The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation?

Abstract Since the reformulation of the amyloid cascade hypothesis to focus on oligomeric aggregates of amyloid beta as the prime toxic species causing Alzheimer's disease, many researchers refocused on detecting a specific molecular assembly of defined size thatis the main trigger of Alzheimer...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Broersen, Kerensa [verfasserIn] Rousseau, Frederic Schymkowitz, Joost

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2010

Schlagwörter:	Amyloid Fibril Islet Amyloid Polypeptide Amyloid Cascade Hypothesis Solution Nuclear Magnetic Resonance Mature Fibril

Anmerkung:	© BioMed Central Ltd 2010

Übergeordnetes Werk:	Enthalten in: Alzheimer's research & therapy - London : BioMed Central, 2009, 2(2010), 4 vom: 14. Juli
Übergeordnetes Werk:	volume:2 ; year:2010 ; number:4 ; day:14 ; month:07

Links:	Volltext

DOI / URN:	10.1186/alzrt36

Katalog-ID:	SPR030811023

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spelling	10.1186/alzrt36 doi (DE-627)SPR030811023 (SPR)alzrt36-e DE-627 ger DE-627 rakwb eng Broersen, Kerensa verfasserin aut The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation? 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © BioMed Central Ltd 2010 Abstract Since the reformulation of the amyloid cascade hypothesis to focus on oligomeric aggregates of amyloid beta as the prime toxic species causing Alzheimer's disease, many researchers refocused on detecting a specific molecular assembly of defined size thatis the main trigger of Alzheimer's disease. The result has been the identification of a host of molecular assemblies containing from two up to a hundred molecules of the amyloid beta peptide, which were all found to impair memory formation in mice. This clearly demonstrates that size is insufficient to define toxicity and peptide conformation has to be taken into account. In this review we discuss the interplay between oligomer size and peptide conformation as the key determinants of the neurotoxicity of the amyloid beta peptide. Amyloid Fibril (dpeaa)DE-He213 Islet Amyloid Polypeptide (dpeaa)DE-He213 Amyloid Cascade Hypothesis (dpeaa)DE-He213 Solution Nuclear Magnetic Resonance (dpeaa)DE-He213 Mature Fibril (dpeaa)DE-He213 Rousseau, Frederic aut Schymkowitz, Joost aut Enthalten in Alzheimer's research & therapy London : BioMed Central, 2009 2(2010), 4 vom: 14. Juli (DE-627)605683557 (DE-600)2506521-X 1758-9193 nnns volume:2 year:2010 number:4 day:14 month:07 https://dx.doi.org/10.1186/alzrt36 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 2 2010 4 14 07
allfields_unstemmed	10.1186/alzrt36 doi (DE-627)SPR030811023 (SPR)alzrt36-e DE-627 ger DE-627 rakwb eng Broersen, Kerensa verfasserin aut The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation? 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © BioMed Central Ltd 2010 Abstract Since the reformulation of the amyloid cascade hypothesis to focus on oligomeric aggregates of amyloid beta as the prime toxic species causing Alzheimer's disease, many researchers refocused on detecting a specific molecular assembly of defined size thatis the main trigger of Alzheimer's disease. The result has been the identification of a host of molecular assemblies containing from two up to a hundred molecules of the amyloid beta peptide, which were all found to impair memory formation in mice. This clearly demonstrates that size is insufficient to define toxicity and peptide conformation has to be taken into account. In this review we discuss the interplay between oligomer size and peptide conformation as the key determinants of the neurotoxicity of the amyloid beta peptide. Amyloid Fibril (dpeaa)DE-He213 Islet Amyloid Polypeptide (dpeaa)DE-He213 Amyloid Cascade Hypothesis (dpeaa)DE-He213 Solution Nuclear Magnetic Resonance (dpeaa)DE-He213 Mature Fibril (dpeaa)DE-He213 Rousseau, Frederic aut Schymkowitz, Joost aut Enthalten in Alzheimer's research & therapy London : BioMed Central, 2009 2(2010), 4 vom: 14. Juli (DE-627)605683557 (DE-600)2506521-X 1758-9193 nnns volume:2 year:2010 number:4 day:14 month:07 https://dx.doi.org/10.1186/alzrt36 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 2 2010 4 14 07
allfieldsGer	10.1186/alzrt36 doi (DE-627)SPR030811023 (SPR)alzrt36-e DE-627 ger DE-627 rakwb eng Broersen, Kerensa verfasserin aut The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation? 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © BioMed Central Ltd 2010 Abstract Since the reformulation of the amyloid cascade hypothesis to focus on oligomeric aggregates of amyloid beta as the prime toxic species causing Alzheimer's disease, many researchers refocused on detecting a specific molecular assembly of defined size thatis the main trigger of Alzheimer's disease. The result has been the identification of a host of molecular assemblies containing from two up to a hundred molecules of the amyloid beta peptide, which were all found to impair memory formation in mice. This clearly demonstrates that size is insufficient to define toxicity and peptide conformation has to be taken into account. In this review we discuss the interplay between oligomer size and peptide conformation as the key determinants of the neurotoxicity of the amyloid beta peptide. Amyloid Fibril (dpeaa)DE-He213 Islet Amyloid Polypeptide (dpeaa)DE-He213 Amyloid Cascade Hypothesis (dpeaa)DE-He213 Solution Nuclear Magnetic Resonance (dpeaa)DE-He213 Mature Fibril (dpeaa)DE-He213 Rousseau, Frederic aut Schymkowitz, Joost aut Enthalten in Alzheimer's research & therapy London : BioMed Central, 2009 2(2010), 4 vom: 14. Juli (DE-627)605683557 (DE-600)2506521-X 1758-9193 nnns volume:2 year:2010 number:4 day:14 month:07 https://dx.doi.org/10.1186/alzrt36 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 2 2010 4 14 07
