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pro vyhledávání: '"J. C. Monboisse"'
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Akademický článek
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Autor:
A. Serikoff, J. C. Monboisse, N. Servent-Saez, J.P. Borel, C.-H. Dupont, M. Paubert-Braquet, André Cavé, Reynald Hocquemiller, C. Fourneau
Publikováno v:
Biomedicine & Pharmacotherapy. 48:43s-47s
Summary An extract of Pygeum africanum bark (Tadenan®) is prescribed for older men suffering from micturitional difficulties due to benign prostatic hyperplasia (BPH). Its mechanism of action is not completely understood. Basic fibroblast growth fac
Autor:
Pai Peng1, Xinman Hu1, Beiduo Wang1, Xuelong Wang1, Shifen Li1, Yongyuan Kang1, Xiaofei Dong1,2, Xiayan Yang3, Qifeng Yu3 qfyu@newmed.cn, Changyou Gao1,2,3,4 cygao@zju.edu.cn
Publikováno v:
Smart Materials in Medicine. Sep2024, Vol. 5 Issue 3, p409-424. 16p.
Publikováno v:
Medicina. 59(5 Pt 2)
Autor:
A, Siméon, F, Monier, H, Emonard, Y, Wegrowski, G, Bellon, J C, Monboisse, P, Gillery, W, Hornebeck, F X, Maquart
Publikováno v:
Current topics in pathology. Ergebnisse der Pathologie. 93
Publikováno v:
The Journal of pathology. 182(2)
Tumour invasion is associated with strong remodelling of the extracellular matrix, including the basement membrane (BM). The major structural component of BMs is type IV collagen, which is composed of an association of three a chains. In this study,
Publikováno v:
The Journal of biological chemistry. 270(46)
Monoclonal antibodies to the alpha L beta 2 integrin inhibit the binding of type I collagen to PMN (polymorphonuclear neutrophil leukocytes) as well as the subsequent stimulation of superoxide production and enzyme secretion-elicited by this collagen
Publikováno v:
The Journal of biological chemistry. 269(41)
Our initial observation that type I collagen activates polymorphonuclear leukocytes (PMN) prompted the testing of the activating potential of type IV collagen. It was noted, however, that type IV collagen isolated from bovine lens capsule did not act
Autor:
J P, Borel, J C, Monboisse
Publikováno v:
Comptes rendus des seances de la Societe de biologie et de ses filiales. 187(2)
The collagens are a family of extracellular fibrillar proteins, characterized by the presence of one or several domains termed "triple helix", that are made of three polypeptide chains folded around each other. They elicit a huge worldwide research a