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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:

Phosphorylation of Nedd4-2 by Sgk1 regulates epithelial Na+ channel cell surface expression
Christophe Debonneville
The EMBO Journal (2001) Vol. 20, Iss. 24, pp. 7052-7059
Open Access | Times Cited: 706

Showing 1-25 of 706 citing articles:

The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction
Michael H. Glickman, Aaron Ciechanover
Physiological Reviews (2002) Vol. 82, Iss. 2, pp. 373-428
Closed Access | Times Cited: 4105
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
Regulation of Membrane Protein Transport by Ubiquitin and Ubiquitin-Binding Proteins
Linda Hicke, Rebecca Dunn
Annual Review of Cell and Developmental Biology (2003) Vol. 19, Iss. 1, pp. 141-172
Closed Access | Times Cited: 1104
Epithelial Sodium Channel/Degenerin Family of Ion Channels: A Variety of Functions for a Shared Structure
Stephan Kellenberger, Laurent Schild
Physiological Reviews (2002) Vol. 82, Iss. 3, pp. 735-767
Closed Access | Times Cited: 1019
Physiological functions of the HECT family of ubiquitin ligases
Daniela Rotin, Sharad Kumar
Nature Reviews Molecular Cell Biology (2009) Vol. 10, Iss. 6, pp. 398-409
Closed Access | Times Cited: 984
mTOR complex 2 (mTORC2) controls hydrophobic motif phosphorylation and activation of serum- and glucocorticoid-induced protein kinase 1 (SGK1)
Juan Manuel García‐Martínez, Dario R. Alessi
Biochemical Journal (2008) Vol. 416, Iss. 3, pp. 375-385
Open Access | Times Cited: 882
(Patho)physiological Significance of the Serum- and Glucocorticoid-Inducible Kinase Isoforms
Florian Läng, Christoph Böhmer, Mònica Palmada, et al.
Physiological Reviews (2006) Vol. 86, Iss. 4, pp. 1151-1178
Closed Access | Times Cited: 674
The Nedd4 family of E3 ubiquitin ligases: functional diversity within a common modular architecture
Robert J. Ingham, Gerald Gish, Tony Pawson
Oncogene (2004) Vol. 23, Iss. 11, pp. 1972-1984
Closed Access | Times Cited: 514
Chloride Sensing by WNK1 Involves Inhibition of Autophosphorylation
Alexander T. Piala, Thomas M. Moon, Radha Akella, et al.
Science Signaling (2014) Vol. 7, Iss. 324
Open Access | Times Cited: 370
Ubiquitin Ligase Nedd4L Targets Activated Smad2/3 to Limit TGF-β Signaling
Sheng Gao, Claudio R. Alarcón, Gopal P. Sapkota, et al.
Molecular Cell (2009) Vol. 36, Iss. 3, pp. 457-468
Open Access | Times Cited: 355
Ubiquitin and Membrane Protein Turnover: From Cradle to Grave
Jason A. MacGurn, Pi-Chiang Hsu, Scott D. Emr
Annual Review of Biochemistry (2012) Vol. 81, Iss. 1, pp. 231-259
Closed Access | Times Cited: 305
Crosstalk in Inflammation: The Interplay of Glucocorticoid Receptor-Based Mechanisms and Kinases and Phosphatases
Ilse M. Beck, Wim Vanden Berghe, Linda Vermeulen, et al.
Endocrine Reviews (2009) Vol. 30, Iss. 7, pp. 830-882
Open Access | Times Cited: 280
Ubiquitination of E3 ligases: self-regulation of the ubiquitin system via proteolytic and non-proteolytic mechanisms
P. de Bie, Aaron Ciechanover
Cell Death and Differentiation (2011) Vol. 18, Iss. 9, pp. 1393-1402
Open Access | Times Cited: 275
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
The Concise Guide to PHARMACOLOGY 2013/14: Ion Channels
S P H Alexander, Helen E. Benson, Elena Faccenda, et al.
British Journal of Pharmacology (2013) Vol. 170, Iss. 8, pp. 1607-1651
Open Access | Times Cited: 271
Collecting Duct Principal Cell Transport Processes and Their Regulation
David Pearce, Rama Soundararajan, Christiane Trimpert, et al.
Clinical Journal of the American Society of Nephrology (2014) Vol. 10, Iss. 1, pp. 135-146
Open Access | Times Cited: 268
Distal Convoluted Tubule
Arohan R. Subramanya, David H. Ellison
Clinical Journal of the American Society of Nephrology (2014) Vol. 9, Iss. 12, pp. 2147-2163
Open Access | Times Cited: 263
International Union of Basic and Clinical Pharmacology. XCI. Structure, Function, and Pharmacology of Acid-Sensing Ion Channels and the Epithelial Na+Channel
Stephan Kellenberger, Laurent Schild
Pharmacological Reviews (2014) Vol. 67, Iss. 1, pp. 1-35
Open Access | Times Cited: 260
Structural Organization of the Mammalian Kidney
Wilhelm Kriz, Brigitte Kaissling
Elsevier eBooks (2012), pp. 595-691
Closed Access | Times Cited: 219
Growth Hormone, Insulin-Like Growth Factor-1, and the Kidney: Pathophysiological and Clinical Implications
Peter Kamenický, Gherardo Mazziotti, Marc Lombès, et al.
Endocrine Reviews (2013) Vol. 35, Iss. 2, pp. 234-281
Open Access | Times Cited: 204
Impaired renal Na+ retention in the sgk1-knockout mouse
Peer Wulff, Volker Vallon, Dan Huang, et al.
Journal of Clinical Investigation (2002) Vol. 110, Iss. 9, pp. 1263-1268
Open Access | Times Cited: 355
Exploitation of KESTREL to identify NDRG family members as physiological substrates for SGK1 and GSK3
James T. Murray, David G. CAMPBELL, Nicholas A. Morrice, et al.
Biochemical Journal (2004) Vol. 384, Iss. 3, pp. 477-488
Open Access | Times Cited: 343
The Mineralocorticoid Receptor: Insights into its Molecular and (Patho)Physiological Biology
Say Viengchareun, Damien Le Menuet, Lætitia Martinerie, et al.
Nuclear Receptor Signaling (2007) Vol. 5, Iss. 1, pp. nrs.05012-nrs.05012
Open Access | Times Cited: 293
Impaired renal Na+ retention in the sgk1-knockout mouse
Peer Wulff, Volker Vallon, Dan Huang, et al.
Journal of Clinical Investigation (2002) Vol. 110, Iss. 9, pp. 1263-1268
Open Access | Times Cited: 273
Activation of the E3 ubiquitin ligase Itch through a phosphorylation-induced conformational change
Ewen Gallagher, Min Gao, Yun‐Cai Liu, et al.
Proceedings of the National Academy of Sciences (2006) Vol. 103, Iss. 6, pp. 1717-1722
Open Access | Times Cited: 269
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