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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:

Sirtuin 7 Plays a Role in Ribosome Biogenesis and Protein Synthesis
Yuan-Chin Tsai, Todd M. Greco, Ileana M. Cristea
Molecular & Cellular Proteomics (2013) Vol. 13, Iss. 1, pp. 73-83
Open Access | Times Cited: 115

Showing 1-25 of 115 citing articles:

Sirtuins in Epigenetic Regulation
Hui Jing, Hening Lin
Chemical Reviews (2015) Vol. 115, Iss. 6, pp. 2350-2375
Open Access | Times Cited: 234
Sirtuin regulation in aging and injury
Ninu Poulose, Raghavan Raju
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (2015) Vol. 1852, Iss. 11, pp. 2442-2455
Open Access | Times Cited: 223
Sirtuins in gamete biology and reproductive physiology: emerging roles and therapeutic potential in female and male infertility
Carla Tatone, Giovanna Di Emidio, Arcangelo Barbonetti, et al.
Human Reproduction Update (2018) Vol. 24, Iss. 3, pp. 267-289
Open Access | Times Cited: 221
SIRT7 antagonizes TGF-β signaling and inhibits breast cancer metastasis
Xiaolong Tang, Lei Shi, Ni Xie, et al.
Nature Communications (2017) Vol. 8, Iss. 1
Open Access | Times Cited: 209
The role of sirtuins in cellular homeostasis
Wioleta Kupis, Jan Pałyga, Ewa Tomal, et al.
Journal of Physiology and Biochemistry (2016) Vol. 72, Iss. 3, pp. 371-380
Open Access | Times Cited: 179
An overview of Sirtuins as potential therapeutic target: Structure, function and modulators
Yijie Wang, Jun He, Mengya Liao, et al.
European Journal of Medicinal Chemistry (2018) Vol. 161, pp. 48-77
Closed Access | Times Cited: 174
Revisiting the role of dihydroorotate dehydrogenase as a therapeutic target for cancer
Joseph T. Madak, Armand Bankhead, Christine R. Cuthbertson, et al.
Pharmacology & Therapeutics (2018) Vol. 195, pp. 111-131
Closed Access | Times Cited: 165
Understanding the Function of Mammalian Sirtuins and Protein Lysine Acylation
Miao Wang, Hening Lin
Annual Review of Biochemistry (2021) Vol. 90, Iss. 1, pp. 245-285
Open Access | Times Cited: 115
Sirtuin Inhibitors as Anticancer Agents
Jing Hu, Hui Jing, Hening Lin
Future Medicinal Chemistry (2014) Vol. 6, Iss. 8, pp. 945-966
Open Access | Times Cited: 156
Sirtuins Are Evolutionarily Conserved Viral Restriction Factors
Emre Koyuncu, Hanna G. Budayeva, Yana Miteva, et al.
mBio (2014) Vol. 5, Iss. 6
Open Access | Times Cited: 135
SIRT7 antagonizes human stem cell aging as a heterochromatin stabilizer
Shijia Bi, Zunpeng Liu, Zeming Wu, et al.
Protein & Cell (2020) Vol. 11, Iss. 7, pp. 483-504
Open Access | Times Cited: 124
SIRT7-dependent deacetylation of the U3-55k protein controls pre-rRNA processing
Sifan Chen, Maximilian Felix Blank, Aishwarya Iyer, et al.
Nature Communications (2016) Vol. 7, Iss. 1
Open Access | Times Cited: 121
Sirt7 promotes adipogenesis in the mouse by inhibiting autocatalytic activation of Sirt1
Jian Fang, Alessandro Ianni, Christian Smolka, et al.
Proceedings of the National Academy of Sciences (2017) Vol. 114, Iss. 40
Open Access | Times Cited: 112
Sirt7 Contributes to Myocardial Tissue Repair by Maintaining Transforming Growth Factor-β Signaling Pathway
Satoshi Araki, Yasuhiro Izumiya, Taku Rokutanda, et al.
Circulation (2015) Vol. 132, Iss. 12, pp. 1081-1093
Open Access | Times Cited: 110
SIRT7 and hepatic lipid metabolism
Bor Luen Tang
Frontiers in Cell and Developmental Biology (2015) Vol. 3
Open Access | Times Cited: 108
The Current State of NAD+‐Dependent Histone Deacetylases (Sirtuins) as Novel Therapeutic Targets
Matthias Schiedel, Dina Robaa, Tobias Rumpf, et al.
Medicinal Research Reviews (2017) Vol. 38, Iss. 1, pp. 147-200
Open Access | Times Cited: 107
The seven faces of SIRT7
Maximilian Felix Blank, Ingrid Grummt
Transcription (2017) Vol. 8, Iss. 2, pp. 67-74
Open Access | Times Cited: 101
SIRT7 Is an RNA-Activated Protein Lysine Deacylase
Zhen Tong, Miao Wang, Yi Wang, et al.
ACS Chemical Biology (2016) Vol. 12, Iss. 1, pp. 300-310
Open Access | Times Cited: 96
Regulation of Serine-Threonine Kinase Akt Activation by NAD + -Dependent Deacetylase SIRT7
Jia Yu, Bo Qin, Fengying Wu, et al.
Cell Reports (2017) Vol. 18, Iss. 5, pp. 1229-1240
Open Access | Times Cited: 91
Sirtuins' control of autophagy and mitophagy in cancer
Michele Aventaggiato, Enza Vernucci, Federica Barreca, et al.
Pharmacology & Therapeutics (2020) Vol. 221, pp. 107748-107748
Closed Access | Times Cited: 88
SIRT7-Dependent Deacetylation of Fibrillarin Controls Histone H2A Methylation and rRNA Synthesis during the Cell Cycle
Aishwarya Iyer, Nicolai Krogh, Peter Tessarz, et al.
Cell Reports (2018) Vol. 25, Iss. 11, pp. 2946-2954.e5
Open Access | Times Cited: 87
HDAC8 cooperates with SMAD3/4 complex to suppress SIRT7 and promote cell survival and migration
Xiaolong Tang, Li Guo, Fengting Su, et al.
Nucleic Acids Research (2020) Vol. 48, Iss. 6, pp. 2912-2923
Open Access | Times Cited: 79
SIRT7 in the aging process
Francisco Alejandro Lagunas‐Rangel
Cellular and Molecular Life Sciences (2022) Vol. 79, Iss. 6
Open Access | Times Cited: 62
SIRT7: the seventh key to unlocking the mystery of aging
Umar Raza, Xiaolong Tang, Zuojun Liu, et al.
Physiological Reviews (2023) Vol. 104, Iss. 1, pp. 253-280
Open Access | Times Cited: 27
SIRT7 orchestrates melanoma progression by simultaneously promoting cell survival and immune evasion via UPR activation
Xiuli Yi, Huina Wang, Yuqi Yang, et al.
Signal Transduction and Targeted Therapy (2023) Vol. 8, Iss. 1
Open Access | Times Cited: 26
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