Structure of an intermediate state in protein folding and aggregation (Q27678629)

6

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Philipp Neudecker

1

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Lewis E. Kay

9

object named as

Lewis E Kay

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author name string

Paul Robustelli

2

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Andrea Cavalli

3

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Patrick Walsh

4

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Patrik Lundström

5

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Simon Sharpe

Protein folding and misfolding

7

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language of work or name

English

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publication date

20 April 2012

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published in

Science

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volume

336

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issue

6079

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page(s)

362-6

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cites work

1 reference

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Folding proteins in fatal ways

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Protein misfolding, functional amyloid, and human disease

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Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide

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Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy

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A Transient and Low-Populated Protein-Folding Intermediate at Atomic Resolution

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Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding

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Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation

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Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: loop flexibility and amyloid aggregation

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Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions

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Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra

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TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts

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Carbonyl CSA restraints from solution NMR for protein structure refinement

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Weak alignment NMR: a hawk-eyed view of biomolecular structure

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Solution structure and ligand-binding site of the SH3 domain of the p85α subunit of phosphatidylinositol 3-kinase

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Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

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

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Primary structure effects on peptide group hydrogen exchange

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