![]() | Zaverio M RuggeriShow email addressDepartment of Molecular Medicine, MERU-Roon Research Center for Vascular Biology, Scripps Research, La Jolla, CA 92037, USA. | Department of Molecular Medicine, MERU-Roon ... |
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Zaverio M Ruggeri:Expert Impact
Concepts for whichZaverio M Ruggerihas direct influence:Willebrand factor,Platelet adhesion,Willebrand disease,Platelet aggregation,Platelet glycoprotein,Factor viii,Thrombus formation,Platelet adherence.
Zaverio M Ruggeri:KOL impact
Concepts related to the work of other authors for whichfor which Zaverio M Ruggeri has influence:Willebrand factor,Platelet aggregation,Endothelial cells,Thrombus formation,Cell adhesion,Shear stress,Blood coagulation.
KOL Resume for Zaverio M Ruggeri
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2022 | Department of Molecular Medicine, MERU-Roon Research Center for Vascular Biology, Scripps Research, La Jolla, CA 92037, USA. |
2021 | Department of Molecular Medicine, MERU-Roon Research Center on Vascular Biology, The Scripps Research Institute, La Jolla, CA, USA |
2020 | From the Department of Molecular Medicine, The Scripps Research Institute, La Jolla, CA (J.Z.-R., H.D., M.S., J.N.O., Z.G., T.W., L.O.M., Z.M.R., J.H.G.). Department of Molecular Medicine, MERU-Roon Research Center on Vascular Biology, The Scripps Research Institute, La Jolla, CA. |
2019 | Department of Molecular Medicine, MERU-Roon Research Center on Vascular Biology, The Scripps Research Institute, La Jolla, CA |
2018 | Department of Molecular Medicine, MERU-Roon Research Center on Vascular Biology and Thrombosis, The Scripps Research Institute, La Jolla, CA; and. |
2017 | The Scripps Research Institute, La Jolla, California Department of Molecular Medicine and. |
2016 | Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California, USA |
2015 | Zaverio M. Ruggeri, MD, The Scripps Research Institute, Maildrop: MEM 175, 10550 North Torrey Pines Road, La Jolla, California 92037, USA, Tel. 858/784 89 50, Fax 858/784 20 26, E-mail: From the Knight Cardiovascular Institute, Oregon Health & Science University, Portland, OR (C.Y.S., Y.N.L., T.A., A.X., T.F., B.P.D., M.T., Y.Q., J.R.L.); Puget Sound Blood Center Research Institute, Seattle, WA (J.A.L., A.M.); and Department of Molecular and Experimental Medicine, Roon Research Center for Arteriosclerosis and Thrombosis, The Scripps Research Institute, La Jolla, CA (Z.R.). Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA THE SCRIPPS RESEARCH INSTITUTE. |
2014 | Molecular and Experimental Medicine, The Scripps Rsch Institute, La Jolla, CA |
2013 | From the Division of Cardiology, Department of Biomedicine, University Hospital and University of Basel, Basel, Switzerland (E.K., M. Mitterhuber, L.X., M. Mochizuki, G.M.K., B.A.K.); Division of Cardiovascular Medicine, Oregon Health & Science University, Portland, OR (Y.Q., A.X., J.R.L.); Department of Pathology and Immunology, Geneva Medical Faculty, Geneva University Hospital, Geneva, Switzerland (V.J., K.-H.K.); Division of Clinical Pharmacology and Toxicology, Geneva University Hospital, Geneva, Switzerland (Y.D.); and Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA (Z.M.R.). Roon Research Center for Arteriosclerosis and Thrombosis, The Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California, United States of America |
2012 | Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA, USA, |
2011 | Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario, Canada., Toronto Platelet Immunobiology Group and Department of Laboratory Medicine, Keenan Research Centre in the Li Ka Shing Knowledge Institute of St. Michael’s Hospital, Toronto, Ontario, Canada., Canadian Blood Services, Toronto, Ontario, Canada., Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California, USA., Department of Medicine, McMaster University, Hamilton, Ontario, Canada., Department of Physiology and Biophysics, University of Arkansas for Medical Sciences, Little Rock, Arkansas, USA., Department of Medicine and, Department of Physiology, University of Toronto, Ontario, Canada. |
2010 | Zaverio M. Ruggeri is in the Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California, USA. |
2009 | Roon Research Center for Arteriosclerosis and Thrombosis, Division of Blood Cell and Vascular Biology, Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California, USA Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA; Molecular and Experimental Medicine, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037 |
2008 | Roon Research Center for Arteriosclerosis and Thrombosis, Division of Blood Cell and Vascular Biology, Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, U.S.A Departments of *Molecular and Experimental Medicine and ‡Molecular and Integrative Neurosciences, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037; and †Immunopathogenesis of Liver Infections Unit, San Raffaele Scientific Institute, Via Olgettina 58, 20132 Milan, Italy Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA, USA |
