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:

A Mighty “Protein Extractor” of the Cell: Structure and Function of the p97/CDC48 ATPase
Yihong Ye, Wai Kwan Tang, Ting Zhang, et al.
Frontiers in Molecular Biosciences (2017) Vol. 4
Open Access | Times Cited: 177

Showing 1-25 of 177 citing articles:

Proteomics of SARS-CoV-2-infected host cells reveals therapy targets
Denisa Bojková, Kevin Klann, Benjamin Koch, et al.
Nature (2020) Vol. 583, Iss. 7816, pp. 469-472
Open Access | Times Cited: 1039

Structure and Function of the 26S Proteasome
Jared A.M. Bard, Ellen A. Goodall, Eric R. Greene, et al.
Annual Review of Biochemistry (2018) Vol. 87, Iss. 1, pp. 697-724
Open Access | Times Cited: 677

VCP/p97-Mediated Unfolding as a Principle in Protein Homeostasis and Signaling
Johannes van den Boom, Hemmo Meyer
Molecular Cell (2017) Vol. 69, Iss. 2, pp. 182-194
Open Access | Times Cited: 347

Ubiquitination of G3BP1 mediates stress granule disassembly in a context-specific manner
Youngdae Gwon, Brian A. Maxwell, Regina‐Maria Kolaitis, et al.
Science (2021) Vol. 372, Iss. 6549
Open Access | Times Cited: 240

NMR spectroscopy captures the essential role of dynamics in regulating biomolecular function
T. Reid Alderson, Lewis E. Kay
Cell (2021) Vol. 184, Iss. 3, pp. 577-595
Closed Access | Times Cited: 160

Structure of the Cdc48 segregase in the act of unfolding an authentic substrate
Ian Cooney, Han Han, Michael G. Stewart, et al.
Science (2019) Vol. 365, Iss. 6452, pp. 502-505
Open Access | Times Cited: 159

ELM—the Eukaryotic Linear Motif resource—2024 update
Manjeet Kumar, Sushama Michael, Jesús Alvarado-Valverde, et al.
Nucleic Acids Research (2023) Vol. 52, Iss. D1, pp. D442-D455
Open Access | Times Cited: 52

Autophagy, aging, and age-related neurodegeneration
Jennifer E. Palmer, Niall Wilson, Sung Min Son, et al.
Neuron (2024)
Open Access | Times Cited: 20

Ubiquitin-dependent chloroplast-associated protein degradation in plants
Qihua Ling, William J. Broad, Raphael Trösch, et al.
Science (2019) Vol. 363, Iss. 6429
Open Access | Times Cited: 136

The Cdc48 unfoldase prepares well-folded protein substrates for degradation by the 26S proteasome
Michal M. Olszewski, Cameron B. Williams, Ken C. Dong, et al.
Communications Biology (2019) Vol. 2, Iss. 1
Open Access | Times Cited: 122

Detection and Degradation of Stalled Nascent Chains via Ribosome-Associated Quality Control
Cole S. Sitron, Onn Brandman
Annual Review of Biochemistry (2020) Vol. 89, Iss. 1, pp. 417-442
Open Access | Times Cited: 87

Mechanistic insight into substrate processing and allosteric inhibition of human p97
Man Pan, Yuanyuan Yu, Huasong Ai, et al.
Nature Structural & Molecular Biology (2021) Vol. 28, Iss. 7, pp. 614-625
Open Access | Times Cited: 75

The CYTOLD and ERTOLD pathways for lipid droplet–protein targeting
Maria-Jesus Olarte, Jessica M. J. Swanson, Tobias C. Walther, et al.
Trends in Biochemical Sciences (2021) Vol. 47, Iss. 1, pp. 39-51
Open Access | Times Cited: 64

Valosin-Containing Protein (VCP)/p97: A Prognostic Biomarker and Therapeutic Target in Cancer
Susan Costantini, Francesca Capone, Andrea Polo, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 18, pp. 10177-10177
Open Access | Times Cited: 60

Out of Control: The Role of the Ubiquitin Proteasome System in Skeletal Muscle during Inflammation
Stefanie Haberecht-Müller, Elke Krüger, Jens Fielitz
Biomolecules (2021) Vol. 11, Iss. 9, pp. 1327-1327
Open Access | Times Cited: 59

Mechanisms and regulation of substrate degradation by the 26S proteasome
Connor Arkinson, Ken C. Dong, Christine L. Gee, et al.
Nature Reviews Molecular Cell Biology (2024)
Closed Access | Times Cited: 10

Ubiquitin-Independent Disassembly by a p97 AAA-ATPase Complex Drives PP1 Holoenzyme Formation
Matthias Weith, Jonas Seiler, Johannes van den Boom, et al.
Molecular Cell (2018) Vol. 72, Iss. 4, pp. 766-777.e6
Open Access | Times Cited: 79

Clinical PARP inhibitors do not abrogate PARP1 exchange at DNA damage sites in vivo
Zhengping Shao, Brian J. Lee, Élise Rouleau-Turcotte, et al.
Nucleic Acids Research (2020) Vol. 48, Iss. 17, pp. 9694-9709
Open Access | Times Cited: 69

Proteasome Inhibitors: Harnessing Proteostasis to Combat Disease
David J. Sherman, Jing Li
Molecules (2020) Vol. 25, Iss. 3, pp. 671-671
Open Access | Times Cited: 64

Determinants of Endoplasmic Reticulum-to-Lipid Droplet Protein Targeting
Maria-Jesus Olarte, Siyoung Kim, Morris E. Sharp, et al.
Developmental Cell (2020) Vol. 54, Iss. 4, pp. 471-487.e7
Open Access | Times Cited: 61

Disposing of misfolded ER proteins: A troubled substrate's way out of the ER
Christina Oikonomou, Linda M. Hendershot
Molecular and Cellular Endocrinology (2019) Vol. 500, pp. 110630-110630
Open Access | Times Cited: 60

Protein translocation by the SecA ATPase occurs by a power‐stroke mechanism
Marco A. Catipovic, Benedikt Bauer, Joseph J. Loparo, et al.
The EMBO Journal (2019) Vol. 38, Iss. 9
Open Access | Times Cited: 58

Coupling of translation quality control and mRNA targeting to stress granules
Stephanie L. Moon, Tatsuya Morisaki, Timothy J. Stasevich, et al.
The Journal of Cell Biology (2020) Vol. 219, Iss. 8
Open Access | Times Cited: 55

A protein quality control pathway at the mitochondrial outer membrane
Meredith B. Metzger, Jessica L. Scales, Mitchell Dunklebarger, et al.
eLife (2020) Vol. 9
Open Access | Times Cited: 51

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