Edwin Antony

This paper identifies a binuclear [Cu2S2] cluster in DPOR that mediates functional asymmetry between its active sites.

The paper reports a cryo-EM structure of a nitrogenase-PII supercomplex in methanogens, revealing a metabolite-gated assembly mechanism for nitrogenase inhibition.

This study identifies a novel mechanism by which a bivalent E2:RING E3 complex facilitates E2 charging through competitive inhibition and accelerated release of charged E2.

This study shows phosphorylation of IGF2BP1 and IGF2BP3 at a conserved serine acts as a configurational switch, altering their RNA binding domain arrangements and affecting mRNA regulation.

This paper identifies two structural elements in HELB essential for its interaction with RPA-coated ssDNA, showing how they facilitate RPA displacement and DNA loop formation.

This study uses single-molecule techniques to show PCNA, Pol δ, and Pif1 collaborate in DNA replication, with PCNA stabilization and diffusion reduction by both Pol δ and Pif1.

This study investigates the interplay between DNA damage tolerance pathways by comparing PCNA occupancy and RPA/Rad51 exchange at stalled replication sites.

This study identifies a feedback mechanism involving Cdk1/Wee1 signaling that primes and tunes RPA phosphorylation, crucial for cell cycle progression and DNA damage response.

The paper identifies a novel tetrameric intermediate in the retroviral integration pathway using biochemical and biophysical methods.

This study investigates the mechanisms of DNA and RNA strand transfer and protein exchange between SSB and RPA using smFRET, revealing dynamic interactions and length-dependent behavior.

The paper uses Cryo-EM to reveal how asymmetry and allostery coordinate long-range electron transfer in the DPOR enzyme through a bi-copper cluster.

This study reveals how Rad52 sorts and stacks Rad51 at DNA junctions to enhance homologous recombination by promoting Rad51 binding to RPA-coated ssDNA.

This study uses single-molecule techniques to show that RPA partially wraps ssDNA and that phosphorylation at Ser-384 modulates this wrapping.

This paper introduces a method to site-specifically encode and label two noncanonical amino acids in proteins, enabling dual modification in living cells.

This study characterizes human HELB as a monomeric helicase that binds ssDNA, hydrolyzes ATP, and clears RPA from ssDNA through translocation.