A glycine zipper motif mediates the formation of toxic β-amyloid oligomers in vitro and in vivo

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 1750-1326

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: A glycine zipper motif mediates the formation of toxic β-amyloid oligomers in vitro and in vivo ; volume:6 ; number:1 ; day:23 ; month:8 ; year:2011 ; pages:1-17 ; date:12.2011
Molecular neurodegeneration ; 6, Heft 1 (23.8.2011), 1-17, 12.2011

Creator: Fonte, Virginia

Contributor: Dostal, Vishantie
Roberts, Christine M.
Gonzales, Patrick
Lacor, Pascale
Magrane, Jordi
Dingwell, Natalie
Fan, Emily Y.
Silverman, Michael A.
Stein, Gretchen H.
Link, Christopher D.
SpringerLink (Online service)

DOI: 10.1186/1750-1326-6-61

URN: urn:nbn:de:1111-2016073067018

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 14.08.2025, 10:47 AM CEST

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Associated

Fonte, Virginia
Dostal, Vishantie
Roberts, Christine M.
Gonzales, Patrick
Lacor, Pascale
Magrane, Jordi
Dingwell, Natalie
Fan, Emily Y.
Silverman, Michael A.
Stein, Gretchen H.
Link, Christopher D.
SpringerLink (Online service)

Other Objects (12)

Erratum to: A glycine zipper motif mediates the formation of toxic beta-amyloid oligomers in vitro and in vivo

Biodistribution of 99mTc Tricarbonyl Glycine Oligomers

A glycine zipper motif is required for the translocation of a T6SS toxic effector into target cells

In vivo induction of membrane damage by β-amyloid peptide oligomers

TIA1 regulates the generation and response to toxic tau oligomers

Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers

Inhibition of AMPA receptor trafficking at hippocampal synapses by β-amyloid oligomers: the mitochondrial contribution

Alzheimer’s disease pathology propagation by exosomes containing toxic amyloid-beta oligomers

QIAD assay for quantitating a compound's efficacy in elimination of toxic Aβ oligomers

Conformational switching within dynamic oligomers underpins toxic gain-of-function by diabetes-associated amyloid

Personenakten

Zipper, Richard

Archivale

Zipper, *Otto

Erratum to: A glycine zipper motif mediates the formation of toxic beta-amyloid oligomers in vitro and in vivo

Biodistribution of 99mTc Tricarbonyl Glycine Oligomers

A glycine zipper motif is required for the translocation of a T6SS toxic effector into target cells

In vivo induction of membrane damage by β-amyloid peptide oligomers

TIA1 regulates the generation and response to toxic tau oligomers

Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers

Inhibition of AMPA receptor trafficking at hippocampal synapses by β-amyloid oligomers: the mitochondrial contribution

Alzheimer’s disease pathology propagation by exosomes containing toxic amyloid-beta oligomers

QIAD assay for quantitating a compound's efficacy in elimination of toxic Aβ oligomers

Conformational switching within dynamic oligomers underpins toxic gain-of-function by diabetes-associated amyloid

Personenakten

Zipper, Richard

Archivale

Zipper, *Otto

Erratum to: A glycine zipper motif mediates the formation of toxic beta-amyloid oligomers in vitro and in vivo

Biodistribution of 99mTc Tricarbonyl Glycine Oligomers

A glycine zipper motif is required for the translocation of a T6SS toxic effector into target cells

In vivo induction of membrane damage by β-amyloid peptide oligomers

TIA1 regulates the generation and response to toxic tau oligomers

Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers

Inhibition of AMPA receptor trafficking at hippocampal synapses by β-amyloid oligomers: the mitochondrial contribution

Alzheimer’s disease pathology propagation by exosomes containing toxic amyloid-beta oligomers

QIAD assay for quantitating a compound's efficacy in elimination of toxic Aβ oligomers

Conformational switching within dynamic oligomers underpins toxic gain-of-function by diabetes-associated amyloid

Personenakten

Zipper, Richard

Archivale

Zipper, *Otto

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A glycine zipper motif mediates the formation of toxic β-amyloid oligomers in vitro and in vivo

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Other Objects (12)

Erratum to: A glycine zipper motif mediates the formation of toxic beta-amyloid oligomers in vitro and in vivo

Biodistribution of 99mTc Tricarbonyl Glycine Oligomers

A glycine zipper motif is required for the translocation of a T6SS toxic effector into target cells

In vivo induction of membrane damage by β-amyloid peptide oligomers

TIA1 regulates the generation and response to toxic tau oligomers

Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers

Inhibition of AMPA receptor trafficking at hippocampal synapses by β-amyloid oligomers: the mitochondrial contribution

Alzheimer’s disease pathology propagation by exosomes containing toxic amyloid-beta oligomers

QIAD assay for quantitating a compound's efficacy in elimination of toxic Aβ oligomers

Conformational switching within dynamic oligomers underpins toxic gain-of-function by diabetes-associated amyloid

Zipper, Richard

Zipper, *Otto

Erratum to: A glycine zipper motif mediates the formation of toxic beta-amyloid oligomers in vitro and in vivo

Biodistribution of 99mTc Tricarbonyl Glycine Oligomers

A glycine zipper motif is required for the translocation of a T6SS toxic effector into target cells

In vivo induction of membrane damage by β-amyloid peptide oligomers

TIA1 regulates the generation and response to toxic tau oligomers

Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers

Inhibition of AMPA receptor trafficking at hippocampal synapses by β-amyloid oligomers: the mitochondrial contribution

Alzheimer’s disease pathology propagation by exosomes containing toxic amyloid-beta oligomers

QIAD assay for quantitating a compound's efficacy in elimination of toxic Aβ oligomers

Conformational switching within dynamic oligomers underpins toxic gain-of-function by diabetes-associated amyloid

Zipper, Richard

Zipper, *Otto

Erratum to: A glycine zipper motif mediates the formation of toxic beta-amyloid oligomers in vitro and in vivo

Biodistribution of 99mTc Tricarbonyl Glycine Oligomers

A glycine zipper motif is required for the translocation of a T6SS toxic effector into target cells

In vivo induction of membrane damage by β-amyloid peptide oligomers

TIA1 regulates the generation and response to toxic tau oligomers

Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers

Inhibition of AMPA receptor trafficking at hippocampal synapses by β-amyloid oligomers: the mitochondrial contribution

Alzheimer’s disease pathology propagation by exosomes containing toxic amyloid-beta oligomers

QIAD assay for quantitating a compound's efficacy in elimination of toxic Aβ oligomers

Conformational switching within dynamic oligomers underpins toxic gain-of-function by diabetes-associated amyloid

Zipper, Richard

Zipper, *Otto

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