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Coexistence of ribbon and helical fibrils originating from hIAPP^sub 20-29^ revealed by quantitative...

Coexistence of ribbon and helical fibrils originating from hIAPP^sub 20-29^ revealed by quantitative...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_1291880677

Coexistence of ribbon and helical fibrils originating from hIAPP^sub 20-29^ revealed by quantitative nanomechanical atomic force microscopy

About this item

Full title

Coexistence of ribbon and helical fibrils originating from hIAPP^sub 20-29^ revealed by quantitative nanomechanical atomic force microscopy

Publisher

Washington: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2013-02, Vol.110 (8), p.2798

Language

English

Formats

Publication information

Publisher

Washington: National Academy of Sciences

More information

Scope and Contents

Contents

Uncontrolled misfolding of proteins leading to the formation of amyloid deposits is associated with more than 40 types of diseases, such as neurodegenerative diseases and type-2 diabetes. These irreversible amyloid fibrils typically assemble in distinct stages. Transitions among the various intermediate stages are the subject of many studies but ar...

Alternative Titles

Full title

Coexistence of ribbon and helical fibrils originating from hIAPP^sub 20-29^ revealed by quantitative nanomechanical atomic force microscopy

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_journals_1291880677

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_1291880677

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

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