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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:

14-3-3-protein regulates Nedd4-2 by modulating interactions between HECT and WW domains
Pavel Pohl, Rohit Joshi, Olívia Petrvalská, et al.
Communications Biology (2021) Vol. 4, Iss. 1
Open Access | Times Cited: 33

Showing 1-25 of 33 citing articles:

Structural insights into the functional roles of 14-3-3 proteins
Veronika Obšilová, Tomáš Obšil
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 77
14‐3‐3 Protein‐Protein Interactions: From Mechanistic Understanding to Their Small‐Molecule Stabilization
B. Somsen, Peter J. Cossar, Michelle R. Arkin, et al.
ChemBioChem (2024) Vol. 25, Iss. 14
Open Access | Times Cited: 9
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: 33
ESR1 inhibits ionizing radiation-induced ferroptosis in breast cancer cells via the NEDD4L/CD71 pathway
Lin Liu, Chen Zhang, Shugen Qu, et al.
Archives of Biochemistry and Biophysics (2022) Vol. 725, pp. 109299-109299
Closed Access | Times Cited: 33
The Role of NEDD4 E3 Ubiquitin–Protein Ligases in Parkinson’s Disease
James A. Conway, Grant Kinsman, Edgar R. Kramer
Genes (2022) Vol. 13, Iss. 3, pp. 513-513
Open Access | Times Cited: 24
Recent advances in structural studies of 14-3-3 protein complexes
Nikolai N. Sluchanko
Advances in protein chemistry and structural biology (2022), pp. 289-324
Closed Access | Times Cited: 23
14-3-3σ-NEDD4L axis promotes ubiquitination and degradation of HIF-1α in colorectal cancer
Sicheng Liu, Rui Guo, Xu Hui, et al.
Cell Reports (2023) Vol. 42, Iss. 8, pp. 112870-112870
Open Access | Times Cited: 12
Unraveling the Potential Role of NEDD4-like E3 Ligases in Cancer
Sujitha Jayaprakash, Mangala Hegde, Bandari BharathwajChetty, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 20, pp. 12380-12380
Open Access | Times Cited: 19
MAGED2 Enhances Expression and Function of NCC at the Cell Surface via cAMP Signaling Under Hypoxia
Aline Radi, Sadiq Nasrah, Michael Auer, et al.
Cells (2025) Vol. 14, Iss. 3, pp. 175-175
Open Access
SGK1 negatively regulates inflammatory immune responses and protects against alveolar bone loss through modulation of TRAF3 activity
Xiao Han, Junling Ren, Hannah Lohner, et al.
Journal of Biological Chemistry (2022) Vol. 298, Iss. 6, pp. 102036-102036
Open Access | Times Cited: 16
Structural basis of ubiquitin ligase Nedd4-2 autoinhibition and regulation by calcium and 14-3-3 proteins
Masa Janosev, Dalibor Košek, Andrej Tekel, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Molecular basis and dual ligand regulation of tetrameric estrogen receptor α/14-3-3ζ protein complex
B. Somsen, Eline Sijbesma, S. Leysen, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 7, pp. 104855-104855
Open Access | Times Cited: 8
The dispensability of 14-3-3 proteins for the regulation of human cardiac sodium channel Nav1.5
Oksana Iamshanova, Anne-Flore Hämmerli, Elise Ramaye, et al.
PLoS ONE (2024) Vol. 19, Iss. 3, pp. e0298820-e0298820
Open Access | Times Cited: 2
NEDD4 and NEDD4L: Ubiquitin Ligases Closely Related to Digestive Diseases
Jiafan Xu, Jiang Wang, Tian Hu, et al.
Biomolecules (2024) Vol. 14, Iss. 5, pp. 577-577
Open Access | Times Cited: 2
Functional mapping of the 14-3-3 hub protein as a guide to design 14-3-3 molecular glues
B. Somsen, Fenna W. B. Craenmehr, Wei-Hong W. Liu, et al.
Chemical Science (2022) Vol. 13, Iss. 44, pp. 13122-13131
Open Access | Times Cited: 8
Nedd4-2 binding to 14-3-3 modulates the accessibility of its catalytic site and WW domains
Rohit Joshi, Pavel Pohl, Dita Strachotová, et al.
Biophysical Journal (2022) Vol. 121, Iss. 7, pp. 1299-1311
Open Access | Times Cited: 7
Fragment Screening Yields a Small‐Molecule Stabilizer of 14‐3‐3 Dimers That Modulates Client Protein Interactions
Hendrik J. Brink, Rick Riemens, Stephanie Thee, et al.
ChemBioChem (2022) Vol. 23, Iss. 17
Open Access | Times Cited: 7
Activation of E3 ubiquitin ligase WWP2 by non‐receptor tyrosine kinase ACK1
Jun Zhu, Ziluo Peng, Xianyan Tian, et al.
IUBMB Life (2023) Vol. 75, Iss. 7, pp. 595-608
Closed Access | Times Cited: 4
Site‐directed mutagenesis improves the practical application of L‐glutamic acid decarboxylase inEscherichia coli
Liu Feng-min, Heng Zhang, Xiangjun Zhang, et al.
Engineering in Life Sciences (2023) Vol. 23, Iss. 4
Open Access | Times Cited: 4
The yeast 14-3-3 proteins Bmh1 and Bmh2 regulate key signaling pathways
Veronika Obšilová, Tomáš Obšil
Frontiers in Molecular Biosciences (2024) Vol. 11
Open Access | Times Cited: 1
NEDD4L mediates ITGB4 ubiquitination and degradation to suppress esophageal carcinoma progression
Yijun Shi, Na Fang, Yutong Wu, et al.
Cell Communication and Signaling (2024) Vol. 22, Iss. 1
Open Access | Times Cited: 1
Look for the Scaffold: Multifaceted Regulation of Enzyme Activity by 14-3-3 Proteins
Veronika Obšilová, Tomáš Obšil
Physiological Research (2024), Iss. Suppl 1, pp. S401-S412
Open Access | Times Cited: 1
Contemporary biophysical approaches for studying 14-3-3 protein-protein interactions
Bethany Thurairajah, Andrew J. Hudson, Richard G. Doveston
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 6
The second intracellular loop of the yeast Trk1 potassium transporter is involved in regulation of activity, and interaction with 14–3-3 proteins
Jakub Masaryk, Deepika Kale, Pavel Pohl, et al.
Computational and Structural Biotechnology Journal (2023) Vol. 21, pp. 2705-2716
Open Access | Times Cited: 3
Regulation of the intestinal Na+/H+ exchanger NHE3 by AMP-activated kinase is dependent on phosphorylation of NHE3 at S555 and S563
Yiran Han, Pritha Bagchi, C. Chris Yun
AJP Cell Physiology (2023) Vol. 326, Iss. 1, pp. C50-C59
Closed Access | Times Cited: 3
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