A. Kaganovich

发表

Phosphorylation of LRRK2 by casein kinase 1α regulates trans-Golgi clustering via differential interaction with ARHGEF7

M. Nalls, M. Cookson, Ruth Chia, 2014, Nature Communications.

Hexokinase activity is required for recruitment of parkin to depolarized mitochondria.

M. Cookson, I. Rudenko, A. Kaganovich, 2014, Human molecular genetics.

A Hexanucleotide Repeat Expansion in C9ORF72 Is the Cause of Chromosome 9p21-Linked ALS-FTD

David Heckerman, Lorne Zinman, Joanne Wuu, 2011, Neuron.

Convergence of signalling pathways in innate immune responses and genetic forms of Parkinson’s disease

A. Mamais, A. Kaganovich, K. Harvey, 2022, Neurobiology of Disease.

Differences in Stability, Activity and Mutation Effects Between Human and Mouse Leucine-Rich Repeat Kinase 2

M. Cookson, A. Dillman, I. Rudenko, 2018, Neurochemical Research.

The G2385R risk factor for Parkinson's disease enhances CHIP-dependent intracellular degradation of LRRK2.

A. Dillman, Ruth Chia, I. Rudenko, 2017, The Biochemical journal.

Divergent Effects of G2019S and R1441C LRRK2 Mutations on LRRK2 and Rab10 Phosphorylations in Mouse Tissues

M. Cookson, V. Baekelandt, L. Civiero, 2020, Cells.

Detection of endogenous S1292 LRRK2 autophosphorylation in mouse tissue as a readout for kinase activity

M. Cookson, A. Mamais, A. Kaganovich, 2018, npj Parkinson's Disease.

LRRK2 kinase activity regulates GCase level and enzymatic activity differently depending on cell type in Parkinson’s disease

L. Civiero, A. Kaganovich, L. Stefanis, 2022, NPJ Parkinson's disease.

Leucine-rich repeat kinase 2 controls protein kinase A activation state through phosphodiesterase 4

M. Cookson, G. Di Benedetto, L. Bubacco, 2018, Journal of Neuroinflammation.

A soluble α-synuclein construct forms a dynamic tetramer

Wei Wang, Gregory A Petsko, Dagmar Ringe, 2011, Proceedings of the National Academy of Sciences.

Association of a common genetic variant with Parkinson’s disease is mediated by microglia

A. Singleton, C. Blauwendraat, J. Gibbs, 2022, Science Translational Medicine.

Kinase activity is required for the toxic effects of mutant LRRK2/dardarin

David W. Miller, M. Cookson, M. Brug, 2006, Neurobiology of Disease.

High-frequency head impact causes chronic synaptic adaptation and long-term cognitive impairment in mice

J. Partridge, Jian-Young Wu, M. Cookson, 2021, Nature Communications.

LRRK2 kinase activity regulates GCase level and enzymatic activity differently depending on cell type in Parkinson’s disease

L. Civiero, A. Kaganovich, L. Stefanis, 2022, npj Parkinson's Disease.

The activities of LRRK2 and GCase are positively correlated in clinical biospecimens and experimental models of Parkinson’s disease

M. Cookson, L. Civiero, A. Kaganovich, 2021, bioRxiv.

LAG3 is not expressed in human and murine neurons and does not modulate α‐synucleinopathies

M. Cookson, S. Hornemann, A. Aguzzi, 2021, bioRxiv.

Unbiased screen for interactors of leucine-rich repeat kinase 2 supports a common pathway for sporadic and familial Parkinson disease

Suneil K. Kalia, M. Nalls, M. Cookson, 2014, Proceedings of the National Academy of Sciences.

TEP1, the yeast homolog of the human tumor suppressor gene PTEN/MMAC1/TEP1, is linked to the phosphatidylinositol pathway and plays a role in the developmental process of sporulation.

G. C. Johnston, G. Petsko, Hong Sun, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Pathogenic LRRK 2 mutations do not alter gene expression in cell model systems or human brain tissue

Michael J. Devine, M. Cookson, J. Hardy, 2017 .

