2019 - Fellow of the American Association for the Advancement of Science (AAAS)
Biochemistry, Stereochemistry, Thrombin, Allosteric regulation and Enzyme are his primary areas of study. The Proteases and Glycoprotein research he does as part of his general Biochemistry study is frequently linked to other disciplines of science, such as Ice crystals, therefore creating a link between diverse domains of science. His studies in Stereochemistry integrate themes in fields like Ligand, Macromolecule, Dissociation, Protein structure and Allosteric enzyme.
Enrico Di Cera has researched Thrombin in several fields, including Anticoagulant, Protein C, Pharmacology and Active site. His research integrates issues of Protein engineering and Conformational change in his study of Allosteric regulation. The concepts of his Enzyme study are interwoven with issues in Molecular mechanism, Mutant, Structural biology, Monovalent Cations and Catalysis.
Enrico Di Cera spends much of his time researching Thrombin, Stereochemistry, Biochemistry, Allosteric regulation and Active site. His Thrombin research integrates issues from Protein C, Fibrinogen, Mutant and Enzyme. His work deals with themes such as Ligand, Hydrolase, Crystallography, Protein structure and Binding site, which intersect with Stereochemistry.
The study incorporates disciplines such as Biophysics and Fibrin in addition to Biochemistry. His Allosteric regulation study integrates concerns from other disciplines, such as Hirudin and Cooperativity. In his work, Prothrombinase is strongly intertwined with Zymogen, which is a subfield of Active site.
Enrico Di Cera focuses on Thrombin, Stereochemistry, Zymogen, Biochemistry and Protein C. The various areas that Enrico Di Cera examines in his Thrombin study include Biophysics, Protease, Gla domain and Active site. Enrico Di Cera interconnects Protein structure, Hydrolase and Allosteric regulation in the investigation of issues within Stereochemistry.
His Zymogen study incorporates themes from Proteases, Structural biology, Clotting factor and Proteolysis. His research on Biochemistry frequently links to adjacent areas such as Thrombomodulin. His Protein C research incorporates elements of Platelet, Fibrinogen, Activator and Pharmacology.
Enrico Di Cera mainly focuses on Stereochemistry, Thrombin, Gla domain, Biochemistry and Ligand. His work carried out in the field of Stereochemistry brings together such families of science as Allosteric enzyme and Mechanism. His Thrombin research is multidisciplinary, incorporating elements of Zymogen, Protease and Active site.
His Active site course of study focuses on Trypsin and Proteases and Thromboplastin. His Gla domain research also works with subjects such as
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Evolution of enzyme cascades from embryonic development to blood coagulation
Maxwell M. Krem;Enrico Di Cera.
Trends in Biochemical Sciences (2002)
Role of Na+ and K+ in Enzyme Function
Michael J. Page;Enrico Di Cera.
Physiological Reviews (2006)
Serine proteases
Enrico Di Cera.
Iubmb Life (2009)
The Na+ Binding Site of Thrombin
Enrico Di Cera;Enriqueta R. Guinto;Alessandro Vindigni;Quoc D. Dang.
Journal of Biological Chemistry (1995)
Thrombin is a Na(+)-activated enzyme.
Christina M. Wells;Enrico Di Cera.
Biochemistry (1992)
Conformational Selection or Induced Fit? A Critical Appraisal of the Kinetic Mechanism
Austin D. Vogt;Enrico Di Cera.
Biochemistry (2012)
Valence screening of water in protein crystals reveals potential Na+ binding sites.
Murad Nayal;Enrico Di Cera.
Journal of Molecular Biology (1996)
Molecular markers of serine protease evolution
Maxwell M. Krem;Enrico Di Cera.
The EMBO Journal (2001)
Characterization of the Bacterial Sensor Protein PhoQ EVIDENCE FOR DISTINCT BINDING SITES FOR Mg2+ AND Ca2+
Elenora García Véscovi;Youhna M. Ayala;Enrico Di Cera;Eduardo A. Groisman.
Journal of Biological Chemistry (1997)
Molecular Dissection of Na+ Binding to Thrombin
Agustin O. Pineda;Christopher J. Carrell;Leslie A. Bush;Swati Prasad.
Journal of Biological Chemistry (2004)
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