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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 13 Apr 2015.

Microtubule-associated protein tau

MAPT, PHF-tau, FTDP-17
This gene encodes the microtubule-associated protein tau (MAPT) whose transcript undergoes complex, regulated alternative splicing, giving rise to several mRNA species. MAPT transcripts are differentially expressed in the nervous system, depending on stage of neuronal maturation and neuron type. MAPT gene mutations have been associated with several neurodegenerative disorders such as Alzheimer's disease, Pick's disease, frontotemporal dementia, cortico-basal degeneration and progressive supranuclear palsy. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: AGE, CAN, HAD, H1, APP
Papers using MAPT antibodies
PANTHER: a library of protein families and subfamilies indexed by function
Jackson George R. et al., In Human Molecular Genetics, 2002
... FTDP-17 mutations in tau transgenic mice provoke lysosomal abnormalities ...
Cortical amino acidergic pathways in Alzheimer's disease
DeFelipe Javier et al., In Frontiers in Neuroanatomy, 1986
... (VGLUT-1, 1:5,000, AB5905: Chemicon); parvalbumin (PV, 1:1,000, AB11427: Abcam, Cambridge, United Kingdom); and an anti-human PHF-tau monoclonal antibody (clone AT8, 1:100, MN1020: Thermo Scientific; Waltham, MA, USA) ...
Papers on MAPT
A strategy focused on MAPT, APP, NCSTN and BACE1 to build blood classifiers for Alzheimer's disease.
Emiliano Aranda-Abreu et al., Jalapa Enríquez, Mexico. In J Theor Biol, 08 May 2015
We focused on MAPT, APP, NCSTN and BACE1 as the basis to build and compare blood classifiers for AD.
Studying Tauopathies in Drosophila: A Fruitful Model.
Chen et al., Baltimore, United States. In Exp Neurol, 07 May 2015
UNASSIGNED: Tauopathies are a group of neurodegenerative disorders that include hereditary frontotemporal dementias (FTDs) such as FTD with parkinsonism linked to chromosome 17 (FTDP-17), as well as sporadic variants of FTDs like progressive supranuclear palsy (PSP), corticobasal degeneration (CBD), and Pick's disease.
In vivo characterization of chronic traumatic encephalopathy using [F-18]FDDNP PET brain imaging.
Kepe et al., Evanston, United States. In Proc Natl Acad Sci U S A, 06 May 2015
This particular [F-18]FDDNP PET imaging pattern in cases of suspected CTE also is primarily consistent with PHF-tau distribution observed at autopsy in subjects with a history of mild TBI and autopsy-confirmed diagnosis of CTE.
Human tau expression reduces adult neurogenesis in a mouse model of tauopathy.
Lamb et al., Cleveland, United States. In Neurobiol Aging, 09 Apr 2015
UNASSIGNED: Accumulation of hyperphosphorylated and aggregated microtubule-associated protein tau (MAPT) is a central feature of a class of neurodegenerative diseases termed tauopathies.
Presymptomatic cognitive and neuroanatomical changes in genetic frontotemporal dementia in the Genetic Frontotemporal dementia Initiative (GENFI) study: a cross-sectional analysis.
Rossor et al., London, United Kingdom. In Lancet Neurol, 31 Mar 2015
In about a third of patients, the disease is caused by autosomal dominant genetic mutations usually in one of three genes: progranulin (GRN), microtubule-associated protein tau (MAPT), or chromosome 9 open reading frame 72 (C9orf72).
A novel mutation P112H in the TARDBP gene associated with frontotemporal lobar degeneration without motor neuron disease and abundant neuritic amyloid plaques.
Grinberg et al., In Acta Neuropathol Commun, Dec 2014
The siblings presented with strikingly similar, although atypical, neuropathological features, including an unclassifiable TDP-43 inclusion pattern, a high burden of tau-negative β-amyloid neuritic plaques with an AD-like biochemical profile, and an unclassifiable 4-repeat tauopathy.
Huntington's disease is a four-repeat tauopathy with tau nuclear rods.
Lucas et al., Madrid, Spain. In Nat Med, Aug 2014
An imbalance of tau isoforms containing either three or four microtubule-binding repeats causes frontotemporal dementia with parkinsonism linked to chromosome 17 (FTDP-17) in families with intronic mutations in the MAPT gene.
