In one paragraphArticle in bioRxiv : the preprint server for biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
2 · The registryThe trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
3 · Its place in the literatureWho cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
4 · The recordCorrections and comments
5 · Who and what moneyAuthors and funding
18 authors.
Megan WangDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.ORCID 0000-0003-3000-3539 Kanta YoneyamaStructural Biology Division, Research Center for Advanced Science and Technology, The University of Tokyo, 4-6-1 Komaba, Meguro-ku, Tokyo 153-8904, Japan.
Rimantė ŽedaveinytėDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.ORCID 0000-0002-0738-6976 Junichiro IshikawaDepartment of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.ORCID 0000-0003-4112-4168 Stephen TangDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.ORCID 0000-0001-5492-9796 Hoang C LeDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.ORCID 0009-0003-7911-881X Tanner WiegandDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.ORCID 0000-0002-0528-268X Josephine L RamirezDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.ORCID 0009-0000-0876-939X Naoto NagahataDepartment of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.ORCID 0009-0009-8890-180X Yanzhe MaDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA.
Dennis J ZhangDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.ORCID 0000-0002-6871-9842 Erick HelmecziMetabolomics Core, Shared Research Resources, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.
Mirela BerisaMetabolomics Core, Shared Research Resources, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.ORCID 0000-0001-7347-9823 Masahiro HiraizumiDepartment of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.ORCID 0000-0002-4340-2937 Keitaro YamashitaStructural Biology Division, Research Center for Advanced Science and Technology, The University of Tokyo, 4-6-1 Komaba, Meguro-ku, Tokyo 153-8904, Japan.ORCID 0000-0002-5442-7582 Hiroshi NishimasuStructural Biology Division, Research Center for Advanced Science and Technology, The University of Tokyo, 4-6-1 Komaba, Meguro-ku, Tokyo 153-8904, Japan.ORCID 0000-0002-2505-1416 Samuel H SternbergDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.ORCID 0000-0001-8240-9114 Funding
Medical Scientist Training ProgramT32GM145440 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI STEVEN L REINER · 2022 to 2026
$7.3MHow dynamic molecular interactions of RNA Binding Proteins drive post-transcriptional gene expression changesR35GM152258 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI Marko Jovanovic · 2024 to 2026
$1.6MMechanisms of reverse transcriptase mediated phage resistance in EnterobacteriaceaeF30AI183830 · NIAID · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Stephen Tang · 2024 to 2026
$158kNIAID NIH HHS F30 AI183830NIGMS NIH HHS R35 GM152258NIGMS NIH HHS T32 GM145440
6 · The paper itselfAbstract
Defense-associated reverse transcriptase (DRT) systems mediate antiviral immunity through distinct modes of cDNA synthesis: Class 1 DRTs catalyze untemplated synthesis, whereas Class 2 DRTs polymerize noncoding RNA-templated products. However, how these distinct modes drive defense remains unclear. Here, we report that DRT3 immunity arises when Class 1 and Class 2 RT activities cooperate to produce self-complementary double-stranded DNA (dsDNA). DRT3a uses a 5'-ACACAC-3' RNA template to synthesize poly-(dTdG) repeats, whereas DRT3b synthesizes poly-(dCdA) repeats without any nucleic acid template. Cryo-electron microscopy reveals that DRT3b forms a hexamer and uses active-site-adjacent residues as deoxyadenosine and deoxycytidine gates to enforce alternating nucleotide addition, representing a unique example of amino acid-templated DNA polymerization. DRT3 is toxic in cells lacking RecBCD, implicating host recombination machinery in limiting dsDNA accumulation, and the phage-encoded RecBCD inhibitor Gam triggers DRT3-mediated abortive infection. These findings reveal how two polymerases with distinct templating strategies generate complementary DNA for defense.
Identifiers
PMID42146563
PMCPMC13174585
What Socratic holds
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LicenceCC BY
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