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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:

Pharmacological chaperoning: A primer on mechanism and pharmacology
Nancy J. Leidenheimer, Katelyn G. Ryder
Pharmacological Research (2014) Vol. 83, pp. 10-19
Open Access | Times Cited: 90

Showing 1-25 of 90 citing articles:

Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis
Justin T. Marinko, Hui Huang, Wesley D. Penn, et al.
Chemical Reviews (2019) Vol. 119, Iss. 9, pp. 5537-5606
Open Access | Times Cited: 226
Pharmacological Chaperones: Design and Development of New Therapeutic Strategies for the Treatment of Conformational Diseases
Marino Convertino, Jhuma Das, Nikolay V. Dokholyan
ACS Chemical Biology (2016) Vol. 11, Iss. 6, pp. 1471-1489
Closed Access | Times Cited: 99
Protein aggregation and therapeutic strategies in SOD1- and TDP-43- linked ALS
Maria Tsekrekou, Μαρία Γιαννάκου, Katerina Papanikolopoulou, et al.
Frontiers in Molecular Biosciences (2024) Vol. 11
Open Access | Times Cited: 13
A novel epileptic encephalopathy mutation in KCNB1 disrupts Kv2.1 ion selectivity, expression, and localization
Isabelle Thiffault, David J. Speca, Daniel C. Austin, et al.
The Journal of General Physiology (2015) Vol. 146, Iss. 5, pp. 399-410
Open Access | Times Cited: 86
Tuning protein folding in lysosomal storage diseases: the chemistry behind pharmacological chaperones
David M. Pereira, Patrı́cia Valentão, Paula B. Andrade
Chemical Science (2018) Vol. 9, Iss. 7, pp. 1740-1752
Open Access | Times Cited: 79
How genetic errors in GPCRs affect their function: Possible therapeutic strategies
Henriette Stoy, Vsevolod V. Gurevich
Genes & Diseases (2015) Vol. 2, Iss. 2, pp. 108-132
Open Access | Times Cited: 69
Tyrosine and tryptophan hydroxylases as therapeutic targets in human disease
Kai Waløen, Rune Kleppe, Aurora Martı́nez, et al.
Expert Opinion on Therapeutic Targets (2016) Vol. 21, Iss. 2, pp. 167-180
Open Access | Times Cited: 69
Current and potential new treatment strategies for creatine deficiency syndromes
Gabriella Fernandes‐Pires, Olivier Braissant
Molecular Genetics and Metabolism (2021) Vol. 135, Iss. 1, pp. 15-26
Open Access | Times Cited: 42
Disulfide Mispairing During Proinsulin Folding in the Endoplasmic Reticulum
Leena Haataja, Nandini Manickam, Ann Soliman, et al.
Diabetes (2016) Vol. 65, Iss. 4, pp. 1050-1060
Open Access | Times Cited: 59
Protein misfolding diseases: Prospects of pharmacological treatment
Alejandra Gámez, Patricia Yuste‐Checa, Sandra Brasil, et al.
Clinical Genetics (2017) Vol. 93, Iss. 3, pp. 450-458
Open Access | Times Cited: 53
Pharmacological Correction of Trafficking Defects in ATP-sensitive Potassium Channels Caused by Sulfonylurea Receptor 1 Mutations
Gregory Martin, Emily A. Rex, Prasanna K. Devaraneni, et al.
Journal of Biological Chemistry (2016) Vol. 291, Iss. 42, pp. 21971-21983
Open Access | Times Cited: 48
Protein Misfolding Diseases and Therapeutic Approaches
Kusum Yadav, Anurag Yadav, Priyanka Vashistha, et al.
Current Protein and Peptide Science (2019) Vol. 20, Iss. 12, pp. 1226-1245
Closed Access | Times Cited: 46
KATP channel mutations in congenital hyperinsulinism: Progress and challenges towards mechanism-based therapies
