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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:

Processing of protein ADP-ribosylation by Nudix hydrolases
Luca Palazzo, Benjamin Thomas, Ann‐Sofie Jemth, et al.
Biochemical Journal (2015) Vol. 468, Iss. 2, pp. 293-301
Open Access | Times Cited: 125

Showing 76-100 of 125 citing articles:

ADP-ribosylation, a multifaceted modification: Functions and mechanisms in aging and aging-related diseases
Wu Hao, Zhao Jialong, Yuan Jiuzhi, et al.
Ageing Research Reviews (2024) Vol. 98, pp. 102347-102347
Open Access | Times Cited: 3
Role of NUDIX Hydrolases in NAD and ADP-Ribose Metabolism in Mammals
Veronika Kulikova, Andrey Nikiforov
Biochemistry (Moscow) (2020) Vol. 85, Iss. 8, pp. 883-894
Closed Access | Times Cited: 21
Mimetics of ADP-Ribosylated Histidine through Copper(I)-Catalyzed Click Chemistry
Hugo Minnee, J.G.M. Rack, Gijsbert A. van der Marel, et al.
Organic Letters (2022) Vol. 24, Iss. 21, pp. 3776-3780
Open Access | Times Cited: 14
Molecular basis for the inhibition of the methyl-lysine binding function of 53BP1 by TIRR
Jiaxu Wang, Zenglin Yuan, Yaqi Cui, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 23
Targeting ADP-ribosylation as an antimicrobial strategy
Giuliana Catara, Annunziata Corteggio, Carmen Valente, et al.
Biochemical Pharmacology (2019) Vol. 167, pp. 13-26
Open Access | Times Cited: 21
Proximal ADP-ribose Hydrolysis in Trypanosomatids is Catalyzed by a Macrodomain
T. Haikarainen, L. Lehtiö
Scientific Reports (2016) Vol. 6, Iss. 1
Open Access | Times Cited: 20
Functional roles of ADP-ribosylation writers, readers and erasers
Ping Li, Yushuang Lei, Qi Jia, et al.
Frontiers in Cell and Developmental Biology (2022) Vol. 10
Open Access | Times Cited: 12
The ADP-ribose hydrolase NUDT5 is important for DNA repair
Hongyun Qi, Roni H. G. Wright, Miguel Beato, et al.
Cell Reports (2022) Vol. 41, Iss. 12, pp. 111866-111866
Open Access | Times Cited: 12
Mono-ADP-ribosylation, a MARylationmultifaced modification of protein, DNA and RNA: characterizations, functions and mechanisms
Hao Wu, Anqi Lu, Jiuzhi Yuan, et al.
Cell Death Discovery (2024) Vol. 10, Iss. 1
Open Access | Times Cited: 2
Molecular mechanisms of cell death by parthanatos: More questions than answers
Rafael Dias de Moura, Priscilla Doria de Mattos, Penélope Ferreira Valente, et al.
Genetics and Molecular Biology (2024) Vol. 47, Iss. suppl 1
Open Access | Times Cited: 2
ADP-Ribosylated Peptide Enrichment and Site Identification: The Phosphodiesterase-Based Method
Casey M. Daniels, Shao‐En Ong, Anthony K. L. Leung
Methods in molecular biology (2017), pp. 79-93
Open Access | Times Cited: 20
Emerging roles of ADP-ribosyl-acceptor hydrolases (ARHs) in tumorigenesis and cell death pathways
Xiangning Bu, Jiro Kato, Joel Moss
Biochemical Pharmacology (2018) Vol. 167, pp. 44-49
Open Access | Times Cited: 20
Disruption of Macrodomain Protein SCO6735 Increases Antibiotic Production in Streptomyces coelicolor
Jasna Lalić, Melanija Posavec Marjanović, Luca Palazzo, et al.
Journal of Biological Chemistry (2016) Vol. 291, Iss. 44, pp. 23175-23187
Open Access | Times Cited: 19
Hydrolytic activity of human Nudt16 enzyme on dinucleotide cap analogs and short capped oligonucleotides
Renata Grzela, Karolina Nasilowska, Maciej Łukaszewicz, et al.
RNA (2018) Vol. 24, Iss. 5, pp. 633-642
Open Access | Times Cited: 19
Structural analyses of NudT16–ADP-ribose complexes direct rational design of mutants with improved processing of poly(ADP-ribosyl)ated proteins
Puchong Thirawatananond, Robert Lyle McPherson, Jasmine Malhi, et al.
Scientific Reports (2019) Vol. 9, Iss. 1
Open Access | Times Cited: 18
Uncommon posttranslational modifications in proteomics: ADP‐ribosylation, tyrosine nitration, and tyrosine sulfation
Aarti Bashyal, Jennifer S. Brodbelt
Mass Spectrometry Reviews (2022) Vol. 43, Iss. 2, pp. 289-326
Closed Access | Times Cited: 10
Hydrofluoric Acid-Based Derivatization Strategy To Profile PARP-1 ADP-Ribosylation by LC–MS/MS
Jean‐Philippe Gagné, Marie-France Langelier, John M. Pascal, et al.
Journal of Proteome Research (2018) Vol. 17, Iss. 7, pp. 2542-2551
Closed Access | Times Cited: 17
Activity-Based Screening Assay for Mono-ADP-Ribosylhydrolases
Sarah Wazir, Mirko M. Maksimainen, Heli I. Alanen, et al.
SLAS DISCOVERY (2020) Vol. 26, Iss. 1, pp. 67-76
Open Access | Times Cited: 16
Selective monitoring of the protein-free ADP-ribose released by ADP-ribosylation reversal enzymes
Samuel Kasson, Nuwani Dharmapriya, In‐Kwon Kim
PLoS ONE (2021) Vol. 16, Iss. 6, pp. e0254022-e0254022
Open Access | Times Cited: 13
Structural and biochemical evidence supporting poly ADP-ribosylation in the bacterium Deinococcus radiodurans
Chao‐Cheng Cho, Chia‐Yu Chien, Yi‐Chih Chiu, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 15
Poly(ADP-ribose): From chemical synthesis to drug design
Mikhail S. Drenichev, Sergey N. Mikhailov
Bioorganic & Medicinal Chemistry Letters (2016) Vol. 26, Iss. 15, pp. 3395-3403
Closed Access | Times Cited: 13
The Arabidopsis thaliana Poly(ADP-Ribose) Polymerases 1 and 2 Modify DNA by ADP-Ribosylating Terminal Phosphate Residues
Sabira Taipakova, A. K. Kuanbay, Christine Saint‐Pierre, et al.
Frontiers in Cell and Developmental Biology (2020) Vol. 8
Open Access | Times Cited: 12
Nudix hydrolase 14 influences plant development and grain chalkiness in rice
Yiran Liu, Wan Zhang, Youhang Wang, et al.
Frontiers in Plant Science (2022) Vol. 13
Open Access | Times Cited: 8
The Complex Network of ADP-Ribosylation and DNA Repair: Emerging Insights and Implications for Cancer Therapy
Ziyuan Li, Aiqin Luo, Bingteng Xie
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 19, pp. 15028-15028
Open Access | Times Cited: 4
A genetically encoded sensor for real-time monitoring of poly-ADP-ribosylation dynamics in-vitro and in cells
Alix Thomas, Kapil Upadhyaya, Daniel S. Bejan, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1

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