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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:

Recruitment of the amyloid precursor protein by γ-secretase at the synaptic plasma membrane
Martina Audagnotto, Alexander Kengo Lorkowski, Matteo Dal Peraro
Biochemical and Biophysical Research Communications (2017) Vol. 498, Iss. 2, pp. 334-341
Open Access | Times Cited: 21

Showing 21 citing articles:

Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer’s Disease, Parkinson’s Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis
Phuong H. Nguyen, Ayyalusamy Ramamoorthy, Bikash R. Sahoo, et al.
Chemical Reviews (2021) Vol. 121, Iss. 4, pp. 2545-2647
Open Access | Times Cited: 538
Emerging Diversity in Lipid–Protein Interactions
Valentina Corradi, Besian I. Sejdiu, Haydeé Mesa‐Galloso, et al.
Chemical Reviews (2019) Vol. 119, Iss. 9, pp. 5775-5848
Open Access | Times Cited: 416
Involvement of Lipids in Alzheimer’s Disease Pathology and Potential Therapies
Hannah Chew, Victoria Solomon, Alfred N. Fonteh
Frontiers in Physiology (2020) Vol. 11
Open Access | Times Cited: 263
Cholesterol as a key player in amyloid β-mediated toxicity in Alzheimer’s disease
Vladimı́r Rudajev, Jiřı́ Novotný
Frontiers in Molecular Neuroscience (2022) Vol. 15
Open Access | Times Cited: 46
Cryo-temperature effects on membrane protein structure and dynamics
Rukmankesh Mehra, Budheswar Dehury, Kasper P. Kepp
Physical Chemistry Chemical Physics (2020) Vol. 22, Iss. 10, pp. 5427-5438
Open Access | Times Cited: 40
Therapeutics of Alzheimer’s Disease: Recent Developments
Scott Burns, Ashley Selman, Ujala Sehar, et al.
Antioxidants (2022) Vol. 11, Iss. 12, pp. 2402-2402
Open Access | Times Cited: 25
Cholesterol-dependent amyloid β production: space for multifarious interactions between amyloid precursor protein, secretases, and cholesterol
Vladimı́r Rudajev, Jiřı́ Novotný
Cell & Bioscience (2023) Vol. 13, Iss. 1
Open Access | Times Cited: 13
Modulating Hinge Flexibility in the APP Transmembrane Domain Alters γ-Secretase Cleavage
Alexander Götz, Nadine Mylonas, Philipp Högel, et al.
Biophysical Journal (2019) Vol. 116, Iss. 11, pp. 2103-2120
Open Access | Times Cited: 37
Influence of membrane lipid composition on the structure and activity of γ-secretase
Rodrigo Aguayo‐Ortiz, John E. Straub, Laura Domı́nguez
Physical Chemistry Chemical Physics (2018) Vol. 20, Iss. 43, pp. 27294-27304
Closed Access | Times Cited: 24
The dynamics of γ-secretase and its substrates
Manuel Hitzenberger, Alexander Götz, Simon Menig, et al.
Seminars in Cell and Developmental Biology (2020) Vol. 105, pp. 86-101
Closed Access | Times Cited: 22
Structural Analysis of the Simultaneous Activation and Inhibition of γ-Secretase Activity in the Development of Drugs for Alzheimer’s Disease
Željko M. Svedružić, Katarina Vrbnjak, Manuel Martinović, et al.
Pharmaceutics (2021) Vol. 13, Iss. 4, pp. 514-514
Open Access | Times Cited: 14
Simulating the γ-secretase enzyme: Recent advances and future directions
Rodrigo Aguayo‐Ortiz, Laura Domı́nguez
Biochimie (2018) Vol. 147, pp. 130-135
Closed Access | Times Cited: 14
The Binding of Different Substrate Molecules at the Docking Site and the Active Site of γ-Secretase Can Trigger Toxic Events in Sporadic and Familial Alzheimer’s Disease
Željko M. Svedružić, Vesna Šendula Jengić, Lucija Ostojić
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 3, pp. 1835-1835
Open Access | Times Cited: 4
Disruption of sphingomyelin synthase 2 gene alleviates cognitive impairment in a mouse model of Alzheimer’s disease
Osamu Uchiumi, Jingyu Zou, Sachiko Yamaki, et al.
Brain Research (2024) Vol. 1835, pp. 148934-148934
Closed Access | Times Cited: 1
Structure and function of the perivascular fluid compartment and vertebral venous plexus: Illumining a novel theory on mechanisms underlying the pathogenesis of Alzheimer's, cerebral small vessel, and neurodegenerative diseases
Michael George Zaki Ghali, Vitaliy Marchenko, M. Gazi Yaşargil, et al.
Neurobiology of Disease (2020) Vol. 144, pp. 105022-105022
Open Access | Times Cited: 10
Herpud1 deficiency could reduce amyloid-β40 expression and thereby suppress homocysteine-induced atherosclerosis by blocking the JNK/AP1 pathway
Feidan Gao, Jie Zhang, Tingjuan Ni, et al.
Journal of Physiology and Biochemistry (2020) Vol. 76, Iss. 3, pp. 383-391
Closed Access | Times Cited: 9
Binding of different substrate molecules at the docking site and the active site of γ-secretase can trigger toxic events in sporadic and familial Alzheimer’s disease
Željko M. Svedružić, Vesna Šendula Jengić, Lucija Ostojić
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 2
Multiscale modeling on biological systems
Marialore Sulpizi, Roland Faller, Sergio Pantano
Biochemical and Biophysical Research Communications (2018) Vol. 498, Iss. 2, pp. 263-263
Open Access | Times Cited: 2
Stabilization / destabilization of the APP transmembrane domain by mutations in the di-glycine hinge alter helical structure and dynamics, and impair cleavage by γ-secretase
Alexander Goetz, Nadine Mylonas, Philipp Hoegel, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2018), pp. 375006
Open Access | Times Cited: 2
Modulating hinge flexibility in the APP transmembrane domain alters γ-secretase cleavage
Alexander Götz, Nadine Mylonas, Philipp Högel, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2018)
Open Access | Times Cited: 2
Structural Analysis of Simultaneous Activation and Inhibition of γ-Secretase Activity in Development of Drugs for Alzheimer’s disease
Željko M. Svedružić, Katarina Vrbnjak, Manuel Martinović, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access
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