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:

Reconstitution defines the roles of p62, NBR1 and TAX1BP1 in ubiquitin condensate formation and autophagy initiation
Eleonora Turco, Adriana Savova, Flora Gere, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 158

Showing 1-25 of 158 citing articles:

The mechanisms and roles of selective autophagy in mammals
Jose Norberto S. Vargas, Maho Hamasaki, Tsuyoshi Kawabata, et al.
Nature Reviews Molecular Cell Biology (2022) Vol. 24, Iss. 3, pp. 167-185
Closed Access | Times Cited: 558

Autophagy genes in biology and disease
Hayashi Yamamoto, Sidi Zhang, Noboru Mizushima
Nature Reviews Genetics (2023) Vol. 24, Iss. 6, pp. 382-400
Open Access | Times Cited: 359

The mitophagy pathway and its implications in human diseases
Shouliang Wang, Haijiao Long, Lianjie Hou, et al.
Signal Transduction and Targeted Therapy (2023) Vol. 8, Iss. 1
Open Access | Times Cited: 220

Selective Autophagy Receptor p62/SQSTM1, a Pivotal Player in Stress and Aging
Anita Kumar, Joslyn Mills, Louis R. Lapierre
Frontiers in Cell and Developmental Biology (2022) Vol. 10
Open Access | Times Cited: 182

The multifaceted role of autophagy in cancer
Ryan C. Russell, Kun‐Liang Guan
The EMBO Journal (2022) Vol. 41, Iss. 13
Open Access | Times Cited: 130

CCT2 is an aggrephagy receptor for clearance of solid protein aggregates
Xinyu Ma, Caijing Lu, Yuting Chen, et al.
Cell (2022) Vol. 185, Iss. 8, pp. 1325-1345.e22
Open Access | Times Cited: 126

ER-phagy: mechanisms, regulation, and diseases connected to the lysosomal clearance of the endoplasmic reticulum
Fulvio Reggiori, Maurizio Molinari
Physiological Reviews (2022) Vol. 102, Iss. 3, pp. 1393-1448
Open Access | Times Cited: 109

Orchestration of selective autophagy by cargo receptors
Elias Adriaenssens, Luca Ferrari, Sascha Martens
Current Biology (2022) Vol. 32, Iss. 24, pp. R1357-R1371
Open Access | Times Cited: 77

Autophagy-Dependent Ferroptosis in Cancer
Fangquan Chen, Xiutao Cai, Rui Kang, et al.
Antioxidants and Redox Signaling (2023) Vol. 39, Iss. 1-3, pp. 79-101
Closed Access | Times Cited: 58

The chaperone-assisted selective autophagy complex dynamics and dysfunctions
B. Tedesco, Leen Vendredy, Vincent Timmerman, et al.
Autophagy (2023) Vol. 19, Iss. 6, pp. 1619-1641
Open Access | Times Cited: 53

Unconventional initiation of PINK1/Parkin mitophagy by Optineurin
Thanh Ngoc Nguyen, Justyna Sawa‐Makarska, Grace Khuu, et al.
Molecular Cell (2023) Vol. 83, Iss. 10, pp. 1693-1709.e9
Open Access | Times Cited: 53

Molecular Mechanisms of Macroautophagy, Microautophagy, and Chaperone-Mediated Autophagy
Hayashi Yamamoto, Takahide Matsui
Journal of Nippon Medical School (2023) Vol. 91, Iss. 1, pp. 2-9
Open Access | Times Cited: 53

Stress granule homeostasis is modulated by TRIM21-mediated ubiquitination of G3BP1 and autophagy-dependent elimination of stress granules
Cuiwei Yang, Zhangshun Wang, Yingjin Kang, et al.
Autophagy (2023) Vol. 19, Iss. 7, pp. 1934-1951
Open Access | Times Cited: 50

Short-distance vesicle transport via phase separation
Hua Qiu, Xiandeng Wu, Xiaoli Ma, et al.
Cell (2024) Vol. 187, Iss. 9, pp. 2175-2193.e21
Closed Access | Times Cited: 27

Large-scale chemoproteomics expedites ligand discovery and predicts ligand behavior in cells
Fabian Offensperger, Gary Tin, Miquel Duran‐Frigola, et al.
Science (2024) Vol. 384, Iss. 6694
Closed Access | Times Cited: 23

Protein quality control machinery: regulators of condensate architecture and functionality
Anitha Rajendran, Carlos A. Castañeda
Trends in Biochemical Sciences (2025)
Closed Access | Times Cited: 2

The interconnective role of the UPS and autophagy in the quality control of cancer mitochondria
Wanting Xu, Lei Dong, Jiyan Dai, et al.
Cellular and Molecular Life Sciences (2025) Vol. 82, Iss. 1
Open Access | Times Cited: 2

NBR1: The archetypal selective autophagy receptor
Nikoline Lander Rasmussen, Athanasios Kournoutis, Trond Lamark, et al.
The Journal of Cell Biology (2022) Vol. 221, Iss. 11
Open Access | Times Cited: 55

Kinase regulation by liquid–liquid phase separation
Tania P. López-Palacios, Joshua L. Andersen
Trends in Cell Biology (2022) Vol. 33, Iss. 8, pp. 649-666
Open Access | Times Cited: 54

Repression of autophagy leads to acrosome biogenesis disruption caused by a sub-chronic oral administration of polystyrene nanoparticles
Lixiao Zhou, Ziying Yu, Yinyin Xia, et al.
Environment International (2022) Vol. 163, pp. 107220-107220
Open Access | Times Cited: 53

Targeted degradation of ⍺-synuclein aggregates in Parkinson’s disease using the AUTOTAC technology
Jihoon Lee, Ki Woon Sung, Eun-Jin Bae, et al.
Molecular Neurodegeneration (2023) Vol. 18, Iss. 1
Open Access | Times Cited: 34

Aggrephagy at a glance
Bernd Bauer, Sascha Martens, Luca Ferrari
Journal of Cell Science (2023) Vol. 136, Iss. 10
Open Access | Times Cited: 30

Autophagy in sarcopenia: Possible mechanisms and novel therapies
Guangyang Xie, Hongfu Jin, Herasimenka Mikhail, et al.
Biomedicine & Pharmacotherapy (2023) Vol. 165, pp. 115147-115147
Open Access | Times Cited: 24

Local membrane source gathering by p62 body drives autophagosome formation
Xuezhao Feng, Daxiao Sun, Yanchang Li, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 22

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