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:

PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities
N Mimica Dukic, Øyvind Strømland, Jonas D. Elsborg, et al.
Science Advances (2023) Vol. 9, Iss. 37
Open Access | Times Cited: 36

Showing 1-25 of 36 citing articles:

ADP-ribosylation from molecular mechanisms to therapeutic implications
Marcin J. Suskiewicz, Evgeniia Prokhorova, J.G.M. Rack, et al.
Cell (2023) Vol. 186, Iss. 21, pp. 4475-4495
Open Access | Times Cited: 64

PARP14 and PARP9/DTX3L regulate interferon-induced ADP-ribosylation
Pulak Kar, Chatrin Chatrin, N Mimica Dukic, et al.
The EMBO Journal (2024) Vol. 43, Iss. 14, pp. 2929-2953
Open Access | Times Cited: 15

PARP14 is a writer, reader, and eraser of mono-ADP-ribosylation
Archimede Torretta, Constantinos Chatzicharalampous, Carmen Ebenwaldner, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 9, pp. 105096-105096
Open Access | Times Cited: 22

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: 21

PARP14 is regulated by the PARP9/DTX3L complex and promotes interferon γ-induced ADP-ribosylation
Victória Chaves Ribeiro, Lilian C. Russo, Nícolas C. Hoch
The EMBO Journal (2024) Vol. 43, Iss. 14, pp. 2908-2928
Open Access | Times Cited: 8

PARP14 is pro- and anti-viral host factor that promotes IFN production and affects the replication of multiple viruses
Srivatsan Parthasarathy, Pradtahna Saenjamsai, Hongping Hao, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 6

Mutation of a highly conserved isoleucine residue in loop 2 of several 𝛽-coronavirus macrodomains indicates that enhanced ADP-ribose binding is detrimental to infection
Catherine M. Kerr, Jessica J. Pfannenstiel, Yousef M. Alhammad, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 5

RACK1 MARylation regulates translation and stress granules in ovarian cancer cells
Sridevi Challa, Tulip Nandu, Hyung Bum Kim, et al.
The Journal of Cell Biology (2025) Vol. 224, Iss. 2
Open Access

Exacerbated salmonellosis in poly(ADP-ribose) polymerase 14 deficient mice
Madhukar Vedantham, Lauri Polari, Tiia Rissanen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Closed Access

Insight into the function of the Golgi membrane protein GOLM1 in cholangiocytes through interactomic analysis
Meghana Nagaraj, Emmagouni Sharath Kumar Goud, Vaishali Chaurasiya, et al.
FEBS Letters (2025)
Closed Access

Parps in immune response: Potential targets for cancer immunotherapy
S Wang, Jingling Huang, T. X. Zeng, et al.
Biochemical Pharmacology (2025) Vol. 234, pp. 116803-116803
Closed Access

Discovery of reversing enzymes for RNA ADP-ribosylation reveals a possible defence module against toxic attack
Yang Lu, M. Schuller, Nathan P. Bullen, et al.
Nucleic Acids Research (2025) Vol. 53, Iss. 4
Open Access

Comprehensive dataset of interactors for the entire PARP family using TurboID proximity labeling
Jiefu Zheng, Yawen Deng, Cong Fang, et al.
Scientific Data (2025) Vol. 12, Iss. 1
Open Access

Specificity of DNA ADP-Ribosylation Reversal by NADARs
Bara Cihlova, Yang Lu, Andreja Mikoč, et al.
Toxins (2024) Vol. 16, Iss. 5, pp. 208-208
Open Access | Times Cited: 3

Cell-Penetrating Peptide-Mediated Biomolecule Transportation in Artificial Lipid Vesicles and Living Cells
Akari Miwa, Koki Kamiya
Molecules (2024) Vol. 29, Iss. 14, pp. 3339-3339
Open Access | Times Cited: 3

Mutation of a highly conserved isoleucine residue in loop 2 of several β-coronavirus macrodomains indicates that enhanced ADP-ribose binding is detrimental for replication
Catherine M. Kerr, Jessica J. Pfannenstiel, Yousef M. Alhammad, et al.
Journal of Virology (2024) Vol. 98, Iss. 11
Closed Access | Times Cited: 3

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: 2

A PARP14/TARG1-Regulated RACK1 MARylation Cycle Drives Stress Granule Dynamics in Ovarian Cancer Cells
Sridevi Challa, Tulip Nandu, Hyung Bum Kim, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 6

Single-cell and bulk RNA sequencing highlights the role of M1-like infiltrating macrophages in antibody-mediated rejection after kidney transplantation
Qidan Pang, Liang Chen, Changyong An, et al.
Heliyon (2024) Vol. 10, Iss. 6, pp. e27865-e27865
Open Access | Times Cited: 1

Regulation of ADP-ribosyltransferase activity by ART domain dimerization in PARP15
Carmen Ebenwaldner, Antonio Ginés García Saura, Simon Ekström, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1

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: 1

Interferon-Induced PARP14-Mediated ADP-Ribosylation in p62 Bodies Requires an Active Ubiquitin-Proteasome System
Rameez Raja, Banhi Biswas, Rachy Abraham, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1

Body‐wide genetic deficiency of poly(ADP‐ribose) polymerase 14 sensitizes mice to colitis
Madhukar Vedantham, Lauri Polari, Anbu Poosakkannu, et al.
The FASEB Journal (2024) Vol. 38, Iss. 13
Open Access | Times Cited: 1

Pathological and physiological roles of ADP-ribosylation: established functions and new insights
Karla L. H. Feijs, Nonso Josephat Ikenga, Roko Žaja
Biological Chemistry (2024) Vol. 405, Iss. 9-10, pp. 567-581
Closed Access | Times Cited: 1

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