Revisiting the Amyloid Cascade Hypothesis: From Anti-Aβ Therapeutics to Auspicious New Ways for Alzheimer’s Disease

Alzheimer’s disease (AD) is the most prevalent neurodegenerative disorder related to age, characterized by the cerebral deposition of fibrils, which are made from the amyloid-β (Aβ), a peptide of 40–42 amino acids. The conversion of Aβ into neurotoxic oligomeric, fibrillar, and protofibrillar assemb...
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Autor*in:	Md. Sahab Uddin [verfasserIn] Md. Tanvir Kabir [verfasserIn] Md. Sohanur Rahman [verfasserIn] Tapan Behl [verfasserIn] Philippe Jeandet [verfasserIn] Ghulam Md Ashraf [verfasserIn] Agnieszka Najda [verfasserIn] May N. Bin-Jumah [verfasserIn] Hesham R. El-Seedi [verfasserIn] Mohamed M. Abdel-Daim [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2020

Schlagwörter:	Aβ tau Alzheimer’s disease amyloid precursor protein aducanumab BAN2401

Übergeordnetes Werk:	In: International Journal of Molecular Sciences - MDPI AG, 2003, 21(2020), 16, p 5858
Übergeordnetes Werk:	volume:21 ; year:2020 ; number:16, p 5858

