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:

Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination
Sagar Bhogaraju, Sissy Kalayil, Yaobin Liu, et al.
Cell (2016) Vol. 167, Iss. 6, pp. 1636-1649.e13
Open Access | Times Cited: 279

Showing 1-25 of 279 citing articles:

Ubiquitin Ligases: Structure, Function, and Regulation
Ning Zheng, Nitzan Shabek
Annual Review of Biochemistry (2017) Vol. 86, Iss. 1, pp. 129-157
Closed Access | Times Cited: 1203
The Ubiquitin Code in the Ubiquitin-Proteasome System and Autophagy
Yong Tae Kwon, Aaron Ciechanover
Trends in Biochemical Sciences (2017) Vol. 42, Iss. 11, pp. 873-886
Closed Access | Times Cited: 667
Ubiquitylation at the crossroads of development and disease
Michael Rapé
Nature Reviews Molecular Cell Biology (2017) Vol. 19, Iss. 1, pp. 59-70
Closed Access | Times Cited: 515
Full length RTN3 regulates turnover of tubular endoplasmic reticulum via selective autophagy
Paolo Grumati, Giulio Morozzi, Soraya Hölper, et al.
eLife (2017) Vol. 6
Open Access | Times Cited: 372
Rab family of small GTPases: an updated view on their regulation and functions
Yuta Homma, Shu Hiragi, Mitsunori Fukuda
FEBS Journal (2020) Vol. 288, Iss. 1, pp. 36-55
Open Access | Times Cited: 337
Principles of Ubiquitin-Dependent Signaling
Eugene Oh, David Akopian, Michael Rapé
Annual Review of Cell and Developmental Biology (2018) Vol. 34, Iss. 1, pp. 137-162
Closed Access | Times Cited: 295
Ubiquitin signaling and autophagy
Paolo Grumati, Ivan Đikić
Journal of Biological Chemistry (2017) Vol. 293, Iss. 15, pp. 5404-5413
Open Access | Times Cited: 285
Post-translational regulation of ubiquitin signaling
Lei Song, Zhao‐Qing Luo
The Journal of Cell Biology (2019) Vol. 218, Iss. 6, pp. 1776-1786
Open Access | Times Cited: 272
Legionella and Coxiella effectors: strength in diversity and activity
Jiazhang Qiu, Zhao‐Qing Luo
Nature Reviews Microbiology (2017) Vol. 15, Iss. 10, pp. 591-605
Closed Access | Times Cited: 247
ADP-Ribosylation, a Multifaceted Posttranslational Modification Involved in the Control of Cell Physiology in Health and Disease
Bernhard Lüscher, Mareike Bütepage, Laura Eckei, et al.
Chemical Reviews (2017) Vol. 118, Iss. 3, pp. 1092-1136
Closed Access | Times Cited: 223
An expanded lexicon for the ubiquitin code
Ivan Đikić, Brenda A. Schulman
Nature Reviews Molecular Cell Biology (2022) Vol. 24, Iss. 4, pp. 273-287
Open Access | Times Cited: 223
Legionnaires’ Disease: State of the Art Knowledge of Pathogenesis Mechanisms of Legionella
Sonia Mondino, Silke Schmidt, Monica Rolando, et al.
Annual Review of Pathology Mechanisms of Disease (2019) Vol. 15, Iss. 1, pp. 439-466
Open Access | Times Cited: 207
A Single Legionella Effector Catalyzes a Multistep Ubiquitination Pathway to Rearrange Tubular Endoplasmic Reticulum for Replication
Kristin M. Kotewicz, Vinay Ramabhadran, Nicole M. Sjoblom, et al.
Cell Host & Microbe (2016) Vol. 21, Iss. 2, pp. 169-181
Open Access | Times Cited: 187
(ADP-ribosyl)hydrolases: structure, function, and biology
J.G.M. Rack, Luca Palazzo, Ivan Ahel
Genes & Development (2020) Vol. 34, Iss. 5-6, pp. 263-284
Open Access | Times Cited: 157
Histone Ubiquitination: An Integrative Signaling Platform in Genome Stability
Francesca Mattiroli, Lorenza Penengo
Trends in Genetics (2021) Vol. 37, Iss. 6, pp. 566-581
Open Access | Times Cited: 155
ER remodeling via ER-phagy
Andrea Gubaš, Ivan Đikić
Molecular Cell (2022) Vol. 82, Iss. 8, pp. 1492-1500
Open Access | Times Cited: 82
ADP-ribosylation from molecular mechanisms to therapeutic implications
Marcin J. Suskiewicz, Evgeniia Prokhorova, J.G.M. Rack, et al.
Cell (2023) Vol. 186, Iss. 21, pp. 4475-4495
Open Access | Times Cited: 70
Ubiquitin—A structural perspective
Rashmi Agrata, David Komander
Molecular Cell (2025) Vol. 85, Iss. 2, pp. 323-346
Closed Access | Times Cited: 2
Ubiquitin is directly linked via an ester to protein-conjugated mono-ADP-ribose
Daniel S. Bejan, Rachel E. Lacoursiere, Jonathan N. Pruneda, et al.
The EMBO Journal (2025)
Open Access | Times Cited: 2
Bacterial pseudokinase catalyzes protein polyglutamylation to inhibit the SidE-family ubiquitin ligases
Miles H. Black, Adam Osinski, Marcin Gradowski, et al.
Science (2019) Vol. 364, Iss. 6442, pp. 787-792
Open Access | Times Cited: 134
ADP‐ribosylation: new facets of an ancient modification
Luca Palazzo, Andreja Mikoč, Ivan Ahel
FEBS Journal (2017) Vol. 284, Iss. 18, pp. 2932-2946
Open Access | Times Cited: 129
Ubiquitin enzymes in the regulation of immune responses
Petra Ebner, Gijs A. Versteeg, Fumiyo Ikeda
Critical Reviews in Biochemistry and Molecular Biology (2017) Vol. 52, Iss. 4, pp. 425-460
Open Access | Times Cited: 123
Regulation of Phosphoribosyl-Linked Serine Ubiquitination by Deubiquitinases DupA and DupB
Dong Hyuk Shin, Rukmini Mukherjee, Yaobin Liu, et al.
Molecular Cell (2019) Vol. 77, Iss. 1, pp. 164-179.e6
Open Access | Times Cited: 120
The ubiquitin–proteasome system in kidney physiology and disease
Catherine Meyer-Schwesinger
Nature Reviews Nephrology (2019) Vol. 15, Iss. 7, pp. 393-411
Closed Access | Times Cited: 118
Inhibition of bacterial ubiquitin ligases by SidJ–calmodulin catalysed glutamylation
Sagar Bhogaraju, Florian Bonn, Rukmini Mukherjee, et al.
Nature (2019) Vol. 572, Iss. 7769, pp. 382-386
Open Access | Times Cited: 117
Page 1 - Next Page

Scroll to top