2007 | Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037 The Scripps Research Institute, La Jolla, California, USA |
2006 | From the Roon Center for Arteriosclerosis and Thrombosis, Division of Experimental Hemostasis and Thrombosis, Department of Molecular and Experimental Medicine, The Scripps Research Institute-MEM 175, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA The Scripps Research Institute, La Jolla, CA 92037; and |
2005 | Department of Molecular and Experimental Medicine, The Scripps Research Institute, 10550 North Torrey Pines Road, 92037, La Jolla, California, USA |
2004 | From the Blood Bank, Centro di Riferimento Oncologico-Istituto di Ricerca e Cura a Carattere Scientifico, National Cancer Institute, Aviano, Italy; and the Roon Research Center for Arteriosclerosis and Thrombosis, Division of Experimental Thrombosis and Hemostasis, Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA Roon Research Center in Arteriosclerosis and Thrombosis, Department of Molecular and Experimental Medicine, Division of Experimental Hemostasis and Thrombosis, The Scripps Research Institute, La Jolla, California 92037 |
2003 | Roon Research Center for Arteriosclerosis and Thrombosis, Division of Experimental Thrombosis and Hemostasis; Division of Cellular Biology, Department of Molecular and Experimental Medicine, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. Departments of Molecular and Experimental Medicine and of Vascular Biology, The Scripps Research Institute, La Jolla, CA, USA |
2002 | From the Section for Microbiology, Immunology and Glycobiology, the Institute of Laboratory Medicine, University of Lund, Lund, Sweden, and Roon Research Center for Arteriosclerosis and Thrombosis, Division of Experimental Hemostasis and Thrombosis, Departments of Molecular and Experimental Medicine and of Vascular Biology, Scripps Research Institute, La Jolla, CA. Roon Research Center for Arteriosclerosis and Thrombosis, Division of Experimental Hemostasis and Thrombosis, Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California 92037 Department of Molecular and Experimental Medicine The Scripps Research Institute, La Jolla, California, USA |
2001 | Departments of Molecular and Experimental Medicine, Scripps Research Institute |
2000 | From the Roon Research Center for Arteriosclerosis and Thrombosis, Division of Experimental Hemostasis and Thrombosis, Department of Molecular and Experimental Medicine, and Department of Vascular Biology, The Scripps Research Institute, La Jolla, USA |
1999 | From the Roon Research Center for Arteriosclerosis and Thrombosis, Division of Experimental Hemostasis and Thrombosis, Departments of Molecular and Experimental Medicine and of Vascular Biology, The Scripps Research Institute, La Jolla, California 92037 |
Concept | World rank |
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platelet glycoprotein ldl | #1 |
dimerization defects | #1 |
pretreatment betagalactosidase | #1 |
vwf exposed | #1 |
molecules normal trp550 | #1 |
atherosclerosis 40 weeks | #1 |
alpha demonstrating | #1 |
kda fragment | #1 |
integrin cultured adenoviruses | #1 |
ap5 binding | #1 |
alpha coding sequence | #1 |
lamellipodia gpvi | #1 |
applaggin unstimulated platelets | #1 |
onechain species | #1 |
vwf wortmannin willebrand | #1 |
alphavbeta3 integrin antigen | #1 |
45kda fragment | #1 |
5a7 antibody surface | #1 |
gpiib iiia addition | #1 |
specific synergy | #1 |
occlusion occlusion rate | #1 |
internalized water molecule | #1 |
gpibix thrombin | #1 |
macrophage content age | #1 |
purified glycocalicin | #1 |
vwf progress | #1 |
thromboinflammatory pathway | #1 |
residues his1 | #1 |
dic pvwf | #1 |
arg1744 gly1745 | #1 |
alpha chain glycoprotein | #1 |
glu149ala | #1 |
multimers released | #1 |
disulfide bond requirements | #1 |
176 kd fragment | #1 |
pi3k platelet activation | #1 |
linked silent polymorphisms | #1 |
nmc4 fab | #1 |
monoclonal distinct epitopes | #1 |
vascular forecasting | #1 |
native vwf | #1 |
gpiib iiia absence | #1 |
remote vessels | #1 |
platelet ljp9 | #1 |
platelet α2β1 density | #1 |
ristocetininduced binding binding | #1 |
pi3k gpibalpha | #1 |
functional domain cells | #1 |
labeled vwf platelets | #1 |
molecules saturation | #1 |
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Prominent publications by Zaverio M Ruggeri
Von Willebrand factor (vWF) was purified from the plasma of a patient with type IIB von Willebrand disease (vWF from such a patient, IIB vWF) who had a normal platelet count and showed no evidence of spontaneous platelet aggregation. Large multimers of IIB vWF were absent from purified preparations and from plasma. Ristocetin-induced platelet aggregation was enhanced by purified IIB vWF. The aggregation of washed normal platelets mixed with IIB vWF (0.4 microgram/ml) required lower ...
