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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:

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

Showing 1-25 of 45 citing articles:

Deubiquitinases: From mechanisms to their inhibition by small molecules
Sven M. Lange, Lee A. Armstrong, Yogesh Kulathu
Molecular Cell (2021) Vol. 82, Iss. 1, pp. 15-29
Open Access | Times Cited: 190
A family of bacterial Josephin-like deubiquitinases with an irreversible cleavage mode
Thomas Hermanns, Susanne Kolek, Matthias Uthoff, et al.
Molecular Cell (2025)
Open Access | Times Cited: 1
Pharmacological Modulation of Ubiquitin-Proteasome Pathways in Oncogenic Signaling
Anmol Sharma, Heena Khan, Thakur Gurjeet Singh, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 21, pp. 11971-11971
Open Access | Times Cited: 50
The Ubiquitination System within Bacterial Host–Pathogen Interactions
Vera Vozandychova, Pavla Stojková, Kamil Hercík, et al.
Microorganisms (2021) Vol. 9, Iss. 3, pp. 638-638
Open Access | Times Cited: 44
The Biochemistry of Cytoplasmic Incompatibility Caused by Endosymbiotic Bacteria
Hongli Chen, Mengwen Zhang, Mark Hochstrasser
Genes (2020) Vol. 11, Iss. 8, pp. 852-852
Open Access | Times Cited: 41
High-throughput matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry–based deubiquitylating enzyme assay for drug discovery
Virginia De Cesare, Jennifer L. Moran, Ryan Traynor, et al.
Nature Protocols (2020) Vol. 15, Iss. 12, pp. 4034-4057
Open Access | Times Cited: 40
Bacterial OTU deubiquitinases regulate substrate ubiquitination upon Legionella infection
Dong Hyuk Shin, Anshu Bhattacharya, Yi-Lin Cheng, et al.
eLife (2020) Vol. 9
Open Access | Times Cited: 40
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
Deubiquitinases in Neurodegeneration
Abudu I. Bello, Rituparna Goswami, Shelby L. Brown, et al.
Cells (2022) Vol. 11, Iss. 3, pp. 556-556
Open Access | Times Cited: 24
The Role of Deubiquitinases in Virus Replication and Host Innate Immune Response
Qinglin Zhang, Qizhen Jia, Wenying Gao, et al.
Frontiers in Microbiology (2022) Vol. 13
Open Access | Times Cited: 20
Staphylococcal SplA and SplB serine proteases target ubiquitin(-like) specific proteases
Felix L. Glinka, Ole Schmöker, Abhishek Singh, et al.
AMB Express (2025) Vol. 15, Iss. 1
Open Access
A cut above: Bacterial deubiquitinases with ubiquitin clippase activity
Mark Hochstrasser
Molecular Cell (2025) Vol. 85, Iss. 6, pp. 1048-1050
Closed Access
An evolutionary approach to systematic discovery of novel deubiquitinases, applied to Legionella
Thomas Hermanns, Ilka Woiwode, Ricardo Guerreiro, et al.
Life Science Alliance (2020) Vol. 3, Iss. 9, pp. e202000838-e202000838
Open Access | Times Cited: 24
Inhibition of papain-like protease PLpro blocks SARS-CoV-2 spread and promotes anti-viral immunity
Dong Hyuk Shin, Rukmini Mukherjee, Diana Grewe, et al.
Research Square (Research Square) (2020)
Open Access | Times Cited: 24
Post-translational Lysine Ac(et)ylation in Bacteria: A Biochemical, Structural, and Synthetic Biological Perspective
Michael Lammers
Frontiers in Microbiology (2021) Vol. 12
Open Access | Times Cited: 23
Ubiquitin-Dependent and Independent Proteasomal Degradation in Host-Pathogen Interactions
Wojciech Białek, James F. Collawn, Rafał Bartoszewski
Molecules (2023) Vol. 28, Iss. 18, pp. 6740-6740
Open Access | Times Cited: 8
Genetic Code Expansion Tools to Study Lysine Acylation
Petra Neumann‐Staubitz, Michael Lammers, Heinz Neumann
Advanced Biology (2021) Vol. 5, Iss. 12
Closed Access | Times Cited: 20
The unity of opposites: Strategic interplay between bacterial effectors to regulate cellular homeostasis
Shalini Iyer, Chittaranjan Das
Journal of Biological Chemistry (2021) Vol. 297, Iss. 6, pp. 101340-101340
Open Access | Times Cited: 19
Recent advances in understanding the role of proteostasis
Kanika Verma, Monika Verma, Aseem Chaphalkar, et al.
Faculty Reviews (2021) Vol. 10
Open Access | Times Cited: 16
Orientia tsutsugamushi OtDUB Is Expressed and Interacts with Adaptor Protein Complexes during Infection
Haley E. Adcox, Jason M. Berk, Mark Hochstrasser, et al.
Infection and Immunity (2022) Vol. 90, Iss. 12
Open Access | Times Cited: 11
Erasing marks: Functions of plant deubiquitylating enzymes in modulating the ubiquitin code
Karin Vogel, Erika Isono
The Plant Cell (2024) Vol. 36, Iss. 9, pp. 3057-3073
Closed Access | Times Cited: 2
Genetic Code Expansion Approaches to Decipher the Ubiquitin Code
Vera Wanka, Maximilian Fottner, Marko Cigler, et al.
Chemical Reviews (2024) Vol. 124, Iss. 20, pp. 11544-11584
Open Access | Times Cited: 2
A host E3 ubiquitin ligase regulates Salmonella virulence by targeting an SPI‐2 effector involved in SIF biogenesis
Kun Meng, Jin Yang, Juan Xue, et al.
mLife (2023) Vol. 2, Iss. 2, pp. 141-158
Open Access | Times Cited: 6
Self-stabilization mechanism encoded by a bacterial toxin facilitates reproductive parasitism
Toshiyuki Harumoto
Current Biology (2023) Vol. 33, Iss. 18, pp. 4021-4029.e6
Open Access | Times Cited: 6
Functional and structural diversity in deubiquitinases of the Chlamydia-like bacterium Simkania negevensis
Vanessa Boll, Thomas Hermanns, Matthias Uthoff, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 6
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