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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:

Membrane-Catalyzed Aggregation of Islet Amyloid Polypeptide Is Dominated by Secondary Nucleation
Barend O. W. Elenbaas, Lucie Khemtémourian, J. Antoinette Killian, et al.
Biochemistry (2022) Vol. 61, Iss. 14, pp. 1465-1472
Open Access | Times Cited: 18

Showing 18 citing articles:

Molecular mechanisms of amyloid formation in living systems
Tessa Sinnige
Chemical Science (2022) Vol. 13, Iss. 24, pp. 7080-7097
Open Access | Times Cited: 41
Imaging Amyloid‐β Membrane Interactions: Ion‐Channel Pores and Lipid‐Bilayer Permeability in Alzheimer's Disease
John H. Viles
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 25
Open Access | Times Cited: 40
Fibril elongation by human islet amyloid polypeptide is the main event linking aggregation to membrane damage
Barend O. W. Elenbaas, Stefanie M. Kremsreiter, Lucie Khemtémourian, et al.
BBA Advances (2023) Vol. 3, pp. 100083-100083
Open Access | Times Cited: 10
The molecular basis for the increased stability of the FUS-LC fibril at the anionic membrane- and air–water interfaces
Sanjoy Paul, Sayantan Mondal, Irina Shenogina, et al.
Chemical Science (2024) Vol. 15, Iss. 34, pp. 13788-13799
Open Access | Times Cited: 2
Global analysis of kinetics reveals the role of secondary nucleation in recombinant spider silk self‐assembly
Veronika Hovanová, Andrej Hovan, Gabriel Žoldák, et al.
Protein Science (2023) Vol. 32, Iss. 8
Open Access | Times Cited: 4
Islet amyloid polypeptide tagged with green fluorescent protein localises to mitochondria and forms filamentous aggregates in Caenorhabditis elegans
Mehmet Akdag, Vera van Schijndel, Tessa Sinnige
Biophysical Chemistry (2024) Vol. 307, pp. 107180-107180
Open Access | Times Cited: 1
Exploring the thermodynamics of protein aggregation: an insight to Huntington's disease therapeutics
Rajinder Singh Kaundal, Tejasvi Pandey, Vivek Pandey
Neuroscience and Behavioral Physiology (2024) Vol. 54, Iss. 7, pp. 1042-1060
Closed Access | Times Cited: 1
Converting the Amyloidogenic Islet Amyloid Polypeptide into a Potent Nonaggregating Peptide Ligand by Side Chain-to-Side Chain Macrocyclization
Margaryta Babych, Michael L. Garelja, Phuong Trang Nguyen, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 37, pp. 25513-25526
Closed Access | Times Cited: 1
Interspecies Variation Affects Islet Amyloid Polypeptide Membrane Binding
Henry M. Sanders, Farzaneh Chalyavi, Caitlyn R. Fields, et al.
Journal of the American Society for Mass Spectrometry (2023) Vol. 34, Iss. 6, pp. 986-990
Open Access | Times Cited: 3
Imaging Amyloid‐β Membrane Interactions: Ion‐Channel Pores and Lipid‐Bilayer Permeability in Alzheimer's Disease
John H. Viles
Angewandte Chemie (2023) Vol. 135, Iss. 25
Open Access | Times Cited: 2
The molecular basis for the increased stability of the FUS-LC fibril at the anionic membrane- and air-water interfaces
Sanjoy Paul, Sayantan Mondal, Irina Shenogina, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Modulation of Biological Membranes Using Small-Molecule Compounds to Counter Toxicity Caused by Amyloidogenic Proteins
Raina Marie Seychell, Adam El Saghir, Neville Vassallo
Membranes (2024) Vol. 14, Iss. 11, pp. 231-231
Open Access
Global kinetic model of lipid-induced alpha-synuclein aggregation and its inhibition by small molecules
Alisdair Stevenson, Roxine Staats, Alexander J. Dear, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Cross-domain binding of anti-fibrillation peptide TNGQ to islet amyloid polypeptide provides cytoprotective effects in giant unilamellar vesicles and pancreatic β-cells
Raliat O. Abioye, Martha S. Yiridoe, Chenyang Wang, et al.
Food & Function (2024)
Closed Access
Interspecies Variation Affects IAPP Membrane Binding
Henry M. Sanders, Farzaneh Chalyavi, Caitlyn R. Fields, et al.
(2023)
Open Access | Times Cited: 1
Islet amyloid polypeptide tagged with green fluorescent protein localises to mitochondria and forms filamentous aggregates inCaenorhabditis elegans
Mehmet Akdag, Vera van Schijndel, Tessa Sinnige
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
From Monomers to Condensates: Golgi-Associated plant Pathogenesis Related protein 1 (GAPR-1) Oligomerization in Saccharomyces cerevisiae
Nafiseh Sirati
(2023)
Open Access
Fibril elongation by human islet amyloid polypeptide is the main event linking aggregation to membrane damage
Barend O. W. Elenbaas, Stefanie M. Kremsreiter, Lucie Khemtémourian, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access
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