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Items: 1 to 20 of 149


Probing structural features of Alzheimer's amyloid-β pores in bilayers using site-specific amino acid substitutions.

Capone R, Jang H, Kotler SA, Kagan BL, Nussinov R, Lal R.

Biochemistry. 2012 Jan 24;51(3):776-85. doi: 10.1021/bi2017427. Epub 2012 Jan 12.


Effects of point substitutions on the structure of toxic Alzheimer's β-amyloid channels: atomic force microscopy and molecular dynamics simulations.

Connelly L, Jang H, Arce FT, Ramachandran S, Kagan BL, Nussinov R, Lal R.

Biochemistry. 2012 Apr 10;51(14):3031-8. doi: 10.1021/bi300257e. Epub 2012 Mar 28.


Familial Alzheimer's disease Osaka mutant (ΔE22) β-barrels suggest an explanation for the different Aβ1-40/42 preferred conformational states observed by experiment.

Jang H, Arce FT, Ramachandran S, Kagan BL, Lal R, Nussinov R.

J Phys Chem B. 2013 Oct 3;117(39):11518-29. doi: 10.1021/jp405389n. Epub 2013 Sep 13.


Atomic force microscopy and MD simulations reveal pore-like structures of all-D-enantiomer of Alzheimer's β-amyloid peptide: relevance to the ion channel mechanism of AD pathology.

Connelly L, Jang H, Arce FT, Capone R, Kotler SA, Ramachandran S, Kagan BL, Nussinov R, Lal R.

J Phys Chem B. 2012 Feb 9;116(5):1728-35. doi: 10.1021/jp2108126. Epub 2012 Jan 25.


Interactions of Aβ25-35 β-barrel-like oligomers with anionic lipid bilayer and resulting membrane leakage: an all-atom molecular dynamics study.

Chang Z, Luo Y, Zhang Y, Wei G.

J Phys Chem B. 2011 Feb 10;115(5):1165-74. doi: 10.1021/jp107558e. Epub 2010 Dec 30.


Dual effects of familial Alzheimer's disease mutations (D7H, D7N, and H6R) on amyloid β peptide: correlation dynamics and zinc binding.

Xu L, Chen Y, Wang X.

Proteins. 2014 Dec;82(12):3286-97. doi: 10.1002/prot.24669. Epub 2014 Oct 21.


Molecular interactions of Alzheimer amyloid-β oligomers with neutral and negatively charged lipid bilayers.

Yu X, Wang Q, Pan Q, Zhou F, Zheng J.

Phys Chem Chem Phys. 2013 Jun 21;15(23):8878-89. doi: 10.1039/c3cp44448a. Epub 2013 Mar 14.


Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.

Jang H, Arce FT, Ramachandran S, Kagan BL, Lal R, Nussinov R.

Chem Soc Rev. 2014 Oct 7;43(19):6750-64. doi: 10.1039/c3cs60459d. Review.


Stability of transmembrane amyloid β-peptide and membrane integrity tested by molecular modeling of site-specific Aβ42 mutations.

Poojari C, Strodel B.

PLoS One. 2013 Nov 7;8(11):e78399. doi: 10.1371/journal.pone.0078399. eCollection 2013.


Activity and architecture of pyroglutamate-modified amyloid-β (AβpE3-42) pores.

Gillman AL, Jang H, Lee J, Ramachandran S, Kagan BL, Nussinov R, Teran Arce F.

J Phys Chem B. 2014 Jul 3;118(26):7335-44. doi: 10.1021/jp5040954. Epub 2014 Jun 24.


Alzheimer Aβ peptide interactions with lipid membranes: fibrils, oligomers and polymorphic amyloid channels.

Tofoleanu F, Buchete NV.

Prion. 2012 Sep-Oct;6(4):339-45. doi: 10.4161/pri.21022. Epub 2012 Aug 9.


β-Barrel topology of Alzheimer's β-amyloid ion channels.

Jang H, Arce FT, Ramachandran S, Capone R, Lal R, Nussinov R.

J Mol Biol. 2010 Dec 17;404(5):917-34. doi: 10.1016/j.jmb.2010.10.025. Epub 2010 Oct 21.


Free energy of lipid bilayer defects affected by Alzheimer's disease-associated amyloid-β42 monomers.

Pobandt T, Knecht V.

J Phys Chem B. 2014 Apr 3;118(13):3507-16. doi: 10.1021/jp410477x. Epub 2014 Mar 20.


Models of toxic beta-sheet channels of protegrin-1 suggest a common subunit organization motif shared with toxic alzheimer beta-amyloid ion channels.

Jang H, Ma B, Lal R, Nussinov R.

Biophys J. 2008 Nov 15;95(10):4631-42. doi: 10.1529/biophysj.108.134551. Epub 2008 Aug 15.


Molecular dynamics simulations of Alzheimer Abeta40 elongation and lateral association.

Zheng J, Ma B, Chang Y, Nussinov R.

Front Biosci. 2008 May 1;13:3919-30.


Mutations that replace aromatic side chains promote aggregation of the Alzheimer's Aβ peptide.

Armstrong AH, Chen J, McKoy AF, Hecht MH.

Biochemistry. 2011 May 17;50(19):4058-67. doi: 10.1021/bi200268w. Epub 2011 Apr 22.


The structures of the E22Δ mutant-type amyloid-β alloforms and the impact of E22Δ mutation on the structures of the wild-type amyloid-β alloforms.

Coskuner O, Wise-Scira O, Perry G, Kitahara T.

ACS Chem Neurosci. 2013 Feb 20;4(2):310-20. doi: 10.1021/cn300149j. Epub 2012 Dec 18.


Point mutations in Aβ result in the formation of distinct polymorphic aggregates in the presence of lipid bilayers.

Pifer PM, Yates EA, Legleiter J.

PLoS One. 2011 Jan 18;6(1):e16248. doi: 10.1371/journal.pone.0016248.

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