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:

Diverse Cellular Roles of Autophagy
Hideaki Morishita, Noboru Mizushima
Annual Review of Cell and Developmental Biology (2019) Vol. 35, Iss. 1, pp. 453-475
Open Access | Times Cited: 321

Showing 1-25 of 321 citing articles:

Alzheimer disease
David S. Knopman, Hélène Amieva, Ronald C. Petersen, et al.
Nature Reviews Disease Primers (2021) Vol. 7, Iss. 1
Open Access | Times Cited: 1503

Autophagy in major human diseases
Daniel J. Klionsky, Giulia Petroni, Ravi K. Amaravadi, et al.
The EMBO Journal (2021) Vol. 40, Iss. 19
Open Access | Times Cited: 1083

Autophagy, ferroptosis, pyroptosis, and necroptosis in tumor immunotherapy
Weitong Gao, Yuqin Wang, Yang Zhou, et al.
Signal Transduction and Targeted Therapy (2022) Vol. 7, Iss. 1
Open Access | Times Cited: 600

Autophagy in inflammation, infection, and immunometabolism
Vojo Deretić
Immunity (2021) Vol. 54, Iss. 3, pp. 437-453
Open Access | Times Cited: 576

Autophagy in kidney homeostasis and disease
Chengyuan Tang, Man J. Livingston, Zhiwen Liu, et al.
Nature Reviews Nephrology (2020) Vol. 16, Iss. 9, pp. 489-508
Open Access | Times Cited: 366

Atg9 is a lipid scramblase that mediates autophagosomal membrane expansion
Kazuaki Matoba, Tetsuya Kotani, Akihisa Tsutsumi, et al.
Nature Structural & Molecular Biology (2020) Vol. 27, Iss. 12, pp. 1185-1193
Closed Access | Times Cited: 345

Autophagy in tumour immunity and therapy
Houjun Xia, Douglas R. Green, Weiping Zou
Nature reviews. Cancer (2021) Vol. 21, Iss. 5, pp. 281-297
Open Access | Times Cited: 288

Microautophagy – distinct molecular mechanisms handle cargoes of many sizes
Sebastian Schuck
Journal of Cell Science (2020) Vol. 133, Iss. 17
Open Access | Times Cited: 268

Molecular pathways of major depressive disorder converge on the synapse
Gabriel R. Fries, Valeria Saldana, Johannes Finnstein, et al.
Molecular Psychiatry (2022) Vol. 28, Iss. 1, pp. 284-297
Open Access | Times Cited: 241

Emerging roles of ATG proteins and membrane lipids in autophagosome formation
Taki Nishimura, Sharon A. Tooze
Cell Discovery (2020) Vol. 6, Iss. 1
Open Access | Times Cited: 218

Autophagy and the hallmarks of aging
Susmita Kaushik, Inmaculada Tasset, Esperanza Arias, et al.
Ageing Research Reviews (2021) Vol. 72, pp. 101468-101468
Open Access | Times Cited: 201

Ferroptosis-driven nanotherapeutics for cancer treatment
Xinzhu Shan, Shumeng Li, Bingjun Sun, et al.
Journal of Controlled Release (2020) Vol. 319, pp. 322-332
Closed Access | Times Cited: 175

Critical role of mitochondrial ubiquitination and the OPTN–ATG9A axis in mitophagy
Koji Yamano, Reika Kikuchi, Waka Kojima, et al.
The Journal of Cell Biology (2020) Vol. 219, Iss. 9
Open Access | Times Cited: 156

STING induces LC3B lipidation onto single-membrane vesicles via the V-ATPase and ATG16L1-WD40 domain
Tara D. Fischer, Chunxin Wang, Benjamin Scott Padman, et al.
The Journal of Cell Biology (2020) Vol. 219, Iss. 12
Open Access | Times Cited: 149

Macroautophagy in CNS health and disease
Christopher J. Griffey, Ai Yamamoto
Nature reviews. Neuroscience (2022) Vol. 23, Iss. 7, pp. 411-427
Open Access | Times Cited: 91

ATG9A and ATG2A form a heteromeric complex essential for autophagosome formation
Alexander R. van Vliet, George N. Chiduza, Sarah Maslen, et al.
Molecular Cell (2022) Vol. 82, Iss. 22, pp. 4324-4339.e8
Open Access | Times Cited: 91

ER ‐phagy: selective autophagy of the endoplasmic reticulum
Keisuke Mochida, Hitoshi Nakatogawa
EMBO Reports (2022) Vol. 23, Iss. 8
Open Access | Times Cited: 83

LC3B is an RNA-binding protein to trigger rapid mRNA degradation during autophagy
Hyun Jung Hwang, Hongseok Ha, Ban Seok Lee, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 78

Organelle transporters and inter-organelle communication as drivers of metabolic regulation and cellular homeostasis
Aakriti Jain, Roberto Zoncu
Molecular Metabolism (2022) Vol. 60, pp. 101481-101481
Open Access | Times Cited: 74

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

Stay in touch with the endoplasmic reticulum
Sha Sun, Zhao Gan, Mingkang Jia, et al.
Science China Life Sciences (2024) Vol. 67, Iss. 2, pp. 230-257
Open Access | Times Cited: 22

Three-step docking by WIPI2, ATG16L1, and ATG3 delivers LC3 to the phagophore
Shanlin Rao, Marvin Skulsuppaisarn, Lisa Strong, et al.
Science Advances (2024) Vol. 10, Iss. 6
Open Access | Times Cited: 19

The STX17-SNAP47-VAMP7/VAMP8 complex is the default SNARE complex mediating autophagosome–lysosome fusion
Fenglei Jian, Shen Wang, Rui Tian, et al.
Cell Research (2024) Vol. 34, Iss. 2, pp. 151-168
Closed Access | Times Cited: 18

ATG9A facilitates the closure of mammalian autophagosomes
Ruheena Javed, Muriel Mari, Einar S Trosdal, et al.
The Journal of Cell Biology (2025) Vol. 224, Iss. 2
Closed Access | Times Cited: 2

Noncanonical roles of ATG5 and membrane atg8ylation in retromer assembly and function
Masroor Ahmad Paddar, Fulong Wang, Einar S Trosdal, et al.
eLife (2025) Vol. 13
Open Access | Times Cited: 2

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