Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranes

10.12688/f1000research.2-221.v2

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Main Authors:	Song J., Qin H., Lim L., Wei Y., Gupta G.
Other Authors:	BIOLOGY
Format:	Article
Published:	2020
Subjects:	alpha synuclein major sperm protein melittin membrane protein unclassified drug aging alpha helix Article homeostasis human hydrogen bond molecular interaction molecular pathology nuclear magnetic resonance protein aggregation protein conformation protein degradation protein determination protein domain protein expression protein folding protein function protein homeostasis protein stability structure analysis upregulation
Online Access:	https://scholarbank.nus.edu.sg/handle/10635/174579
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Institution:	National University of Singapore

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spelling	sg-nus-scholar.10635-1745792024-11-15T07:53:04Z Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranes Song J. Qin H. Lim L. Wei Y. Gupta G. BIOLOGY DEAN'S OFFICE (DUKE-NUS MEDICAL SCHOOL) BIOLOGICAL SCIENCES DUKE-NUS MEDICAL SCHOOL alpha synuclein major sperm protein melittin membrane protein unclassified drug aging alpha helix Article homeostasis human hydrogen bond molecular interaction molecular pathology nuclear magnetic resonance protein aggregation protein conformation protein degradation protein determination protein domain protein expression protein folding protein function protein homeostasis protein stability structure analysis upregulation 10.12688/f1000research.2-221.v2 F1000Research 2 2-221.v2 2020-09-08T02:16:29Z 2020-09-08T02:16:29Z 2014 Article Song J., Qin H., Lim L., Wei Y., Gupta G. (2014). Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranes. F1000Research 2 : 2-221.v2. ScholarBank@NUS Repository. https://doi.org/10.12688/f1000research.2-221.v2 2046-1402 https://scholarbank.nus.edu.sg/handle/10635/174579 Unpaywall 20200831
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	alpha synuclein major sperm protein melittin membrane protein unclassified drug aging alpha helix Article homeostasis human hydrogen bond molecular interaction molecular pathology nuclear magnetic resonance protein aggregation protein conformation protein degradation protein determination protein domain protein expression protein folding protein function protein homeostasis protein stability structure analysis upregulation
spellingShingle	alpha synuclein major sperm protein melittin membrane protein unclassified drug aging alpha helix Article homeostasis human hydrogen bond molecular interaction molecular pathology nuclear magnetic resonance protein aggregation protein conformation protein degradation protein determination protein domain protein expression protein folding protein function protein homeostasis protein stability structure analysis upregulation Song J. Qin H. Lim L. Wei Y. Gupta G. Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranes
description	10.12688/f1000research.2-221.v2
author2	BIOLOGY
author_facet	BIOLOGY Song J. Qin H. Lim L. Wei Y. Gupta G.
format	Article
author	Song J. Qin H. Lim L. Wei Y. Gupta G.
author_sort	Song J.
title	Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranes
title_short	Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranes
title_full	Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranes
title_fullStr	Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranes
title_full_unstemmed	Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranes
title_sort	resolving the paradox for protein aggregation diseases: nmr structure and dynamics of the membrane-embedded p56s-msp causing als imply a common mechanism for aggregation-prone proteins to attack membranes
publishDate	2020
url	https://scholarbank.nus.edu.sg/handle/10635/174579
_version_	1821206735879143424

Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranes

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