(Q87676281)

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Location and conformation of amyloid β(25-35) peptide and its sequence-shuffled peptides within membranes: implications for aggregation and toxicity in PC12 cells

scientific article published on 11 April 2014

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scholarly article

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14 March 2020

Location and conformation of amyloid β(25-35) peptide and its sequence-shuffled peptides within membranes: implications for aggregation and toxicity in PC12 cells (English)

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14 March 2020

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Hui-Hsu Gavin Tsai

1

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14 March 2020

Jian-Bin Lee

2

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14 March 2020

Yuan-Ci Shih

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14 March 2020

Lei Wan

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14 March 2020

Fa-Kuen Shieh

5

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14 March 2020

Chin-Yu Chen

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14 March 2020

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11 April 2014

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14 March 2020

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14 March 2020

9

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14 March 2020

5

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14 March 2020

1002-1011

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14 March 2020

Abeta-generating enzymes: recent advances in beta- and gamma-secretase research

1 reference

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Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of beta-amyloid-mediated cell death

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A comparative study of beta-amyloid peptides Abeta1-42 and Abeta25-35 toxicity in organotypic hippocampal slice cultures

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In vivo conversion of racemized beta-amyloid ([D-Ser 26]A beta 1-40) to truncated and toxic fragments ([D-Ser 26]A beta 25-35/40) and fragment presence in the brains of Alzheimer's patients

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7 January 2021

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Conformations and biological activities of amyloid beta peptide 25-35.

1 reference

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7 January 2021

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Correlation among secondary structure, amyloid precursor protein accumulation, and neurotoxicity of amyloid beta(25-35) peptide as analyzed by single alanine substitution

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Abeta(31-35) and Abeta(25-35) fragments of amyloid beta-protein induce cellular death through apoptotic signals: Role of the redox state of methionine-35.

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Channel formation by a neurotoxic prion protein fragment

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7 January 2021

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The channel hypothesis of Alzheimer's disease: current status

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Electrophysiologic properties of channels induced by Abeta25-35 in planar lipid bilayers

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Abeta(31-35) peptide induce apoptosis in PC 12 cells: contrast with Abeta(25-35) peptide and examination of underlying mechanisms.

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Structural determination of Abeta25-35 micelles by molecular dynamics simulations

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Effects of solvent on the structure of the Alzheimer amyloid-beta(25-35) peptide

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Folding and membrane insertion of amyloid-beta (25-35) peptide and its mutants: implications for aggregation and neurotoxicity

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The stability of monomeric intermediates controls amyloid formation: Abeta25-35 and its N27Q mutant

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7 January 2021

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Neuronal membranes are key to the pathogenesis of Alzheimer's disease: the role of both raft and non-raft membrane domains

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7 January 2021

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An Implicit Membrane Generalized Born Theory for the Study of Structure, Stability, and Interactions of Membrane Proteins

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7 January 2021

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Structures of beta-amyloid peptide 1-40, 1-42, and 1-55-the 672-726 fragment of APP-in a membrane environment with implications for interactions with gamma-secretase

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7 January 2021

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Multidimensional free-energy calculations using the weighted histogram analysis method

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7 January 2021

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Three-dimensional structures of the amyloid beta peptide (25-35) in membrane-mimicking environment

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A revised set of potentials for beta-turn formation in proteins

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Amyloid-beta fibril formation is not necessarily required for microglial activation by the peptides.

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Reversible random coil-beta-sheet transition of the Alzheimer beta-amyloid fragment (25-35).

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Solution structure of amyloid beta-peptide (25-35) in different media

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Peptide partitioning properties from direct insertion studies

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Identifiers

10.1002/CMDC.201400062

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24729535%20AND%20SRC:MED&resulttype=core&format=json

14 March 2020

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24729535%20AND%20SRC:MED&resulttype=core&format=json

14 March 2020

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