Conformational transitions in factor VIIa: can we stabilize the inactive form of the enzyme?
De
Cristofaro Raimondo
CR
Hemostasis Research Center, Institute of Medical Semeiotics, Catholic University School of Medicine, Rome, Italy. rdecristofaro@rm.unicatt.it
D020816:Amino Acid Motifs; D000925:Anticoagulants / Q000737:chemistry / Q000494:pharmacology; D020134:Catalytic Domain; D015195:Drug Design; D004789:Enzyme Activation / Q000187:drug effects; D015942:Factor VIIa / Q000037:antagonists & inhibitors / Q000737:chemistry*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry / Q000494:pharmacology; D010456:Peptides, Cyclic / Q000737:chemistry / Q000494:pharmacology; D011487:Protein Conformation / Q000187:drug effects; D015842:Serine Proteinase Inhibitors / Q000737:chemistry / Q000494:pharmacology
D000925:Anticoagulants; C463960:PN 7051; D010446:Peptide Fragments; D010456:Peptides, Cyclic; D015842:Serine Proteinase Inhibitors; D015942:Factor VIIa