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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

TAR DNA binding protein

TDP-43, TARDBP, TAR DNA-binding protein 43, TAR DNA-binding protein
HIV-1, the causative agent of acquired immunodeficiency syndrome (AIDS), contains an RNA genome that produces a chromosomally integrated DNA during the replicative cycle. Activation of HIV-1 gene expression by the transactivator Tat is dependent on an RNA regulatory element (TAR) located downstream of the transcription initiation site. The protein encoded by this gene is a transcriptional repressor that binds to chromosomally integrated TAR DNA and represses HIV-1 transcription. In addition, this protein regulates alternate splicing of the CFTR gene. A similar pseudogene is present on chromosome 20. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Als, FUS, CAN, AGE, Ubiquitin
Papers using TDP-43 antibodies
Divergent network connectivity changes in behavioural variant frontotemporal dementia and Alzheimer's disease
Supplier
Warren Jason D. et al., In Brain, 2009
... A primary antibody was applied recognizing the TDP-43 protein at amino acids 1–261 (1 : 800, Abnova).
Papers on TDP-43
Orthogonal matrix factorization enables integrative analysis of multiple RNA binding proteins.
New
Curk et al., Ljubljana, Slovenia. In Bioinformatics, Feb 2016
We have integrated the largest data compendium to date, which includes 31 CLIP experiments on 19 RBPs involved in splicing (such as hnRNPs, U2AF2, ELAVL1, TDP-43, and FUS) and processing of 3'UTR (Ago, IGF2BP).
New in vitro models to study amyotrophic lateral sclerosis.
New
Ferraiuolo et al., Sheffield, United Kingdom. In Brain Pathol, Feb 2016
The identification of mutations in transactive response DNA-binding protein gene (TARDBP), fused in sarcoma (FUS) and, more recently, a GGGGCC-hexanucleotide repeat expansion in chromosome 9 open reading frame 72 (C9ORF72) and their link with familial ALS have provided new avenues of investigation and hypotheses on the pathophysiology of this devastating disease.
Phosphorylation of TAR DNA-binding Protein of 43 kDa (TDP-43) by Truncated Casein Kinase 1δ Triggers Mislocalization and Accumulation of TDP-43.
New
Hasegawa et al., Tokyo, Japan. In J Biol Chem, Feb 2016
UNASSIGNED: Intracellular aggregates of phosphorylated TDP-43 are a major component of ubiquitin-positive inclusions in brains of patients with frontotemporal lobar degeneration (FTLD) and amyotrophic lateral sclerosis (ALS), and are considered a pathological hallmark.
Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA.
New
Impact
Hipp et al., Martinsried, Germany. In Science, Feb 2016
Here, we analyzed the compartment specificity of aggregate toxicity using artificial β-sheet proteins, as well as fragments of mutant huntingtin and TAR DNA binding protein-43 (TDP-43).
Large-scale screening in sporadic amyotrophic lateral sclerosis identifies genetic modifiers in C9orf72 repeat carriers.
New
van Es et al., Utrecht, Netherlands. In Neurobiol Aging, Jan 2016
To dissect the genetic architecture of sporadic ALS, we undertook a large sequencing study in 755 apparently sporadic ALS cases and 959 controls, analyzing 10 ALS genes: SOD1, C9orf72, TARDBP, FUS, ANG, CHMP2B, ATXN2, NIPA1, SMN1, and UNC13A.
[Spreading of protein misfolding: A new paradigm in neurology].
Review
New
Duyckaerts et al., Paris, France. In Rev Neurol (paris), Dec 2015
Lastly, the propagation may remain 'central' for TDP-43 in behavioral variant frontotemporal dementia, following only pathways of the encephalic neural network.
TDP-43 repression of nonconserved cryptic exons is compromised in ALS-FTD.
New
Impact
Wong et al., Baltimore, United States. In Science, Sep 2015
Cytoplasmic aggregation of TDP-43, accompanied by its nuclear clearance, is a key common pathological hallmark of amyotrophic lateral sclerosis and frontotemporal dementia (ALS-FTD).
Neurodegeneration. C9ORF72 repeat expansions in mice cause TDP-43 pathology, neuronal loss, and behavioral deficits.
New
Impact
Petrucelli et al., Jacksonville, United States. In Science, Jul 2015
Brains of 6-month-old mice contained nuclear RNA foci, inclusions of poly(Gly-Pro), poly(Gly-Ala), and poly(Gly-Arg) dipeptide repeat proteins, as well as TDP-43 pathology.
