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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:

TEX264 Is an Endoplasmic Reticulum-Resident ATG8-Interacting Protein Critical for ER Remodeling during Nutrient Stress
Heeseon An, Alban Ordureau, João A. Paulo, et al.
Molecular Cell (2019) Vol. 74, Iss. 5, pp. 891-908.e10
Open Access | Times Cited: 250

Showing 1-25 of 250 citing articles:

Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)1
Daniel J. Klionsky, Amal Kamal Abdel‐Aziz, Sara Abdelfatah, et al.
Autophagy (2021) Vol. 17, Iss. 1, pp. 1-382
Open Access | Times Cited: 1992
Selective Autophagy: ATG8 Family Proteins, LIR Motifs and Cargo Receptors
Terje Johansen, Trond Lamark
Journal of Molecular Biology (2019) Vol. 432, Iss. 1, pp. 80-103
Open Access | Times Cited: 580
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: 580
A Diversity of Selective Autophagy Receptors Determines the Specificity of the Autophagy Pathway
Vladimir Kirkin, Vladimir V. Rogov
Molecular Cell (2019) Vol. 76, Iss. 2, pp. 268-285
Open Access | Times Cited: 460
TMTpro reagents: a set of isobaric labeling mass tags enables simultaneous proteome-wide measurements across 16 samples
Jiaming Li, Jonathan G. Van Vranken, Laura Pontano Vaites, et al.
Nature Methods (2020) Vol. 17, Iss. 4, pp. 399-404
Open Access | Times Cited: 394
Selective autophagy of intracellular organelles: Recent research advances
Wen Li, Pengcheng He, Yuge Huang, et al.
Theranostics (2020) Vol. 11, Iss. 1, pp. 222-256
Open Access | Times Cited: 344
Protein quality control in the secretory pathway
Zhihao Sun, Jeffrey L. Brodsky
The Journal of Cell Biology (2019) Vol. 218, Iss. 10, pp. 3171-3187
Open Access | Times Cited: 330
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: 325
Autophagy: Regulator of cell death
ShiZuo Liu, ShuaiJie Yao, Huan Yang, et al.
Cell Death and Disease (2023) Vol. 14, Iss. 10
Open Access | Times Cited: 313
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: 293
Mechanisms of Selective Autophagy
Trond Lamark, Terje Johansen
Annual Review of Cell and Developmental Biology (2021) Vol. 37, Iss. 1, pp. 143-169
Open Access | Times Cited: 285
A Genome-wide ER-phagy Screen Highlights Key Roles of Mitochondrial Metabolism and ER-Resident UFMylation
Jin Rui Liang, Emily Lingeman, Thao Luong, et al.
Cell (2020) Vol. 180, Iss. 6, pp. 1160-1177.e20
Open Access | Times Cited: 237
ER-Phagy: Quality Control and Turnover of Endoplasmic Reticulum
Haruka Chino, Noboru Mizushima
Trends in Cell Biology (2020) Vol. 30, Iss. 5, pp. 384-398
Open Access | Times Cited: 227
A cross-kingdom conserved ER-phagy receptor maintains endoplasmic reticulum homeostasis during stress
Madlen Stephani, Lorenzo Picchianti, Alexander Gajic, et al.
eLife (2020) Vol. 9
Open Access | Times Cited: 197
New insights regarding SNARE proteins in autophagosome-lysosome fusion
Xiaoyu Tian, Junlin Teng, Jianguo Chen
Autophagy (2020) Vol. 17, Iss. 10, pp. 2680-2688
Open Access | Times Cited: 158
A guide to the regulation of selective autophagy receptors
Andrea Gubaš, Ivan Ðikić
FEBS Journal (2021) Vol. 289, Iss. 1, pp. 75-89
Open Access | Times Cited: 158
Autophagy and organelle homeostasis in cancer
Dannah Miller, Andrew Thorburn
Developmental Cell (2021) Vol. 56, Iss. 7, pp. 906-918
Open Access | Times Cited: 155
Autophagy Assays for Biological Discovery and Therapeutic Development
Noboru Mizushima, Leon O. Murphy
Trends in Biochemical Sciences (2020) Vol. 45, Iss. 12, pp. 1080-1093
Open Access | Times Cited: 149
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: 113
ER-Phagy, ER Homeostasis, and ER Quality Control: Implications for Disease
Susan Ferro‐Novick, Fulvio Reggiori, Jeffrey L. Brodsky
Trends in Biochemical Sciences (2021) Vol. 46, Iss. 8, pp. 630-639
Open Access | Times Cited: 112
A proteome-wide atlas of drug mechanism of action
Dylan C. Mitchell, Miljan Kuljanin, Jiaming Li, et al.
Nature Biotechnology (2023) Vol. 41, Iss. 6, pp. 845-857
Closed Access | Times Cited: 89
ER remodeling via ER-phagy
Andrea Gubaš, Ivan Ðikić
Molecular Cell (2022) Vol. 82, Iss. 8, pp. 1492-1500
Open Access | Times Cited: 84
ER ‐phagy: selective autophagy of the endoplasmic reticulum
Keisuke Mochida, Hitoshi Nakatogawa
EMBO Reports (2022) Vol. 23, Iss. 8
Open Access | Times Cited: 83
Brain-derived autophagosome profiling reveals the engulfment of nucleoid-enriched mitochondrial fragments by basal autophagy in neurons
Juliet Goldsmith, Alban Ordureau, J. Wade Harper, et al.
Neuron (2022) Vol. 110, Iss. 6, pp. 967-976.e8
Open Access | Times Cited: 81
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