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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:

YfmK is an N ε -lysine acetyltransferase that directly acetylates the histone-like protein HBsu in Bacillus subtilis
Valerie J. Carabetta, Todd M. Greco, Ileana M. Cristea, et al.
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 9, pp. 3752-3757
Open Access | Times Cited: 43

Showing 1-25 of 43 citing articles:

Post-translational Protein Acetylation: An Elegant Mechanism for Bacteria to Dynamically Regulate Metabolic Functions
David G. Christensen, Xueshu Xie, Nathan Basisty, et al.
Frontiers in Microbiology (2019) Vol. 10
Open Access | Times Cited: 144
YiaC and CobB regulate lysine lactylation in Escherichia coli
Hanyang Dong, Jianji Zhang, Hui Zhang, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 63
Nucleoid-associated proteins shape chromatin structure and transcriptional regulation across the bacterial kingdom
Haley M. Amemiya, Jeremy W. Schroeder, Peter L. Freddolino
Transcription (2021) Vol. 12, Iss. 4, pp. 182-218
Open Access | Times Cited: 56
Dual lysine and N‐terminal acetyltransferases reveal the complexity underpinning protein acetylation
Willy V. Bienvenut, Annika Brünje, J. Boyer, et al.
Molecular Systems Biology (2020) Vol. 16, Iss. 7
Open Access | Times Cited: 69
Acetylation of glucosyltransferases regulates Streptococcus mutans biofilm formation and virulence
Qizhao Ma, Yangyang Pan, Chen Yang, et al.
PLoS Pathogens (2021) Vol. 17, Iss. 12, pp. e1010134-e1010134
Open Access | Times Cited: 36
Acetylation of a fungal effector that translocates host PR1 facilitates virulence
Jingtao Li, Xiaoying Ma, Chenyang Wang, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 27
Three‐dimensional chromosome re‐modelling: The integral mechanism of transcription regulation in bacteria
Fatema‐Zahra M. Rashid, Remus T. Dame
Molecular Microbiology (2023) Vol. 120, Iss. 1, pp. 60-70
Open Access | Times Cited: 14
Rok from B. subtilis: Bridging genome structure and transcription regulation
Amanda M. Erkelens, Bert van Erp, Wilfried J. J. Meijer, et al.
Molecular Microbiology (2024)
Open Access | Times Cited: 5
Protein Acetyltransferases Mediate Bacterial Adaptation to a Diverse Environment
Aiswarya Dash, Rahul Modak
Journal of Bacteriology (2021) Vol. 203, Iss. 19
Open Access | Times Cited: 28
Acetylation of Lactate Dehydrogenase Negatively Regulates the Acidogenicity of Streptococcus mutans
Qizhao Ma, Yangyang Pan, Yang Chen, et al.
mBio (2022) Vol. 13, Iss. 5
Open Access | Times Cited: 19
Plant PR1 rescues condensation of the plastid iron-sulfur protein by a fungal effector
Jingtao Li, Limei Yang, Shuzhi Ding, et al.
Nature Plants (2024)
Closed Access | Times Cited: 4
Aeromonas hydrophila CobQ is a new type of NAD+- and Zn2+-independent protein lysine deacetylase
Yuqian Wang, Guibin Wang, Lishan Zhang, et al.
(2025)
Open Access
Propionylation of Fis K32 in Salmonella enterica serovar Typhi: a key modification affecting pathogenicity
Hao Tang, Ziyang Zhan, X. Liu, et al.
Future Microbiology (2025), pp. 1-9
Closed Access
Aeromonas hydrophila CobQ is a new type of NAD+- and Zn2+-independent protein lysine deacetylase
Yuqian Wang, Guibin Wang, Lishan Zhang, et al.
eLife (2025) Vol. 13
Open Access
Methyltransferase DnmA is responsible for genome-wide N6-methyladenosine modifications at non-palindromic recognition sites in Bacillus subtilis
Taylor M. Nye, Lieke A. van Gijtenbeek, Amanda G Stevens, et al.
Nucleic Acids Research (2020) Vol. 48, Iss. 10, pp. 5332-5348
Open Access | Times Cited: 31
Influence of Nε-Lysine Acetylation on the Formation of Protein Aggregates and Antibiotic Persistence in E. coli
Karolina Stojowska‐Swędrzyńska, Dorota Kuczyńska‐Wiśnik, Ewa Laskowska
Molecules (2024) Vol. 29, Iss. 2, pp. 383-383
Open Access | Times Cited: 2
TmcA functions as a lysine 2-hydroxyisobutyryltransferase to regulate transcription
Hanyang Dong, Yujie Zhao, Changfen Bi, et al.
Nature Chemical Biology (2021) Vol. 18, Iss. 2, pp. 142-151
Closed Access | Times Cited: 17
Recent Contributions of Proteomics to Our Understanding of Reversible Nε-Lysine Acylation in Bacteria
Liya Popova, Rachel A. Carr, Valerie J. Carabetta
Journal of Proteome Research (2024) Vol. 23, Iss. 8, pp. 2733-2749
Open Access | Times Cited: 2
Nε-lysine acetylation of the histone-like protein HBsu influences antibiotic survival and persistence in Bacillus subtilis
Rachel A. Carr, Trichina Tucker, Precious M. Newman, et al.
Frontiers in Microbiology (2024) Vol. 15
Open Access | Times Cited: 2
Fpa (YlaN) is an iron(II) binding protein that functions to relieve Fur-mediated repression of gene expression in Staphylococcus aureus
Jeffrey M. Boyd, Kylie Ryan Kaler, Karla Esquilín-Lebrón, et al.
mBio (2024) Vol. 15, Iss. 11
Open Access | Times Cited: 2
Addressing the Possibility of a Histone-Like Code in Bacteria
Valerie J. Carabetta
Journal of Proteome Research (2020) Vol. 20, Iss. 1, pp. 27-37
Open Access | Times Cited: 16
Nε-Lysine Acetylation of the Histone-Like Protein HBsu Regulates the Process of Sporulation and Affects the Resistance Properties of Bacillus subtilis Spores
Jackson Luu, Connor M. Mott, Olivia Schreiber, et al.
Frontiers in Microbiology (2022) Vol. 12
Open Access | Times Cited: 10
YlaN is an iron(II) binding protein that functions to relieve Fur-mediated repression of gene expression inStaphylococcus aureus
Jeffrey M. Boyd, Karla Esquilín-Lebrón, Courtney J. Campbell, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 5
Methods for characterizing protein acetylation during viral infection
Laura A. Murray‐Nerger, Ashton N. Combs, Pranav Rekapalli, et al.
Methods in enzymology on CD-ROM/Methods in enzymology (2019), pp. 587-620
Open Access | Times Cited: 12
Proteomic Analysis of Lysine Acetylation and Succinylation to Investigate the Pathogenicity of Virulent Pseudomonas syringae pv. tomato DC3000 and Avirulent Line Pseudomonas syringae pv. tomato DC3000 avrRpm1 on Arabidopsis thaliana
Yongqiang Ding, Yangxuan Liu, Kexin Yang, et al.
Genes (2024) Vol. 15, Iss. 4, pp. 499-499
Open Access | Times Cited: 1
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