Research Topic

Structural and Molecular Biology of Alzheimer's Disease

About this Research Topic

Alzheimer’s disease (AD) is a complex disease affecting, directly and indirectly, millions of people worldwide. In AD brain, accumulation of senile plaques of amyloid-ß (Aß) and neurofibrillary tangles of tau have been observed as pathological hallmarks of Alzheimer’s disease for more than 100 years. However, it has been only in the last decades that the structural and molecular aspects of the disease become to be elucidated.
Familial cases of the disease have helped us discerning how the amyloid precursor protein (APP) cleaves into products that assemble into toxic amyloid oligomers, and structural studies are shedding light into the oligomerization process and the identification of the toxic conformations. Interaction of native Aβ molecules with modified forms of Aβ, has been identified in human amyloid plaques and leads to the initiation of pathological AD-like processes. At the same time, identification of tau mutations in AD-like diseases and the fact that tau pathology strongly correlates with Alzheimer’s disease progression has placed this protein on the focus of numerous molecular and structural studies to understand how post-translational modifications and different conformations lead to toxicity.
Therefore, the identification of specific molecular partners of Aβ and tau, the investigation of the species formed by processing of precursors and/or by their post-translational modifications, as well as the understanding of the molecular mechanism of their interactions in normal and pathological cases is important for creation of the effective methods of AD diagnostics and for the rational design of AD-modifying drugs aimed at blocking pathological Aβ or tau oligomerization and aggregation.
In addition, genomic studies on sporadic late-onset forms of the disease, which account for more than 95% of all cases, have recently brought many more players to the field and have uncovered new AD related proteins. Insights into APOE conformations, which have been strongly associated with AD, and into proteins coding for new AD risk genes such as BIN1, CLU, ABCA7, PICALM or TREM2, are helping to understand the etiology and pathogenic mechanisms, as well as expanding the research on AD to novel areas such as lipoprotein metabolism, neuroinflammation or endocytosis.
This research topic will focus on AD from the perspective of the molecules involved in its pathogenicity. It will bring together recent experimental studies and will review our current knowledge on the structure and molecular biology that is behind the disease mechanisms, aspects that are essential to define the therapeutic strategies for this disease.


Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.

Alzheimer’s disease (AD) is a complex disease affecting, directly and indirectly, millions of people worldwide. In AD brain, accumulation of senile plaques of amyloid-ß (Aß) and neurofibrillary tangles of tau have been observed as pathological hallmarks of Alzheimer’s disease for more than 100 years. However, it has been only in the last decades that the structural and molecular aspects of the disease become to be elucidated.
Familial cases of the disease have helped us discerning how the amyloid precursor protein (APP) cleaves into products that assemble into toxic amyloid oligomers, and structural studies are shedding light into the oligomerization process and the identification of the toxic conformations. Interaction of native Aβ molecules with modified forms of Aβ, has been identified in human amyloid plaques and leads to the initiation of pathological AD-like processes. At the same time, identification of tau mutations in AD-like diseases and the fact that tau pathology strongly correlates with Alzheimer’s disease progression has placed this protein on the focus of numerous molecular and structural studies to understand how post-translational modifications and different conformations lead to toxicity.
Therefore, the identification of specific molecular partners of Aβ and tau, the investigation of the species formed by processing of precursors and/or by their post-translational modifications, as well as the understanding of the molecular mechanism of their interactions in normal and pathological cases is important for creation of the effective methods of AD diagnostics and for the rational design of AD-modifying drugs aimed at blocking pathological Aβ or tau oligomerization and aggregation.
In addition, genomic studies on sporadic late-onset forms of the disease, which account for more than 95% of all cases, have recently brought many more players to the field and have uncovered new AD related proteins. Insights into APOE conformations, which have been strongly associated with AD, and into proteins coding for new AD risk genes such as BIN1, CLU, ABCA7, PICALM or TREM2, are helping to understand the etiology and pathogenic mechanisms, as well as expanding the research on AD to novel areas such as lipoprotein metabolism, neuroinflammation or endocytosis.
This research topic will focus on AD from the perspective of the molecules involved in its pathogenicity. It will bring together recent experimental studies and will review our current knowledge on the structure and molecular biology that is behind the disease mechanisms, aspects that are essential to define the therapeutic strategies for this disease.


Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.

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Submission Deadlines

30 November 2017 Manuscript
15 December 2017 Manuscript Extension

Participating Journals

Manuscripts can be submitted to this Research Topic via the following journals:

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Topic Editors

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Submission Deadlines

30 November 2017 Manuscript
15 December 2017 Manuscript Extension

Participating Journals

Manuscripts can be submitted to this Research Topic via the following journals:

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