0000000000430668

AUTHOR

Joost C. M. Meijers

showing 3 related works from this author

Atherothrombosis and Thromboembolism: Position Paper from the Second Maastricht Consensus Conference on Thrombosis

2018

AbstractAtherothrombosis is a leading cause of cardiovascular mortality and long-term morbidity. Platelets and coagulation proteases, interacting with circulating cells and in different vascular beds, modify several complex pathologies including atherosclerosis. In the second Maastricht Consensus Conference on Thrombosis, this theme was addressed by diverse scientists from bench to bedside. All presentations were discussed with audience members and the results of these discussions were incorporated in the final document that presents a state-of-the-art reflection of expert opinions and consensus recommendations regarding the following five topics: 1. Risk factors, biomarkers and plaque inst…

0301 basic medicinemedicine.medical_specialtyanticoagulantsADJUST ANTIPLATELET THERAPYPERCUTANEOUS CORONARY INTERVENTION030204 cardiovascular system & hematologyarterial thrombosisArticleantiplatelet therapyACTIVATED PROTEIN-CRED-BLOOD-CELLS03 medical and health sciences0302 clinical medicineVITAMIN-K ANTAGONISTSInternal medicineatherothrombosisIschaemic strokeNONVALVULAR ATRIAL-FIBRILLATIONmedicinePlateletatrial fibrillationACUTE ISCHEMIC-STROKEcoagulationATOMIC-FORCE MICROSCOPYCardiovascular mortalityischaemic strokeAtomic force microscopybusiness.industryConsensus conferenceHematologymedicine.diseaseThrombosis030104 developmental biologymyocardial infarctionCoagulationplateletsDIRECT ORAL ANTICOAGULANTSCardiologyPosition paperSYMPTOMATIC VENOUS THROMBOEMBOLISMatherosclerosisbusiness
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Mapping of the Discontinuous H-kininogen Binding Site of Plasma Prekallikrein

1999

Plasma prekallikrein, a zymogen of the contact phase system, circulates in plasma as heterodimeric complex with H-kininogen. The binding is mediated by the prekallikrein heavy chain consisting of four apple domains, A1 to A4, to which H-kininogen binds with high specificity and affinity (K(D) = 1.2 x 10(-8) M). Previous work had demonstrated that a discontinuous kininogen-binding site is formed by a proximal part located in A1, a distal part exposed by A4, and other yet unidentified portion(s) of the kallikrein heavy chain. To detect relevant binding segment(s) we recombinantly expressed single apple domains and found a rank order of binding affinity for kininogen of A2 > A4 approximately A…

Kininogen bindingKininogenChemistryHigh-molecular-weight kininogenPrekallikreinCell BiologyKallikreinPlasma protein bindingBiochemistryBiochemistryZymogenBinding siteMolecular Biologycirculatory and respiratory physiologyJournal of Biological Chemistry
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Mapping of the Discontinuous Kininogen Binding Site of Prekallikrein

1996

Prekallikrein, the precursor to the serine proteinase kallikrein, circulates in plasma in an equimolar complex with H-kininogen. The binding to H-kininogen is mediated by the kallikrein heavy chain consisting of four "apple" domains, A1-A4, which attaches to H-kininogen with high specificity and affinity (KD = 83 nM). At least two distinct portions of the kallikrein heavy chain form this H-kininogen binding site: a proximal segment located in the NH2-terminal fragment of the heavy chain encompassing A1, and distal segment(s) located in COOH-terminal fragment spanning domains A2-A4. The proximal binding segment has been located to amino acid positions 56-86 of A1. To precisely map the distal…

Kininogen bindingchemistry.chemical_classificationChemistryPrekallikreinCell BiologyKallikreinBiochemistryMolecular biologyEpitopelaw.inventionAmino acidSerinelawRecombinant DNABinding siteMolecular Biologycirculatory and respiratory physiologyJournal of Biological Chemistry
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