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc Journal toc

DOI / URN:	10.3390/ijms21165858

Katalog-ID:	DOAJ038682303

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spelling	10.3390/ijms21165858 doi (DE-627)DOAJ038682303 (DE-599)DOAJ7079fb3906ed4feba9d8e5d410f9987e DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Md. Sahab Uddin verfasserin aut Revisiting the Amyloid Cascade Hypothesis: From Anti-Aβ Therapeutics to Auspicious New Ways for Alzheimer’s Disease 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Alzheimer’s disease (AD) is the most prevalent neurodegenerative disorder related to age, characterized by the cerebral deposition of fibrils, which are made from the amyloid-β (Aβ), a peptide of 40–42 amino acids. The conversion of Aβ into neurotoxic oligomeric, fibrillar, and protofibrillar assemblies is supposed to be the main pathological event in AD. After Aβ accumulation, the clinical symptoms fall out predominantly due to the deficient brain clearance of the peptide. For several years, researchers have attempted to decline the Aβ monomer, oligomer, and aggregate levels, as well as plaques, employing agents that facilitate the reduction of Aβ and antagonize Aβ aggregation, or raise Aβ clearance from brain. Unluckily, broad clinical trials with mild to moderate AD participants have shown that these approaches were unsuccessful. Several clinical trials are running involving patients whose disease is at an early stage, but the preliminary outcomes are not clinically impressive. Many studies have been conducted against oligomers of Aβ which are the utmost neurotoxic molecular species. Trials with monoclonal antibodies directed against Aβ oligomers have exhibited exciting findings. Nevertheless, Aβ oligomers maintain equivalent states in both monomeric and aggregation forms; so, previously administered drugs that precisely decrease Aβ monomer or Aβ plaques ought to have displayed valuable clinical benefits. In this article, Aβ-based therapeutic strategies are discussed and several promising new ways to fight against AD are appraised. Aβ tau Alzheimer’s disease amyloid precursor protein aducanumab BAN2401 Biology (General) Chemistry Md. Tanvir Kabir verfasserin aut Md. Sohanur Rahman verfasserin aut Tapan Behl verfasserin aut Philippe Jeandet verfasserin aut Ghulam Md Ashraf verfasserin aut Agnieszka Najda verfasserin aut May N. Bin-Jumah verfasserin aut Hesham R. El-Seedi verfasserin aut Mohamed M. Abdel-Daim verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 21(2020), 16, p 5858 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:21 year:2020 number:16, p 5858 https://doi.org/10.3390/ijms21165858 kostenfrei https://doaj.org/article/7079fb3906ed4feba9d8e5d410f9987e kostenfrei https://www.mdpi.com/1422-0067/21/16/5858 kostenfrei https://doaj.org/toc/1661-6596 Journal toc kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ 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_70 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_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 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 21 2020 16, p 5858
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allfieldsGer	10.3390/ijms21165858 doi (DE-627)DOAJ038682303 (DE-599)DOAJ7079fb3906ed4feba9d8e5d410f9987e DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Md. Sahab Uddin verfasserin aut Revisiting the Amyloid Cascade Hypothesis: From Anti-Aβ Therapeutics to Auspicious New Ways for Alzheimer’s Disease 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Alzheimer’s disease (AD) is the most prevalent neurodegenerative disorder related to age, characterized by the cerebral deposition of fibrils, which are made from the amyloid-β (Aβ), a peptide of 40–42 amino acids. The conversion of Aβ into neurotoxic oligomeric, fibrillar, and protofibrillar assemblies is supposed to be the main pathological event in AD. After Aβ accumulation, the clinical symptoms fall out predominantly due to the deficient brain clearance of the peptide. For several years, researchers have attempted to decline the Aβ monomer, oligomer, and aggregate levels, as well as plaques, employing agents that facilitate the reduction of Aβ and antagonize Aβ aggregation, or raise Aβ clearance from brain. Unluckily, broad clinical trials with mild to moderate AD participants have shown that these approaches were unsuccessful. Several clinical trials are running involving patients whose disease is at an early stage, but the preliminary outcomes are not clinically impressive. Many studies have been conducted against oligomers of Aβ which are the utmost neurotoxic molecular species. Trials with monoclonal antibodies directed against Aβ oligomers have exhibited exciting findings. Nevertheless, Aβ oligomers maintain equivalent states in both monomeric and aggregation forms; so, previously administered drugs that precisely decrease Aβ monomer or Aβ plaques ought to have displayed valuable clinical benefits. In this article, Aβ-based therapeutic strategies are discussed and several promising new ways to fight against AD are appraised. Aβ tau Alzheimer’s disease amyloid precursor protein aducanumab BAN2401 Biology (General) Chemistry Md. Tanvir Kabir verfasserin aut Md. Sohanur Rahman verfasserin aut Tapan Behl verfasserin aut Philippe Jeandet verfasserin aut Ghulam Md Ashraf verfasserin aut Agnieszka Najda verfasserin aut May N. Bin-Jumah verfasserin aut Hesham R. El-Seedi verfasserin aut Mohamed M. Abdel-Daim verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 21(2020), 16, p 5858 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:21 year:2020 number:16, p 5858 https://doi.org/10.3390/ijms21165858 kostenfrei https://doaj.org/article/7079fb3906ed4feba9d8e5d410f9987e kostenfrei https://www.mdpi.com/1422-0067/21/16/5858 kostenfrei https://doaj.org/toc/1661-6596 Journal toc kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ 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_70 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_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 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 21 2020 16, p 5858
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language	English
source	In International Journal of Molecular Sciences 21(2020), 16, p 5858 volume:21 year:2020 number:16, p 5858
sourceStr	In International Journal of Molecular Sciences 21(2020), 16, p 5858 volume:21 year:2020 number:16, p 5858
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Aβ tau Alzheimer’s disease amyloid precursor protein aducanumab BAN2401 Biology (General) Chemistry
isfreeaccess_bool	true
container_title	International Journal of Molecular Sciences
authorswithroles_txt_mv	Md. Sahab Uddin @@aut@@ Md. Tanvir Kabir @@aut@@ Md. Sohanur Rahman @@aut@@ Tapan Behl @@aut@@ Philippe Jeandet @@aut@@ Ghulam Md Ashraf @@aut@@ Agnieszka Najda @@aut@@ May N. Bin-Jumah @@aut@@ Hesham R. El-Seedi @@aut@@ Mohamed M. Abdel-Daim @@aut@@
