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PINK1 encodes a serine/threonine protein kinase that localizes to mitochondria. Zusätzlich bieten wir Ihnen PINK1 Proteine (13) und und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 239 products:
Human Polyclonal PINK1 Primary Antibody für ELISA, ICC - ABIN249446
Weihofen, Ostaszewski, Minami, Selkoe: Pink1 Parkinson mutations, the Cdc37/Hsp90 chaperones and Parkin all influence the maturation or subcellular distribution of Pink1. in Human molecular genetics 2008
Show all 85 Pubmed References
Human Polyclonal PINK1 Primary Antibody für WB - ABIN151937
Meijer, Karimi-Busheri, Huang, Weinfeld, Young: Pnk1, a DNA kinase/phosphatase required for normal response to DNA damage by gamma-radiation or camptothecin in Schizosaccharomyces pombe. in The Journal of biological chemistry 2002
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Human Polyclonal PINK1 Primary Antibody für WB - ABIN1882117
Rogaeva, Johnson, Lang, Gulick, Gwinn-Hardy, Kawarai, Sato, Morgan, Werner, Nussbaum, Petit, Okun, McInerney, Mandel, Groen, Fernandez, Postuma, Foote: Analysis of the PINK1 gene in a large cohort of cases with Parkinson disease. in Archives of neurology 2004
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Human Polyclonal PINK1 Primary Antibody für SimWes, WB - ABIN152067
Xiong, Wang, Chen, Choo, Ma, Tang, Xia, Jiang, Ronai, Zhuang, Zhang: Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradation. in The Journal of clinical investigation 2009
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Human Monoclonal PINK1 Primary Antibody für IHC, WB - ABIN2115285
Zhou, Huang, Shao, May, Prou, Perier, Dauer, Schon, Przedborski: The kinase domain of mitochondrial PINK1 faces the cytoplasm. in Proceedings of the National Academy of Sciences of the United States of America 2008
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Human Polyclonal PINK1 Primary Antibody für ELISA, WB - ABIN566297
Liu, Ye, Miller, Yuan, Zhang, Tian, Nie, Imae, Arai, Li, Cheng, Shi: Ablation of ALCAT1 mitigates hypertrophic cardiomyopathy through effects on oxidative stress and mitophagy. in Molecular and cellular biology 2012
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Human Polyclonal PINK1 Primary Antibody für WB - ABIN652208
Berthier, Jiménez-Sáinz, Pulido: PINK1 regulates histone H3 trimethylation and gene expression by interaction with the polycomb protein EED/WAIT1. in Proceedings of the National Academy of Sciences of the United States of America 2013
Human Monoclonal PINK1 Primary Antibody für ICC, IF - ABIN4345677
Ko, Park, Park, Koh: PPAR-γ activation attenuates deltamethrin-induced apoptosis by regulating cytosolic PINK1 and inhibiting mitochondrial dysfunction. in Toxicology letters 2016
Drosophila CHIP protects against mitochondrial dysfunction by acting downstream of Pink1 in parallel with Parkin (zeige PARK2 Antikörper)
Maintenance of tissue homeostasis upon reduction of Pink1 or Parkin (zeige PARK2 Antikörper) appears to result from reduction of age- and stress-induced intestinal stem cell proliferation, in part, through induction of ISC senescence.
activation of endoplasmic reticulum stress by defective mitochondria is neurotoxic in pink1 and parkin (zeige PARK2 Antikörper) flies and that the reduction of this signalling is neuroprotective, independently of defective mitochondria.
autophosphorylation of PINK1 is essential for the mitochondrial translocation of Parkin (zeige PARK2 Antikörper) and for subsequent phosphorylation and activation of Parkin (zeige PARK2 Antikörper).
A pink1 genomic knock-in allele was generated to monitor the dynamic expression pattern of PINK1. The spatiotemporal expression pattern of PINK1 correlates with the cell-type specific mitochondrial clearance or persistence. PINK1 and PARKIN (zeige PARK2 Antikörper) function epistatically to mediate timely specific mitophagy during Drosophila midgut metamorphosis.
Our data indicate that PINK1 and Parkin (zeige PARK2 Antikörper) play an important role in FUS (zeige FUS Antikörper)-induced neurodegeneration. This study has uncovered a previously unknown link between FUS (zeige FUS Antikörper) proteinopathy and PINK1/Parkin (zeige PARK2 Antikörper) genes, providing new insights into the pathogenesis of FUS (zeige FUS Antikörper) proteinopathy.
we show that overexpression of Drosophila Clu (zeige CLU Antikörper) complements PINK1, but not parkin (zeige PARK2 Antikörper), mutant muscles. Thus, Clu (zeige CLU Antikörper) is essential for mitochondrial homeostasis and functions in concert with Parkin (zeige PARK2 Antikörper) and VCP (zeige vcp Antikörper) for Marf (zeige MFN2 Antikörper) degradation to promote damaged mitochondrial clearance.
In addition, a PINK1 mutant, which induced mitochondrial enlargement and had been considered as a Drosophila model of Parkinson's disease (PD), caused fly muscle defects, and the loss of vimar could rescue these defects. Furthermore, we found that the mammalian homolog of Vimar, RAP1GDS1 (zeige RAP1GDS1 Antikörper), played a similar role in regulating mitochondrial morphology, suggesting a functional conservation of this GEF (zeige SLC2A4RG Antikörper) member.
