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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:

Phosphoproteomic Approach to Characterize Protein Mono- and Poly(ADP-ribosyl)ation Sites from Cells
Casey M. Daniels, Shao‐En Ong, Anthony K. L. Leung
Journal of Proteome Research (2014) Vol. 13, Iss. 8, pp. 3510-3522
Open Access | Times Cited: 113

Showing 26-50 of 113 citing articles:

The C-terminal domain of p53 orchestrates the interplay between non-covalent and covalent poly(ADP-ribosyl)ation of p53 by PARP1
Arthur Fischbach, Annika Krüger, Stephanie Hampp, et al.
Nucleic Acids Research (2017) Vol. 46, Iss. 2, pp. 804-822
Open Access | Times Cited: 95
Comprehensive ADP‐ribosylome analysis identifies tyrosine as an ADP‐ribose acceptor site
Deena M. Leslie Pedrioli, Mario Leutert, Vera Bilan, et al.
EMBO Reports (2018) Vol. 19, Iss. 8
Open Access | Times Cited: 91
Mechanism of phosphoribosyl-ubiquitination mediated by a single Legionella effector
Anıl Aktürk, David J. Wasilko, Xiaochun Wu, et al.
Nature (2018) Vol. 557, Iss. 7707, pp. 729-733
Open Access | Times Cited: 86
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
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
PARP1: Structural insights and pharmacological targets for inhibition
Jacob O. Spiegel, Bennett Van Houten, Jacob D. Durrant
DNA repair (2021) Vol. 103, pp. 103125-103125
Open Access | Times Cited: 63
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
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: 15
Combining Higher-Energy Collision Dissociation and Electron-Transfer/Higher-Energy Collision Dissociation Fragmentation in a Product-Dependent Manner Confidently Assigns Proteomewide ADP-Ribose Acceptor Sites
Vera Bilan, Mario Leutert, Paolo Nanni, et al.
Analytical Chemistry (2016) Vol. 89, Iss. 3, pp. 1523-1530
Closed Access | Times Cited: 82
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
Fishing the PTM proteome with chemical approaches using functional solid phases
Ying Zhang, Cheng Zhang, Hucong Jiang, et al.
Chemical Society Reviews (2015) Vol. 44, Iss. 22, pp. 8260-8287
Closed Access | Times Cited: 79
Identifying Family-Member-Specific Targets of Mono-ARTDs by Using a Chemical Genetics Approach
Ian Carter-O’Connell, Haihong Jin, Rory K. Morgan, et al.
Cell Reports (2016) Vol. 14, Iss. 3, pp. 621-631
Open Access | Times Cited: 79
New directions in poly(ADP‐ribose) polymerase biology
Florian J. Bock, Paul Chang
FEBS Journal (2016) Vol. 283, Iss. 22, pp. 4017-4031
Open Access | Times Cited: 77
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
The Conserved Macrodomain Is a Potential Therapeutic Target for Coronaviruses and Alphaviruses
Anthony K. L. Leung, Diane E. Griffin, Jürgen Bosch, et al.
Pathogens (2022) Vol. 11, Iss. 1, pp. 94-94
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
Phosphoribosyl modification of poly-ubiquitin chains at the Legionella-containing vacuole prohibiting autophagy adaptor recognition
Min Wan, Marena E. Minelli, Qiuye Zhao, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 6
Quantitative site-specific ADP-ribosylation profiling of DNA-dependent PARPs
Jean‐Philippe Gagné, Chantal Éthier, Daniel Defoy, et al.
DNA repair (2015) Vol. 30, pp. 68-79
Closed Access | Times Cited: 62
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
Biological significance of co- and post-translational modifications of the yeast 26S proteasome
Hisashi Hirano, Yayoi Kimura, Ayuko Kimura
Journal of Proteomics (2015) Vol. 134, pp. 37-46
Closed Access | Times Cited: 61
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
A Cell-Line-Specific Atlas of PARP-Mediated Protein Asp/Glu-ADP-Ribosylation in Breast Cancer
Yuanli Zhen, Yajie Zhang, Yonghao Yu
Cell Reports (2017) Vol. 21, Iss. 8, pp. 2326-2337
Open Access | Times Cited: 58
Macrodomain ADP-ribosylhydrolase and the pathogenesis of infectious diseases
Anthony K. L. Leung, Robert Lyle McPherson, Diane E. Griffin
PLoS Pathogens (2018) Vol. 14, Iss. 3, pp. e1006864-e1006864
Open Access | Times Cited: 54
Optimization of LTQ-Orbitrap Mass Spectrometer Parameters for the Identification of ADP-Ribosylation Sites
Florian Rosenthal, Paolo Nanni, Simon Barkow‐Oesterreicher, et al.
Journal of Proteome Research (2015) Vol. 14, Iss. 9, pp. 4072-4079
Closed Access | Times Cited: 52

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