Known for Iib Vwf | Willebrand Factor | Fibrinogen Binding | Platelet Aggregation | Membrane Glycoprotein |
Glycoprotein (GP) IIb-IIIa is the major fibrinogen receptor on platelets and participates in platelet aggregation at the site of a wound. Integrin alpha v beta 3, which contains an identical beta-subunit, is expressed on endothelial cells and also serves as a fibrinogen receptor. Here, we demonstrate by several criteria that purified GPIIb-IIIa and integrin alpha v beta 3 bind to distinct sites on fibrinogen. First, a plasmin-generated fragment of fibrinogen lacking the RGD sequence at ...
Known for Beta 3 | Integrin Alpha | Glycoprotein Iib | Rgd Sequence | Fibrinogen Binding |
We have generated antibodies against a synthetic peptide corresponding to the sequence of human von Willebrand factor (vWF) between residues Glu1737-Ser1750 which includes the Arg-Gly-Asp sequence common to several adhesive molecules. Two anti-peptide antibodies, one polyclonal, and one monoclonal reacted with native vWF and inhibited its binding to platelet glycoprotein (GP) IIb-IIIa, but showed negligible cross-reactivity with fibrinogen, fibronectin, and vitronectin, three other ...
Known for Willebrand Factor | Amino Acid | Adhesive Molecules | Vwf Residues | Sequence Antibodies |
Affinity modulation of the alpha IIb beta 3 integrin (platelet GPIIb-IIIa) is an intrinsic property of the receptor.
[ PUBLICATION ]
To analyze the basis of affinity modulation of integrin function, we studied cloned stable Chinese hamster ovary cell lines expressing recombinant integrins of the beta 3 family (alpha IIb beta 3 and alpha v beta 3). Antigenic and peptide recognition specificities of the recombinant receptors resembled those of the native receptors found in platelets or endothelial cells. The alpha IIb beta 3-expressing cell line (A5) bound RGD peptides and immobilized fibrinogen (Fg) but not soluble ...
Known for Beta 3 | Alpha Iib | Affinity Modulation | Intrinsic Property | Pac1 Platelets |
Three preparations of purified von Willebrand factor (vWF), obtained from unrelated patients affected by type IIB von Willebrand disease, were found to have normal sialic acid content (between 129 and 170 nmol/mg of vWF, as compared with 158 +/- 17 nmol/mg in four normal preparations) and to induce platelet aggregation in the presence of physiologic levels of divalent cations and without addition of ristocetin. A monoclonal antibody that blocks the vWF binding domain of the platelet ...
Known for Platelet Aggregation | Vwf Gpib | Willebrand Factor | Gpiib Iiia | Binding Domain |
Binding of the adhesive ligand fibrinogen and the monoclonal antibody PAC1 to platelet glycoprotein (GP) IIb-IIIa is dependent on cell activation and inhibited by Arg-Gly-Asp (RGD)-containing peptides. Previously, we identified a sequence in a hypervariable region of PAC1 (mu-CDR3) that mimics the activity of the antibody. Here we examine whether monoclonal antibodies to this idiotypic determinant in PAC1 can mimic GP IIb-IIIa by binding to fibrinogen. Mice were immunized with a peptide ...