Buffy has a role enhancing the loss of parkin (zeige PARK2 Antikörper) and suppressing the loss of Pink1 phenotypes in Drosophila
PINK1-dependent mitophagy suppresses neural neurodegeneration by removing damaged mitochondria.
Pink1-depleted zebrafish are the first vertebrate model of PINK1 deficiency with loss of dopaminergic neurons.
Our findings suggest that a lack of pink1 in zebrafish alters many vital and critical pathways in addition to the HIF signaling pathway.
Distinct groups of dopaminergic neurons are sensitive to targeted loss of Pink1 factor in a morphant fish model of toxin-induced Parkinson's disease.
Morpholino-mediated loss of pink1 function in zebrafish profoundly affects the development of dopaminergic neurons in the ventral diencephalon and affects behaviour of the zebrafish larvae, namely their response to tactile stimuli and locomotor behavior.
Here we review the evidence supporting PINK1/Parkin (zeige PARK2 Antikörper) mitophagy in vivo and its causative role in neurodegeneration, and outline outstanding questions for future investigations.
PINK1 utilises a lowly populated yet more suitable C-terminally retracted (Ub-CR) conformation of Ub for efficient phosphorylation.
PINK1 was downregulated in the brains of patients with Alzheimer's disease.
PINK1 mutation is associated with Alzheimer disease.
PINK1 silencing impaired BECN1 (zeige BECN1 Antikörper) enrichment at mitochondria-associated membranes independently of PARK2 (zeige PARK2 Antikörper), suggesting a novel role for PINK1 in regulating mitophagy.
an impaired PINK1-PARK2 (zeige PARK2 Antikörper)-mediated neuroimmunology pathway contributes to septic death.
We demonstrated that miR (zeige MLXIP Antikörper)-27a and miR (zeige MLXIP Antikörper)-27b regulate PINK1 expression and autophagic clearance of damaged mitochondria
The effects of variants in the Parkin (zeige PARK2 Antikörper), PINK1, and DJ-1 (zeige PARK7 Antikörper) genes along with evidence for their pathogenicity have been summarized. (Review)
data suggest that ROS (zeige ROS1 Antikörper) may act as a trigger for the induction of Parkin (zeige PARK2 Antikörper)/PINK1-dependent mitophagy.
Adipogenic process can be dissected into 3 stages according to the participation of PARL (zeige PARL Antikörper)-PINK1-Parkin (zeige PARK2 Antikörper) system. Findings reveal the sequential adipogenic events directed by PARL (zeige PARL Antikörper)-PINK1-Parkin (zeige PARK2 Antikörper) system, add more evidence supporting the convergence of pathogenesis leading to neurodegenerative and metabolic disease
Loss of Atad3a (zeige ATAD3A Antikörper) caused accumulation of Pink1 and activated mitophagy.
PTEN-induced putative kinase 1 interacts with and phosphorylates serines 322 and 613 of PARIS to control its ubiquitination and clearance by parkin (zeige PARK2 Antikörper). PINK1 phosphorylation of PARIS alleviates PARIS toxicity, as well as repression of PGC-1alpha (zeige PPARGC1A Antikörper) promoter activity.
Findings highlight a novel mechanism by which PINK1-dependent signalling promotes the rescue of amyloid pathology and amyloid-beta-mediated mitochondrial and synaptic dysfunctions in a transgenic mouse Alzheimer's disease model.
study identifies a new role of Dual-AKAP1 (zeige AKAP1 Antikörper) in regulating mitochondrial trafficking through Miro-2 (zeige RHOT2 Antikörper), and supports a model in which PINK1 and mitochondrial PKA participate in a similar neuroprotective signaling pathway to maintain dendrite connectivity
Study showed that apoptosis is an important form of cellular degeneration in lipopolysaccharide (LPS (zeige TLR4 Antikörper)-sensitized hypoxic-ischemic (HI) injury in the immature brain. Loss of PINK1 can protect the immature brain against cell apoptosis induced by LPS (zeige TLR4 Antikörper)-sensitized HI injury. Moreover, alpha-Syn plays a neuroprotective role in LPS (zeige TLR4 Antikörper)-sensitized HI brain damage in PINK1-knockout neonatal mice
the results suggest that BNIP3 (zeige BNIP3 Antikörper) plays a vital role in regulating PINK1 mitochondrial outer membrane localization, the proteolytic process of PINK1 and PINK1/parkin (zeige PARK2 Antikörper)-mediated mitophagy under physiological conditions.
lack of PINK1 causes increased excitatory transmission and neurotransmitter release in the hippocampus, which might lead to the cognitive decline often observed in Parkinson's disease
The identification of PINK1 and Parkin (zeige PARK2 Antikörper) as suppressors of an immune-response-eliciting pathway provoked by inflammation suggests new insights into Parkinson's disease pathology.
PINK1 deficiency causes defects in GFAP (zeige GFAP Antikörper)-positive astrogliogenesis during brain development.
This gene encodes a serine/threonine protein kinase that localizes to mitochondria. It is thought to protect cells from stress-induced mitochondrial dysfunction. Mutations in this gene cause one form of autosomal recessive early-onset Parkinson disease.
, PTEN induced putative kinase 1
, PTEN-Induced kinase 1
, PTEN-induced putative kinase 1
, serine/threonine-protein kinase PINK1, mitochondrial
, serine/threonine-protein kinase PINK1, mitochondrial-like
, PTEN-induced putative kinase protein 1
, protein kinase BRPK