Zobrazeno 1 - 10
of 46
pro vyhledávání: '"K, Ohlin"'
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Publikováno v:
Lymphology. 41(2)
In 1987 we noticed excess adipose tissue in a patient with arm lymphedema and later, objective studies confirmed this clinical finding in patients with non-pitting arm lymphedema following breast cancer. A prospective study was begun in 1993, and its
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Autor:
A K, Ohlin, R A, Marlar
Publikováno v:
Thrombosis and haemostasis. 81(3)
It has been suggested that an impaired thrombomodulin (TM) function could constitute an abnormality leading to thromboembolic disease (TED). The TM gene from 51 unrelated American patients with TED and 100 American blood donors was screened for mutat
Publikováno v:
Thrombosis and haemostasis. 78(1)
Thrombomodulin (TM) is the endothelial cell cofactor for protein C activation. Since deficiencies of other protein C system proteins are known to cause thrombotic disease, then defects in the gene coding for TM could be responsible for inherited thro
OBJECTIVES--To evaluate an increase in plasma concentration of thiobarbituric acid reactive substances as a non-invasive biochemical test of reperfusion after thrombolysis and to investigate the relation between the inflammatory response after acute
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f261992eef0f64421fa2753939bd7d2a
https://europepmc.org/articles/PMC483802/
https://europepmc.org/articles/PMC483802/
Autor:
A K, Ohlin
Publikováno v:
Lakartidningen. 91(43)
Publikováno v:
Methods in enzymology. 222
Publikováno v:
The Journal of biological chemistry. 267(2)
The structural domains of protein C involved in its interaction with thrombin-thrombomodulin on the endothelial cell surface have been investigated using isolated intact domains of bovine protein C produced from controlled proteolytic digests of the
Publikováno v:
The Journal of biological chemistry. 266(4)
Blood coagulation factor IX is composed of discrete domains with an NH2-terminal vitamin K-dependent gamma-carboxyglutamic acid (Gla)-containing region, followed by two domains that are homologous with the epidermal growth factor (EGF) precursor and