A liver-enriched long non-coding RNA, lncLSTR, regulates systemic lipid metabolism in mice.
New
Impact
Cao et al., Bethesda, United States. In Cell Metab, Apr 2015
LncLSTR forms a molecular complex with TDP-43 to regulate expression of Cyp8b1, a key enzyme in the bile acid synthesis pathway, and engenders an in vivo bile pool that induces apoC2 expression through FXR.
C9orf72 expansions in frontotemporal dementia and amyotrophic lateral sclerosis.
Review
New
Impact
Warren et al., London, United Kingdom. In Lancet Neurol, Mar 2015
Like in many patients with FTD and ALS, neuronal inclusions that contain TARDBP are seen, but are not universal, and the characteristic pathological finding is of dipeptide repeat (DPR) proteins, formed by unconventional repeat-associated non-ATG translation.
[RNA processing TDP-43 protein has a main pathological role in FTLD and ALS].
Review
Koza, In Postepy Biochem, 2014
TDP-43 is mainly a nuclear protein belonging to the heterogeneous ribonucleoproteins family.
ALS Patient Stem Cells for Unveiling Disease Signatures of Motoneuron Susceptibility: Perspectives on the Deadly Mitochondria, ER Stress and Calcium Triad.
Review
Sareen et al., Los Angeles, United States. In Front Cell Neurosci, 2014
Mutations in superoxide dismutase-1 (SOD1), TAR DNA-binding protein 43 (TARDBP/TDP-43) and C9orf72, have been identified in subsets of familial and sporadic patients.
The established and emerging roles of astrocytes and microglia in amyotrophic lateral sclerosis and frontotemporal dementia.
Review
Chung et al., Sydney, Australia. In Front Cell Neurosci, 2014
Recent genetic discoveries conclusively link the two diseases, and several common molecular players have been identified (TDP-43, FUS, C9ORF72).
Golgi Fragmentation in ALS Motor Neurons. New Mechanisms Targeting Microtubules, Tethers, and Transport Vesicles.
Review
Rabouille et al., Marseille, France. In Front Neurosci, 2014
Here, we present the different mechanisms that may underlie Golgi fragmentation in animal and cellular models of ALS linked to mutations in SOD1, TARDBP (TDP-43), VAPB, and C9Orf72 and we propose a novel one based on findings in progressive motor neuronopathy (pmn) mice.
Sporadic inclusion body myositis: clinical, pathological, and genetic analysis of eight Polish patients.
Kaminska et al., Warsaw, Poland. In Folia Neuropathol, 2014
Pathological deposits of TDP-43 were found in muscles in all sIBM as well as in control cases.
TDP-43: a new player on the AD field?
Review
GeneRIF
Wolozin et al., Boston, United States. In Exp Neurol, 2012
[review] TDP-43 may be linked to disease via loss-of-function mutations in which pathological TDP-43 fails to exercise its critical role in maintaining cellular homeostasis.
Cellular ageing, increased mortality and FTLD-TDP-associated neuropathology in progranulin knockout mice.
GeneRIF
Kumar-Singh et al., Antwerp, Belgium. In J Pathol, 2012
Progranulin deficiency in mice leads to reduced survival in adulthood and increased cellular ageing accompanied by hyperphosphorylation of TDP-43.
Targeted depletion of TDP-43 expression in the spinal cord motor neurons leads to the development of amyotrophic lateral sclerosis-like phenotypes in mice.
GeneRIF
Shen et al., Taipei, Taiwan. In J Biol Chem, 2012
loss of TDP-43 function could be one major cause for neurodegeneration in ALS with TDP-43 proteinopathies.
Autoregulation of TDP-43 mRNA levels involves interplay between transcription, splicing, and alternative polyA site selection.
GeneRIF
Baralle et al., Trieste, Italy. In Genes Dev, 2012
A complex interplay was uncovered between transcription, splicing, and 3' end processing to effect autoregulation of TDP-43.
ALS-associated ataxin 2 polyQ expansions enhance stress-induced caspase 3 activation and increase TDP-43 pathological modifications.
GeneRIF
Gitler et al., Stanford, United States. In J Neurosci, 2012
Ataxin 2 intermediate-length polyQ expansions contribute to amyotrophic lateral sclerosis-by enhancing stress-induced TDP-43 pathological modifications via caspase 3 activation.
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