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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:

Computing the Pathogenicity of Alzheimer’s Disease Presenilin 1 Mutations
Ning Tang, Budheswar Dehury, Kasper P. Kepp
Journal of Chemical Information and Modeling (2019) Vol. 59, Iss. 2, pp. 858-870
Open Access | Times Cited: 21

Showing 21 citing articles:

The amyloid cascade hypothesis: an updated critical review
Kasper P. Kepp, Nikolaos K. Robakis, Poul Flemming Høilund‐Carlsen, et al.
Brain (2023) Vol. 146, Iss. 10, pp. 3969-3990
Open Access | Times Cited: 101
Contribution of the Presenilins in the cell biology, structure and function of γ-secretase
Abril Escamilla‐Ayala, Rosanne Wouters, Ragna Sannerud, et al.
Seminars in Cell and Developmental Biology (2020) Vol. 105, pp. 12-26
Open Access | Times Cited: 55
Cerebral microvascular endothelial glycocalyx damage, its implications on the blood–brain barrier and a possible contributor to cognitive impairment
Patrice Stoddart, Simon C. Satchell, Raina Ramnath
Brain Research (2022) Vol. 1780, pp. 147804-147804
Open Access | Times Cited: 22
β-amyloid: The known unknowns
Scott Ayton, Ashley I. Bush
Ageing Research Reviews (2020) Vol. 65, pp. 101212-101212
Closed Access | Times Cited: 37
Side-by-side comparison of Notch- and C83 binding to γ-secretase in a complete membrane model at physiological temperature
Budheswar Dehury, Ning Tang, Rukmankesh Mehra, et al.
RSC Advances (2020) Vol. 10, Iss. 52, pp. 31215-31232
Open Access | Times Cited: 29
Data set and fitting dependencies when estimating protein mutant stability: Toward simple, balanced, and interpretable models
Kristoffer T. Bæk, Kasper P. Kepp
Journal of Computational Chemistry (2022) Vol. 43, Iss. 8, pp. 504-518
Open Access | Times Cited: 17
Revisiting the Impact of Neurodegenerative Proteins in Epilepsy: Focus on Alpha-Synuclein, Beta-Amyloid, and Tau
Yam Nath Paudel, Efthalia Angelopoulou, Christina Piperi, et al.
Biology (2020) Vol. 9, Iss. 6, pp. 122-122
Open Access | Times Cited: 26
A computer-simulated mechanism of familial Alzheimer’s disease: Mutations enhance thermal dynamics and favor looser substrate-binding to γ-secretase
Budheswar Dehury, Arun Kumar Somavarapu, Kasper P. Kepp
Journal of Structural Biology (2020) Vol. 212, Iss. 3, pp. 107648-107648
Open Access | Times Cited: 22
Survival of the cheapest: how proteome cost minimization drives evolution
Kasper P. Kepp
Quarterly Reviews of Biophysics (2020) Vol. 53
Open Access | Times Cited: 14
Potential improvement of the thermal stability of sweet-tasting proteins by structural calculations
Ning Tang, Jiachen Liu, Yongqiang Cheng
Food Chemistry (2020) Vol. 345, pp. 128750-128750
Closed Access | Times Cited: 14
Computational analysis of Alzheimer-causing mutations in amyloid precursor protein and presenilin 1
Rukmankesh Mehra, Kasper P. Kepp
Archives of Biochemistry and Biophysics (2019) Vol. 678, pp. 108168-108168
Open Access | Times Cited: 14
Computing the Pathogenicity of Wilson’s Disease ATP7B Mutations: Implications for Disease Prevalence
Ning Tang, Thomas Damgaard Sandahl, Peter Ott, et al.
Journal of Chemical Information and Modeling (2019) Vol. 59, Iss. 12, pp. 5230-5243
Open Access | Times Cited: 11
Understanding familial Alzheimer's disease: The fit‐stay‐trim mechanism of γ‐secretase
Rukmankesh Mehra, Kasper P. Kepp
Wiley Interdisciplinary Reviews Computational Molecular Science (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 9
Active site geometry stabilization of a presenilin homolog by the lipid bilayer promotes intramembrane proteolysis
Lukas P. Feilen, Shuyu Chen, Akio Fukumori, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 5
Computational prediction and molecular mechanism of γ-secretase modulators
Rukmankesh Mehra, Kasper P. Kepp
European Journal of Pharmaceutical Sciences (2020) Vol. 157, pp. 105626-105626
Open Access | Times Cited: 7
Computational saturation mutagenesis to explore the effect of pathogenic mutations on extra-cellular domains of TREM2 associated with Alzheimer’s and Nasu-Hakola disease
Preety Sthutika Swain, Sunita Panda, Sanghamitra Pati, et al.
Journal of Molecular Modeling (2023) Vol. 29, Iss. 11
Closed Access | Times Cited: 2
An insight into Alzheimer’s disease and its on-setting novel genes
Jaanaky Vigneswaran, Sivaloganathan Anogh Muthukumar, Mohamed Shafras, et al.
The Egyptian Journal of Neurology Psychiatry and Neurosurgery (2021) Vol. 57, Iss. 1
Open Access | Times Cited: 5
Benchmarking Computational Methods for Estimating the Pathogenicity of Wilson’s Disease Mutations
Ning Tang, Thomas Damgaard Sandahl, Peter Ott, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2019)
Open Access | Times Cited: 2
Membrane dynamics of Notch-bound γ-secretase produces two distinct Notch conformations
Ning Tang, Budheswar Dehury, Kasper P. Kepp
bioRxiv (Cold Spring Harbor Laboratory) (2019)
Open Access | Times Cited: 1
Survival of the cheapest: How proteome cost minimization drives evolution
Kasper P. Kepp
arXiv (Cornell University) (2020)
Closed Access
Active site geometry stabilization of a presenilin homolog by the lipid bilayer promotes intramembrane proteolysis
Lukas P. Feilen, Shuyu Chen, Akio Fukumori, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access
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