Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Takako Yoshida-Moriguchi"'
Autor:
Kevin P. Campbell, David Venzke, John Glushka, M. Osman Sheikh, Mary E. Anderson, Lance Wells, Takako Yoshida-Moriguchi, Melina Galizzi, Kelley W. Moremen, Alison V. Nairn
Publikováno v:
Glycobiology
Mutations in multiple genes required for proper O-mannosylation of α-dystroglycan are causal for congenital/limb-girdle muscular dystrophies and abnormal brain development in mammals. Previously, we and others further elucidated the functional O-man
Autor:
Cristin Crawley, Matthew Skinner, Luis Z. Avila, Kishore Raghupathi, Yunxiang Zhu, Takako Yoshida-Moriguchi, Robert J. Miller, Pradeep K. Dhal, Peter Pipenhagen, Grace Chang
Publikováno v:
ACS Biomaterials Science & Engineering. 4:558-565
Hyaluronic acid (HA) microgels were investigated as biocompatible and biodegradable reagents for facilitating endosomolysis in human cells. Employing inverse emulsion templates, HA microgels were prepared by cross-linking aqueous sodium hyaluronate d
Publikováno v:
Glycobiology
Associations between cells and the basement membrane are critical for a variety of biological events including cell proliferation, cell migration, cell differentiation and the maintenance of tissue integrity. Dystroglycan is a highly glycosylated bas
Autor:
David Venzke, Kevin P. Campbell, Fumiaki Saito, Biming Wu, Takako Yoshida-Moriguchi, Steven A. Moore, Kiichiro Matsumura, Matthew M. Goddeeris
Publikováno v:
Nature. 503:136-140
The dense glycan coat that surrounds every cell is essential for cellular development and physiological function1, and it is becoming appreciated that its composition is highly dynamic. Post-translational addition of the polysaccharide repeating unit
Autor:
Tobias Willer, Hane Lee, Liping Yu, Mary E. Anderson, Kevin P. Campbell, Takako Yoshida-Moriguchi, David Venzke, Stanley F. Nelson, Tamieka Whyte, Francesco Muntoni
Publikováno v:
Science. 341:896-899
Dissecting Dystrophies Defects in α-dystroglycan lead to various congenital muscular dystrophies, and its ability to bind to extracellular matrix (ECM) is dependent on formation of a specific O-linked sugar structure. Previous efforts to understand
Autor:
Erhard Hohenester, Marco Moracci, Andrea Strazzulli, Kevin P. Campbell, Takako Yoshida-Moriguchi, Mary E. Anderson, Tianqing Zheng, Liping Yu, David Briggs, David Venzke
Publikováno v:
Nature chemical biology
Nature chemical biology 12 (2016): 810–814. doi:10.1038/NCHEMBIO.2146
info:cnr-pdr/source/autori:Briggs, David C.; Yoshida-Moriguchi, Takako; Zheng, Tianqing; Venzke, David; Anderson, Mary E.; Strazzulli, Andrea; Moracci, Marco; Yu, Liping; Hohenester, Erhard; Campbell, Kevin P./titolo:Structural basis of laminin binding to the LARGE glycans on dystroglycan/doi:10.1038%2FNCHEMBIO.2146/rivista:Nature chemical biology/anno:2016/pagina_da:810/pagina_a:814/intervallo_pagine:810–814/volume:12
Nature chemical biology 12 (2016): 810–814. doi:10.1038/NCHEMBIO.2146
info:cnr-pdr/source/autori:Briggs, David C.; Yoshida-Moriguchi, Takako; Zheng, Tianqing; Venzke, David; Anderson, Mary E.; Strazzulli, Andrea; Moracci, Marco; Yu, Liping; Hohenester, Erhard; Campbell, Kevin P./titolo:Structural basis of laminin binding to the LARGE glycans on dystroglycan/doi:10.1038%2FNCHEMBIO.2146/rivista:Nature chemical biology/anno:2016/pagina_da:810/pagina_a:814/intervallo_pagine:810–814/volume:12
Dystroglycan is a highly glycosylated extracellular matrix receptor with essential functions in skeletal muscle and the nervous system. Reduced matrix binding by alpha-dystroglycan (alpha-DG) due to perturbed glycosylation is a pathological feature o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::612d47131cd9b56c0548f5e1f334d3fb
http://hdl.handle.net/11588/662489
http://hdl.handle.net/11588/662489
Autor:
John A. Faulkner, Kevin P. Campbell, Stefan Kunz, Ulrike Mayer, Renzhi Han, Motoi Kanagawa, Takako Yoshida-Moriguchi, David E. Muirhead, Daniel E. Michele, Steven A. Moore, Katsuya Miyake, Paul L. McNeil, Rainer Ng, Susan T. Iannaccone, Erik P. Rader, Michael B. A. Oldstone
Publikováno v:
Proceedings of the National Academy of Sciences. 106:12573-12579
Skeletal muscle basal lamina is linked to the sarcolemma through transmembrane receptors, including integrins and dystroglycan. The function of dystroglycan relies critically on posttranslational glycosylation, a common target shared by a genetically
Publikováno v:
The FASEB Journal. 27
Autor:
Mary E. Anderson, Zihan Zhu, Kevin P. Campbell, Takako Yoshida-Moriguchi, Kei-ichiro Inamori, Tobias Willer, Yuji Hara
Publikováno v:
Glycobiology
LARGE-dependent modification enables α-dystroglycan (α-DG) to bind to its extracellular matrix ligands. Mutations in the LARGE gene and several others involved in O-mannosyl glycan synthesis have been identified in congenital and limb-girdle muscul
Autor:
Mary E. Anderson, Yuji Hara, Kevin P. Campbell, Takako Yoshida-Moriguchi, Kei-ichiro Inamori, Liping Yu
Publikováno v:
Science (New York, N.Y.). 335(6064)
Going LARGE Dystroglycan (DG) is a highly glycosylated extracellular matrix (ECM) receptor involved in a variety of physiological processes, including maintenance of skeletal muscle membrane integrity and the structure and function of the central ner