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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:

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

Showing 20 citing articles:

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: 39
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
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
The mechanism of linear ubiquitination in regulating cell death and correlative diseases
Liyuan Gao, Wei Zhang, Xiao Hui Shi, et al.
Cell Death and Disease (2023) Vol. 14, Iss. 10
Open Access | Times Cited: 23
Legionella metaeffector MavL reverses ubiquitin ADP-ribosylation via a conserved arginine-specific macrodomain
Zhengrui Zhang, Jiaqi Fu, J.G.M. Rack, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 6
Comparison of Phosphoribosyl Ubiquitin Probes Targeting Legionella Dup Enzymes
Max S. Kloet, Rishov Mukhopadhyay, Rukmini Mukherjee, et al.
Bioconjugate Chemistry (2025)
Closed Access
Four of a Kind: A Complete Collection of ADP-Ribosylated Histidine Isosteres Using Cu(I)- and Ru(II)-Catalyzed Click Chemistry
Hugo Minnee, Hayley Chung, J.G.M. Rack, et al.
The Journal of Organic Chemistry (2023) Vol. 88, Iss. 15, pp. 10801-10809
Open Access | Times Cited: 9
Immunomodulatory roles of PARPs: Shaping the tumor microenvironment, one ADP-ribose at a time
Deja M. Brooks, Sudarshan Anand, Michael S. Cohen
Current Opinion in Chemical Biology (2023) Vol. 77, pp. 102402-102402
Open Access | Times Cited: 9
Chemical synthesis and functional evaluation of glycopeptides and glycoproteins containing rare glycosyl amino acid linkages
Weizhun Yang, Sherif Ramadan, Yan Zu, et al.
Natural Product Reports (2024) Vol. 41, Iss. 9, pp. 1403-1440
Closed Access | Times Cited: 3
Solid‐Phase Synthesis and Biological Evaluation of Peptides ADP‐Ribosylated at Histidine
Hugo Minnee, J.G.M. Rack, Gijsbert A. van der Marel, et al.
Angewandte Chemie International Edition (2023) Vol. 63, Iss. 4
Open Access | Times Cited: 8
Synthetic Dual Cysteine-ADP Ribosylated Peptides from the Androgen Receptor are Recognized by the DTX3L/PARP9 Complex
Sven Wijngaarden, Chunsong Yang, Carlos Vela‐Rodríguez, et al.
ACS Chemical Biology (2023) Vol. 18, Iss. 11, pp. 2377-2384
Open Access | Times Cited: 7
Capturing Legionella pneumophila effector enzymes using a ubiquitin derived photo-activatable probe
Max S. Kloet, Gerbrand J. van der Heden van Noort
Frontiers in Molecular Biosciences (2024) Vol. 11
Open Access | Times Cited: 2
Reversal of tyrosine-linked ADP-ribosylation by ARH3 and PARG
J.G.M. Rack, Jim Voorneveld, Edoardo José Longarini, et al.
Journal of Biological Chemistry (2024), pp. 107838-107838
Open Access | Times Cited: 2
Development of covalent probes to captureLegionella pneumophilaeffector enzymes
Max S. Kloet, Rishov Mukhopadhyay, Rukmini Mukherjee, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Protecting‐Group‐Free Synthesis of ADP‐Ribose and Dinucleoside Di‐/Triphosphate Derivatives via P(V)‐P(V) Coupling Reaction
Rui Hagino, Ryo Kuwabara, Naoko Komura, et al.
Chemistry - A European Journal (2024) Vol. 30, Iss. 41
Open Access | Times Cited: 1
Covalent Probes To Capture Legionella pneumophila Dup Effector Enzymes
Max S. Kloet, Rishov Mukhopadhyay, Rukmini Mukherjee, et al.
Journal of the American Chemical Society (2024)
Open Access | Times Cited: 1
PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities
N Mimica Dukic, Øyvind Strømland, Deeksha Munnur, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 3
Direct and Stereoselective Protecting‐Group‐Free N‐ADP‐Ribosylation through Traceless Staudinger Ligation
Rui Hagino, Naoko Komura, Akihiro Imamura, et al.
European Journal of Organic Chemistry (2024) Vol. 27, Iss. 22
Closed Access
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
Solid‐Phase Synthesis and Biological Evaluation of Peptides ADP‐Ribosylated at Histidine
Hugo Minnee, J.G.M. Rack, Gijsbert A. van der Marel, et al.
Angewandte Chemie (2023) Vol. 136, Iss. 4
Open Access
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