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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:

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

Showing 1-25 of 52 citing articles:

PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes
Rebecca Gupte, Ziying Liu, W. Lee Kraus
Genes & Development (2017) Vol. 31, Iss. 2, pp. 101-126
Open Access | Times Cited: 618
Serine ADP-Ribosylation Depends on HPF1
Juán José Bonfiglio, Pietro Fontana, Qi Zhang, et al.
Molecular Cell (2017) Vol. 65, Iss. 5, pp. 932-940.e6
Open Access | Times Cited: 315
ADP-Ribosylation, a Multifaceted Posttranslational Modification Involved in the Control of Cell Physiology in Health and Disease
Bernhard Lüscher, Mareike Bütepage, Laura Eckei, et al.
Chemical Reviews (2017) Vol. 118, Iss. 3, pp. 1092-1136
Closed Access | Times Cited: 224
Serine is a new target residue for endogenous ADP-ribosylation on histones
Orsolya Leidecker, Juán José Bonfiglio, Thomas Colby, et al.
Nature Chemical Biology (2016) Vol. 12, Iss. 12, pp. 998-1000
Open Access | Times Cited: 220
Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue
Rita Martello, Mario Leutert, Stephanie Jungmichel, et al.
Nature Communications (2016) Vol. 7, Iss. 1
Open Access | Times Cited: 212
Ubiquitin is directly linked via an ester to protein-conjugated mono-ADP-ribose
Daniel S. Bejan, Rachel E. Lacoursiere, Jonathan N. Pruneda, et al.
The EMBO Journal (2025)
Open Access | Times Cited: 3
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
Common errors in mass spectrometry‐based analysis of post‐translational modifications
Min‐Sik Kim, Jun Zhong, Akhilesh Pandey
PROTEOMICS (2015) Vol. 16, Iss. 5, pp. 700-714
Open Access | Times Cited: 126
Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase
Jeannette Abplanalp, Mario Leutert, Emilie Frugier, et al.
Nature Communications (2017) Vol. 8, Iss. 1
Open Access | Times Cited: 116
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: 92
An HPF1/PARP1-Based Chemical Biology Strategy for Exploring ADP-Ribosylation
Juán José Bonfiglio, Orsolya Leidecker, Helen Dauben, et al.
Cell (2020) Vol. 183, Iss. 4, pp. 1086-1102.e23
Open Access | Times Cited: 90
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
Legionella pneumophila modulates host energy metabolism by ADP-ribosylation of ADP/ATP translocases
Jiaqi Fu, Mowei Zhou, Marina Gritsenko, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 44
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: 24
Defeating Major Contaminants in Fe3+- Immobilized Metal Ion Affinity Chromatography (IMAC) Phosphopeptide Enrichment
Clément M. Potel, Miao‐Hsia Lin, Albert J. R. Heck, et al.
Molecular & Cellular Proteomics (2018) Vol. 17, Iss. 5, pp. 1028-1034
Open Access | Times Cited: 83
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
AvrRpm1 Functions as an ADP-Ribosyl Transferase to Modify NOI-domain Containing Proteins, Including Arabidopsis and Soybean RPM1-interacting Protein 4
Thomas J. Redditt, Eui‐Hwan Chung, Hana Zand Karimi, et al.
The Plant Cell (2019), pp. tpc.00020.2019-tpc.00020.2019
Open Access | Times Cited: 65
Pathogen hijacks programmed cell death signaling by arginine ADPR-deacylization of caspases
Ting Peng, Xinyuan Tao, Zhujun Xia, et al.
Molecular Cell (2022) Vol. 82, Iss. 10, pp. 1806-1820.e8
Open Access | Times Cited: 30
Poly(ADP-Ribose) Polymerases in Host-Pathogen Interactions, Inflammation, and Immunity
Pamlea N. Brady, Anupam Goel, Margaret A. Johnson
Microbiology and Molecular Biology Reviews (2019) Vol. 83, Iss. 1
Open Access | Times Cited: 46
Mass spectrometry for serine ADP-ribosylation? Think o-glycosylation!
Juán José Bonfiglio, Thomas Colby, Ivan Matić
Nucleic Acids Research (2017) Vol. 45, Iss. 11, pp. 6259-6264
Open Access | Times Cited: 47
New Quantitative Mass Spectrometry Approaches Reveal Different ADP-ribosylation Phases Dependent On the Levels of Oxidative Stress
Vera Bilan, Nathalie Selevsek, Hans A. V. Kistemaker, et al.
Molecular & Cellular Proteomics (2017) Vol. 16, Iss. 5, pp. 949-958
Open Access | Times Cited: 45
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
Poly(ADP-Ribose) polymerase 1 as a key regulator of DNA repair
С. Н. Ходырева, Olga I. Lavrik
Molecular Biology (2016) Vol. 50, Iss. 4, pp. 580-595
Closed Access | Times Cited: 30
A Study into the ADP-Ribosylome of IFN-γ-Stimulated THP-1 Human Macrophage-like Cells Identifies ARTD8/PARP14 and ARTD9/PARP9 ADP-Ribosylation
Hideyuki Higashi, Takashi Maejima, Lang Ho Lee, et al.
Journal of Proteome Research (2019) Vol. 18, Iss. 4, pp. 1607-1622
Open Access | Times Cited: 28
Gas-Phase Fragmentation of ADP-Ribosylated Peptides: Arginine-Specific Side-Chain Losses and Their Implication in Database Searches
Peter Gehrig, Kathrin Nowak, Christian Panse, et al.
Journal of the American Society for Mass Spectrometry (2020) Vol. 32, Iss. 1, pp. 157-168
Closed Access | Times Cited: 27
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