F
F. I. Pareti
Researcher at University of Milan
Publications - 33
Citations - 2018
F. I. Pareti is an academic researcher from University of Milan. The author has contributed to research in topics: Platelet & Von Willebrand factor. The author has an hindex of 19, co-authored 33 publications receiving 1971 citations.
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Journal ArticleDOI
1-deamino-8-d-arginine vasopressin: a new pharmacological approach to the management of haemophilia and von willebrand's disease
TL;DR: D.D.A.V.P. appears a promision pharmacological alternative to plasma concentrates in the management of some patients with haemophilis and von Willebrand's disease.
Journal ArticleDOI
Effects of monoclonal antibodies against the platelet glycoprotein IIb/IIIa complex on thrombosis and hemostasis in the baboon.
Stephen R. Hanson,F. I. Pareti,Zaverio M. Ruggeri,Ulla M. Marzec,Thomas J. Kunicki,Robert R. Montgomery,Theodore S. Zimmerman,Laurence A. Harker +7 more
TL;DR: ABVs that functionally alter the platelet GP IIb/IIIa complex may produce immediate, potent, and transient, antihemostatic, and antithrombotic effects in baboons.
Journal ArticleDOI
Proteolysis of von Willebrand Factor and Shear Stress–Induced Platelet Aggregation in Patients With Aortic Valve Stenosis
F. I. Pareti,Antonella Lattuada,Caterina Bressi,Marco Zanobini,Angelo Sala,Agostino Steffan,Zaverio M. Ruggeri +6 more
TL;DR: Improvement after corrective surgery suggests that the passage of blood through a stenosed aortic valve may result in shear forces that induce vWF interaction with platelets in the circulation and, in turn, trigger platelet clearance, vWF degradation, and the impairment of primary hemostasis.
Journal Article
Platelets and the vessel wall: how much aspirin?
Journal ArticleDOI
Isolation and characterization of a collagen binding domain in human von Willebrand factor.
F. I. Pareti,Yoshihiro Fujimura,Judith A. Dent,Linda Z. Holland,Theodore S. Zimmerman,Zaverio M. Ruggeri +5 more
TL;DR: The studies precisely define a domain in the von Willebrand factor subunit that interacts with type I collagen that recognizes the same interaction site as the intact molecule.