Pathogenic LRRK2 Mutations Do Not Alter Gene Expression in Cell Model Systems or Human Brain Tissue

Michael J. Devine, M. Cookson, J. Hardy, 2011, PloS one.

The Parkinson Disease-associated Leucine-rich Repeat Kinase 2 (LRRK2) Is a Dimer That Undergoes Intramolecular Autophosphorylation*

M. Cookson, V. Baekelandt, S. Jain, 2008, Journal of Biological Chemistry.

Mutations in Auxilin cause parkinsonism via impaired clathrin-mediated trafficking at the Golgi apparatus and synapse

M. Cookson, J. Bonifacino, Chengyu Liu, 2019, bioRxiv.

Transcriptional signatures in iPSC-derived neurons are reproducible across labs when differentiation protocols are closely matched

M. Cookson, S. Finkbeiner, A. Kaganovich, 2021, Stem cell research.

Mutations in LRRK2/dardarin associated with Parkinson disease are more toxic than equivalent mutations in the homologous kinase LRRK1

M. P. van der Brug, A. Beilina, A. Kaganovich, 2007, Journal of neurochemistry.

Transcriptome analysis of LRRK2 knock-out microglia cells reveals alterations of inflammatory- and oxidative stress-related pathways upon treatment with α-synuclein fibrils

M. Cookson, L. Bubacco, A. Mamais, 2019, Neurobiology of Disease.

The Parkinson’s Disease Protein LRRK2 Interacts with the GARP Complex to Promote Retrograde Transport to the trans-Golgi Network

M. Cookson, J. Bonifacino, A. Beilina, 2020, Cell reports.

Leucine-rich repeat kinase 2 controls protein kinase A activation state through phosphodiesterase 4

M. Cookson, G. Di Benedetto, L. Bubacco, 2018, Journal of Neuroinflammation.

Extracellular clusterin limits the uptake of α‐synuclein fibrils by murine and human astrocytes

M. Cookson, L. Bubacco, A. Kaganovich, 2020, Glia.

Mutations in LRRK2 linked to Parkinson disease sequester Rab8a to damaged lysosomes and regulate transferrin-mediated iron uptake in microglia

A. Beilina, A. Mamais, A. Kaganovich, 2021, PLoS biology.

Pathogenic mutations in Leucine-rich repeat kinase 2 sequester Rab8a to damaged lysosomes and regulate transferrin-mediated iron uptake in microglia

M. Cookson, A. Beilina, A. Mamais, 2020, bioRxiv.

The Parkinson’s Disease P rotein LRRK2 Interacts with the GARP Complex to Promote Retrograde Transport to the trans-Golgi Network

M. Cookson, J. Bonifacino, A. Beilina, 2020 .

Detection of endogenous S1292 LRRK2 autophosphorylation in mouse tissue as a readout for kinase activity.

M. Cookson, A. Mamais, A. Kaganovich, 2018, NPJ Parkinson's disease.

The G2385R variant of leucine-rich repeat kinase 2 associated with Parkinson's disease is a partial loss-of-function mutation.

M. Cookson, Ruth Chia, I. Rudenko, 2012, The Biochemical journal.

The Parkinson's Disease Associated LRRK2 Exhibits Weaker In Vitro Phosphorylation of 4E-BP Compared to Autophosphorylation

M. Cookson, A. Beilina, A. Kaganovich, 2010, PloS one.

Molecular changes in the absence of severe pathology in the pulvinar in dementia with Lewy bodies

I. McKeith, A. Khundakar, P. Hanson, 2018, Movement disorders : official journal of the Movement Disorder Society.

LRRK2 mediates microglial neurotoxicity via NFATc2 in rodent models of synucleinopathies

A. Singleton, M. Cookson, E. Masliah, 2020, Science Translational Medicine.

LRRK2-mediated microglial activation via NFATc2: a novel mechanism of neurotoxic inflammation in synucleinopathies

E. Masliah, R. Rissman, A. Beilina, 2020, The Journal of Immunology.