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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:

Molecular Recognition of M1-Linked Ubiquitin Chains by Native and Phosphorylated UBAN Domains
Lina Herhaus, Henry van den Bedem, Sean Tang, et al.
Journal of Molecular Biology (2019) Vol. 431, Iss. 17, pp. 3146-3156
Open Access | Times Cited: 22

Showing 22 citing articles:

Receptor-interacting protein kinase 1 (RIPK1) as a therapeutic target
Lauren Mifflin, Dimitry Ofengeim, Junying Yuan
Nature Reviews Drug Discovery (2020) Vol. 19, Iss. 8, pp. 553-571
Open Access | Times Cited: 341
Mechanisms underlying ubiquitin-driven selective mitochondrial and bacterial autophagy
Ellen A. Goodall, Felix Kraus, J. Wade Harper
Molecular Cell (2022) Vol. 82, Iss. 8, pp. 1501-1513
Open Access | Times Cited: 76
TNIP1 inhibits selective autophagy via bipartite interaction with LC3/GABARAP and TAX1BP1
François Le Guerroué, Eric Bunker, William M. Rosencrans, et al.
Molecular Cell (2023) Vol. 83, Iss. 6, pp. 927-941.e8
Open Access | Times Cited: 23
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: 21
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
TBK1 phosphorylation activates LIR-dependent degradation of the inflammation repressor TNIP1
Jianwen Zhou, Nikoline Lander Rasmussen, Hallvard Lauritz Olsvik, et al.
The Journal of Cell Biology (2022) Vol. 222, Iss. 2
Open Access | Times Cited: 20
Conformational Analyses of the AHD1-UBAN Region of TNIP1 Highlight Key Amino Acids for Interaction with Ubiquitin
Michael L. Samulevich, Liam E. Carman, Rambon Shamilov, et al.
Biomolecules (2025) Vol. 15, Iss. 3, pp. 453-453
Open Access
LUBAC-mediated linear ubiquitination: a crucial regulator of immune signaling
Kazuhiro Iwaï
Proceedings of the Japan Academy Series B (2021) Vol. 97, Iss. 3, pp. 120-133
Open Access | Times Cited: 25
Old and New Concepts in Ubiquitin and NEDD8 Recognition
Elena Santonico
Biomolecules (2020) Vol. 10, Iss. 4, pp. 566-566
Open Access | Times Cited: 27
Biochemistry, Pathophysiology, and Regulation of Linear Ubiquitination: Intricate Regulation by Coordinated Functions of the Associated Ligase and Deubiquitinase
Yasuhiro Fuseya, Kazuhiro Iwaï
Cells (2021) Vol. 10, Iss. 10, pp. 2706-2706
Open Access | Times Cited: 18
ABIN1 is a signal‐induced autophagy receptor that attenuates NF‐κB activation by recognizing linear ubiquitin chains
Yutaka Shinkawa, Koshi Imami, Yasuhiro Fuseya, et al.
FEBS Letters (2022) Vol. 596, Iss. 9, pp. 1147-1164
Open Access | Times Cited: 11
The ‘dark matter’ of ubiquitin-mediated processes: opportunities and challenges in the identification of ubiquitin-binding domains
Elizabeth Radley, Joanna Long, Kevin C. Gough, et al.
Biochemical Society Transactions (2019) Vol. 47, Iss. 6, pp. 1949-1962
Closed Access | Times Cited: 17
Repressive Control of Keratinocyte Cytoplasmic Inflammatory Signaling
Liam E. Carman, Michael L. Samulevich, Brian J. Aneskievich
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 15, pp. 11943-11943
Open Access | Times Cited: 4
Investigating Protein-Protein Interactions of Autophagy-Involved TNIP1
Michael L. Samulevich, Liam E. Carman, Brian J. Aneskievich
Methods in molecular biology (2024)
Closed Access | Times Cited: 1
Structures, functions, and inhibitors of LUBAC and its related diseases
Shuo Ning, Lingling Luo, Beiming Yu, et al.
Journal of Leukocyte Biology (2022) Vol. 112, Iss. 4, pp. 799-811
Closed Access | Times Cited: 7
An atypical GABARAP binding module drives the pro-autophagic potential of the AML-associated NPM1c variant
Hannah Mende, Anshu Khatri, Carolin Lange, et al.
Cell Reports (2023) Vol. 42, Iss. 12, pp. 113484-113484
Open Access | Times Cited: 3
Mechanisms underlying linear ubiquitination and implications in tumorigenesis and drug discovery
Jack Li, Sijin Liu, Shitao Li
Cell Communication and Signaling (2023) Vol. 21, Iss. 1
Open Access | Times Cited: 3
The Anti-Inflammatory Protein TNIP1 Is Intrinsically Disordered with Structural Flexibility Contributed by Its AHD1-UBAN Domain
Rambon Shamilov, Olga Vinogradova, Brian J. Aneskievich
Biomolecules (2020) Vol. 10, Iss. 11, pp. 1531-1531
Open Access | Times Cited: 6
Structural and Biochemical Basis for Higher-Order Assembly between A20-Binding Inhibitor of NF-κB 1 (ABIN1) and M1-Linked Ubiquitins
Jhen‐Yi Hong, Su‐Chang Lin, Bai-Jiun Kuo, et al.
Journal of Molecular Biology (2021) Vol. 433, Iss. 18, pp. 167116-167116
Closed Access | Times Cited: 5
TNIP1 inhibits Mitophagy via interaction with FIP200 and TAX1BP1
François Le Guerroué, Achim Werner, Chunxin Wang, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 3
Characterization of interferon-stimulated gene 15 from Bostrychus sinensis: cloning, expression and functional analyses
Bin Shen, Jing Xu, Linjie Chen, et al.
Fish & Shellfish Immunology (2024) Vol. 154, pp. 109887-109887
Closed Access
TBK1 phosphorylation activates LIR-dependent degradation of the inflammation repressor TNIP1
Jianwen Zhou, Nikoline Lander Rasmussen, Hallvard Lauritz Olsvik, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 1
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