allfieldsSound	10.1186/alzrt36 doi (DE-627)SPR030811023 (SPR)alzrt36-e DE-627 ger DE-627 rakwb eng Broersen, Kerensa verfasserin aut The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation? 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © BioMed Central Ltd 2010 Abstract Since the reformulation of the amyloid cascade hypothesis to focus on oligomeric aggregates of amyloid beta as the prime toxic species causing Alzheimer's disease, many researchers refocused on detecting a specific molecular assembly of defined size thatis the main trigger of Alzheimer's disease. The result has been the identification of a host of molecular assemblies containing from two up to a hundred molecules of the amyloid beta peptide, which were all found to impair memory formation in mice. This clearly demonstrates that size is insufficient to define toxicity and peptide conformation has to be taken into account. In this review we discuss the interplay between oligomer size and peptide conformation as the key determinants of the neurotoxicity of the amyloid beta peptide. Amyloid Fibril (dpeaa)DE-He213 Islet Amyloid Polypeptide (dpeaa)DE-He213 Amyloid Cascade Hypothesis (dpeaa)DE-He213 Solution Nuclear Magnetic Resonance (dpeaa)DE-He213 Mature Fibril (dpeaa)DE-He213 Rousseau, Frederic aut Schymkowitz, Joost aut Enthalten in Alzheimer's research & therapy London : BioMed Central, 2009 2(2010), 4 vom: 14. Juli (DE-627)605683557 (DE-600)2506521-X 1758-9193 nnns volume:2 year:2010 number:4 day:14 month:07 https://dx.doi.org/10.1186/alzrt36 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 2 2010 4 14 07
language	English
source	Enthalten in Alzheimer's research & therapy 2(2010), 4 vom: 14. Juli volume:2 year:2010 number:4 day:14 month:07
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container_title	Alzheimer's research & therapy
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author	Broersen, Kerensa
spellingShingle	Broersen, Kerensa misc Amyloid Fibril misc Islet Amyloid Polypeptide misc Amyloid Cascade Hypothesis misc Solution Nuclear Magnetic Resonance misc Mature Fibril The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation?
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topic_title	The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation? Amyloid Fibril (dpeaa)DE-He213 Islet Amyloid Polypeptide (dpeaa)DE-He213 Amyloid Cascade Hypothesis (dpeaa)DE-He213 Solution Nuclear Magnetic Resonance (dpeaa)DE-He213 Mature Fibril (dpeaa)DE-He213
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title	The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation?
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title_full	The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation?
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title_sort	culprit behind amyloid beta peptide related neurotoxicity in alzheimer's disease: oligomer size or conformation?
title_auth	The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation?
abstract	Abstract Since the reformulation of the amyloid cascade hypothesis to focus on oligomeric aggregates of amyloid beta as the prime toxic species causing Alzheimer's disease, many researchers refocused on detecting a specific molecular assembly of defined size thatis the main trigger of Alzheimer's disease. The result has been the identification of a host of molecular assemblies containing from two up to a hundred molecules of the amyloid beta peptide, which were all found to impair memory formation in mice. This clearly demonstrates that size is insufficient to define toxicity and peptide conformation has to be taken into account. In this review we discuss the interplay between oligomer size and peptide conformation as the key determinants of the neurotoxicity of the amyloid beta peptide. © BioMed Central Ltd 2010
abstractGer	Abstract Since the reformulation of the amyloid cascade hypothesis to focus on oligomeric aggregates of amyloid beta as the prime toxic species causing Alzheimer's disease, many researchers refocused on detecting a specific molecular assembly of defined size thatis the main trigger of Alzheimer's disease. The result has been the identification of a host of molecular assemblies containing from two up to a hundred molecules of the amyloid beta peptide, which were all found to impair memory formation in mice. This clearly demonstrates that size is insufficient to define toxicity and peptide conformation has to be taken into account. In this review we discuss the interplay between oligomer size and peptide conformation as the key determinants of the neurotoxicity of the amyloid beta peptide. © BioMed Central Ltd 2010
abstract_unstemmed	Abstract Since the reformulation of the amyloid cascade hypothesis to focus on oligomeric aggregates of amyloid beta as the prime toxic species causing Alzheimer's disease, many researchers refocused on detecting a specific molecular assembly of defined size thatis the main trigger of Alzheimer's disease. The result has been the identification of a host of molecular assemblies containing from two up to a hundred molecules of the amyloid beta peptide, which were all found to impair memory formation in mice. This clearly demonstrates that size is insufficient to define toxicity and peptide conformation has to be taken into account. In this review we discuss the interplay between oligomer size and peptide conformation as the key determinants of the neurotoxicity of the amyloid beta peptide. © BioMed Central Ltd 2010
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title_short	The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation?
url	https://dx.doi.org/10.1186/alzrt36
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