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César Carrasco-López

Researcher at Princeton University

Publications -  35
Citations -  1232

César Carrasco-López is an academic researcher from Princeton University. The author has contributed to research in topics: Peptidoglycan & Lipase. The author has an hindex of 14, co-authored 33 publications receiving 902 citations. Previous affiliations of César Carrasco-López include New York University Abu Dhabi & University of Los Andes.

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How allosteric control of Staphylococcus aureus penicillin binding protein 2a enables methicillin resistance and physiological function

TL;DR: The identification of an allosteric binding domain—a remarkable 60 Å distant from the dd-transpeptidase active site—discovered by crystallographic analysis of a soluble construct of PBP2a opens an unprecedented realm for β-lactam antibiotic structure-based design.
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Activation of Bacterial Thermoalkalophilic Lipases Is Spurred by Dramatic Structural Rearrangements

TL;DR: The combination of structural and biochemical studies indicate that the lid opening is not mediated by temperature but triggered by interaction with lipid substrate, and the first structure of a member of the lipase family I.5 showing an open configuration is reported.
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Enolase as a plasminogen binding protein in Leishmania mexicana

TL;DR: It is shown that the purified recombinant enolase has plasminogen binding activity indicating that, at the surface of the parasite, the protein may function as one of the plAsminogen receptors.
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Optogenetic control of protein binding using light-switchable nanobodies.

TL;DR: The development of opto-nanobodies (OptoNBs), a versatile class of chimeric photoswitchable proteins whose binding to proteins of interest can be enhanced or inhibited upon blue light illumination, represents a step towards programmable photos witchable regulation of a wide variety of target proteins.
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Disruption of allosteric response as an unprecedented mechanism of resistance to antibiotics.

TL;DR: Ceftaroline is able to inhibit penicillin-binding protein 2a (PBP2a) by triggering an allosteric conformational change that leads to the opening of the active site, an event that impairs cell-wall biosynthesis and leads to bacterial death.