Defining the Dynamic Conformational Networks of Cross-β Peptide Assembly

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Amyloid scaffolds as alternative chlorosomes.Expanding the informational chemistries of life: peptide/RNA networks.Design of multi-phase dynamic chemical networks.Covalent Tethering and Residues with Bulky Hydrophobic Side Chains Enable Self-Assembly of Distinct Amyloid Structures.

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Defining the Dynamic Conformational Networks of Cross-β Peptide Assembly

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http://www.wikidata.org/entity/Q58074760

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im April 2015 veröffentlichter wissenschaftlicher Artikel

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wetenschappelijk artikel

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наукова стаття, опублікована у квітні 2015

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Defining the Dynamic Conformational Networks of Cross-β Peptide Assembly

@en

Defining the Dynamic Conformational Networks of Cross-β Peptide Assembly

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Defining the Dynamic Conformational Networks of Cross-β Peptide Assembly

@en

Defining the Dynamic Conformational Networks of Cross-β Peptide Assembly

@nl

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Defining the Dynamic Conformational Networks of Cross-β Peptide Assembly

@en

Defining the Dynamic Conformational Networks of Cross-β Peptide Assembly

@nl

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Defining the Dynamic Conformational Networks of Cross-β Peptide Assembly

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Allisandra K. Mowles

http://www.w3.org/2001/XMLSchema#string

Anil K. Mehta

http://www.w3.org/2001/XMLSchema#string

Chen Liang

http://www.w3.org/2001/XMLSchema#string

David G. Lynn

http://www.w3.org/2001/XMLSchema#string

Jillian E. Smith

http://www.w3.org/2001/XMLSchema#string

Michael Tseng

http://www.w3.org/2001/XMLSchema#string

Noel Li

http://www.w3.org/2001/XMLSchema#string

Sha Li

http://www.w3.org/2001/XMLSchema#string

P2860

Darwinian evolution of prions in cell culture

Mechanisms of protein seeding in neurodegenerative diseases

Self-propagation of pathogenic protein aggregates in neurodegenerative diseases

Length-dependent stability and strand length limits in antiparallel -sheet secondary structure

Towards a Pharmacophore for Amyloid

Molecular basis for amyloid- polymorphism

The Hofmeister effect on amyloid formation using yeast prion protein

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

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

Environmental conditions affect the kinetics of nucleation of amyloid fibrils and determine their morphology.

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763-769

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scholarly article

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10.1002/IJCH.201500012

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6-7

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P478

http://www.w3.org/2001/XMLSchema#string

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2015-04-21T00:00:00Z

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Defining the Dynamic Conformational Networks of Cross-β Peptide Assembly

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P2860

P2860

Defining the Dynamic Conformational Networks of Cross-β Peptide Assembly

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P1433

P1476

P2093

P2860

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P356

P433

P478

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P1433

P1476

P2093

P2860

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P31

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