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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:

Biological significance of co- and post-translational modifications of the yeast 26S proteasome
Hisashi Hirano, Yayoi Kimura, Ayuko Kimura
Journal of Proteomics (2015) Vol. 134, pp. 37-46
Closed Access | Times Cited: 61

Showing 1-25 of 61 citing articles:

Proteasomal and Autophagic Degradation Systems
Ivan Đikić
Annual Review of Biochemistry (2017) Vol. 86, Iss. 1, pp. 193-224
Open Access | Times Cited: 964
The life cycle of the 26S proteasome: from birth, through regulation and function, and onto its death
Ido Livneh, Victoria Cohen‐Kaplan, Chen Cohen-Rosenzweig, et al.
Cell Research (2016) Vol. 26, Iss. 8, pp. 869-885
Open Access | Times Cited: 293
Proteasome Inhibitor Drugs
Lloyd D. Fricker
The Annual Review of Pharmacology and Toxicology (2019) Vol. 60, Iss. 1, pp. 457-476
Open Access | Times Cited: 231
Dynamic Regulation of the 26S Proteasome: From Synthesis to Degradation
Richard S. Marshall, Richard D. Vierstra
Frontiers in Molecular Biosciences (2019) Vol. 6
Open Access | Times Cited: 194
The ubiquitin-proteasome system and autophagy: Coordinated and independent activities
Victoria Cohen‐Kaplan, Ido Livneh, Noa Avni, et al.
The International Journal of Biochemistry & Cell Biology (2016) Vol. 79, pp. 403-418
Closed Access | Times Cited: 157
Proteasomes and Several Aspects of Their Heterogeneity Relevant to Cancer
А. В. Морозов, В. Л. Карпов
Frontiers in Oncology (2019) Vol. 9
Open Access | Times Cited: 100
Structure, Dynamics and Function of the 26S Proteasome
Youdong Mao
Sub-cellular biochemistry/Subcellular biochemistry (2020), pp. 1-151
Open Access | Times Cited: 96
RETRACTED: Proteasome storage granules protect proteasomes from autophagic degradation upon carbon starvation
Richard S. Marshall, Richard D. Vierstra
eLife (2018) Vol. 7
Open Access | Times Cited: 91
The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges
Grazia R. Tundo, Diego Sbardella, Anna Maria Santoro, et al.
Pharmacology & Therapeutics (2020) Vol. 213, pp. 107579-107579
Open Access | Times Cited: 88
Control of protein degradation by N-terminal acetylation and the N-end rule pathway
Kha The Nguyen, Sang-Hyeon Mun, Chang Seok Lee, et al.
Experimental & Molecular Medicine (2018) Vol. 50, Iss. 7, pp. 1-8
Open Access | Times Cited: 87
Regulation of Proteasome Activity by (Post-)transcriptional Mechanisms
Suzan Kors, Karlijne W. Geijtenbeek, Eric A. Reits, et al.
Frontiers in Molecular Biosciences (2019) Vol. 6
Open Access | Times Cited: 84
Proteostatic regulation in neuronal compartments
Stefano L. Giandomenico, Beatriz Álvarez-Castelao, Erin M. Schuman
Trends in Neurosciences (2021) Vol. 45, Iss. 1, pp. 41-52
Open Access | Times Cited: 46
New trends in synthetic drugs and natural products targeting 20S proteasomes in cancers
Hind Atta, Nouran Alzahaby, Nadia Μ. Hamdy, et al.
Bioorganic Chemistry (2023) Vol. 133, pp. 106427-106427
Closed Access | Times Cited: 15
Biological consequences of structural and functional proteasome diversity
А. В. Морозов, В. Л. Карпов
Heliyon (2018) Vol. 4, Iss. 10, pp. e00894-e00894
Open Access | Times Cited: 46
Proteasome: a Nanomachinery of Creative Destruction
Anna A. Kudriaeva, Alexey A. Belogurov
Biochemistry (Moscow) (2019) Vol. 84, Iss. S1, pp. 159-192
Closed Access | Times Cited: 36
Molecular Basis for K63-Linked Ubiquitination Processes in Double-Strand DNA Break Repair: A Focus on Kinetics and Dynamics
Brian L. Lee, Anamika Singh, J. N. Mark Glover, et al.
Journal of Molecular Biology (2017) Vol. 429, Iss. 22, pp. 3409-3429
Open Access | Times Cited: 38
N-terminomics – its past and recent advancements
Prashant Kaushal, Cheolju Lee
Journal of Proteomics (2020) Vol. 233, pp. 104089-104089
Closed Access | Times Cited: 31
Lipids of Yeasts and Filamentous Fungi and Their Importance to Biotechnology
Volkmar Passoth, Bettina Müller
Grand challenges in biology and biotechnology (2025), pp. 163-227
Closed Access
Lipids of Yeasts and Filamentous Fungi and Their Importance for Biotechnology
Volkmar Passoth
Springer eBooks (2017), pp. 149-204
Closed Access | Times Cited: 31
Conformational switching in the coiled-coil domains of a proteasomal ATPase regulates substrate processing
Aaron Snoberger, Evan J. Brettrager, David M. Smith
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 31
Tuning the proteasome to brighten the end of the journey
Thibault Mayor, Michal Sharon, Michael H. Glickman
AJP Cell Physiology (2016) Vol. 311, Iss. 5, pp. C793-C804
Open Access | Times Cited: 29
Towards deciphering proteomes via the proteoform, protein speciation, moonlighting and protein code concepts
Peter R. Jungblut, Bernd Thiede, Hartmut Schlüter
Journal of Proteomics (2016) Vol. 134, pp. 1-4
Closed Access | Times Cited: 28
The Role and Regulation of Autophagy and the Proteasome During Aging and Senescence in Plants
Haojie Wang, Jos H. M. Schippers
Genes (2019) Vol. 10, Iss. 4, pp. 267-267
Open Access | Times Cited: 28
The Proteasome System in Health and Disease
Olivier Coux, Barbara A. Zieba, Silke Meiners
Advances in experimental medicine and biology (2020), pp. 55-100
Closed Access | Times Cited: 24
Selective microautophagy of proteasomes is initiated by ESCRT-0 and is promoted by proteasome ubiquitylation
Jianhui Li, Mark Hochstrasser
Journal of Cell Science (2022) Vol. 135, Iss. 4
Open Access | Times Cited: 16
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