P. D. B. Olinares

This study determines cryo-EM structures of SARS-CoV-2 NiRAN domain catalytic intermediates, revealing structural mechanisms for NMPylation and deRNAylation/capping, and explaining substrate preference for capping.

The paper develops covalent inhibitors for conformationally dynamic helicases using electrophilic scout fragments and a function-first approach, targeting SARS-CoV-2 nsp13 and human helicases BLM and WRN.

This study investigates how MeCP2 interacts with methylated DNA and nucleosomes, revealing distinct dynamics that influence its function in gene repression and Rett syndrome.

This study uses cryo-EM to reveal how the SARS-CoV-2 RTC discriminates between natural NTPs and the antiviral remdesivir triphosphate, providing insights for antiviral design.

This study characterizes the structural architecture and conformational variability of the human shelterin complex using multiple biophysical methods.

This study investigates how the MIDAS domain of Mdn1 forms catch bonds with two different UBL substrates under force, revealing force-dependent binding lifetime changes.

The paper shows that immune responses to African trypanosome VSGs are focused on immunodominant epitopes, enabling immune evasion through epitope variation.

The paper investigates TACAN's functionality as a mechanosensitive ion channel and finds it does not exhibit mechanosensitive activity, instead showing structural features related to fatty acid elongase.

This paper presents a large repertoire of high-affinity nanobodies against SARS-CoV-2 Spike protein with potent neutralization properties and resistance to viral variants.

This paper shows that SARS-CoV-2 RdRp undergoes backtracking, which may aid proofreading and antiviral resistance.

The paper presents cryo-EM structures of the SARS-CoV-2 holo-RdRp complex with nsp13 helicase, revealing interactions and a new therapeutic target.

The paper uses cryo-EM to visualize Mfd interacting with stalled RNA polymerase complexes, revealing its mechanism for initiating transcription-coupled repair.