PuSH - Publication Server of Helmholtz Zentrum München: Stabilization and structural analysis of a membrane-associated hIAPP aggregation intermediate.

Information

Clues to quality of journals

Open Access Policy of Helmholtz Association 2016

CC Licencences

Publication Metrics

Navigation

Home

Deutsch

EVA: Electronic Publishing

New EVA Application

Research

Advanced Search

Browse by ...

... HMGU-Authors/Consortia

... Organizational Structure

... Journal

... Publication Type

... Research Data

... Arbeitsgruppen

... Publication Year

Publication overview

Statistics

Statistics (last 5 years)

OA Publications

Publish

Submit Publication

Import publication from...

...EVA

Report missing publication

Highlights

Support & Contact

Contact persons

Help

Data protection

Helmholtz Open Science

JANE Journal Estimator

SHERPA/RoMEO

DOAJ

Export:

Text

Endnote (RIS) BIB

BibTeX

Rodriguez Camargo, D.C.* ; Korshavn, K.J.* ; Jussupow, A.* ; Raltchev, K.* ; Goricanec, D.* ; Fleisch, M. ; Sarkar, R.* ; Xue, K. ; Aichler, M. ; Mettenleiter, G. ; Walch, A.K. ; Camilloni, C.* ; Hagn, F. ; Reif, B. ; Ramamoorthy, A.*

Stabilization and structural analysis of a membrane-associated hIAPP aggregation intermediate.

eLife 6:e31226 (2017)

Publ. Version/Full Text

Postprint

Research data

DOI

PMC

	Open Access Gold

Abstract
Metrics
Extra information

Membrane-assisted amyloid formation is implicated in human diseases, and many of the aggregating species accelerate amyloid formation and induce cell death. While structures of membrane-associated intermediates would provide tremendous insights into the pathology and aid in the design of compounds to potentially treat the diseases, it has not been feasible to overcome the challenges posed by the cell membrane. Here we use NMR experimental constraints to solve the structure of a type-2 diabetes related human islet amyloid polypeptide intermediate stabilized in nanodiscs. ROSETTA and MD simulations resulted in a unique b-strand structure distinct from the conventional amyloid b-hairpin and revealed that the nucleating NFGAIL region remains flexible and accessible within this isolated intermediate, suggesting a mechanism by which membrane-associated aggregation may be propagated. The ability of nanodiscs to trap amyloid intermediates as demonstrated could become one of the most powerful approaches to dissect the complicated misfolding pathways of protein aggregation.

Impact Factor

Scopus SNIP

Web of Science
Times Cited

Scopus
Cited By

Altmetric

7.725

1.377