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OpenAlex Citation Counts

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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

UG/Abi: a highly diverse family of prokaryotic reverse transcriptases associated with defense functions
Mario Rodríguez Mestre, Linyi Gao, Shiraz A. Shah, et al.
Nucleic Acids Research (2022) Vol. 50, Iss. 11, pp. 6084-6101
Open Access | Times Cited: 26

Showing 1-25 of 26 citing articles:

A host of armor: Prokaryotic immune strategies against mobile genetic elements
David Mayo-Muñoz, Rafael Pinilla‐Redondo, Nils Birkholz, et al.
Cell Reports (2023) Vol. 42, Iss. 7, pp. 112672-112672
Open Access | Times Cited: 64
A conserved family of immune effectors cleaves cellular ATP upon viral infection
François Rousset, Erez Yirmiya, Shahar Nesher, et al.
Cell (2023) Vol. 186, Iss. 17, pp. 3619-3631.e13
Open Access | Times Cited: 47
Prokaryotic Gabija complex senses and executes nucleotide depletion and DNA cleavage for antiviral defense
Rui Cheng, Fengtao Huang, Xueling Lu, et al.
Cell Host & Microbe (2023) Vol. 31, Iss. 8, pp. 1331-1344.e5
Open Access | Times Cited: 31
De novo gene synthesis by an antiviral reverse transcriptase
Stephen Tang, Valentin Conte, Dennis J. Zhang, et al.
Science (2024) Vol. 386, Iss. 6717
Open Access | Times Cited: 13
Phage-triggered reverse transcription assembles a toxic repetitive gene from a noncoding RNA
Max E. Wilkinson, David Li, Linyi Gao, et al.
Science (2024) Vol. 386, Iss. 6717
Closed Access | Times Cited: 12
Structure-functional characterization of Lactococcus AbiA phage defense system
Marta Gapińska, Weronika Zajko, Krzysztof Skowronek, et al.
Nucleic Acids Research (2024) Vol. 52, Iss. 8, pp. 4723-4738
Open Access | Times Cited: 5
A mobile genetic element-derived primase-polymerase harbors multiple activities implicated in DNA replication and repair
Pan Fu, Yuwei Wang, Yanqiu Liu, et al.
Nucleic Acids Research (2025) Vol. 53, Iss. 2
Open Access
Next-Generation Sequencing Methods to Determine the Accuracy of Retroviral Reverse Transcriptases: Advantages and Limitations
Javier Martínez del Río, Luis Menéndez‐Arias
Viruses (2025) Vol. 17, Iss. 2, pp. 173-173
Open Access
A conserved family of immune effectors cleaves cellular ATP upon viral infection
François Rousset, Erez Yirmiya, Shahar Nesher, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 12
The novel anti-phage system Shield co-opts an RmuC domain to mediate phage defense across Pseudomonas species
Elliot Macdonald, Rosanna C. T. Wright, James P. R. Connolly, et al.
PLoS Genetics (2023) Vol. 19, Iss. 6, pp. e1010784-e1010784
Open Access | Times Cited: 12
Eco-evolutionary significance of domesticated retroelements in microbial genomes
Blair G. Paul, A. Murat Eren
Mobile DNA (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 13
Tricking phages with a reverse move
Ilya А. Osterman, Rotem Sorek
Science (2024) Vol. 386, Iss. 6717, pp. 25-26
Closed Access | Times Cited: 2
Virus-like Particles from Wolbachia-Infected Cells May Include a Gene Transfer Agent
Ann M. Fallon, Elissa M. Carroll
Insects (2023) Vol. 14, Iss. 6, pp. 516-516
Open Access | Times Cited: 5
De novo gene synthesis by an antiviral reverse transcriptase
Stephen Tang, Valentin Conte, Dennis J. Zhang, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Aeromonas trota Is Highly Refractory to Acquire Exogenous Genetic Material
Jorge Erick Otero-Olarra, Gilda Díaz-Cárdenas, Ma. Guadalupe Aguilera‐Arreola, et al.
Microorganisms (2024) Vol. 12, Iss. 6, pp. 1091-1091
Open Access | Times Cited: 1
Shield co-opts an RmuC domain to mediate phage defence acrossPseudomonasspecies
Elliot Macdonald, Henrik Strahl, Tim R. Blower, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 5
To Be Mobile or Not: The Variety of Reverse Transcriptases and Their Recruitment by Host Genomes
Irina R. Arkhipova, Irina A. Yushenova
Biochemistry (Moscow) (2023) Vol. 88, Iss. 11, pp. 1754-1762
Open Access | Times Cited: 2
Hot Spots of Site-Specific Integration into the Sinorhizobium meliloti Chromosome
Maria E. Vladimirova, Marina L. Roumiantseva, Alla S. Saksaganskaia, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 19, pp. 10421-10421
Open Access
Spacer acquisition in type VI CRISPR-Cas systems associated with reverse transcriptase-Cas1 fusion proteins
María Dolores Molina-Sánchez, Francisco Martínez‐Abarca, Vicenta Millan, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Exploring the Frozen Armory: Antiphage Defense Systems in Cold-Adapted Bacteria with a Focus on CRISPR-Cas Systems
Greta Daae Sandsdalen, Animesh Kumar, Erik Hjerde
Microorganisms (2024) Vol. 12, Iss. 5, pp. 1028-1028
Open Access
The role of noncoding RNAs in bacterial immunity
David Mayo-Muñoz, Huijuan Li, Mario Rodríguez Mestre, et al.
Trends in Microbiology (2024)
Open Access
Adaptive immunity of type VI CRISPR-Cas systems associated with reverse transcriptase–Cas1 fusion proteins
María Dolores Molina-Sánchez, Francisco Martínez‐Abarca, Vicenta Millán, et al.
Nucleic Acids Research (2024)
Open Access
Prokaryotic Gabija complex senses and executes nucleotide depletion and DNA cleavage for antiviral defense
Rui Cheng, Fengtao Huang, Xueling Lu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
A novel thermostable and processive reverse transcriptase from a group II intron ofAnoxybacillus flavithermus
Igor P. Oscorbin, М. Л. Филипенко
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
A Novel Thermostable and Processive Reverse Transcriptase from a Group II Intron of Anoxybacillus flavithermus
Igor P. Oscorbin, М. Л. Филипенко
Biomolecules (2023) Vol. 14, Iss. 1, pp. 49-49
Open Access
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