Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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 26-50 of 125 citing articles:

An HPF1/PARP1-Based Chemical Biology Strategy for Exploring ADP-Ribosylation
Juán José Bonfiglio, Orsolya Leidecker, Helen Dauben, et al.
Cell (2020) Vol. 183, Iss. 4, pp. 1086-1102.e23
Open Access | Times Cited: 90
ADP-ribosylation of DNA and RNA
Joséphine Groslambert, Evgeniia Prokhorova, Ivan Ahel
DNA repair (2021) Vol. 105, pp. 103144-103144
Open Access | Times Cited: 80
Poly(ADP-Ribose) Glycohydrolase (PARG) vs. Poly(ADP-Ribose) Polymerase (PARP) – Function in Genome Maintenance and Relevance of Inhibitors for Anti-cancer Therapy
Daniel Harrision, Polly Gravells, Ruth Thompson, et al.
Frontiers in Molecular Biosciences (2020) Vol. 7
Open Access | Times Cited: 75
DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on protein substrates
Kang Zhu, Marcin J. Suskiewicz, Andrea Hloušek-Kasun, et al.
Science Advances (2022) Vol. 8, Iss. 40
Open Access | Times Cited: 67
PARPs and ADP-ribosylation: Deciphering the complexity with molecular tools
Morgan Dasovich, Anthony K. L. Leung
Molecular Cell (2023) Vol. 83, Iss. 10, pp. 1552-1572
Open Access | Times Cited: 34
Molecular basis for the reversible ADP-ribosylation of guanosine bases
M. Schuller, Roberto Raggiaschi, Petra Mikolčević, et al.
Molecular Cell (2023) Vol. 83, Iss. 13, pp. 2303-2315.e6
Open Access | Times Cited: 28
DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on nucleic acids
Kang Zhu, Marcin J. Suskiewicz, Chatrin Chatrin, et al.
Nucleic Acids Research (2023) Vol. 52, Iss. 2, pp. 801-815
Open Access | Times Cited: 24
Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens
J.G.M. Rack, Rosa Morra, Eva Barkauskaite, et al.
Molecular Cell (2015) Vol. 59, Iss. 2, pp. 309-320
Open Access | Times Cited: 84
ADP-Ribosyltransferases and Poly ADP-Ribosylation
Chao Liu, Xiaochun Yu
Current Protein and Peptide Science (2015) Vol. 16, Iss. 6, pp. 491-501
Open Access | Times Cited: 82
Poly-ADP ribosylation in DNA damage response and cancer therapy
Wei‐Hsien Hou, Shih-Hsun Chen, Xiaochun Yu
Mutation Research/Reviews in Mutation Research (2017) Vol. 780, pp. 82-91
Open Access | Times Cited: 72
ENPP1 processes protein ADP‐ribosylation in vitro
Luca Palazzo, Casey M. Daniels, Joanne E. Nettleship, et al.
FEBS Journal (2016) Vol. 283, Iss. 18, pp. 3371-3388
Open Access | Times Cited: 71
ELTA: Enzymatic Labeling of Terminal ADP-Ribose
Yoshinari Ando, Elad Elkayam, Robert Lyle McPherson, et al.
Molecular Cell (2019) Vol. 73, Iss. 4, pp. 845-856.e5
Open Access | Times Cited: 65
PARP, transcription and chromatin modeling
Melanija Posavec Marjanović, Kerryanne Crawford, Ivan Ahel
Seminars in Cell and Developmental Biology (2016) Vol. 63, pp. 102-113
Open Access | Times Cited: 64
Dna is a New Target of Parp3
E. A. Belousova, Alexander A. Ishchenko, Olga I. Lavrik
Scientific Reports (2018) Vol. 8, Iss. 1
Open Access | Times Cited: 62
ADP-ribosylation systems in bacteria and viruses
Petra Mikolčević, Andrea Hloušek-Kasun, Ivan Ahel, et al.
Computational and Structural Biotechnology Journal (2021) Vol. 19, pp. 2366-2383
Open Access | Times Cited: 48
Why structure and chain length matter: on the biological significance underlying the structural heterogeneity of poly(ADP-ribose)
Julia M. Reber, Aswin Mangerich
Nucleic Acids Research (2021) Vol. 49, Iss. 15, pp. 8432-8448
Open Access | Times Cited: 45
Multifaceted regulation and functions of 53BP1 in NHEJ‑mediated DSB repair (Review)
Tiantian Lei, Suya Du, Zhe Peng, et al.
International Journal of Molecular Medicine (2022) Vol. 50, Iss. 1
Open Access | Times Cited: 32
Serine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signalling
Pietro Fontana, Sara C. Buch-Larsen, Osamu Suyari, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 19
NUDT16 regulates CtIP PARylation to dictate homologous recombination repair
Zhen Zhang, William E. Samsa, Zihua Gong
Nucleic Acids Research (2024) Vol. 52, Iss. 7, pp. 3761-3777
Open Access | Times Cited: 8
Legionella metaeffector MavL reverses ubiquitin ADP-ribosylation via a conserved arginine-specific macrodomain
Zhengrui Zhang, Jiaqi Fu, J.G.M. Rack, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 6
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
PARPs in genome stability and signal transduction: implications for cancer therapy
Luca Palazzo, Ivan Ahel
Biochemical Society Transactions (2018) Vol. 46, Iss. 6, pp. 1681-1695
Open Access | Times Cited: 59
MacroD1 Is a Promiscuous ADP-Ribosyl Hydrolase Localized to Mitochondria
Thomas Agnew, Deeksha Munnur, Kerryanne Crawford, et al.
Frontiers in Microbiology (2018) Vol. 9
Open Access | Times Cited: 49
Synthetic α- and β-Ser-ADP-ribosylated Peptides Reveal α-Ser-ADPr as the Native Epimer
Jim Voorneveld, J.G.M. Rack, Ivan Ahel, et al.
Organic Letters (2018) Vol. 20, Iss. 13, pp. 4140-4143
Open Access | Times Cited: 47
Poly( ADP ‐ribosyl)ation of BRD 7 by PARP 1 confers resistance to DNA ‐damaging chemotherapeutic agents
Kaishun Hu, Wenjing Wu, Yu Li, et al.
EMBO Reports (2019) Vol. 20, Iss. 5
Open Access | Times Cited: 47

Scroll to top