• Publications
  • Influence
Prevention of vascular and neural dysfunction in diabetic rats by C-peptide.
Synthetic reverse sequence and all-D-amino acid C-peptides were equipotent to native C-PEptide, which indicates that the effects of C- peptide on diabetic vascular and neural dysfunction were mediated by nonchiral interactions instead of stereospecific receptors or binding sites.
Conformational selection or induced fit? A critical appraisal of the kinetic mechanism.
It is shown that conformational selection is associated with a rich repertoire of kinetic properties, with k(obs) decreasing or increasing with [L] depending on the relative magnitude of the rate of ligand dissociation, k(off), and the rates of conformational isomerization, r.
Molecular Dissection of Na+ Binding to Thrombin*
The role of the water network uncovered in this study establishes a new paradigm for the allosteric regulation of thrombin and other Na+-activated enzymes involved in blood coagulation and the immune response.
Characterization of the Bacterial Sensor Protein PhoQ
Cumulatively, these experiments demonstrate that Mg2+ can bind to the sensing domain of PhoQ and establish the presence of distinct binding sites for Mg 2+ and Ca2+ in thePhoQ protein.
Crystal structure of the large fragment of Thermus aquaticus DNA polymerase I at 2.5-A resolution: structural basis for thermostability.
The crystal structure of the large fragment of the Thermus aquaticus DNA polymerase (Klentaq1), determined at 2.5-A resolution, demonstrates a compact two-domain architecture. The C-terminal domain
An allosteric switch controls the procoagulant and anticoagulant activities of thrombin.
The allosteric properties of thrombin, which has targeted two distinct conformational states toward its two fundamental and competing roles in hemostasis, are paradigmatic of a molecular strategy that is likely to be exploited by other proteases in the blood coagulation cascade.
Structural identification of the pathway of long-range communication in an allosteric enzyme
The crystal structure of the thrombin-PAR1 complex, solved at 2.2-Å resolution, reveals the details of this long-range allosteric communication in terms of a network of polar interactions.
Predicting Ca(2+)-binding sites in proteins.
  • M. Nayal, E. Di Cera
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences…
  • 18 January 1994
The valence is a tool of pinpoint accuracy for locating cation-binding sites, which can also be exploited in engineering high-affinity binding sites and characterizing the linkage between structural components and functional energetics for molecular recognition of metal ions by proteins.
Role of Na+ and K+ in enzyme function.
From this analysis, M+ complexation has the potential to be an efficient regulator of enzyme catalysis and stability and offers novel strategies for protein engineering to improve enzyme function.
A Structural Perspective on Enzymes Activated by Monovalent Cations*
  • E. Di Cera
  • Biology
    Journal of Biological Chemistry
  • 20 January 2006
Progress in the structural biology of enzymes activated by monovalent cations enables a simple classification of these functionally diverse enzymes and reveals unanticipated connections with ion transporters.