(Q30887148)

27 June 2017

title

Full-length rat amylin forms fibrils following substitution of single residues from human amylin (English)

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27 June 2017

8

Ueli Aebi

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27 June 2017

Janelle Green

1

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27 June 2017

Claire Goldsbury

2

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27 June 2017

Thierry Mini

3

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27 June 2017

Shabir Sunderji

4

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27 June 2017

Peter Frey

5

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27 June 2017

Joerg Kistler

6

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27 June 2017

Garth Cooper

7

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27 June 2017

language of work or name

English

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publication date

1 February 2003

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Journal of Molecular Biology

27 June 2017

published in

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27 June 2017

volume

326

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27 June 2017

issue

4

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27 June 2017

page(s)

1147-1156

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Review: history of the amyloid fibril

27 June 2017

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Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red.

7 January 2021

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Amyloid peptides are toxic via a common oxidative mechanism

7 January 2021

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Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus

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The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles.

7 January 2021

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"Cross-beta" conformation in proteins.

7 January 2021

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High-resolution electron microscopic analysis of the amyloid fibril

7 January 2021

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Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix

7 January 2021

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Transthyretin fibrillogenesis entails the assembly of monomers: a molecular model for in vitro assembled transthyretin amyloid-like fibrils

7 January 2021

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Molecular modeling of the Abeta1-42 peptide from Alzheimer's disease.

7 January 2021

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7 January 2021

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7 January 2021

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Architecture and Polymorphism of Fibrillar Supramolecular Assemblies Produced by in Vitro Aggregation of Human Calcitonin

7 January 2021

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Polymorphic Fibrillar Assembly of Human Amylin

7 January 2021

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Amyloid Fibril Formation from Full-Length and Fragments of Amylin

7 January 2021

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7 January 2021

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Observation of metastable Abeta amyloid protofibrils by atomic force microscopy

7 January 2021

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Synthetic peptide homologous to beta protein from Alzheimer disease forms amyloid-like fibrils in vitro

7 January 2021

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Examination of the Structure of the Transthyretin Amyloid Fibril by Image Reconstruction from Electron Micrographs

7 January 2021

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Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide. An experimental support for the key role of the phenylalanine residue in amyloid formation

7 January 2021

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Amyloid fibrils formed from a segment of the pancreatic islet amyloid protein

7 January 2021

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Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin

7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis

7 January 2021

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Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology

7 January 2021

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Islet amyloid polypeptide: identification of long-range contacts and local order on the fibrillogenesis pathway

7 January 2021

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Thioflavine T interaction with amyloid β-sheet structures

7 January 2021

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Watching amyloid fibrils grow by time-lapse atomic force microscopy

7 January 2021

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

7 January 2021

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7 January 2021

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7 January 2021

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Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits

7 January 2021

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Conformation and fibrillogenesis of Alzheimer A beta peptides with selected substitution of charged residues.

7 January 2021

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Zinc-induced Alzheimer's Abeta1-40 aggregation is mediated by conformational factors.

7 January 2021

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7 January 2021

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A possible role for pi-stacking in the self-assembly of amyloid fibrils

7 January 2021

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Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases

7 January 2021

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Kinetic partitioning of protein folding and aggregation.

7 January 2021

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Folding and aggregation are selectively influenced by the conformational preferences of the alpha-helices of muscle acylphosphatase.

7 January 2021

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Monitoring biomolecular interactions by time-lapse atomic force microscopy

7 January 2021

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10.1016/S0022-2836(02)01377-3

7 January 2021

Identifiers

DOI

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27 June 2017

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