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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:

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

Showing 1-25 of 40 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
From 1957 to Nowadays: A Brief History of Epigenetics
Paul Peixoto, Pierre‐François Cartron, Aurélien A. Sérandour, et al.
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 20, pp. 7571-7571
Open Access | Times Cited: 140
The Role of Electron Transfer Dissociation in Modern Proteomics
Nicholas M. Riley, Joshua J. Coon
Analytical Chemistry (2017) Vol. 90, Iss. 1, pp. 40-64
Open Access | Times Cited: 156
Emerging roles of eraser enzymes in the dynamic control of protein ADP-ribosylation
Julia O’Sullivan, Maria Tedim Ferreira, Jean‐Philippe Gagné, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 141
The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome
Ivo A. Hendriks, Sara C. Buch-Larsen, Evgeniia Prokhorova, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 81
The Expanding Constellation of Histone Post-Translational Modifications in the Epigenetic Landscape
Vincenzo Cavalieri
Genes (2021) Vol. 12, Iss. 10, pp. 1596-1596
Open Access | Times Cited: 70
PARP Power: A Structural Perspective on PARP1, PARP2, and PARP3 in DNA Damage Repair and Nucleosome Remodelling
Lotte van Beek, Éilís McClay, Saleha Patel, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 10, pp. 5112-5112
Open Access | Times Cited: 68
Preserving ester-linked modifications reveals glutamate and aspartate mono-ADP-ribosylation by PARP1 and its reversal by PARG
Edoardo José Longarini, Ivan Matić
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 16
Functional Interplay between Histone H2B ADP-Ribosylation and Phosphorylation Controls Adipogenesis
Dan Huang, Cristel V. Camacho, Rohit Setlem, et al.
Molecular Cell (2020) Vol. 79, Iss. 6, pp. 934-949.e14
Open Access | Times Cited: 58
Specific and shared biological functions of PARP2 – is PARP2 really a lil’ brother of PARP1?
Magdolna Szántó, José Yélamos, Péter Bai
Expert Reviews in Molecular Medicine (2024) Vol. 26
Open Access | Times Cited: 8
PARP1 condensates differentially partition DNA repair proteins and enhance DNA ligation
Christopher Chin Sang, Gaelen Moore, Maria Tereshchenko, et al.
EMBO Reports (2024)
Closed Access | Times Cited: 8
Noval advance of histone modification in inflammatory skin diseases and related treatment methods
Lichen Zhang, Rongrong Chai, Zongguang Tai, et al.
Frontiers in Immunology (2024) Vol. 14
Open Access | Times Cited: 7
Decoding Chromatin Ubiquitylation: A Chemical Biology Perspective
Pauline Franz, Beat Fierz
Journal of Molecular Biology (2024) Vol. 436, Iss. 7, pp. 168442-168442
Open Access | Times Cited: 6
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
Bridging of nucleosome-proximal DNA double-strand breaks by PARP2 enhances its interaction with HPF1
Guillaume Gaullier, Genevieve Roberts, Uma M. Muthurajan, et al.
PLoS ONE (2020) Vol. 15, Iss. 11, pp. e0240932-e0240932
Open Access | Times Cited: 43
The multifaceted role of PARP1 in RNA biogenesis
Rebekah Eleazer, Yvonne Fondufe‐Mittendorf
Wiley Interdisciplinary Reviews - RNA (2020) Vol. 12, Iss. 2
Open Access | Times Cited: 41
Epigenetic Mechanisms in DNA Double Strand Break Repair: A Clinical Review
Alejandra Fernández, Connor O’Leary, Kenneth J. O’Byrne, et al.
Frontiers in Molecular Biosciences (2021) Vol. 8
Open Access | Times Cited: 34
Linking DNA repair and cell cycle progression through serine ADP-ribosylation of histones
Julien Brustel, Tetsuya Muramoto, Kazuki Fumimoto, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 24
NAD-capped RNAs – a redox cofactor meets RNA
Maik Wolfram-Schauerte, Katharina Höfer
Trends in Biochemical Sciences (2022) Vol. 48, Iss. 2, pp. 142-155
Closed Access | Times Cited: 20
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
PARP1 condensates differentially partition DNA repair proteins and enhance DNA ligation
Christopher Chin Sang, Gaelen Moore, Maria Tereshchenko, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 3
Fluctuations of Histone Chemical Modifications in Breast, Prostate, and Colorectal Cancer: An Implication of Phytochemicals as Defenders of Chromatin Equilibrium
Marek Samec, Alena Líšková, Lenka Koklesová, et al.
Biomolecules (2019) Vol. 9, Iss. 12, pp. 829-829
Open Access | Times Cited: 24
Nonspecific Binding of RNA to PARP1 and PARP2 Does Not Lead to Catalytic Activation
Meagan Y Nakamoto, Johannes Rudolph, Deborah S. Wuttke, et al.
Biochemistry (2019) Vol. 58, Iss. 51, pp. 5107-5111
Open Access | Times Cited: 21
DNA damage and repair in the nucleosome: insights from computational methods
Natacha Gillet, Élise Dumont, Emmanuelle Bignon
Biophysical Reviews (2024) Vol. 16, Iss. 3, pp. 345-356
Closed Access | Times Cited: 2
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
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