Looking Ahead: POLQ in the Future of Immuno-Oncology

POLQ Involved in DNA Repair
The most well-known and widely studied mechanisms of double-stranded DNA break (DSB) repairs are homologous recombination (HR) and classical non-homologous end joining (C-NHEJ). HR is almost error-free due to formatting by the homologous sister chromosome. C-NHEJ relies on direct ligation of double-stranded DNA ends and only ever presents errors at the junction points. Recently, a
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Discovering the Emerging Importance of PARG in Immunity

PARG in Human Immunity
Poly (ADP-ribose) glycohydrolase (PARG), along with poly (ADP-ribose) polymerase 1 (PARP1) are the principal elements of the DNA damage response (DDR). When single-strand breaks occur in cellular DNA, PARP1 mediates the poly ADP ribosylation of itself and target proteins, such as histones, promoting the decompaction of chromatin and recruiting relevant enzymes to initiate DNA repair.
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Helicases as Powerful Tools in Innate Immunity

Helicases Used in Innate Immunity
Helicases are among the largest and most highly conserved families of enzymatic proteins in eukaryotic organisms. These proteins utilize NTP hydrolysis (usually ATP) to drive their recognition, remodeling, and response to target DNA or RNA.1 Nearly every aspect of nucleic acid metabolism is mediated by helicases. DNA helicases function in replication, repair, recombination, transcription, chromosome
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Resolving the Many Roles of DHX36

DHX36 RNA Helicase Unwinds G4 RNA Structures
While most researchers are familiar with canonical DNA structures, primarily B (but also even A or Z) DNA, an even more exotic form exerts a vast influence over nearly every aspect of nucleic acid function. In both DNA and RNA, tracts of guanine with at least four consecutive members can self-associate via Hoogsten base pairing
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NSP14 – A Promising SARS-CoV-2 Therapeutic Target

NSP14 - Coronavirus Target
Non-Structural Proteins of Coronaviruses Coronaviruses have complex RNA-synthesizing machinery composed of many non-structural proteins (NSPs). While one-third of the viral genome encodes for structural proteins such as the spike, envelope, and nucleocapsid proteins, the remaining two-thirds encodes for NSPs. NSP genes are located within the 5’-region of the genome and studies have revealed that NSPs
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RIG-I: Important Sensor of Cytosolic RNA

RIGI Cytosolic RNA Sensor
RIG-I-Like Receptors Retinoic acid-inducible gene 1 (RIG-I) is a cytoplasmic RNA helicase member of the RIG-I-like receptor (RLR) family of proteins. RIG-I is highly conserved within vertebrates. Structurally, RIG-I is comprised of three main functional domains – Caspase Activation and Recruitment Domain (CARD) for signal transduction, DExD/ H-box RNA helicase domain, and C-terminal domain for
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