publishDateDaySort_date	2020-01-01T00:00:00Z
hierarchy_top_id	316340715
id	DOAJ038682303
language_de	englisch
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callnumber-first	Q - Science
author	Md. Sahab Uddin
spellingShingle	Md. Sahab Uddin misc QH301-705.5 misc QD1-999 misc Aβ misc tau misc Alzheimer’s disease misc amyloid precursor protein misc aducanumab misc BAN2401 misc Biology (General) misc Chemistry Revisiting the Amyloid Cascade Hypothesis: From Anti-Aβ Therapeutics to Auspicious New Ways for Alzheimer’s Disease
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topic_title	QH301-705.5 QD1-999 Revisiting the Amyloid Cascade Hypothesis: From Anti-Aβ Therapeutics to Auspicious New Ways for Alzheimer’s Disease Aβ tau Alzheimer’s disease amyloid precursor protein aducanumab BAN2401
topic	misc QH301-705.5 misc QD1-999 misc Aβ misc tau misc Alzheimer’s disease misc amyloid precursor protein misc aducanumab misc BAN2401 misc Biology (General) misc Chemistry
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title	Revisiting the Amyloid Cascade Hypothesis: From Anti-Aβ Therapeutics to Auspicious New Ways for Alzheimer’s Disease
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title_full	Revisiting the Amyloid Cascade Hypothesis: From Anti-Aβ Therapeutics to Auspicious New Ways for Alzheimer’s Disease
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author_browse	Md. Sahab Uddin Md. Tanvir Kabir Md. Sohanur Rahman Tapan Behl Philippe Jeandet Ghulam Md Ashraf Agnieszka Najda May N. Bin-Jumah Hesham R. El-Seedi Mohamed M. Abdel-Daim
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title_sort	revisiting the amyloid cascade hypothesis: from anti-aβ therapeutics to auspicious new ways for alzheimer’s disease
callnumber	QH301-705.5
title_auth	Revisiting the Amyloid Cascade Hypothesis: From Anti-Aβ Therapeutics to Auspicious New Ways for Alzheimer’s Disease
abstract	Alzheimer’s disease (AD) is the most prevalent neurodegenerative disorder related to age, characterized by the cerebral deposition of fibrils, which are made from the amyloid-β (Aβ), a peptide of 40–42 amino acids. The conversion of Aβ into neurotoxic oligomeric, fibrillar, and protofibrillar assemblies is supposed to be the main pathological event in AD. After Aβ accumulation, the clinical symptoms fall out predominantly due to the deficient brain clearance of the peptide. For several years, researchers have attempted to decline the Aβ monomer, oligomer, and aggregate levels, as well as plaques, employing agents that facilitate the reduction of Aβ and antagonize Aβ aggregation, or raise Aβ clearance from brain. Unluckily, broad clinical trials with mild to moderate AD participants have shown that these approaches were unsuccessful. Several clinical trials are running involving patients whose disease is at an early stage, but the preliminary outcomes are not clinically impressive. Many studies have been conducted against oligomers of Aβ which are the utmost neurotoxic molecular species. Trials with monoclonal antibodies directed against Aβ oligomers have exhibited exciting findings. Nevertheless, Aβ oligomers maintain equivalent states in both monomeric and aggregation forms; so, previously administered drugs that precisely decrease Aβ monomer or Aβ plaques ought to have displayed valuable clinical benefits. In this article, Aβ-based therapeutic strategies are discussed and several promising new ways to fight against AD are appraised.
abstractGer	Alzheimer’s disease (AD) is the most prevalent neurodegenerative disorder related to age, characterized by the cerebral deposition of fibrils, which are made from the amyloid-β (Aβ), a peptide of 40–42 amino acids. The conversion of Aβ into neurotoxic oligomeric, fibrillar, and protofibrillar assemblies is supposed to be the main pathological event in AD. After Aβ accumulation, the clinical symptoms fall out predominantly due to the deficient brain clearance of the peptide. For several years, researchers have attempted to decline the Aβ monomer, oligomer, and aggregate levels, as well as plaques, employing agents that facilitate the reduction of Aβ and antagonize Aβ aggregation, or raise Aβ clearance from brain. Unluckily, broad clinical trials with mild to moderate AD participants have shown that these approaches were unsuccessful. Several clinical trials are running involving patients whose disease is at an early stage, but the preliminary outcomes are not clinically impressive. Many studies have been conducted against oligomers of Aβ which are the utmost neurotoxic molecular species. Trials with monoclonal antibodies directed against Aβ oligomers have exhibited exciting findings. Nevertheless, Aβ oligomers maintain equivalent states in both monomeric and aggregation forms; so, previously administered drugs that precisely decrease Aβ monomer or Aβ plaques ought to have displayed valuable clinical benefits. In this article, Aβ-based therapeutic strategies are discussed and several promising new ways to fight against AD are appraised.
abstract_unstemmed	Alzheimer’s disease (AD) is the most prevalent neurodegenerative disorder related to age, characterized by the cerebral deposition of fibrils, which are made from the amyloid-β (Aβ), a peptide of 40–42 amino acids. The conversion of Aβ into neurotoxic oligomeric, fibrillar, and protofibrillar assemblies is supposed to be the main pathological event in AD. After Aβ accumulation, the clinical symptoms fall out predominantly due to the deficient brain clearance of the peptide. For several years, researchers have attempted to decline the Aβ monomer, oligomer, and aggregate levels, as well as plaques, employing agents that facilitate the reduction of Aβ and antagonize Aβ aggregation, or raise Aβ clearance from brain. Unluckily, broad clinical trials with mild to moderate AD participants have shown that these approaches were unsuccessful. Several clinical trials are running involving patients whose disease is at an early stage, but the preliminary outcomes are not clinically impressive. Many studies have been conducted against oligomers of Aβ which are the utmost neurotoxic molecular species. Trials with monoclonal antibodies directed against Aβ oligomers have exhibited exciting findings. Nevertheless, Aβ oligomers maintain equivalent states in both monomeric and aggregation forms; so, previously administered drugs that precisely decrease Aβ monomer or Aβ plaques ought to have displayed valuable clinical benefits. In this article, Aβ-based therapeutic strategies are discussed and several promising new ways to fight against AD are appraised.
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title_short	Revisiting the Amyloid Cascade Hypothesis: From Anti-Aβ Therapeutics to Auspicious New Ways for Alzheimer’s Disease
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