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:
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
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
Showing 8 citing articles:
DNA stimulates the deacetylase SIRT6 to mono-ADP-ribosylate proteins with histidine repeats
Nicholas Pederson, Katharine L. Diehl
Journal of Biological Chemistry (2025), pp. 108532-108532
Open Access
Nicholas Pederson, Katharine L. Diehl
Journal of Biological Chemistry (2025), pp. 108532-108532
Open Access
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
Rui Hagino, Ryo Kuwabara, Naoko Komura, et al.
Chemistry - A European Journal (2024) Vol. 30, Iss. 41
Open Access | Times Cited: 1
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
Nicholas Pederson, Katharine L. Diehl
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
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
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
Hugo Minnee, Jeroen D. C. Codée, Dmitri V. Filippov
ChemBioChem (2024)
Open Access
The quest to identify ADP-ribosylation readers: methodological advances
S. Weijers, Michiel Vermeulen, Katarzyna W. Kliza
Trends in Biochemical Sciences (2024) Vol. 49, Iss. 11, pp. 1000-1013
Closed Access
S. Weijers, Michiel Vermeulen, Katarzyna W. Kliza
Trends in Biochemical Sciences (2024) Vol. 49, Iss. 11, pp. 1000-1013
Closed 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
Hugo Minnee, J.G.M. Rack, Gijsbert A. van der Marel, et al.
Angewandte Chemie (2023) Vol. 136, Iss. 4
Open Access
