Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Noriko Sumida"'
Autor:
Prapaporn Jongwattanapisan, Masahiko Terajima, Patricia A. Miguez, William Querido, Hideaki Nagaoka, Noriko Sumida, Elizabeth Grace Gurysh, Kristy M. Ainslie, Nancy Pleshko, Lalith Perera, Mitsuo Yamauchi
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-11 (2018)
Abstract We have reported that recombinant biglycan (BGN) core protein accelerates bone formation in vivo by enhancing bone morphogenetic protein (BMP)-2 function. The purpose of the present study was to identify the specific domain (“effector”)
Externí odkaz:
https://doaj.org/article/86b12ac6f51546d392392532a8bb8bf5
Autor:
Masahiko Terajima, Yuki Taga, Wayne A Cabral, Ying Liu, Masako Nagasawa, Noriko Sumida, Yukako Kayashima, Prashant Chandrasekaran, Lin Han, Nobuyo Maeda, Irina Perdivara, Shunji Hattori, Joan C Marini, Mitsuo Yamauchi
Publikováno v:
PLoS Genetics, Vol 15, Iss 6, p e1008196 (2019)
Covalent intermolecular cross-linking of collagen is essential for tissue stability. Recent studies have demonstrated that cyclophilin B (CypB), an endoplasmic reticulum (ER)-resident peptidyl-prolyl cis-trans isomerase, modulates lysine (Lys) hydrox
Externí odkaz:
https://doaj.org/article/972c451e742c44a0933743c55be8b896
Autor:
Yukako Kayashima, Mitsuo Yamauchi, Marnisa Sricholpech, Yuki Taga, Shunji Hattori, Masahiko Terajima, Noriko Sumida, Nobuyo Maeda
Publikováno v:
Biochemistry
Glycosylation in type I collagen occurs as O-linked galactosyl- (G-) lesser and glucosylgalactosyl-hydrox-ylysine (GG-Hyl); however, its biological significance is still not well understood. To investigate the function of this modification in bone, w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf644ffb96b8fbc8769d51bd332af099
https://europepmc.org/articles/PMC7887705/
https://europepmc.org/articles/PMC7887705/
Autor:
Wayne A. Cabral, Shunji Hattori, Prashant Chandrasekaran, Noriko Sumida, Joan C. Marini, Irina Perdivara, Mitsuo Yamauchi, Nobuyo Maeda, Yukako Kayashima, Yuki Taga, Masahiko Terajima, Lin Han, Ying Liu, Masako Nagasawa
Publikováno v:
PLoS Genetics, Vol 15, Iss 6, p e1008196 (2019)
PLoS Genetics
PLoS Genetics
Covalent intermolecular cross-linking of collagen is essential for tissue stability. Recent studies have demonstrated that cyclophilin B (CypB), an endoplasmic reticulum (ER)-resident peptidyl-prolyl cis-trans isomerase, modulates lysine (Lys) hydrox
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20c1c70bbe43af06b9a060c5f82cb4db
https://doaj.org/article/972c451e742c44a0933743c55be8b896
https://doaj.org/article/972c451e742c44a0933743c55be8b896
Autor:
Wayne A. Cabral, Yulong Chen, Shunji Hattori, Mitsuo Yamauchi, Noriko Sumida, Masahiko Terajima, Masako Nagasawa, Jonathan M. Kurie, Yuki Taga, Joan C. Marini, Guo Hou-Fu, Sirivimol Srisawasdi
Publikováno v:
Journal of Biological Chemistry. 291:9501-9512
Covalent intermolecular cross-linking provides collagen fibrils with stability. The cross-linking chemistry is tissue-specific and determined primarily by the state of lysine hydroxylation at specific sites. A recent study on cyclophilin B (CypB) nul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a50e37106aa4093e7f1b66a95c43dfb
https://doi.org/10.1074/jbc.m115.699470
https://doi.org/10.1074/jbc.m115.699470
Autor:
Mitsuo Yamauchi, Hideaki Nagaoka, Kristy M. Ainslie, Noriko Sumida, Lalith Perera, Masahiko Terajima, Prapaporn Jongwattanapisan, Elizabeth Grace Gurysh, Patricia A. Miguez, William Querido, Nancy Pleshko
Publikováno v:
Scientific Reports
Scientific Reports, Vol 8, Iss 1, Pp 1-11 (2018)
Scientific Reports, Vol 8, Iss 1, Pp 1-11 (2018)
We have reported that recombinant biglycan (BGN) core protein accelerates bone formation in vivo by enhancing bone morphogenetic protein (BMP)-2 function. The purpose of the present study was to identify the specific domain (“effector”) within th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::499c0c58a8579708a14708f5b3fac17e
http://europepmc.org/articles/PMC5935668
http://europepmc.org/articles/PMC5935668
Autor:
Masahiko Terajima, Yuki Taga, Mitsuo Yamauchi, Noriko Sumida, Joan C. Marini, Wayne A. Cabral, Shunji Hattori, Masako Nagasawa
Publikováno v:
Journal of proteome research. 16(8)
Cyclophilin B (CypB) is an endoplasmic reticulum-resident protein that regulates collagen folding, and also contributes to prolyl 3-hydroxylation (P3H) and lysine (Lys) hydroxylation of collagen. In this study, we characterized dentin type I collagen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::470077613cdcb1b4788073d5d47541ca
https://pubmed.ncbi.nlm.nih.gov/28696707
https://pubmed.ncbi.nlm.nih.gov/28696707