Pub Date : 2003-01-31DOI: 10.2174/1567204043396514
K. Conway, E. W. Baxter, K. Felsenstein, A. Reitz
Alzheimers Disease (AD) is a progressive neurodegenerative disorder marked by loss of memory, cognition, and behavioral stability. AD is defined pathologically by extracellular neuritic plaques comprised of fibrillar deposits of β-amyloid peptide (Aβ) and neurofibrillary tangles comprised of paired helical filaments of hyperphosphorylated tau. Current therapies for AD, such as cholinesterase inhibitors, treat the symptoms but do not modify the progression of the disease. The etiology of AD is unclear. However, data from familial AD mutations (FAD) strongly support the “amyloid cascade hypothesis” of AD, i.e. that neurodegeneration in AD is initiated by the formation of neurotoxic β-amyloid (Aβ) aggregates, all FAD mutations increase levels of Aβ peptide or density of Aβ deposits. The likely link between Aβ aggregation and AD pathology emphasizes the need for a better understanding of the mechanisms of Aβ production. This review summarizes current therapeutic strategies directed at lowering Aβ levels and decreasing levels of toxic Aβ aggregates through (1) inhibition of the processing of amyloid precursor protein (APP) to Aβ peptide, (2) inhibition, reversal or clearance of Aβ aggregation, (3) cholesterol reduction and (4) Aβ immunization.
{"title":"Emerging β-Amyloid Therapies for the Treatment of Alzheimer's Disease","authors":"K. Conway, E. W. Baxter, K. Felsenstein, A. Reitz","doi":"10.2174/1567204043396514","DOIUrl":"https://doi.org/10.2174/1567204043396514","url":null,"abstract":"Alzheimers Disease (AD) is a progressive neurodegenerative disorder marked by loss of memory, cognition, and behavioral stability. AD is defined pathologically by extracellular neuritic plaques comprised of fibrillar deposits of β-amyloid peptide (Aβ) and neurofibrillary tangles comprised of paired helical filaments of hyperphosphorylated tau. Current therapies for AD, such as cholinesterase inhibitors, treat the symptoms but do not modify the progression of the disease. The etiology of AD is unclear. However, data from familial AD mutations (FAD) strongly support the “amyloid cascade hypothesis” of AD, i.e. that neurodegeneration in AD is initiated by the formation of neurotoxic β-amyloid (Aβ) aggregates, all FAD mutations increase levels of Aβ peptide or density of Aβ deposits. The likely link between Aβ aggregation and AD pathology emphasizes the need for a better understanding of the mechanisms of Aβ production. This review summarizes current therapeutic strategies directed at lowering Aβ levels and decreasing levels of toxic Aβ aggregates through (1) inhibition of the processing of amyloid precursor protein (APP) to Aβ peptide, (2) inhibition, reversal or clearance of Aβ aggregation, (3) cholesterol reduction and (4) Aβ immunization.","PeriodicalId":286890,"journal":{"name":"Frontiers in Medicinal Chemistry - Online","volume":"1 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2003-01-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"116468102","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1900-01-01DOI: 10.2174/1567204052931078
A. Gruber, S. Hanson
{"title":"Potential New Targets for Antithrombotic Therapy","authors":"A. Gruber, S. Hanson","doi":"10.2174/1567204052931078","DOIUrl":"https://doi.org/10.2174/1567204052931078","url":null,"abstract":"","PeriodicalId":286890,"journal":{"name":"Frontiers in Medicinal Chemistry - Online","volume":"9 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"127307004","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1900-01-01DOI: 10.2174/1567204052931023
C. Dinsmore, I. M. Bell
{"title":"Inhibitors of Farnesyltransferase and Geranylgeranyltransferase-I for Antitumor Therapy: Substrate-Based Design, Conformational Constraint and Biological Activity","authors":"C. Dinsmore, I. M. Bell","doi":"10.2174/1567204052931023","DOIUrl":"https://doi.org/10.2174/1567204052931023","url":null,"abstract":"","PeriodicalId":286890,"journal":{"name":"Frontiers in Medicinal Chemistry - Online","volume":"C-31 2","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"132502754","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1900-01-01DOI: 10.2174/1567204043396451
C. Metcalf, M. V. Schravendijk, D. Dalgarno, T. Sawyer
{"title":"Targeting Protein Kinases for Bone Disease: Discovery and Development of Src Inhibitors","authors":"C. Metcalf, M. V. Schravendijk, D. Dalgarno, T. Sawyer","doi":"10.2174/1567204043396451","DOIUrl":"https://doi.org/10.2174/1567204043396451","url":null,"abstract":"","PeriodicalId":286890,"journal":{"name":"Frontiers in Medicinal Chemistry - Online","volume":"64 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"132531238","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1900-01-01DOI: 10.2174/1567204043396389
A. Wagman, J. Nuss
{"title":"Current Therapies and Emerging Targets for the Treatment of Diabetes","authors":"A. Wagman, J. Nuss","doi":"10.2174/1567204043396389","DOIUrl":"https://doi.org/10.2174/1567204043396389","url":null,"abstract":"","PeriodicalId":286890,"journal":{"name":"Frontiers in Medicinal Chemistry - Online","volume":"24 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"133797612","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1900-01-01DOI: 10.2174/1567204043396398
J. Barchi, N. Neamati
{"title":"New Paradigms in Drug Design and Discovery","authors":"J. Barchi, N. Neamati","doi":"10.2174/1567204043396398","DOIUrl":"https://doi.org/10.2174/1567204043396398","url":null,"abstract":"","PeriodicalId":286890,"journal":{"name":"Frontiers in Medicinal Chemistry - Online","volume":"1 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"129693223","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1900-01-01DOI: 10.2174/1567204052931122
J. Arts, S. D. Schepper, K. V. Emelen
{"title":"Histone Deacetylase Inhibitors: From Chromatin Remodelling to Experimental Cancer Therapeutics","authors":"J. Arts, S. D. Schepper, K. V. Emelen","doi":"10.2174/1567204052931122","DOIUrl":"https://doi.org/10.2174/1567204052931122","url":null,"abstract":"","PeriodicalId":286890,"journal":{"name":"Frontiers in Medicinal Chemistry - Online","volume":"18 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"121930187","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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