Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

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

Showing 24 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
Exploring the Versatility of the Covalent Thiol–Alkyne Reaction with Substituted Propargyl Warheads: A Deciding Role for the Cysteine Protease
Elma Mons, Robbert Q. Kim, Bjorn R. van Doodewaerd, et al.
Journal of the American Chemical Society (2021) Vol. 143, Iss. 17, pp. 6423-6433
Open Access | Times Cited: 53
The Legionella pneumophila Dot/Icm type IV secretion system and its effectors
Daniel C. Lockwood, Himani Amin, Tiago R. D. Costa, et al.
Microbiology (2022) Vol. 168, Iss. 5
Open Access | Times Cited: 31
Ubiquitin‐targeted bacterial effectors: rule breakers of the ubiquitin system
Cameron G. Roberts, Tyler G. Franklin, Jonathan N. Pruneda
The EMBO Journal (2023) Vol. 42, Iss. 18
Open Access | Times Cited: 19
Exploitation of the Host Ubiquitin System: Means by Legionella pneumophila
Jingjing Luo, Lidong Wang, Lei Song, et al.
Frontiers in Microbiology (2021) Vol. 12
Open Access | Times Cited: 27
Mechanism of Lys6 poly-ubiquitin specificity by the L. pneumophila deubiquitinase LotA
Gus D. Warren, Tomoe Kitao, Tyler G. Franklin, et al.
Molecular Cell (2022) Vol. 83, Iss. 1, pp. 105-120.e5
Open Access | Times Cited: 19
Mitofusin 2 displays fusion-independent roles in proteostasis surveillance
Mariana Joaquim, Selver Altin, Maria-Bianca Bulimaga, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
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
Mitochondria, mitophagy, and the role of deubiquitinases as novel therapeutic targets in liver pathology
Elham Aryapour, Thomas Kietzmann
Journal of Cellular Biochemistry (2022) Vol. 123, Iss. 10, pp. 1634-1646
Open Access | Times Cited: 15
A widely distributed family of eukaryotic and bacterial deubiquitinases related to herpesviral large tegument proteins
Ilka Erven, Elena Theres Abraham, Thomas Hermanns, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 15
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
A structural basis for the diverse linkage specificities within the ZUFSP deubiquitinase family
Thomas Hermanns, C. Pichlo, Ulrich Baumann, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 13
Deubiquitinating Enzyme USP7 Is Required for Self-Renewal and Multipotency of Human Bone Marrow-Derived Mesenchymal Stromal Cells
You Ji Kim, Kwang Hwan Park, Kyoungmi Lee, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 15, pp. 8674-8674
Open Access | Times Cited: 10
The Coxiella burnetii effector EmcB is a deubiquitinase that inhibits RIG-I signaling
Jeffrey K. Duncan-Lowey, Emerson Crabill, Abigail Jarret, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 11
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
Bacterial usurpation of the OTU deubiquitinase fold
Jonathan N. Pruneda, Justine Nguyen, Hiroki Nagai, et al.
FEBS Journal (2023) Vol. 291, Iss. 15, pp. 3303-3316
Open Access | Times Cited: 2
Legionella longbeachae Regulates the Association of Polyubiquitinated Proteins on Bacterial Phagosome with Multiple Deubiquitinases
Yunjia Shi, Hongtao Liu, Kelong Ma, et al.
Microbiology Spectrum (2023) Vol. 11, Iss. 2
Open Access | Times Cited: 2
The structural basis for deubiquitination by the fingerless USP-type effector TssM
Thomas Hermanns, Matthias Uthoff, Ulrich Baumann, et al.
Life Science Alliance (2023) Vol. 7, Iss. 2, pp. e202302422-e202302422
Open Access | Times Cited: 2
Bioinformatical Approaches to the Discovery and Classification of Novel Deubiquitinases
Thomas Hermanns, Kay Hofmann
Methods in molecular biology (2022), pp. 135-149
Closed Access | Times Cited: 4
Global atlas of predicted functional domains in Legionella pneumophila Dot/Icm translocated effectors
D. Patel, P.J. Stogios, Lukasz Jaroszewski, et al.
Molecular Systems Biology (2024)
Closed Access
Mechanism of Lys6 poly-ubiquitin specificity by the L. pneumophila deubiquitinase LotA
Gus D. Warren, Tomoe Kitao, Tyler G. Franklin, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 2
The RPA complex orchestrates K63-linked deubiquitination via ZUP1
Benjamin M. Foster, Martin Attwood, Kay Y. Chong, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
Phylogenomics of Life Kingdom's Deubiquitinases
A. S. Evpak, Peter V. Evseev, Anna A. Kudriaeva, et al.
(2023), pp. 273-278
Closed Access
Page 1

Scroll to top