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:

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

Showing 1-25 of 82 citing articles:

Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein
Jian Lei, Yuri Kusov, Rolf Hilgenfeld
Antiviral Research (2017) Vol. 149, pp. 58-74
Open Access | Times Cited: 724

Therapeutic Potential of NAD-Boosting Molecules: The In Vivo Evidence
Luis A. Rajman, Karolina Chwalek, David Sinclair
Cell Metabolism (2018) Vol. 27, Iss. 3, pp. 529-547
Open Access | Times Cited: 710

microRNAs Biogenesis, Functions and Role in Tumor Angiogenesis
Tiziana Annese, Roberto Tamma, Michelina De Giorgis, et al.
Frontiers in Oncology (2020) Vol. 10
Open Access | Times Cited: 211

The role of poly ADP-ribosylation in the first wave of DNA damage response
Chao Liu, Aditi Vyas, Muzaffer Ahmad Kassab, et al.
Nucleic Acids Research (2017) Vol. 45, Iss. 14, pp. 8129-8141
Open Access | Times Cited: 198

Molecular genetics and targeted therapy of WNT-related human diseases (Review)
Masuko Katoh, Masaru Katoh
International Journal of Molecular Medicine (2017)
Open Access | Times Cited: 186

PARP2 mediates branched poly ADP-ribosylation in response to DNA damage
Qian Chen, Muzaffer Ahmad Kassab, Françoise Dantzer, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 147

Reversible mono‐ADP‐ribosylation of DNA breaks
Deeksha Munnur, Ivan Ahel
FEBS Journal (2017) Vol. 284, Iss. 23, pp. 4002-4016
Open Access | Times Cited: 142

The Enigmatic Function of PARP1: From PARylation Activity to PAR Readers
Tatiana Kamaletdinova, Zahra Fanaei‐Kahrani, Zhao‐Qi Wang
Cells (2019) Vol. 8, Iss. 12, pp. 1625-1625
Open Access | Times Cited: 133

Post-translational add-ons mark the path in exosomal protein sorting
Olga Moreno-Gonzalo, Irene Fernández‐Delgado, Francisco Sánchez‐Madrid
Cellular and Molecular Life Sciences (2017) Vol. 75, Iss. 1, pp. 1-19
Open Access | Times Cited: 112

Super-resolution imaging identifies PARP1 and the Ku complex acting as DNA double-strand break sensors
Guang Yang, Chao Liu, Shih-Hsun Chen, et al.
Nucleic Acids Research (2018) Vol. 46, Iss. 7, pp. 3446-3457
Open Access | Times Cited: 103

Wnt Signaling in the Regulation of Immune Cell and Cancer Therapeutics
Muhammad Haseeb, Rameez Hassan Pirzada, Qurat Ul Ain, et al.
Cells (2019) Vol. 8, Iss. 11, pp. 1380-1380
Open Access | Times Cited: 93

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

Truncated PARP1 mediates ADP-ribosylation of RNA polymerase III for apoptosis
Qian Chen, Kai Ma, Xiuhua Liu, et al.
Cell Discovery (2022) Vol. 8, Iss. 1
Open Access | Times Cited: 31

PARylated PDHE1α generates acetyl-CoA for local chromatin acetylation and DNA damage repair
Jun Zhang, Feng Chen, Yuan Tian, et al.
Nature Structural & Molecular Biology (2023) Vol. 30, Iss. 11, pp. 1719-1734
Closed Access | Times Cited: 22

Cellular Compartmentation and the Redox/Nonredox Functions of NAD+
Chaitanya A. Kulkarni, Paul S. Brookes
Antioxidants and Redox Signaling (2019) Vol. 31, Iss. 9, pp. 623-642
Open Access | Times Cited: 52

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

ADP‐ribosylation of histone variant H2AX promotes base excision repair
Qian Chen, Chunjing Bian, Xin Wang, et al.
The EMBO Journal (2020) Vol. 40, Iss. 2
Open Access | Times Cited: 44

Comparative Transcriptomics of Cold Growth and Adaptive Features of a Eury- and Steno-Psychrophile
Isabelle Raymond‐Bouchard, Julien Tremblay, Ianina Altshuler, et al.
Frontiers in Microbiology (2018) Vol. 9
Open Access | Times Cited: 41

PARP1 Enhances Influenza A Virus Propagation by Facilitating Degradation of Host Type I Interferon Receptor
Chuan Xia, Jennifer J. Wolf, Chuankai Sun, et al.
Journal of Virology (2020) Vol. 94, Iss. 7
Open Access | Times Cited: 38

Signaling pathways involved in cell cycle arrest during the DNA breaks
Fatemeh Sadoughi, Jamal Hallajzadeh, Zatollah Asemi, et al.
DNA repair (2021) Vol. 98, pp. 103047-103047
Closed Access | Times Cited: 31

Uncovering the Invisible: Mono-ADP-ribosylation Moved into the Spotlight
Ann-Katrin Hopp, Michael O. Hottiger
Cells (2021) Vol. 10, Iss. 3, pp. 680-680
Open Access | Times Cited: 28

Protein modification in neurodegenerative diseases
Shahin Ramazi, Maedeh Dadzadi, Mona Darvazi, et al.
MedComm (2024) Vol. 5, Iss. 8
Open Access | Times Cited: 4

The Role of NAD+-Dependent Signal Mechanisms in Cancer Development and Treatment
Ting Lu, Zheng‐Hong Qin, Junchao Wu
(2025), pp. 533-564
Closed Access

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