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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:

Nudix hydrolases degrade protein-conjugated ADP-ribose
Casey M. Daniels, Puchong Thirawatananond, Shao‐En Ong, et al.
Scientific Reports (2015) Vol. 5, Iss. 1
Open Access | Times Cited: 62

Showing 26-50 of 62 citing articles:

Mechanism of 53BP1 activity regulation by RNA-binding TIRR and a designer protein
Maria Victoria Botuyan, Gaofeng Cui, Pascal Drané, et al.
Nature Structural & Molecular Biology (2018) Vol. 25, Iss. 7, pp. 591-600
Open Access | Times Cited: 46
The nucleosomal surface is the main target of histone ADP-ribosylation in response to DNA damage
Kelly R. Karch, Marie-France Langelier, John M. Pascal, et al.
Molecular BioSystems (2017) Vol. 13, Iss. 12, pp. 2660-2671
Open Access | Times Cited: 40
Design, synthesis and evaluation of inhibitors of the SARS-CoV-2 nsp3 macrodomain
Lavinia M. Sherrill, Elva E. Joya, AnnMarie Walker, et al.
Bioorganic & Medicinal Chemistry (2022) Vol. 67, pp. 116788-116788
Open Access | Times Cited: 20
dELTA-MS: A Mass Spectrometry-Based Proteomics Approach for Identifying ADP-Ribosylation Sites and Forms
Isabel Uribe, Emily Zahn, Richard Searfoss, et al.
Journal of Proteome Research (2025)
Closed Access
Proteomic Analysis of the Downstream Signaling Network of PARP1
Yuanli Zhen, Yonghao Yu
Biochemistry (2018) Vol. 57, Iss. 4, pp. 429-440
Open Access | Times Cited: 36
Targeting dePARylation for cancer therapy
Muzaffer Ahmad Kassab, Lily Yu, Xiaochun Yu
Cell & Bioscience (2020) Vol. 10, Iss. 1
Open Access | Times Cited: 30
Multiple Roles for Mono- and Poly(ADP-Ribose) in Regulating Stress Responses
Hongyun Qi, Brendan D. Price, Tovah A. Day
Trends in Genetics (2018) Vol. 35, Iss. 2, pp. 159-172
Open Access | Times Cited: 30
Poly(ADP-Ribosylation) in Age-Related Neurological Disease
Leeanne McGurk, Olivia M. Rifai, Nancy M. Bonini
Trends in Genetics (2019) Vol. 35, Iss. 8, pp. 601-613
Open Access | Times Cited: 28
ADP-ribosylation and intracellular traffic: an emerging role for PARP enzymes
Giovanna Grimaldi, Daniela Corda
Biochemical Society Transactions (2019) Vol. 47, Iss. 1, pp. 357-370
Closed Access | Times Cited: 27
Identification of NAD-RNA species and ADPR-RNA decapping in Archaea
José Vicente Gomes‐Filho, Ruth Breuer, Hector Gabriel Morales-Filloy, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 8
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
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
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
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
Site-specific analysis of the Asp- and Glu-ADP-ribosylated proteome by quantitative mass spectrometry
Peng Li, Yuanli Zhen, Yonghao Yu
Methods in enzymology on CD-ROM/Methods in enzymology (2019), pp. 301-321
Open Access | Times Cited: 17
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
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
Roles of Nicotinamide Adenine Dinucleotide (NAD+) in Biological Systems
Palmiro Poltronieri, Nataša Čereković
Challenges (2018) Vol. 9, Iss. 1, pp. 3-3
Open Access | Times Cited: 12
Poly‐ADP‐ribosylation dynamics, signaling, and analysis
Rasha Q. Al‐Rahahleh, Robert W. Sobol
Environmental and Molecular Mutagenesis (2024)
Closed Access | Times Cited: 1
Discovery of Drug-like Ligands for the Mac1 Domain of SARS-CoV-2 Nsp3
Rajdeep S. Virdi, Robert Bavisotto, Nicholas C. Hopper, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 7

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