The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production (Q24309767)

Erratum: The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-β production

GOA release 2020-03-11

corrigendum / erratum

1 reference

12 July 2019

http://api.crossref.org/works?select=update-to&filter=doi:10.1038/NATURE05606

author name string

Lucia Pastorino

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Anyang Sun

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Pei-Jung Lu

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Xiao Zhen Zhou

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Martin Balastik

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Greg Finn

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Gerburg Wulf

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Jormay Lim

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Shi-Hua Li

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Xiaojiang Li

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Weiming Xia

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Linda K Nicholson

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Kun Ping Lu

Pathways towards and away from Alzheimer's disease

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language of work or name

English

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publication date

23 March 2006

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published in

Nature

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volume

440

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issue

7083

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page(s)

528-34

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APP processing is regulated by cytoplasmic phosphorylation

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Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism

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The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein

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Pin1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and tau proteins

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Pin1 acts catalytically to promote a conformational change in Cdc25.

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Role of the prolyl isomerase Pin1 in protecting against age-dependent neurodegeneration.

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Evidence for a novel late-onset Alzheimer disease locus on chromosome 19p13.2.

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Intraneuronal Alzheimer abeta42 accumulates in multivesicular bodies and is associated with synaptic pathology

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Phosphorylation-induced structural changes in the amyloid precursor protein cytoplasmic tail detected by NMR.

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Transient structure of the amyloid precursor protein cytoplasmic tail indicates preordering of structure for binding to cytosolic factors

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Function of WW domains as phosphoserine- or phosphothreonine-binding modules

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Role of Phosphorylation in Determining the Backbone Dynamics of the Serine/Threonine-Proline Motif and Pin1 Substrate Recognition†

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1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides

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Modeling breast cancer in vivo and ex vivo reveals an essential role of Pin1 in tumorigenesis

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BACE (beta-secretase) modulates the processing of APLP2 in vivo

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Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid beta-protein in both transfected cells and transgenic mice

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Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease

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Correlative Memory Deficits, Abeta Elevation, and Amyloid Plaques in Transgenic Mice

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Pin1 regulates centrosome duplication, and its overexpression induces centrosome amplification, chromosome instability, and oncogenesis

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