A
Abel Baerga-Ortiz
Researcher at University of Cambridge
Publications - 15
Citations - 759
Abel Baerga-Ortiz is an academic researcher from University of Cambridge. The author has contributed to research in topics: Thrombomodulin & Thrombin. The author has an hindex of 12, co-authored 13 publications receiving 734 citations. Previous affiliations of Abel Baerga-Ortiz include University of California, San Diego & University of Puerto Rico.
Papers
More filters
Journal ArticleDOI
Epitope mapping of a monoclonal antibody against human thrombin by H/D-exchange mass spectrometry reveals selection of a diverse sequence in a highly conserved protein
TL;DR: The epitope of a monoclonal antibody raised against human thrombin has been determined by hydrogen/deuterium exchange coupled to MALDI mass spectrometry and turned out to be the more structured of two surface regions in which higher sequence variation between the three species is seen.
Journal ArticleDOI
Solvent accessibility of the thrombin-thrombomodulin interface
TL;DR: The kinetics of solvent accessibility at the protein-protein interface between thrombin and a fragment of thrombomodulin, TMEGF45, have been monitored by amide hydrogen/deuterium (H/2H) exchange detected by MALDI-TOF mass spectrometry.
Journal ArticleDOI
Molecular basis of Celmer's rules: stereochemistry of catalysis by isolated ketoreductase domains from modular polyketide synthases.
Alexandros P. Siskos,Abel Baerga-Ortiz,Shilpa Bali,Viktor Stein,Hassan Mamdani,Dieter Spiteller,Bojana Popovic,Jonathan B. Spencer,James Staunton,Kira J. Weissman,Peter F. Leadlay +10 more
TL;DR: A system is reported for the recombinant expression of individual ketoreductase (KR) domains from modular polyketide synthases (PKSs) and scrutiny of their intrinsic specificity and stereospecificity toward surrogate diketide substrates, demonstrating the fine energetic balance between alternative modes of presentation of ketoacylthioester substrates to KR active sites.
Journal ArticleDOI
Directed mutagenesis alters the stereochemistry of catalysis by isolated ketoreductase domains from the erythromycin polyketide synthase.
Abel Baerga-Ortiz,Bojana Popovic,Alexandros P. Siskos,Helen M. O'Hare,Dieter Spiteller,Mark G. Williams,Nuria E. Campillo,Jonathan B. Spencer,Peter F. Leadlay +8 more
TL;DR: Modelling of ketoreductase domains showed that conserved amino acids previously correlated with production of alternative alcohol configurations lie in the active site, confirming the role of key residues in stereocontrol and suggesting an additional way to make rational alterations in polyketide antibiotic structure.
Journal ArticleDOI
Electrostatic dependence of the thrombin-thrombomodulin interaction.
TL;DR: Results show that the thrombin-TM456 interaction is extremely rapid and nearly completely electrostatically steered.