David Dulin

The paper determines the structure of norovirus NS3 and proposes it functions as an RNA translocase.

The paper investigates how RfaH and NusG regulate RNA polymerase pausing during transcription of long operons in E. coli, showing RfaH extends transcription runs and compensates for NusA's pause-inducing effect.

This study identifies a two-pronged mechanism by which CMX521 inhibits SARS-CoV-2 RNA-dependent RNA polymerase through biochemical assays and single-molecule techniques.

The paper provides tools and methods for analyzing high-throughput single-molecule biophysics data using first-passage time and maximum likelihood estimation to model kinetic behavior.

This paper introduces a multimodal platform combining magnetic tweezers and TIRF for high-throughput single-molecule analysis, enabling real-time, parallel measurements of force, torque, fluorescence, and temperature.

This study identifies the role of the ω subunit in stabilizing RNA polymerase to balance processivity and collision resolution during transcription.

This paper develops an in-situ force calibration method for magnetic tweezers and uses it to reveal how MTERF1 causes directional transcription termination through DNA unwinding and a kinetic barrier.

This study shows that the coronavirus helicase enhances RNA synthesis through duplex RNA by tenfold by forming a directional complex with the polymerase, revealing an active coupling mechanism that modulates replication dynamics.

This study shows that coronavirus polymerase template switching is driven by nsp13-helicase and is enhanced by remdesivir and molnupiravir, leading to defective RNA production.

This study shows that arabinose nucleotides inhibit SARS-CoV-2 and poliovirus polymerases by causing long pauses due to the 2'-endo conformation of the incorporated nucleotides.

The paper shows that the SARS-CoV-2 polymerase core RTC undergoes a conformational change after RNA binding to become elongation-competent, which is essential for viral RNA synthesis.

The paper uses single-molecule magnetic tweezers to study how TAV2b-derived peptides affect dsRNA structure and stability, finding they underwind and stabilize the duplex.

This study shows MDA5 compacts dsRNA via ATP-dependent loop extrusion, stabilizing the structure through CARD domain oligomerization.