Sulfated low molecular weight lignins, allosteric inhibitors of coagulation proteinases via the heparin binding site, significantly alter the active site of thrombin and factor xa compared to heparin

Thrombosis Research

Volumn 134, Issue 5, 2014, Pages 1123-1129

  Henry, Brian L ^a   Desai, Umesh R ^b  

^a UNIVERSITY OF PITTSBURGH MEDICAL CENTER   (United States)

^b VIRGINIA COMMONWEALTH UNIVERSITY   (United States)

Author keywords

Allosteric mechanism; Anticoagulation; Exosite II; Heparin; Sulfated lignins; Thrombin

Indexed keywords

4 AMINOBENZAMIDINE; AMINO ACID; ANTICOAGULANT AGENT; BLOOD CLOTTING FACTOR 10A; CHROMOGENIC SUBSTRATE; HEPARIN; LIGNIN; PROTEINASE; SERINE; THROMBIN; CDSO3 COMPOUND; KRAFT LIGNIN;

ALLOSTERISM; ANTICOAGULATION; ARTICLE; BINDING SITE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME SUBSTRATE COMPLEX; GEOMETRY; HUMAN; HYDROLYSIS; MICHAELIS CONSTANT; PRIORITY JOURNAL; BLOOD CLOTTING; CHEMISTRY; DRUG EFFECTS; METABOLISM;

ANTICOAGULANTS; BINDING SITES; BLOOD COAGULATION; CATALYTIC DOMAIN; FACTOR XA; HEPARIN; HUMANS; HYDROLYSIS; LIGNIN; THROMBIN;

EID: 84927610134     PISSN: 00493848     EISSN: 18792472     Source Type: Journal    
DOI: 10.1016/j.thromres.2014.08.024     Document Type: Article

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