Known for Gp Iib | Platelet Glycoprotein | Idiotypic Antibodies | Fibrinogen Binding | Monoclonal Antibody |
von Willebrand factor binds to platelets and induces aggregation in platelet-type but not type IIB von Willebrand disease.
[ PUBLICATION ]
Platelet-type von Willebrand disease (vWD) and pseudo-vWD are two recently described intrinsic platelet defects characterized by enhanced ristocetin-induced agglutination in platelet-rich plasma. A similar finding is also typical of type IIB vWD, where it has been related to a von Willebrand factor (vWF) rather than a platelet abnormality. Platelet aggregation induced by unmodified human vWF in the absence of other stimuli has been reported in pseudo-vWD. In this study we demonstrate ...
Known for Willebrand Factor | Type Iib | Platelets Aggregation | Vwf Platelet | Pseudo Vwd |
A molecular model of RGD ligands. Antibody D gene segments that direct specificity for the integrin alpha IIb beta 3.
[ PUBLICATION ]
Following an ill-defined activation event, the Arg-Gly-Asp (RGD) recognition site of the platelet integrin, glycoprotein IIb-IIIa (alpha IIb beta 3), can bind to fluid-phase, RGD-containing protein ligands, such as fibrinogen, or to the murine monoclonal IgM, PAC-1, which contains the sequence Arg-Tyr-Asp (RYD) within the third complementarity-determining region of its heavy chain (H3). PAC-1 has thus become a widely exploited marker of platelet alpha IIb beta 3 activation. In this ...
Known for Alpha Iib | Beta 3 | Rgd Ligands | Antibody Binding | Heavy Chain |
Inhibition of platelet function with synthetic peptides designed to be high-affinity antagonists of fibrinogen binding to platelets
[ PUBLICATION ]
We have constructed synthetic peptides modeled on the sequences of (i) Arg-Gly-Asp, present in fibrinogen, fibronectin, and von Willebrand factor, and of (ii) the fibrinogen gamma chain (gamma 400-411) His-His-Leu-Gly-Gly-Ala-Lys-Gln-Ala-Gly-Asp-Val. The concentration of each peptide that inhibits 50% of 125I-labeled fibrinogen binding to thrombin-stimulated platelets (IC50) was then determined. The IC50 for (gamma 400-411) was 48-180 microM at a fibrinogen concentration of 60 ...
Known for Synthetic Peptides | Fibrinogen Binding | Platelet Function | Gly Asp | Willebrand Factor |
Activation of platelets in blood perfusing angioplasty-damaged coronary arteries. Flow cytometric detection.
[ PUBLICATION ]
Fluorescence-activated flow cytometry has been used to investigate platelet activation in blood flowing through atherosclerotic coronary arteries after sustaining mechanical damage induced by percutaneous transluminal angioplasty (PTCA). For flow cytometry, platelets and platelet-derived microparticles were identified by biotinylated anti-glycoprotein (GP) Ib monoclonal antibody (mAb) and a fluorophore, phycoerythrin-streptavidin. Activated platelets were detected by using a panel of ...
Known for Patients Ptca | Platelets Blood | Cytometric Detection | Activation Platelet | Coronary Angiography |
We have evaluated the subunit composition of plasma von Willebrand factor (vWF) and found evidence that cleavage is present in normal individuals, increased in IIA and IIB von Willebrand disease (vWD), but decreased or absent in variants with aberrant structure of individual oligomers. vWF was rapidly purified from plasma on an analytical scale by monoclonal antibody immunoaffinity chromatography in the presence of protease inhibitors. After reduction and electrophoresis in 5% ...
Known for Subunit Composition | Normal Individuals | Aberrant Structure | Plasma Willebrand | 140 Kd |
In this study we have used two new monoclonal antibodies, designated LJP5 and LJP9, as well as a previously described one, AP2, all specific for the platelet membrane glycoprotein (GP)IIb/IIIa complex. None of them reacted with dissociated GPIIb or GPIIIa. The monovalent Fab fragment of both LJP5 and LJP9 bound to unstimulated platelets in a saturable manner, but binding was markedly decreased after platelets had been incubated at 37 degrees C in the absence of added extracellular ...
Known for Fibrinogen Binding | Willebrand Factor | Platelet Membrane | Iiia Complex | Monoclonal Antibodies |