Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Robert N. Ono"'
Autor:
Gerhard Sengle, Ko Tsutsui, Douglas R Keene, Sara F Tufa, Eric J Carlson, Noe L Charbonneau, Robert N Ono, Takako Sasaki, Mary K Wirtz, John R Samples, Liselotte I Fessler, John H Fessler, Kiyotoshi Sekiguchi, Susan J Hayflick, Lynn Y Sakai
Publikováno v:
PLoS Genetics, Vol 8, Iss 1, p e1002425 (2012)
Fibrillin-1 is a ubiquitous extracellular matrix molecule that sequesters latent growth factor complexes. A role for fibrillin-1 in specifying tissue microenvironments has not been elucidated, even though the concept that fibrillin-1 provides extrace
Externí odkaz:
https://doaj.org/article/f3d4e5a100c84ffc8be2e4a6ffbeff33
Publikováno v:
Journal of Biological Chemistry. 286:5087-5099
The specific functions of the prodomains of TGFβ superfamily members are largely unknown. Interactions are known between prodomains of TGFβ-1–3 and latent TGFβ-binding proteins and between prodomains of BMP-2, -4, -7, and -10 and GDF-5 and fibri
Publikováno v:
Journal of Molecular Biology. 381:1025-1039
Bone morphogenetic proteins (BMPs) are morphogens with long-range signaling activities. BMP-7 is secreted as a stable complex consisting of a growth factor noncovalently associated with two propeptides. In other transforming growth factor-beta-like g
Autor:
Douglas R. Keene, Zenzo Isogai, Lynn Y. Sakai, Hans Peter Bächinger, Chiu Liang Kuo, Gerhard Sengle, Robert N. Ono, Noriko Hazeki
Publikováno v:
Journal of Biological Chemistry. 282:4007-4020
Current models of the elastic properties and structural organization of fibrillin-containing microfibrils are based primarily on microscopic analyses of microfibrils liberated from connective tissues after digestion with crude collagenase. Results pr
Autor:
Noe L. Charbonneau, Lynn Y. Sakai, Robert N. Ono, Kate E. Gregory, Chiu-Liang Kuo, Douglas R. Keene, Hans Peter Bächinger
Publikováno v:
Journal of Biological Chemistry. 280:27970-27980
Biochemical and biophysical methods are used to show that BMP-7 is secreted as a stable complex consisting of the processed growth factor dimer noncovalently associated with its two prodomain propeptide chains and that the BMP-7 complex is structural
Autor:
Lynn Y. Sakai, Hans Peter Bächinger, Holger Notbohm, Dieter P. Reinhardt, Robert N. Ono, Peter K. Müller
Publikováno v:
Journal of Biological Chemistry. 275:12339-12345
Most extracellular proteins consist of various modules with distinct functions. Mutations in one common type, the calcium-binding epidermal growth factor-like module (cbEGF), can lead to a variety of genetic disorders. Here, we describe as a model sy
Publikováno v:
Journal of Biological Chemistry. 275:2205-2210
Fibrillins are the major constituents of extracellular microfibrils. How fibrillin molecules assemble into microfibrils is not known. Sequential extractions and pulse-chase labeling of organ cultures of embryonic chick aortae revealed rapid formation
Autor:
Nancy Jensen Biery, Lygia da Veiga Pereira, Lynn Y. Sakai, Jenny Tian, Harry C. Dietz, Sui Ying Lee, Tracie E. Bunton, Konstantinos Andrikopoulos, Douglas R. Keene, Dieter P. Reinhardt, Francesco Ramirez, Robert N. Ono
Publikováno v:
Nature Genetics. 17:218-222
Aortic aneurysm and dissection account for about 2% of all deaths in industrialized countries; they are also components of several genetic diseases, including Marfan syndrome (MFS). The vascular phenotype of MFS results from mutations in fibrillin-1
Publikováno v:
Journal of Biological Chemistry. 272:1231-1236
The calcium-binding epidermal growth factor (cbEGF)-like domain is a structural motif that is present in many matrix proteins throughout the animal kingdom from invertebrates to mammals. This module has been demonstrated to bind calcium in the microm
Publikováno v:
The Journal of biological chemistry. 286(7)
The specific functions of the prodomains of TGFβ superfamily members are largely unknown. Interactions are known between prodomains of TGFβ-1–3 and latent TGFβ-binding proteins and between prodomains of BMP-2, -4, -7, and -10 and GDF-5 and fibri