvia Torelli, Adnan Manzur, Megan Devereaux, Marco Cuellar, Sally Prouty, Saul Ocampo Landa, Liping Yu, Junyu Xiao, Jack E Dixon, Francesco Muntoni, Kevin P Campbell
Publikováno v:
eLife, Vol 9 (2020)
Matriglycan [-GlcA-β1,3-Xyl-α1,3-]n serves as a scaffold in many tissues for extracellular matrix proteins containing laminin-G domains including laminin, agrin, and perlecan. Like-acetyl-glucosaminyltransferase 1 (LARGE1) synthesizes and extends m
Externí odkaz:
https://doaj.org/article/17d3f0ccf58a40a8a791f30363198f9e
Publikováno v:
Physiology. 38
Mutations in glycosyltransferases involved in the O-mannosyl processing and formation of matriglycan on alpha-dystroglycan (αDG) constitute a subset of limb girdle muscular dystrophies referred to as dystroglycanopathies. Patients exhibit a range of
Autor:
Caryl Handelman, Megan Devereaux, Sally Prouty, Steven G. Friedenberg, Jeffrey M. Hord, Katie M. Minor, Jonah N. Cullen, Mary E. Anderson, Ling T. Guo, David Venzke, James R. Mickelson, G. Diane Shelton, Kevin P. Campbell
Publikováno v:
Neuromuscul Disord
Neuromuscular disorders : NMD, vol 31, iss 11
Neuromuscular disorders : NMD, vol 31, iss 11
Alpha-dystroglycan (αDG) is a highly glycosylated cell surface protein with a significant role in cell-to-extracellular matrix interactions in muscle. αDG interaction with extracellular ligands relies on the activity of the LARGE1 glycosyltransfera
Autor:
Hidehiko Okuma, Mary E. Anderson, Tiandi Yang, Saul Ocampo Landa, Sally Prouty, Junyu Xiao, Jack E. Dixon, Ameya S Walimbe, Marco Cuellar, Adnan Y. Manzur, Megan Devereaux, Francesco Muntoni, Jeffrey M. Hord, Kevin P. Campbell, Soumya Joseph, Liping Yu, Silvia Torelli, David Venzke, Takahiro Yonekawa
Publikováno v:
eLife
eLife, Vol 9 (2020)
eLife, Vol 9 (2020)
Matriglycan [-GlcA-β1,3-Xyl-α1,3-]n serves as a scaffold in many tissues for extracellular matrix proteins containing laminin-G domains including laminin, agrin, and perlecan. Like-acetyl-glucosaminyltransferase 1 (LARGE1) synthesizes and extends m
Autor:
Mary E. Anderson, Junyu Xiao, Tiandi Yang, Marco Cuellar, Soumya Joseph, Francesco Muntoni, Adnan Y. Manzur, Sally Prouty, Megan Devereaux, Jack E. Dixon, Hidehiko Okuma, Jeffrey M. Hord, Liping Yu, Takahiro Yonekawa, Silvia Torelli, David Venzke, Ameya S Walimbe, Kevin P. Campbell, Saul Ocampo Landa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9d8b0dbb03569a769a91e81c3aecf616
https://doi.org/10.7554/elife.61388.sa2
https://doi.org/10.7554/elife.61388.sa2
Autor:
Ameya S. Walimbe, Hidehiko Okuma, Soumya Joseph, Tiandi Yang, Takahiro Yonekawa, Jeffrey M. Hord, David Venzke, Mary E. Anderson, Silvia Torelli, Adnan Manzur, Megan Devereaux, Marco Cuellar, Sally Prouty, Saul Ocampo Landa, Liping Yu, Junyu Xiao, Jack E. Dixon, Francesco Muntoni, Kevin P. Campbell
Matriglycan [-GlcA-β1,3-Xyl-α1,3-]n serves as a scaffold in many tissues for extracellular matrix proteins containing laminin-G domains including laminin, agrin, and perlecan. Like-acetylglucosaminyltransferase-1 (LARGE) synthesizes and extends mat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6985a500080cff9398621e011bbbb38d
https://doi.org/10.1101/2020.04.06.007948
https://doi.org/10.1101/2020.04.06.007948