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:

Cryo-EM structure of the human Sirtuin 6–nucleosome complex
Un Seng Chio, Othman Rechiche, Alysia R. Bryll, et al.
Science Advances (2023) Vol. 9, Iss. 15
Open Access | Times Cited: 22

Showing 22 citing articles:

Antiaging Strategies and Remedies: A Landscape of Research Progress and Promise
Rumiana Tenchov, Janet M. Sasso, Xinmei Wang, et al.
ACS Chemical Neuroscience (2024) Vol. 15, Iss. 3, pp. 408-446
Open Access | Times Cited: 11

Structural basis of SIRT7 nucleosome engagement and substrate specificity
Carlos Moreno–Yruela, Babatunde Ekundayo, Polina N. Foteva, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 1

Mechanisms of DNA Methylation Regulatory Function and Crosstalk with Histone Lysine Methylation
Bailey M. Tibben, Scott B. Rothbart
Journal of Molecular Biology (2023) Vol. 436, Iss. 7, pp. 168394-168394
Closed Access | Times Cited: 18

Binding to nucleosome poises human SIRT6 for histone H3 deacetylation
Ekaterina Smirnova, Emmanuelle Bignon, Patrick Schultz, et al.
eLife (2024) Vol. 12
Open Access | Times Cited: 6

Substrates and Cyclic Peptide Inhibitors of the Oligonucleotide‐Activated Sirtuin 7**
Julie E. Bolding, Alexander L. Nielsen, I. M. Jensen, et al.
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 49
Open Access | Times Cited: 12

Structural and Enzymatic Plasticity of SIRT6 Deacylase Activity
Zhipeng A. Wang, Jonathan Markert, Samuel D. Whedon, et al.
Journal of Biological Chemistry (2025), pp. 108446-108446
Open Access

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

Deciphering histone H4 lysine acetylation and methylation via sortase-mediated semisynthesis
Yihang Xiao, Kun Zou, Jin‐Yu Terence Yang, et al.
Cell Reports Physical Science (2023) Vol. 4, Iss. 11, pp. 101638-101638
Open Access | Times Cited: 7

Revealing chromatin-specific functions of histone deacylases
Carlos Moreno–Yruela, Beat Fierz
Biochemical Society Transactions (2024) Vol. 52, Iss. 1, pp. 353-365
Open Access | Times Cited: 2

Binding to nucleosome poises human SIRT6 for histone H3 deacetylation
Ekaterina Smirnova, Emmanuelle Bignon, Patrick Schultz, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 4

Structure of the complete Saccharomyces cerevisiae Rpd3S-nucleosome complex
Jonathan Markert, Seychelle M. Vos, Lucas Farnung
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 4

The (patho)physiological roles of the individual deacylase activities of a sirtuin
Weiping Zheng
Chemical Biology & Drug Design (2024) Vol. 103, Iss. 2
Closed Access | Times Cited: 1

Binding to nucleosome poises human SIRT6 for histone H3 deacetylation
Ekaterina Smirnova, Emmanuelle Bignon, Patrick Schultz, et al.
(2024)
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

Deciphering the Allosteric Activation Mechanism of SIRT6 Using Molecular Dynamics Simulations
Zhiyuan Zhao, Jintong Du, Yu Du, et al.
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 18, pp. 5896-5902
Open Access | Times Cited: 2

Structural basis of SIRT7 nucleosome engagement and substrate specificity
Carlos Moreno–Yruela, Babatunde Ekundayo, Polina N. Foteva, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

Binding to nucleosome poises human SIRT6 for histone H3 deacetylation
Ekaterina Smirnova, Emmanuelle Bignon, Patrick Schultz, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 1

Substrates and Cyclic Peptide Inhibitors of the Oligonucleotide‐Activated Sirtuin 7**
Julie E. Bolding, Alexander L. Nielsen, I. M. Jensen, et al.
Angewandte Chemie (2023) Vol. 135, Iss. 49
Open Access | Times Cited: 1

Substrates and Cyclic Peptide Inhibitors of the Oligonucleotide Activated SIRT7
Julie E. Bolding, Alexander L. Nielsen, I. M. Jensen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access

Binding to nucleosome poises human SIRT6 for histone H3 deacetylation
Ekaterina Smirnova, Emmanuelle Bignon, Patrick Schultz, et al.
(2023)
Open Access

Binding to nucleosome poises human SIRT6 for histone H3 deacetylation
Ekaterina Smirnova, Emmanuelle Bignon, Patrick Schultz, et al.
(2023)
Open Access

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