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:

Linear ubiquitin chains: enzymes, mechanisms and biology
Katrin Rittinger, Fumiyo Ikeda
Open Biology (2017) Vol. 7, Iss. 4, pp. 170026-170026
Open Access | Times Cited: 94

Showing 1-25 of 94 citing articles:

RING-Between-RING E3 Ligases: Emerging Themes amid the Variations
Katja K. Dove, Rachel E. Klevit
Journal of Molecular Biology (2017) Vol. 429, Iss. 22, pp. 3363-3375
Open Access | Times Cited: 130

RBR ligase–mediated ubiquitin transfer: a tale with many twists and turns
Helen Walden, Katrin Rittinger
Nature Structural & Molecular Biology (2018) Vol. 25, Iss. 6, pp. 440-445
Closed Access | Times Cited: 129

Mitochondria at the interface between neurodegeneration and neuroinflammation
Verian Bader, Konstanze F. Winklhofer
Seminars in Cell and Developmental Biology (2019) Vol. 99, pp. 163-171
Closed Access | Times Cited: 113

Fragment-Based Covalent Ligand Screening Enables Rapid Discovery of Inhibitors for the RBR E3 Ubiquitin Ligase HOIP
Henrik Johansson, Yi‐Chun Isabella Tsai, Ken G. M. Fantom, et al.
Journal of the American Chemical Society (2019) Vol. 141, Iss. 6, pp. 2703-2712
Open Access | Times Cited: 111

The AAA+ ATPase p97, a cellular multitool
Lasse Stach, Paul S. Freemont
Biochemical Journal (2017) Vol. 474, Iss. 17, pp. 2953-2976
Open Access | Times Cited: 102

Linear Ubiquitin Chains: Cellular Functions and Strategies for Detection and Quantification
Gunnar Dittmar, Konstanze F. Winklhofer
Frontiers in Chemistry (2020) Vol. 7
Open Access | Times Cited: 87

A protein quality control pathway regulated by linear ubiquitination
Eva M. van Well, Verian Bader, Maria Patra, et al.
The EMBO Journal (2019) Vol. 38, Iss. 9
Open Access | Times Cited: 83

The Evolving Role of TRAFs in Mediating Inflammatory Responses
Bipandeep Dhillon, Fatemah Aleithan, Zahi Abdul‐Sater, et al.
Frontiers in Immunology (2019) Vol. 10
Open Access | Times Cited: 79

Non-lysine ubiquitylation: Doing things differently
Ian R. Kelsall
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 44

Chain reactions: molecular mechanisms of RBR ubiquitin ligases
Thomas R. Cotton, Bernhard C. Lechtenberg
Biochemical Society Transactions (2020) Vol. 48, Iss. 4, pp. 1737-1750
Open Access | Times Cited: 57

The linear ubiquitin chain assembly complex (LUBAC) generates heterotypic ubiquitin chains
Alan Rodriguez Carvajal, Irina Grishkovskaya, Carlos Gómez-Díaz, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 48

TNF receptor-associated factor 6 (TRAF6) plays crucial roles in multiple biological systems through polyubiquitination-mediated NF-κB activation
Mizuki Yamamoto, Jin Gohda, Taishin Akiyama, et al.
Proceedings of the Japan Academy Series B (2021) Vol. 97, Iss. 4, pp. 145-160
Open Access | Times Cited: 47

Atypical Ubiquitination and Parkinson’s Disease
О.А. Бунеева, A. E. Medvedev
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 7, pp. 3705-3705
Open Access | Times Cited: 34

Acetylation, Phosphorylation, Ubiquitination (Oh My!): Following Post-Translational Modifications on the Ubiquitin Road
Rachel E. Lacoursiere, Dania Hadi, Gary S. Shaw
Biomolecules (2022) Vol. 12, Iss. 3, pp. 467-467
Open Access | Times Cited: 32

The mechanism of linear ubiquitination in regulating cell death and correlative diseases
Liyuan Gao, Wei Zhang, Xiao Hui Shi, et al.
Cell Death and Disease (2023) Vol. 14, Iss. 10
Open Access | Times Cited: 19

NEMO reshapes the α-Synuclein aggregate interface and acts as an autophagy adapter by co-condensation with p62
Nikolas Furthmann, Verian Bader, Lena Angersbach, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 18

Roles of ubiquitin in autophagy and cell death
Carlos Gómez-Díaz, Fumiyo Ikeda
Seminars in Cell and Developmental Biology (2018) Vol. 93, pp. 125-135
Open Access | Times Cited: 54

An Update on Autoinflammatory Diseases: Relopathies
Annemarie Steiner, Cassandra R. Harapas, Seth L. Masters, et al.
Current Rheumatology Reports (2018) Vol. 20, Iss. 7
Closed Access | Times Cited: 52

Small-molecule inhibitors of linear ubiquitin chain assembly complex (LUBAC), HOIPINs, suppress NF-κB signaling
Ken Katsuya, Daisuke Oikawa, Kiyosei Iio, et al.
Biochemical and Biophysical Research Communications (2019) Vol. 509, Iss. 3, pp. 700-706
Closed Access | Times Cited: 51

Molecular bases for HOIPINs-mediated inhibition of LUBAC and innate immune responses
Daisuke Oikawa, Yusuke Sato, Fumiaki Ohtake, et al.
Communications Biology (2020) Vol. 3, Iss. 1
Open Access | Times Cited: 47

Bacterial DUBs: deubiquitination beyond the seven classes
Thomas Hermanns, Kay Hofmann
Biochemical Society Transactions (2019) Vol. 47, Iss. 6, pp. 1857-1866
Closed Access | Times Cited: 45

Linear Ubiquitin Code: Its Writer, Erasers, Decoders, Inhibitors, and Implications in Disorders
Daisuke Oikawa, Yusuke Sato, Hidefumi Ito, et al.
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 9, pp. 3381-3381
Open Access | Times Cited: 42

The ubiquitin ligation machinery in the defense against bacterial pathogens
Ishita Tripathi‐Giesgen, Christian Behrends, Arno F. Alpi
EMBO Reports (2021) Vol. 22, Iss. 11
Open Access | Times Cited: 40

Functions and Molecular Mechanisms of Deltex Family Ubiquitin E3 Ligases in Development and Disease
Lidong Wang, Xiaodan Sun, Jingni He, et al.
Frontiers in Cell and Developmental Biology (2021) Vol. 9
Open Access | Times Cited: 33

The Many Roles of Ubiquitin in NF-κB Signaling
Gilles Courtois, Marie‐Odile Fauvarque
Biomedicines (2018) Vol. 6, Iss. 2, pp. 43-43
Open Access | Times Cited: 44

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