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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:

A Hairpin Motif in the Amyloid-β Peptide Is Important for Formation of Disease-Related Oligomers
Mohammed Khaled, Isabel Rönnbäck, Leopold L. Ilag, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 33, pp. 18340-18354
Open Access | Times Cited: 36

Showing 1-25 of 36 citing articles:

A brief history of amyloid aggregation simulations
Hebah Fatafta, Mohammed Khaled, Batuhan Kav, et al.
Wiley Interdisciplinary Reviews Computational Molecular Science (2024) Vol. 14, Iss. 1
Closed Access | Times Cited: 9
Selective recognition and discrimination of single isomeric changes in peptide strands with a host : guest sensing array
Junyi Chen, Parisa Fasihianifard, Alexie Andrea P. Raz, et al.
Chemical Science (2024) Vol. 15, Iss. 5, pp. 1885-1893
Open Access | Times Cited: 8
Perspective for Molecular Dynamics Simulation Studies of Amyloid-β Aggregates
Hisashi Okumura
The Journal of Physical Chemistry B (2023) Vol. 127, Iss. 51, pp. 10931-10940
Closed Access | Times Cited: 13
Hairpin trimer transition state of amyloid fibril
Levent Sari, Sofia Bali, Łukasz A. Joachimiak, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 5
Precision proteoform design for 4R tau isoform selective templated aggregation
Andrew P. Longhini, Austin DuBose, Samuel Lobo, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 15
Open Access | Times Cited: 4
A turn for the worse: Aβ β-hairpins in Alzheimer’s disease
Sarah M. Ruttenberg, James S. Nowick
Bioorganic & Medicinal Chemistry (2024) Vol. 105, pp. 117715-117715
Open Access | Times Cited: 4
Structures prediction and replica exchange molecular dynamics simulations of α-synuclein: A case study for intrinsically disordered proteins
Orkid Coskuner‐Weber
International Journal of Biological Macromolecules (2024) Vol. 276, pp. 133813-133813
Closed Access | Times Cited: 4
Impact of Amidation on Aβ25–35 Aggregation
Judith C. E. Etaka, Yan Lü, Wei Kang, et al.
The Journal of Physical Chemistry B (2025)
Closed Access
Sampling Conformational Ensembles of Highly Dynamic Proteins via Generative Deep Learning
Talant Ruzmetov, Ta I Hung, Saisri Padmaja Jonnalagedda, et al.
Journal of Chemical Information and Modeling (2025)
Closed Access
Geometry based prediction of tau protein sites and motifs associated with misfolding and aggregation
Masumi Sugiyama, Kenneth S. Kosik, Eleni Panagiotou
Scientific Reports (2025) Vol. 15, Iss. 1
Open Access
Multi-target approach to Alzheimer’s disease prevention and treatment: antioxidant, anti-inflammatory, and amyloid- modulating mechanisms
Kashif Abbas, Mohd Rais Mustafa, Mudassir Alam, et al.
Neurogenetics (2025) Vol. 26, Iss. 1
Closed Access
Transition Metal Ion FRET-Based Probe to Study Cu(II)-Mediated Amyloid-β Ligand Binding
Ri Wu, Despoina Svingou, Jonas B. Metternich, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 3, pp. 2102-2112
Closed Access | Times Cited: 3
Peptide Self-Assembly into Amyloid Fibrils: Unbiased All-Atom Simulations
Bradley L. Nilsson, Gizem Çelebi Torabfam, Cristiano L. Dias
The Journal of Physical Chemistry B (2024) Vol. 128, Iss. 14, pp. 3320-3328
Open Access | Times Cited: 3
Nanoplastic Stimulates the Amyloidogenesis of Parkinson's Alpha‐Synuclein NACore
Xiufang Liang, Nikolaos K. Andrikopoulos, Huayuan Tang, et al.
Small (2023) Vol. 20, Iss. 14
Open Access | Times Cited: 8
Sampling Conformational Ensembles of Highly Dynamic Proteins via Generative Deep Learning
Talant Ruzmetov, Ta I Hung, Saisri Padmaja Jonnalagedda, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 2
Why Is Arginine the Only Amino Acid That Inhibits Polyglutamine Monomers from Taking on Toxic Conformations?
Shoichi Tanimoto, Hisashi Okumura
ACS Chemical Neuroscience (2024) Vol. 15, Iss. 15, pp. 2925-2935
Open Access | Times Cited: 2
Investigating a Novel Neurodegenerative Disease Toxic Mechanism Involving Lipid Binding Specificity of Amyloid Oligomers
Sarah S. Hirschbeck, Edward T. Lindberg, Joshua H. Jang, et al.
ACS Chemical Neuroscience (2024) Vol. 15, Iss. 7, pp. 1523-1532
Closed Access | Times Cited: 1
Computational analysis of hydrogen bonds network dynamics in the water layers surrounding Aβ(1-42) and Aβ(1-40) peptide dimers
Hamed Zahraee, Zahra Khoshbin, Seyed Shahriar Arab, et al.
Journal of Molecular Liquids (2024) Vol. 408, pp. 125342-125342
Closed Access | Times Cited: 1
Analysis of Protein-Protein and Protein-Membrane Interactions by Isotope-Edited Infrared Spectroscopy
Suren A. Tatulian
Physical Chemistry Chemical Physics (2024) Vol. 26, Iss. 33, pp. 21930-21953
Open Access | Times Cited: 1
Survey of the Aβ-peptide structural diversity: molecular dynamics approaches
Anna P. Tolstova, Alexei A. Adzhubei, Maria A. Strelkova, et al.
Biophysical Reviews (2024) Vol. 16, Iss. 6, pp. 701-722
Closed Access | Times Cited: 1
Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer’s Disease, Parkinson’s Disease and Prionopathies
Ondrej Cehlár, Stefana Njemoga, Miloš Horváth, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 23, pp. 13049-13049
Open Access | Times Cited: 1
Precision Proteoform Design for 4R Tau Isoform Selective Templated Aggregation
Andrew P. Longhini, Austin DuBose, Samuel Lobo, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 2
Helix-to-sheet transition of the Aβ42 peptide revealed using an enhanced sampling strategy and Markov state model
Huilin Wen, Hao Ouyang, Hao Shang, et al.
Computational and Structural Biotechnology Journal (2023) Vol. 23, pp. 688-699
Open Access | Times Cited: 2
Sequence-based identification of amyloidogenic β-hairpins reveals a prostatic acid phosphatase fragment promoting semen amyloid formation
Laetitia Heid, Emil Dandanell Agerschou, Asuka A. Orr, et al.
Computational and Structural Biotechnology Journal (2023) Vol. 23, pp. 417-430
Open Access | Times Cited: 2
Can local heating and molecular crowders disintegrate amyloid aggregates?
Naresh Kumar, Prabir Khatua, Sudipta Kumar Sinha
Chemical Science (2024) Vol. 15, Iss. 16, pp. 6095-6105
Open Access
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