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:

Serine ADP-ribosylation marks nucleosomes for ALC1-dependent chromatin remodeling
Jugal Mohapatra, Kyuto Tashiro, Ryan Beckner, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 28

Showing 1-25 of 28 citing articles:

The expanding universe of PARP1-mediated molecular and therapeutic mechanisms
Dan Huang, W. Lee Kraus
Molecular Cell (2022) Vol. 82, Iss. 12, pp. 2315-2334
Open Access | Times Cited: 159
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: 75
HPF1-dependent histone ADP-ribosylation triggers chromatin relaxation to promote the recruitment of repair factors at sites of DNA damage
Rebecca Smith, Siham Zentout, Magdalena B. Rother, et al.
Nature Structural & Molecular Biology (2023) Vol. 30, Iss. 5, pp. 678-691
Open Access | Times Cited: 45
Modular antibodies reveal DNA damage-induced mono-ADP-ribosylation as a second wave of PARP1 signaling
Edoardo José Longarini, Helen Dauben, Carolina Locatelli, et al.
Molecular Cell (2023) Vol. 83, Iss. 10, pp. 1743-1760.e11
Open Access | Times Cited: 38
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
The DNA damage response in the chromatin context: A coordinated process
Juliette Dabin, Margherita Mori, Sophie E. Polo
Current Opinion in Cell Biology (2023) Vol. 82, pp. 102176-102176
Open Access | Times Cited: 30
Chemoenzymatic and Synthetic Approaches To Investigate Aspartate- and Glutamate-ADP-Ribosylation
Kyuto Tashiro, Sven Wijngaarden, Jugal Mohapatra, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 25, pp. 14000-14009
Open Access | Times Cited: 25
ADP-ribose contributions to genome stability and PARP enzyme trapping on sites of DNA damage; paradigm shifts for a coming-of-age modification
Élise Rouleau-Turcotte, John M. Pascal
Journal of Biological Chemistry (2023) Vol. 299, Iss. 12, pp. 105397-105397
Open Access | Times Cited: 25
The Interplay Between Chromatin Remodeling and DNA Double-strand Break Repair: Implications for Cancer Biology and Therapeutics
Liu‐Jun He, Jaeyoung Moon, Chenghui Cai, et al.
DNA repair (2025) Vol. 146, pp. 103811-103811
Open Access | Times Cited: 1
Structure and dynamics of the chromatin remodeler ALC1 bound to a PARylated nucleosome
Luka Bačić, Guillaume Gaullier, Anton Sabantsev, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 33
Arginine ADP-Ribosylation: Chemical Synthesis of Post-Translationally Modified Ubiquitin Proteins
Jim Voorneveld, Max S. Kloet, Sven Wijngaarden, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 45, pp. 20582-20589
Open Access | Times Cited: 20
Asymmetric nucleosome PARylation at DNA breaks mediates directional nucleosome sliding by ALC1
Luka Bačić, Guillaume Gaullier, Jugal Mohapatra, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 4
Histone ADP-ribosylation promotes resistance to PARP inhibitors by facilitating PARP1 release from DNA lesions
Siham Zentout, Victor Imburchia, Catherine Chapuis, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 25
Closed Access | Times Cited: 4
Dispensability of HPF1 for cellular removal of DNA single-strand breaks
Kristyna Hrychova, Kamila Burdová, Zuzana Polackova, et al.
Nucleic Acids Research (2024) Vol. 52, Iss. 18, pp. 10986-10998
Open Access | Times Cited: 4
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
PARticular MARks: Histone ADP-ribosylation and the DNA Damage Response
Cem Özdemir, Laura R. Purkey, Anthony Sanchez, et al.
DNA repair (2024) Vol. 140, pp. 103711-103711
Closed Access | Times Cited: 3
The function and regulation of ADP-ribosylation in the DNA damage response
Lena Duma, Ivan Ahel
Biochemical Society Transactions (2023) Vol. 51, Iss. 3, pp. 995-1008
Open Access | Times Cited: 8
Acidic patch histone mutations and their effects on nucleosome remodeling
Hai T. Dao, Linh T D Pham
Biochemical Society Transactions (2022) Vol. 50, Iss. 2, pp. 907-919
Closed Access | Times Cited: 11
The fast-growing business of Serine ADP-ribosylation
Edoardo José Longarini, Ivan Matić
DNA repair (2022) Vol. 118, pp. 103382-103382
Closed Access | Times Cited: 11
A Protein Semisynthesis-Based Strategy to Investigate the Functional Impact of Linker Histone Serine ADP-Ribosylation
Kyuto Tashiro, Jugal Mohapatra, Chad A. Brautigam, et al.
ACS Chemical Biology (2022) Vol. 17, Iss. 4, pp. 810-815
Open Access | Times Cited: 10
Macrodomain Mac1 of SARS-CoV-2 Nonstructural Protein 3 Hydrolyzes Diverse ADP-ribosylated Substrates
Chanbora Chea, Duck‐Yeon Lee, Jiro Kato, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 6
DNA stimulates SIRT6 to mono-ADP-ribosylate proteins within histidine repeats
Nicholas Pederson, Katharine L. Diehl
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
ADP-ribosylome analysis reveals homogeneous DNA-damage-induced serine ADP-ribosylation across wild-type and BRCA-mutant breast cancer cell lines
Holda A. Anagho, Meeli Mullari, Aurél Prósz, et al.
Cell Reports (2024) Vol. 43, Iss. 7, pp. 114433-114433
Open Access | Times Cited: 1
Mono‐ADP‐ribosylation of peptides: an overview of synthetic and chemoenzymatic methodologies
Hugo Minnee, Jeroen D. C. Codée, Dmitri V. Filippov
ChemBioChem (2024)
Open Access
Page 1 - Next Page

Scroll to top