Lipid-induced conformational transition of amyloid beta peptide fragments (Q43060750)

13 November 2017

Lipid-induced conformational transition of amyloid beta peptide fragments (English)

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13 November 2017

Nagarajan Sureshbabu

1

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13 November 2017

R Kirubagaran

2

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13 November 2017

H Thangarajah

3

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13 November 2017

E J Padma Malar

4

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13 November 2017

R Jayakumar

5

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13 November 2017

18 May 2010

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13 November 2017

15

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Journal of Molecular Neuroscience

inferred from page(s)

published in

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13 November 2017

41

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13 November 2017

3

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13 November 2017

368-382

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https://scigraph.springernature.com/pub.10.1007/s12031-010-9380-7

13 November 2017

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Amyloid beta protein (Abeta) starts to deposit as plasma membrane-bound form in diffuse plaques of brains from hereditary cerebral hemorrhage with amyloidosis-Dutch type, Alzheimer disease and nondemented aged subjects

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Aggregation and metal-binding properties of mutant forms of the amyloid A beta peptide of Alzheimer's disease.

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Self-association of beta-amyloid peptide (1-40) in solution and binding to lipid membranes.

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On the nucleation of amyloid beta-protein monomer folding

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Rotational freedom of tryptophan residues in proteins and peptides.

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Acceleration of amyloid fibril formation by specific binding of Abeta-(1-40) peptide to ganglioside-containing membrane vesicles

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In vitro formation of amyloid fibrils from two synthetic peptides of different lengths homologous to Alzheimer's disease beta-protein

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12 December 2020

Phosphatidylinositol and inositol involvement in Alzheimer amyloid-beta fibril growth and arrest

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1H NMR of A beta amyloid peptide congeners in water solution. Conformational changes correlate with plaque competence

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Structural, kinetic and cytotoxicity aspects of 12-28 beta-amyloid protein fragment: a reappraisal

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12 December 2020

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

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12 December 2020

Effects of sulfate ions on Alzheimer beta/A4 peptide assemblies: implications for amyloid fibril-proteoglycan interactions

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12 December 2020

Structure of beta-amyloid fibrils and its relevance to their neurotoxicity: implications for the pathogenesis of Alzheimer's disease.

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Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type.

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The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Abeta protofibril formation

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Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs

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12 December 2020

Amyloid-beta oligomers: their production, toxicity and therapeutic inhibition

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Ten to fourteen residue peptides of Alzheimer's disease protein are sufficient for amyloid fibril formation and its characteristic x-ray diffraction pattern

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Membrane protein folding and stability: physical principles

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12 December 2020

Comparison of the aggregation properties, secondary structure and apoptotic effects of wild-type, Flemish and Dutch N-terminally truncated amyloid beta peptides

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Environment- and mutation-dependent aggregation behavior of Alzheimer amyloid beta-protein

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Effects of the mutations Glu22 to Gln and Ala21 to Gly on the aggregation of a synthetic fragment of the Alzheimer's amyloid beta/A4 peptide.

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12 December 2020

Point substitution in the central hydrophobic cluster of a human beta-amyloid congener disrupts peptide folding and abolishes plaque competence

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12 December 2020

Lipid-induced conformational transition of the amyloid core fragment Abeta(28-35) and its A30G and A30I mutants

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12 December 2020

Amyloid-induced aggregation and precipitation of soluble proteins: an electrostatic contribution of the Alzheimer's beta(25-35) amyloid fibril

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Linkage and mutational analysis of familial Alzheimer disease kindreds for the APP gene region

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Circular dichroism and aggregation studies of amyloid beta (11-8) fragment and its variants.

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12 December 2020

Alzheimer's disease: genes, proteins, and therapy

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Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum?

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Extracellular amyloid formation and associated pathology in neural grafts.

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Structural analysis of amyloid ? peptide fragment (25-35) in different microenvironments

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Charge states rather than propensity for beta-structure determine enhanced fibrillogenesis in wild-type Alzheimer's beta-amyloid peptide compared to E22Q Dutch mutant

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NMR studies of amyloid beta-peptides: proton assignments, secondary structure, and mechanism of an alpha-helix----beta-sheet conversion for a homologous, 28-residue, N-terminal fragment

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pH-dependent structural transitions of Alzheimer amyloid peptides

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Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum

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Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain

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12 December 2020

Charge alterations of E22 enhance the pathogenic properties of the amyloid beta-protein

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12 December 2020

Properties of integral membrane protein structures: derivation of an implicit membrane potential.

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12 December 2020

Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state

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12 December 2020

Physiological production of the beta-amyloid protein and the mechanism of Alzheimer's disease

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12 December 2020

Peptides homologous to the amyloid protein of Alzheimer's disease containing a glutamine for glutamic acid substitution have accelerated amyloid fibril formation.

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12 December 2020

Unique physicochemical profile of beta-amyloid peptide variant Abeta1-40E22G protofibrils: conceivable neuropathogen in arctic mutant carriers

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12 December 2020

Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy

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12 December 2020

An amyloid beta-protein fragment, A beta[12-28], equipotently impairs post-training memory processing when injected into different limbic system structures.

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12 December 2020

Prolines and amyloidogenicity in fragments of the Alzheimer's peptide beta/A4

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12 December 2020

10.1007/S12031-010-9380-7

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13 November 2017

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