Assmaa ElSheikh, Show‐Ling Shyng
Frontiers in Endocrinology (2023) Vol. 14
Open Access | Times Cited: 15
Non-radioactive Rb+ Efflux Assay for Screening KATP Channel Modulators
Assmaa ElSheikh, Camden Driggers, Show‐Ling Shyng
Methods in molecular biology (2024), pp. 191-210
Closed Access | Times Cited: 5
Azasugar inhibitors as pharmacological chaperones for Krabbe disease
Chris H. Hill, Agnete H. Viuff, Samantha J. Spratley, et al.
Chemical Science (2015) Vol. 6, Iss. 5, pp. 3075-3086
Open Access | Times Cited: 47
Folding, misfolding, and regulation of intracellular traffic of G protein‐coupled receptors involved in the hypothalamic–pituitary–gonadal axis
Alfredo Ulloa‐Aguirre, Ross C. Anderson, Teresa Zariñán, et al.
Andrology (2025)
Open Access
AI-Based Discovery and CryoEM Structural Elucidation of a KATP Channel Pharmacochaperone
Assmaa ElSheikh, Camden Driggers, Ha H. Truong, et al.
(2025)
Open Access
Pharmacological chaperones for the misfolded melanocortin-4 receptor associated with human obesity
Hui Huang, Wei Wang, Ya‐Xiong Tao
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (2017) Vol. 1863, Iss. 10, pp. 2496-2507
Closed Access | Times Cited: 39
L-type Calcium Channel Blockers Enhance Trafficking and Function of Epilepsy-associated α1(D219N) Subunits of GABAA Receptors
Dong-Yun Han, Bo-Jhih Guan, Yajuan Wang, et al.
ACS Chemical Biology (2015) Vol. 10, Iss. 9, pp. 2135-2148
Closed Access | Times Cited: 38
Proteostatic Tactics in the Strategy of Sterol Regulation
Margaret A. Wangeline, Nidhi Vashistha, Randolph Y. Hampton
Annual Review of Cell and Developmental Biology (2017) Vol. 33, Iss. 1, pp. 467-489
Open Access | Times Cited: 38
Conformational Response to Ligand Binding in Phosphomannomutase2
Giuseppina Andreotti, Israel Cabeza de Vaca, Angelita Poziello, et al.
Journal of Biological Chemistry (2014) Vol. 289, Iss. 50, pp. 34900-34910
Open Access | Times Cited: 37
Comparison of the -Adrenergic Receptor Antagonists Landiolol and Esmolol: Receptor Selectivity, Partial Agonism, and Pharmacochaperoning Actions
S. Nasrollahi Shirazi, Sonja Sučić, Qian Yang, et al.
Journal of Pharmacology and Experimental Therapeutics (2016) Vol. 359, Iss. 1, pp. 73-81
Open Access | Times Cited: 36
β-Glucose-1,6-Bisphosphate Stabilizes Pathological Phophomannomutase2 Mutants In Vitro and Represents a Lead Compound to Develop Pharmacological Chaperones for the Most Common Disorder of Glycosylation, PMM2-CDG
Maria Monticelli, Ludovica Liguori, Mariateresa Allocca, et al.
International Journal of Molecular Sciences (2019) Vol. 20, Iss. 17, pp. 4164-4164
Open Access | Times Cited: 35
Pharmacological chaperone approaches for rescuing GPCR mutants: Current state, challenges, and screening strategies
Pieter Beerepoot, Reza Nazari, Ali Salahpour
Pharmacological Research (2016) Vol. 117, pp. 242-251
Closed Access | Times Cited: 34
Pharmacoperone drugs: targeting misfolded proteins causing lysosomal storage-, ion channels-, and G protein-coupled receptors-associated conformational disorders
Zhi-Shuai Hou, Alfredo Ulloa‐Aguirre, Ya‐Xiong Tao
Expert Review of Clinical Pharmacology (2018) Vol. 11, Iss. 6, pp. 611-624
Closed Access | Times Cited: 34
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