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Advances in ion mobility spectrometry–mass spectrometry reveal key insights into amyloid assembly()

Interfacing ion mobility spectrometry to mass spectrometry (IMS–MS) has enabled mass spectrometric analyses to extend into an extra dimension, providing unrivalled separation and structural characterization of lowly populated species in heterogeneous mixtures. One biological system that has benefitt...

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Detalles Bibliográficos
Autores principales: Woods, L.A., Radford, S.E., Ashcroft, A.E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Pub. Co 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3787735/
https://www.ncbi.nlm.nih.gov/pubmed/23063533
http://dx.doi.org/10.1016/j.bbapap.2012.10.002
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author Woods, L.A.
Radford, S.E.
Ashcroft, A.E.
author_facet Woods, L.A.
Radford, S.E.
Ashcroft, A.E.
author_sort Woods, L.A.
collection PubMed
description Interfacing ion mobility spectrometry to mass spectrometry (IMS–MS) has enabled mass spectrometric analyses to extend into an extra dimension, providing unrivalled separation and structural characterization of lowly populated species in heterogeneous mixtures. One biological system that has benefitted significantly from such advances is that of amyloid formation. Using IMS–MS, progress has been made into identifying transiently populated monomeric and oligomeric species for a number of different amyloid systems and has led to an enhanced understanding of the mechanism by which small molecules modulate amyloid formation. This review highlights recent advances in this field, which have been accelerated by the commercial availability of IMS–MS instruments. This article is part of a Special Issue entitled: Mass spectrometry in structural biology.
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spelling pubmed-37877352013-10-03 Advances in ion mobility spectrometry–mass spectrometry reveal key insights into amyloid assembly() Woods, L.A. Radford, S.E. Ashcroft, A.E. Biochim Biophys Acta Review Interfacing ion mobility spectrometry to mass spectrometry (IMS–MS) has enabled mass spectrometric analyses to extend into an extra dimension, providing unrivalled separation and structural characterization of lowly populated species in heterogeneous mixtures. One biological system that has benefitted significantly from such advances is that of amyloid formation. Using IMS–MS, progress has been made into identifying transiently populated monomeric and oligomeric species for a number of different amyloid systems and has led to an enhanced understanding of the mechanism by which small molecules modulate amyloid formation. This review highlights recent advances in this field, which have been accelerated by the commercial availability of IMS–MS instruments. This article is part of a Special Issue entitled: Mass spectrometry in structural biology. Elsevier Pub. Co 2013-06 /pmc/articles/PMC3787735/ /pubmed/23063533 http://dx.doi.org/10.1016/j.bbapap.2012.10.002 Text en © 2013 Elsevier B.V. https://creativecommons.org/licenses/by/3.0/ Open Access under CC BY 3.0 (https://creativecommons.org/licenses/by/3.0/) license
spellingShingle Review
Woods, L.A.
Radford, S.E.
Ashcroft, A.E.
Advances in ion mobility spectrometry–mass spectrometry reveal key insights into amyloid assembly()
title Advances in ion mobility spectrometry–mass spectrometry reveal key insights into amyloid assembly()
title_full Advances in ion mobility spectrometry–mass spectrometry reveal key insights into amyloid assembly()
title_fullStr Advances in ion mobility spectrometry–mass spectrometry reveal key insights into amyloid assembly()
title_full_unstemmed Advances in ion mobility spectrometry–mass spectrometry reveal key insights into amyloid assembly()
title_short Advances in ion mobility spectrometry–mass spectrometry reveal key insights into amyloid assembly()
title_sort advances in ion mobility spectrometry–mass spectrometry reveal key insights into amyloid assembly()
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3787735/
https://www.ncbi.nlm.nih.gov/pubmed/23063533
http://dx.doi.org/10.1016/j.bbapap.2012.10.002
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