| Year | Reference (first author, journal) | Main ASCC3 function/claim | Evidence type | Key quantitative/detail | URL/DOI |
|---|---|---|---|---|---|
| 2024 | Miścicka, *Nucleic Acids Research* | ASCC disassembles stalled ribosomal complexes; ribosomal collision is not strictly required once ZNF598-dependent ubiquitination is in place, refining the ASCC3-mediated RQC model (pqac-00000011, pqac-00000012, pqac-00000013) | In vitro reconstitution, ribosome splitting assays, toe-printing, ubiquitination biochemistry, mechanistic interpretation from cryo-EM-informed model | ASCC activity required an mRNA 3′ overhang of ≥30–35 nt downstream of the P site; K63R ubiquitin still allowed ~50% release of leading ribosomes in one assay context (pqac-00000011, pqac-00000012) | https://doi.org/10.1093/nar/gkae087 |
| 2024 | Li, *Frontiers in Genetics* | Biallelic human ASCC3 variants cause neurodevelopmental/neuromuscular syndrome with developmental delay and motor-language impairment, expanding the Mendelian disease spectrum (pqac-00000023) | Clinical case report, trio-WES, trio-CNV-seq, literature review | 3 new families; review of 11 previously reported variants; reported compound heterozygous variants included c.[489dup];[1897C>T], c.[2314C>T];[5002T>A], c.[5113G>T];[718delG] (pqac-00000023) | https://doi.org/10.3389/fgene.2024.1382275 |
| 2023 | Jia, *Nature Communications* | ASCC3 is a dual-engine Ski2-like helicase; TRIP4 stimulates helicase activity and helps route ASCC3 toward specific functions, with TRIP4 and ALKBH3 binding mutually exclusive (pqac-00000010) | Cryo-EM, DNA–protein XL-MS, in vitro and cellular functional assays | Defined tandem N- and C-terminal Ski2-like helicase cassettes; showed TRIP4 positions an ASCH domain next to the C-terminal cassette and stimulates DNA threading/unwinding (pqac-00000010) | https://doi.org/10.1038/s41467-023-37528-3 |
| 2023 | Kito, *The EMBO Journal* | ASCC3 associates with scanning ribosomes and promotes translation initiation/scanning on a subset of mRNAs, extending its role beyond collided-ribosome splitting (pqac-00000008, pqac-00000009) | Sel-TCP-MS, Sel-TCP-seq, TCP-seq, Ribo-seq, luciferase reporters | ASCC3 localized predominantly to 5′ UTRs; knockdown impaired 43S preinitiation complex loading and scanning dynamics for selected transcripts (pqac-00000008, pqac-00000009) | https://doi.org/10.15252/embj.2022112869 |
| 2023 | Ao, *Journal for ImmunoTherapy of Cancer* | In NSCLC, ASCC3 promotes tumor progression and immunosuppression by stabilizing STAT3 via CAND1 and dampening type I interferon responses; supports biomarker/combination-therapy relevance (pqac-00000016, pqac-00000018, pqac-00000019, pqac-00000020, pqac-00000021) | TCGA/GEO analyses, IHC, RNA-seq, Co-IP/MS, mouse models, flow cytometry | RNA-seq after ASCC3 knockdown identified 480 affected genes; TCGA immune analysis used ASCC3-high vs ASCC3-low split at median 2.62; experiments reported significance up to p<0.0001 (pqac-00000017, pqac-00000019, pqac-00000020) | https://doi.org/10.1136/jitc-2023-007766 |
| 2020 | Juszkiewicz, *Molecular Cell* | ASCC containing ASCC3 disassembles the leading ribosome in collided queues in an ATP-dependent manner, establishing ASCC3 as a mammalian RQC helicase (pqac-00000004, pqac-00000015) | Biochemical reconstitution in mammalian cell-free system | Showed ASCC-dependent splitting generates 60S–nascent chain complexes for downstream RQC and requires ZNF598-dependent 40S ubiquitination (pqac-00000015) | https://doi.org/10.1016/j.molcel.2020.06.006 |
| 2020 | Jia, *Nature Communications* | ASCC3 is the largest ASCC subunit, a dual-cassette Ski2-like helicase that provides ssDNA for ALKBH3-mediated alkylation damage repair; ASCC2–ASCC3 interfaces are altered by cancer mutations (pqac-00000000) | Structural analysis, interaction mapping, biochemical affinity measurements, cancer-mutation analysis | Defined conserved ASCC2–ASCC3 interface and showed somatic cancer mutations reduce binding affinity; ASCC3 translocates 3′→5′ to support repair substrate generation (pqac-00000000) | https://doi.org/10.1038/s41467-020-19221-x |
| 2018 | Soll, *Journal of Biological Chemistry* | ASCC3 is the DNA helicase/scaffold of the ASCC alkylation damage response, generating the single-stranded substrate required for ALKBH3-mediated dealkylation and coordinating ASCC assembly (pqac-00000003) | Cell biology, co-IP, recombinant interaction assays, CRISPR/Cas9 knockout | ASCC3 and ASCC2 formed nuclear foci upon alkylation damage; ASCC1 knockout increased ASCC3 foci but many lacked ASCC2, indicating regulated complex assembly (pqac-00000003) | https://doi.org/10.1074/jbc.RA117.000114 |


*Table: This table summarizes the most relevant ASCC3 papers identified in this run, prioritizing 2023-2024 while retaining foundational studies. It highlights ASCC3’s main validated functions in alkylation repair, ribosome quality control, translation initiation, and human disease or cancer relevance, with concise methodological and quantitative details.*