Atomic structures of amyloid cross-beta spines reveal varied steric zippers (Q27644644)

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Anders Østergaard Madsen

object named as

Anders Ø Madsen

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Michael R Sawaya

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Shilpa Sambashivan

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Rebecca Nelson

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Magdalena I Ivanova

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Stuart A Sievers

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Marcin I Apostol

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Michael J Thompson

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Melinda Balbirnie

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Jed J W Wiltzius

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Heather T McFarlane

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Christian Riekel

Aspects on human amyloid forms and their fibril polypeptides

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language of work or name

English

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publication date

24 May 2007

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published in

Nature

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volume

447

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issue

7143

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page(s)

453-7

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cites work

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Amyloid fibrillogenesis: themes and variations

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The X-ray interpretation of denaturation and the structure of the seed globulins

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The Structure of Amyloid Fibrils by Electron Microscopy and X-Ray Diffraction

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X-ray diffraction studies on amyloid filaments

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Common core structure of amyloid fibrils by synchrotron X-ray diffraction.

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Correlation of structural elements and infectivity of the HET-s prion

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New model for crystalline polyglutamine assemblies and their connection with amyloid fibrils

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A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR

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High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy

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Structural insights into a yeast prion illuminate nucleation and strain diversity

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Structures for amyloid fibrils

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3D structure of Alzheimer's amyloid-beta(1-42) fibrils

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Structural and dynamic features of Alzheimer's Abeta peptide in amyloid fibrils studied by site-directed spin labeling.

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Polymorphic fibril formation by residues 10-40 of the Alzheimer's beta-amyloid peptide

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Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis

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Abeta amyloid fibrils possess a core structure highly resistant to hydrogen exchange

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General structural motifs of amyloid protofilaments

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Structure of the cross-beta spine of amyloid-like fibrils

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An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid

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Cross-beta order and diversity in nanocrystals of an amyloid-forming peptide

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Architecture of Ure2p prion filaments: the N-terminal domains form a central core fiber

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Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure.

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The 3D profile method for identifying fibril-forming segments of proteins

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An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibril

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A systematic screen of beta(2)-microglobulin and insulin for amyloid-like segments

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The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation

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Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins

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Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB

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Structure and texture of fibrous crystals formed by Alzheimer's abeta(11-25) peptide fragment

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Molecular basis for amyloid fibril formation and stability

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Molecular determinants of amyloid deposition in Alzheimer's disease: conformational studies of synthetic beta-protein fragments.

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Direct visualisation of the beta-sheet structure of synthetic Alzheimer's amyloid

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A model for Ure2p prion filaments and other amyloids: the parallel superpleated beta-structure

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The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin

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Protein-only transmission of three yeast prion strains

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Conformational variations in an infectious protein determine prion strain differences

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Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils

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Conformational diversity in a yeast prion dictates its seeding specificity

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Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids

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Strain-specific morphologies of yeast prion amyloid fibrils

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The physical basis of how prion conformations determine strain phenotypes

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Shape complementarity at protein/protein interfaces

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Identifiers

DOI

10.1038/NATURE05695

1 reference

Consolidated OpenCitations Corpus – April 2017

Dimensions Publication ID

1008757821

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Fatcat ID

release_xmsmk2uvubaahdq6s7vtoj3yoq

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1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

17468747

1 reference

Consolidated OpenCitations Corpus – April 2017