about
Rigidification of the autolysis loop enhances Na+ binding to thrombinCrystallographic and Kinetic Evidence of Allostery in a Trypsin-like ProteaseCrystal Structures of Prethrombin-2 Reveal Alternative Conformations under Identical Solution Conditions and the Mechanism of Zymogen ActivationAutoactivation of Thrombin PrecursorsCrystal Structure of Prothrombin Reveals Conformational Flexibility and Mechanism of ActivationEssential role of conformational selection in ligand bindingThe linker connecting the two kringles plays a key role in prothrombin activationLoop Electrostatics Asymmetry Modulates the Preexisting Conformational Equilibrium in ThrombinThrombin inhibition by serpins disrupts exosite IIProthrombin structure: unanticipated features and opportunities.Why Ser and not Thr brokers catalysis in the trypsin foldWEDGE: an anticoagulant thrombin mutant produced by autoactivation.Costimulatory Effects of an Immunodominant Parasite Antigen Paradoxically Prevent Induction of Optimal CD8 T Cell Protective Immunity.Conformational selection in trypsin-like proteases.How the Linker Connecting the Two Kringles Influences Activation and Conformational Plasticity of ProthrombinHistone H4 promotes prothrombin autoactivation.Rational Design of Protein C Activators.Structural Architecture of Prothrombin in Solution Revealed by Single Molecule Spectroscopy.Dual effect of histone H4 on prothrombin activation.Fibrinogen-elongated gamma chain inhibits thrombin-induced platelet response, hindering the interaction with different receptorsFormation of methionine sulfoxide by peroxynitrite at position 1606 of von Willebrand factor inhibits its cleavage by ADAMTS-13: A new prothrombotic mechanism in diseases associated with oxidative stress.Oxidized von Willebrand factor is efficiently cleaved by serine proteases from primary granules of leukocytes: divergence from ADAMTS-13.Oxidation of Met1606 in von Willebrand factor is a risk factor for thrombotic and septic complications in chronic renal failure.Modeling ADAMTS13-von Willebrand factor interaction: Implications for oxidative stress-related cardiovascular diseases and type 2A von Willebrand disease.Apolipoprotein L1 confers pH-switchable ion permeability to phospholipid vesicles.Structure of prothrombin in the closed form reveals new details on the mechanism of activation.β2 -Glycoprotein I binds to thrombin and selectively inhibits the enzyme procoagulant functions.Molecular mapping of α-thrombin (αT)/β2-glycoprotein I (β2GpI) interaction reveals how β2GpI affects αT functions.Peptide ligand-based ELISA reagents for antibody detectionStructure of Coagulation Factor II: Molecular Mechanism of Thrombin Generation and Development of Next-Generation AnticoagulantsEndocrine disruption of androgenic activity by perfluoroalkyl substances: clinical and experimental evidenceReversible covalent direct thrombin inhibitorsAntibodies to Domain I of β(2)Glycoprotein I are in close relation to patients risk categories in Antiphospholipid Syndrome (APS)RNase A oligomerization through 3D domain swapping is favoured by a residue located far from the swapping domainsA Multimodality Approach to Assessing Factor I Genetic Variants in Atypical Hemolytic Uremic SyndromeEnhancing the anticoagulant profile of meizothrombinDiscovery and characterization of 2 novel subpopulations of aPS/PT antibodies in patients at high risk of thrombosisLupus anticoagulant identifies two distinct groups of patients with different antibody patternsThe J-elongated conformation of β2-glycoprotein I predominates in solution: Implications for our understanding of antiphospholipid syndrome
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description
hulumtues
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researcher
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ricercatore
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wetenschapper
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հետազոտող
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name
Nicola Pozzi
@ast
Nicola Pozzi
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Nicola Pozzi
@es
Nicola Pozzi
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Nicola Pozzi
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type
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Nicola Pozzi
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Nicola Pozzi
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Nicola Pozzi
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Nicola Pozzi
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Nicola Pozzi
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prefLabel
Nicola Pozzi
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Nicola Pozzi
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Nicola Pozzi
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Nicola Pozzi
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Nicola Pozzi
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19235774600
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P214
P2798
P31
P396
IT\ICCU\CFIV\269913
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0000-0003-2309-7100
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1981-01-01T00:00:00Z
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