Frontotemporal dementia and its subtypes: a genome-wide association study.
Momeni et al., Lubbock, United States. In Lancet Neurol, Jul 2014
Mutations in three genes-MAPT, GRN, and C9orf72--have been associated with FTD.
Frontotemporal lobar degeneration: a clinical approach.
Miller et al., San Francisco, United States. In Semin Neurol, Apr 2014
Parkinsonism presents in all syndromes, especially cases with tau pathology and MAPT or GRN mutations.
Genetics of dementia.
Kwok et al., Sydney, Australia. In Lancet, Apr 2014
In this Review, we focus on the evidence for, and the approach to, genetic testing in Alzheimer's disease (APP, PSEN1, and PSEN2 genes), frontotemporal dementia (MAPT, GRN, C9ORF72, and other genes), and other familial dementias.
Physiological and pathological phosphorylation of tau by Cdk5.
Hisanaga et al., Hachiōji, Japan. In Front Mol Neurosci, 2013
Hyperphosphorylation of microtubule-associated protein tau is one of the major pathological events in Alzheimer's disease (AD) and other related neurodegenerative diseases, including frontotemporal dementia with parkinsonism linked to chromosome 17 (FTDP-17).
Genetics and genomics of Parkinson's disease.
Farrer et al., Vancouver, Canada. In Genome Med, 2013
Recent discoveries in sporadic, Mendelian and more complex forms of parkinsonism provide novel insight into disease etiology; 28 genes, including those encoding alpha-synuclein (SNCA), leucine-rich repeat kinase 2 (LRRK2) and microtubule-associated protein tau (MAPT), have been linked and/or associated with PD.
Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of Parkinsonism.
Baekelandt et al., Leuven, Belgium. In Front Genet, 2013
Another gene, microtubule associated protein tau (MAPT), has been genetically linked to a dominant form of frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17) and genome-wide association studies report a strong association between MAPT and sporadic PD.
Tau pathology and neurodegeneration.
Goedert et al., Cambridge, United Kingdom. In Lancet Neurol, 2013
The pathway leading from soluble and monomeric to hyperphosphorylated, insoluble and filamentous tau protein is at the centre of many human neurodegenerative diseases, collectively referred to as tauopathies.
New perspective on parkinsonism in frontotemporal lobar degeneration.
Chung et al., South Korea. In J Mov Disord, 2013
The genes associated with parkinsonism are microtubule associated protein tau (MAPT), progranulin (GRN or PGRN), and chromosome 9 open reading frame 72 (C9ORF72) repeat expansion.
Dual-specificity tyrosine phosphorylation-regulated kinase 1A (Dyrk1A) modulates serine/arginine-rich protein 55 (SRp55)-promoted Tau exon 10 inclusion.
Liu et al., Nantong, China. In J Biol Chem, 2012
Phosphorylation of SRp55 by Dyrk1A suppressed its ability to promote Tau exon 10 inclusion.
Loss of fused in sarcoma (FUS) promotes pathological Tau splicing.
Edbauer et al., München, Germany. In Embo Rep, 2012
Tau mRNA is identified as a physiological splicing target of FUS.
Cyclic AMP-dependent protein kinase regulates 9G8-mediated alternative splicing of tau exon 10.
Liu et al., China. In Febs Lett, 2012
Cyclic AMP-dependent protein kinase regulates 9G8-mediated alternative splicing of tau exon 10
Acute administration of L-DOPA induces changes in methylation metabolites, reduced protein phosphatase 2A methylation, and hyperphosphorylation of Tau protein in mouse brain.
Sontag et al., Dallas, United States. In J Neurosci, 2012
These findings reveal a novel mechanism involving methylation-dependent pathways in L-dopa induces PP2A hypomethylation and increases Tau phosphorylation, which may be potentially detrimental to neuronal cells.
Fibril-forming motifs are essential and sufficient for the fibrillization of human Tau.
Liang et al., Wuhan, China. In Plos One, 2011
Fibril-forming motifs play a key role in the fibrillization of human Tau protein and could be the determinants of amyloidogenic proteins tending to misfold.
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