Kanae Iijima-Ando

发表

Drosophila models of Alzheimer's amyloidosis: the challenge of dissecting the complex mechanisms of toxicity of amyloid-beta 42.

Koichi M Iijima, Kanae Iijima-Ando, Koichi Iijima, 2008, Journal of Alzheimer's disease : JAD.

JNK/FOXO-mediated Neuronal Expression of Fly Homologue of Peroxiredoxin II Reduces Oxidative Stress and Extends Life Span*

W. Lee, Koichi M Iijima, Kanae Iijima-Ando, 2009, The Journal of Biological Chemistry.

Transgenic cAMP response element reporter flies for monitoring circadian rhythms.

Kanae Iijima-Ando, J. Yin, 2005, Methods in enzymology.

Interaction of N-Terminal Acetyltransferase with the Cytoplasmic Domain of β-Amyloid Precursor Protein and Its Effect on Aβ Secretion

Y. Kirino, Toshiharu Suzuki, M. Asaumi, 2005 .

Interaction of N-terminal acetyltransferase with the cytoplasmic domain of beta-amyloid precursor protein and its effect on A beta secretion.

Y. Kirino, Toshiharu Suzuki, M. Asaumi, 2005, Journal of biochemistry.

Tau Ser262 phosphorylation is critical for Abeta42-induced tau toxicity in a transgenic Drosophila model of Alzheimer's disease.

Kanae Iijima-Ando, A. Gatt, Koichi M. Iijima, 2010, Human molecular genetics.

Tau Ser 262 phosphorylation is critical for A b 42-induced tau toxicity in a transgenic Drosophila model of Alzheimer ’ s disease

Kanae Iijima-Ando, A. Gatt, Koichi M. Iijima, 2010 .

Membrane-Microdomain Localization of Amyloid β-Precursor Protein (APP) C-terminal Fragments Is Regulated by Phosphorylation of the Cytoplasmic Thr668 Residue*

Toshiharu Suzuki, J. Elliott, M. Nishimura, 2012, The Journal of Biological Chemistry.

Residue 668 Phosphorylation of the Cytoplasmic Thr C-terminal Fragments Is Regulated by-Precursor Protein ( APP ) β Amyloid Membrane-Microdomain Localization of Molecular Bases of Disease :

Toshiharu Suzuki, J. Elliott, M. Nishimura, 2012 .

Transgenic Drosophila models of Alzheimer’s disease and tauopathies

Kanae Iijima-Ando, Koichi M. Iijima, 2010, Brain Structure and Function.

Drosophila Model of Alzheimer’s Amyloidosis

Y. Zhong, Kanae Iijima-Ando, Koichi M. Iijima, 2009 .

cAMP-response element-binding protein and heat-shock protein 70 additively suppress polyglutamine-mediated toxicity in Drosophila.

Priscilla Wu, E. Drier, Kanae Iijima-Ando, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Loss of Axonal Mitochondria Promotes Tau-Mediated Neurodegeneration and Alzheimer's Disease–Related Tau Phosphorylation Via PAR-1

E. Suzuki, B. Lu, Kanae Iijima-Ando, 2012, PLoS genetics.

Overexpression of Neprilysin Reduces Alzheimer Amyloid-β42 (Aβ42)-induced Neuron Loss and Intraneuronal Aβ42 Deposits but Causes a Reduction in cAMP-responsive Element-binding Protein-mediated Transcription, Age-dependent Axon Pathology, and Premature Death in Drosophila*

I. Hakker, Y. Zhong, Stephen A Hearn, 2008, Journal of Biological Chemistry.

Aβ42 Mutants with Different Aggregation Profiles Induce Distinct Pathologies in Drosophila

I. Hakker, Y. Zhong, Stephen A Hearn, 2008, PloS one.

A DNA damage-activated checkpoint kinase phosphorylates tau and enhances tau-induced neurodegeneration.

Kanae Iijima-Ando, A. Gatt, Lijuan Zhao, 2010, Human molecular genetics.

Mitochondrial Mislocalization Underlies Aβ42-Induced Neuronal Dysfunction in a Drosophila Model of Alzheimer's Disease

Stephen A Hearn, Kanae Iijima-Ando, A. Gatt, 2009, PloS one.

Regulation of Energy Stores and Feeding by Neuronal and Peripheral CREB Activity in Drosophila

Kanae Iijima-Ando, Lijuan Zhao, Koichi M. Iijima, 2009, PloS one.

Physiological Mouse Brain Aβ Levels Are Not Related to the Phosphorylation State of Threonine-668 of Alzheimer's APP

Y. Sano, S. Itohara, S. Takeda, 2006, PloS one.

Tau Ser262 phosphorylation is critical for Abeta42-induced tau toxicity in a transgenic Drosophila model of Alzheimer's disease.

Kanae Iijima-Ando, A. Gatt, Koichi M. Iijima, 2010, Human molecular genetics.

Aβ42 Mutants with Different Aggregation Profiles Induce Distinct Pathologies in Drosophila

I. Hakker, Y. Zhong, Kanae Iijima-Ando, 2008, PloS one.