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Items: 1 to 20 of 112

1.

A three-stage kinetic model of amyloid fibrillation.

Lee CC, Nayak A, Sethuraman A, Belfort G, McRae GJ.

Biophys J. 2007 May 15;92(10):3448-58. Epub 2007 Feb 26.

2.

Stop-and-go kinetics in amyloid fibrillation.

Ferkinghoff-Borg J, Fonslet J, Andersen CB, Krishna S, Pigolotti S, Yagi H, Goto Y, Otzen D, Jensen MH.

Phys Rev E Stat Nonlin Soft Matter Phys. 2010 Jul;82(1 Pt 1):010901. Epub 2010 Jul 1.

PMID:
20866557
4.

Sequence determinants regulating fibrillation of human alpha-synuclein.

Koo HJ, Lee HJ, Im H.

Biochem Biophys Res Commun. 2008 Apr 11;368(3):772-8. doi: 10.1016/j.bbrc.2008.01.140. Epub 2008 Feb 7.

PMID:
18261982
5.

Replica exchange molecular dynamics simulations of amyloid peptide aggregation.

Cecchini M, Rao F, Seeber M, Caflisch A.

J Chem Phys. 2004 Dec 1;121(21):10748-56.

PMID:
15549960
6.

Scanning tunneling microscopy reveals single-molecule insights into the self-assembly of amyloid fibrils.

Kalashnyk N, Nielsen JT, Nielsen EH, Skrydstrup T, Otzen DE, Lægsgaard E, Wang C, Besenbacher F, Nielsen NC, Linderoth TR.

ACS Nano. 2012 Aug 28;6(8):6882-9. doi: 10.1021/nn301708d. Epub 2012 Jul 10.

PMID:
22779709
7.

Role of elongation and secondary pathways in S6 amyloid fibril growth.

Lorenzen N, Cohen SI, Nielsen SB, Herling TW, Christiansen G, Dobson CM, Knowles TP, Otzen D.

Biophys J. 2012 May 2;102(9):2167-75. doi: 10.1016/j.bpj.2012.03.047.

8.

Self-folding and aggregation of amyloid nanofibrils.

Paparcone R, Cranford SW, Buehler MJ.

Nanoscale. 2011 Apr;3(4):1748-55. doi: 10.1039/c0nr00840k. Epub 2011 Feb 23.

PMID:
21347488
9.

Dynamics of protofibril elongation and association involved in Aβ42 peptide aggregation in Alzheimer's disease.

Ghosh P, Kumar A, Datta B, Rangachari V.

BMC Bioinformatics. 2010 Oct 7;11 Suppl 6:S24. doi: 10.1186/1471-2105-11-S6-S24.

10.

Glucagon amyloid-like fibril morphology is selected via morphology-dependent growth inhibition.

Andersen CB, Otzen D, Christiansen G, Rischel C.

Biochemistry. 2007 Jun 19;46(24):7314-24. Epub 2007 May 25.

PMID:
17523599
11.

Influence of dendrimer's structure on its activity against amyloid fibril formation.

Klajnert B, Cortijo-Arellano M, Cladera J, Bryszewska M.

Biochem Biophys Res Commun. 2006 Jun 23;345(1):21-8. Epub 2006 Apr 24.

PMID:
16674918
12.

Structure of core domain of fibril-forming PHF/Tau fragments.

Inouye H, Sharma D, Goux WJ, Kirschner DA.

Biophys J. 2006 Mar 1;90(5):1774-89. Epub 2005 Dec 9.

13.

Kinetics of insulin aggregation: disentanglement of amyloid fibrillation from large-size cluster formation.

Manno M, Craparo EF, Martorana V, Bulone D, San Biagio PL.

Biophys J. 2006 Jun 15;90(12):4585-91. Epub 2006 Mar 31.

14.

Evaluation of β-Amyloid Peptides Fibrillation Induced by Nanomaterials Based on Molecular Dynamics and Surface Plasmon Resonance.

Hou Y, Li P, Zhou H, Zhu X, Chen H, Lee J, Koh K, Shen Z, Chen H.

J Nanosci Nanotechnol. 2015 Feb;15(2):1110-6.

PMID:
26353619
15.

Influence of the protein context on the polyglutamine length-dependent elongation of amyloid fibrils.

Huynen C, Willet N, Buell AK, Duwez AS, Jerôme C, Dumoulin M.

Biochim Biophys Acta. 2015 Mar;1854(3):239-48. doi: 10.1016/j.bbapap.2014.12.002. Epub 2014 Dec 6.

PMID:
25489872
16.

Understanding amyloid fibril nucleation and aβ oligomer/drug interactions from computer simulations.

Nguyen P, Derreumaux P.

Acc Chem Res. 2014 Feb 18;47(2):603-11. doi: 10.1021/ar4002075. Epub 2013 Dec 24. Review.

PMID:
24368046
17.

Mass spectroscopic analysis of Sup35NM prion polymerization.

Goncharov VA.

Biophys J. 2005 Dec;89(6):4139-48. Epub 2005 Sep 30. Erratum in: Biophys J. 2006 Jul 15;91(2):776.

18.

Sampling the self-assembly pathways of KFFE hexamers.

Wei G, Mousseau N, Derreumaux P.

Biophys J. 2004 Dec;87(6):3648-56. Epub 2004 Sep 17.

19.

Kinetics of fibril formation by polyalanine peptides.

Nguyen HD, Hall CK.

J Biol Chem. 2005 Mar 11;280(10):9074-82. Epub 2004 Dec 10.

20.

Simulations of nucleation and elongation of amyloid fibrils.

Zhang J, Muthukumar M.

J Chem Phys. 2009 Jan 21;130(3):035102. doi: 10.1063/1.3050295.

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