Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Maria Selander"'
Publikováno v:
Biochemistry. 29:8111-8118
Blood coagulation factor X is composed of discrete domains, two of which are homologous to the epidermal growth factor (EGF). The N-terminal EGF like domain in factor X (fX-EGF{sub N}), residues 45-86 of the intact protein contains a {beta}-hydroxyla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eb60ff7b031c5996c695bc0d7a3ed657
https://doi.org/10.1021/bi00487a018
https://doi.org/10.1021/bi00487a018
Publikováno v:
Current Aspects of Blood Coagulation, Fibrinolysis, and Platelets ISBN: 9784431701231
Blood coagulation results form a series of activations of zymogens of serine proteases by limited proteolytic cleavage. These reactions form what is commonly referred to as a procoagulant cascade. The final zymogen activation is the conversion of pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::14eab708b9fd3f46939c1d550d10992e
https://doi.org/10.1007/978-4-431-68323-0_1
https://doi.org/10.1007/978-4-431-68323-0_1
Autor:
Torbjoern Drakenberg, Johan Stenflo, Olle Teleman, Magnus Ullner, Maria Selander, Egon Persson
Publikováno v:
Ullner, M, Selander, M, Persson, E, Stenflo, J, Drakenberg, T & Teleman, O 1992, ' Three-dimensional structure of the apo form of the N-terminal EGF-like module of blood coagulation factor X as determined by NMR spectroscopy and simulated folding ', Biochemistry, vol. 31, no. 26, pp. 5974-5983 . https://doi.org/10.1021/bi00141a004
The three-dimensional structure of a 42-residue fragment containing the N-terminal EGF-like module of blood coagulation factor X was determined by means of 2D NMR spectroscopy and computer simulation. The spectroscopic data consisted of 370 NOE dista
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cb6e8fb8dbe6ce3784c516f43528e45
https://cris.vtt.fi/en/publications/e7c37a33-e772-4057-b9db-89581aabbc04
https://cris.vtt.fi/en/publications/e7c37a33-e772-4057-b9db-89581aabbc04
Autor:
Torbjörn Drakenberg, Sara Linse, Ann-Kristin Öhlin, Egon Persson, Johan Stenflo, Maria Selander
Publikováno v:
Scopus-Elsevier
Coagulation factor X is a vitamin K-dependent protein composed of discrete domains or modules. A proteolytically modified derivative of factor X that lacks the NH2-terminal gamma-carboxyglutamic acid (Gla)-containing region retains one Ca2+ binding s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1583702a9a62bb54b36d55f7af46a214
https://doi.org/10.1016/s0021-9258(19)84792-0
https://doi.org/10.1016/s0021-9258(19)84792-0
Autor:
Johan Stenflo, C Valcarce, Ingemar Björk, Sara Linse, Egon Persson, Torbjörn Drakenberg, Maria Selander, Jan Astermark, Ann-Kristin Öhlin
Publikováno v:
Scopus-Elsevier
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95bd04cae462573dcebddcd36bf2b733
http://www.scopus.com/inward/record.url?eid=2-s2.0-0025867206&partnerID=MN8TOARS
http://www.scopus.com/inward/record.url?eid=2-s2.0-0025867206&partnerID=MN8TOARS