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Protein Science : a Publication of the Protein Society|January 1, 1992
The sequence HGLGHGHEQQHGLGHGH in the light chain of high molecular weight kininogen serves as a primary structural feature for zinc-dependent binding to an anionic surfaceR A DeLa Cadena, R W Colman
Trends in Pharmacological Sciences|July 1, 1991
Structure and functions of human kininogensR A DeLa Cadena, R W Colman
The Journal of Biological Chemistry|February 5, 1993
Deletion mutagenesis of high molecular weight kininogen light chain. Identification of two anionic surface binding subdomainsS P Kunapuli, R A DeLa Cadena, R W Colman
Thrombosis and Haemostasis|April 2, 1992
Bacterial expression of biologically active high molecular weight kininogen light chainS P Kunapuli, R A DeLa Cadena, R W Colman
British Journal of Haematology|May 1, 1994
An autoantibody to human plasma prekallikrein blocks activation of the contact systemJ D Page, R A DeLa Cadena, J E Humphries, et al.
Thrombosis and Haemostasis|February 12, 1998
Expression of thrombospondin 1 on the surface of activated platelets mediates their interaction with the heavy chains of human kininogens through Lys 244-Pro 254R A DeLa Cadena, S P Kunapuli, D A Walz, et al.
European Journal of Biochemistry|January 15, 1998
High-molecular-mass and low-molecular-mass kininogens block plasmin-induced platelet aggregation by forming a complex with kringle 5 of plasminogen/plasminT E Selim, H R Ghoneim, A B Uknis, et al.
The Hematology Journal : the Official Journal of the European Haematology Association|March 29, 2002
High molecular mass kininogen inhibits cathepsin G-induced platelet activation by forming a complex with cathepsin GT E Selim, H R Ghoneim, H A Abdel Ghaffar, et al.
Immunopharmacology|June 1, 1996
Activation of the contact and fibrinolytic systems after intravenous administration of endotoxin to normal human volunteers: correlation with the cytokine profileR A DeLa Cadena, A Majluf-Cruz, A Stadnicki, et al.
The Journal of Biological Chemistry|April 1, 1994
The shape of high molecular weight kininogen. Organization into structural domains, changes with activation, and interactions with prekallikrein, as determined by electron microscopyJ W Weisel, C Nagaswami, J L Woodhead, et al.
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