Microfluidic confinement enables monitoring of oligomeric forms of 1-40 β-amyloid peptide in kinetic study by AFM.
- DOI
- 10.1016/j.jcis.2026.141599
- Published
- 2026 Sep 14
- Container
- Journal of colloid and interface science
- Publisher
- Not recorded
- Open access
- unknown
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Cite this work
BibTeX
@article{allodium:10.1016/j.jcis.2026.141599,
title = {Microfluidic confinement enables monitoring of oligomeric forms of 1-40 β-amyloid peptide in kinetic study by AFM.},
author = {Greco P and Lazar AN and Lugli F and Albonetti C and Bystrenova E and Bianchi M and Fadiga L and Zerbetto F and Biscarini F},
year = {2026},
journal = {Journal of colloid and interface science},
doi = {10.1016/j.jcis.2026.141599},
url = {https://doi.org/10.1016/j.jcis.2026.141599}
}RIS
TY - JOUR TI - Microfluidic confinement enables monitoring of oligomeric forms of 1-40 β-amyloid peptide in kinetic study by AFM. AU - Greco P AU - Lazar AN AU - Lugli F AU - Albonetti C AU - Bystrenova E AU - Bianchi M AU - Fadiga L AU - Zerbetto F AU - Biscarini F PY - 2026 JO - Journal of colloid and interface science DO - 10.1016/j.jcis.2026.141599 UR - https://doi.org/10.1016/j.jcis.2026.141599 ER -
APA
P, G., AN, L., F, L., C, A., E, B., M, B., L, F., F, Z., & F, B. (2026). Microfluidic confinement enables monitoring of oligomeric forms of 1-40 β-amyloid peptide in kinetic study by AFM.. Journal of colloid and interface science. https://doi.org/10.1016/j.jcis.2026.141599
Source records
- pubmed · retrieved 2026-09-25T10:56:12.121Z