Physiological Functions of APP Family Proteins | Zendy

Ulrike Müller | Zendy; Hui Zheng | Zendy

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Physiological Functions of APP Family Proteins

Author(s) -

Ulrike Müller,

Hui Zheng

Publication year - 2011

Publication title -

cold spring harbor perspectives in medicine

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.853

H-Index - 105

eISSN - 2472-5412

pISSN - 2157-1422

DOI - 10.1101/cshperspect.a006288

Subject(s) - amyloid precursor protein , cerebral amyloid angiopathy , context (archaeology) , neuroscience , disease , alzheimer's disease , amyloid (mycology) , biology , point mutation , mutation , medicine , bioinformatics , genetics , dementia , gene , pathology , paleontology

Biochemical and genetic evidence establishes a central role of the amyloid precursor protein (APP) in Alzheimer disease (AD) pathogenesis. Biochemically, deposition of the β-amyloid (Aβ) peptides produced from proteolytic processing of APP forms the defining pathological hallmark of AD; genetically, both point mutations and duplications of wild-type APP are linked to a subset of early onset of familial AD (FAD) and cerebral amyloid angiopathy. As such, the biological functions of APP and its processing products have been the subject of intense investigation, and the past 20+ years of research have met with both excitement and challenges. This article will review the current understanding of the physiological functions of APP in the context of APP family members.

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