Cite the Following Article
Molecular dynamics simulations of mechanical failure in polymorphic arrangements of amyloid fibrils containing structural defects
Hlengisizwe Ndlovu, Alison E. Ashcroft, Sheena E. Radford and Sarah A. Harris
Beilstein J. Nanotechnol. 2013, 4, 429–440.
https://doi.org/10.3762/bjnano.4.50
How to Cite
Ndlovu, H.; Ashcroft, A. E.; Radford, S. E.; Harris, S. A. Beilstein J. Nanotechnol. 2013, 4, 429–440. doi:10.3762/bjnano.4.50
Download Citation
Citation data can be downloaded as file using the "Download" button or used for copy/paste from the text window
below.
Citation data in RIS format can be imported by all major citation management software, including EndNote,
ProCite, RefWorks, and Zotero.
Citations to This Article
Up to 20 of the most recent references are displayed here.
Scholarly Works
- Zein, H. F.; Sutthibutpong, T. Roles of Tryptophan and Charged Residues on the Polymorphisms of Amyloids Formed by K-Peptides of Hen Egg White Lysozyme Investigated through Molecular Dynamics Simulations. International journal of molecular sciences 2023, 24, 2626. doi:10.3390/ijms24032626
- Verma, P.; Panda, B.; Singh, K. P.; Pandit, S. B. Optimal Protein Sequence Design Mitigates Mechanical Failure in Silk β-Sheet Nanocrystals. ACS biomaterials science & engineering 2021, 7, 3156–3165. doi:10.1021/acsbiomaterials.1c00447
- Radamaker, L.; Baur, J. D.; Huhn, S.; Haupt, C.; Hegenbart, U.; Schönland, S.; Bansal, A.; Schmidt, M.; Fändrich, M. Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis. Nature communications 2021, 12, 1–10. doi:10.1038/s41467-021-21126-2
- Radamaker, L.; Baur, J. D.; Huhn, S.; Haupt, C.; Hegenbart, U.; Schönland, S.; Bansal, A.; Schmidt, M.; Fändrich, M. Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis. Cold Spring Harbor Laboratory 2020. doi:10.1101/2020.10.12.332569
- Ozgur, B.; Sayar, M. Assembly of Triblock Amphiphilic Peptides into One-Dimensional Aggregates and Network Formation. The journal of physical chemistry. B 2016, 120, 10243–10257. doi:10.1021/acs.jpcb.6b07545
- Lee, M.; Choi, H.; Na, S. Effects of End-Terminal Capping on Transthyretin (105-115) Amyloid Protofibrils Using Steered Molecular Dynamics. Journal of Nanomaterials 2016, 2016, 1863065–10. doi:10.1155/2016/1863065
- Baek, I.; Lee, M.; Na, S. Understanding structural characteristics of out-of-register hIAPP amyloid proteins via molecular dynamics. RSC Advances 2016, 6, 77666–77672. doi:10.1039/c6ra19100b
- Chang, H. J.; Baek, I.; Lee, M.; Na, S. Influence of Aromatic Residues on the Material Characteristics of Aβ Amyloid Protofibrils at the Atomic Scale. Chemphyschem : a European journal of chemical physics and physical chemistry 2015, 16, 2403–2414. doi:10.1002/cphc.201500244
- Lee, M.; Chang, H. J.; Kim, D.; Lee, Y.; Suh, H.; Ahn, N.; Yoon, G.; Na, S. Relationship between structural composition and material properties of polymorphic hIAPP fibrils. Biophysical chemistry 2015, 199, 1–8. doi:10.1016/j.bpc.2015.02.002
- Choi, B.; Yoon, G.; Lee, S. W.; Eom, K. Mechanical deformation mechanisms and properties of amyloid fibrils. Physical chemistry chemical physics : PCCP 2014, 17, 1379–1389. doi:10.1039/c4cp03804e
- Jang, H.; Arce, F. T.; Ramachandran, S.; Kagan, B. L.; Lal, R.; Nussinov, R. Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs. Chemical Society reviews 2014, 43, 6750–6764. doi:10.1039/c3cs60459d
