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Exon ligation is proofread by the DExD/H-box ATPase Prp22p
To produce messenger RNA, the spliceosome excises introns from precursor (pre)-mRNA and splices the flanking exons. To establish fidelity, the spliceosome discriminates against aberrant introns, butExpand
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Neuroprotective Function of DJ-1 in Parkinson's Disease
Parkinson's disease (PD) is caused by dopaminergic neuronal death in the substantia nigra, resulting in a reduced level of dopamine in the striatum. Oxidative stress and mitochondrial dysfunction areExpand
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Monomer DJ-1 and Its N-Terminal Sequence Are Necessary for Mitochondrial Localization of DJ-1 Mutants
DJ-1 is a novel oncogene and also a causative gene for familial Parkinson’s disease (park7). DJ-1 has multiple functions that include transcriptional regulation, anti-oxidative reaction and chaperoneExpand
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Oxidative Status of DJ-1-dependent Activation of Dopamine Synthesis through Interaction of Tyrosine Hydroxylase and 4-Dihydroxy-l-phenylalanine (l-DOPA) Decarboxylase with DJ-1*
Parkinson disease (PD) is caused by loss of dopamine, which is synthesized from tyrosine by two enzymes, tyrosine hydroxylase (TH) and 4-dihydroxy-l-phenylalanine decarboxylase (DDC). DJ-1 is aExpand
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DJ-1 binds to mitochondrial complex I and maintains its activity.
Parkinson's disease (PD) is caused by neuronal cell death, and oxidative stress and mitochondrial dysfunction are thought to be responsible for onset of PD. DJ-1, a causative gene product of aExpand
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Identification of heterochromatin protein 1 (HP1) as a phosphorylation target by Pim‐1 kinase and the effect of phosphorylation on the transcriptional repression function of HP1 1
Pim‐1, a protooncogene product, is a serine/threonine kinase and is thought to play a role in signal transduction in blood cells. Few phosphorylated target proteins for Pim‐1, however, have beenExpand
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Pim‐1 translocates sorting nexin 6/TRAF4‐associated factor 2 from cytoplasm to nucleus
Pim‐1, an oncogene product of serine/threonine kinase, has been found to play roles in apoptosis induction/suppression, cell‐cycle progression and transcriptional regulation by phosphorylating theExpand
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PAP-1, the mutated gene underlying the RP9 form of dominant retinitis pigmentosa, is a splicing factor.
PAP-1 is an in vitro phosphorylation target of the Pim-1 oncogene. Although PAP-1 binds to Pim-1, it is not a substrate for phosphorylation by Pim-1 in vivo. PAP-1 has recently been implicated as theExpand
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Association of PAP-1 and Prp3p, the products of causative genes of dominant retinitis pigmentosa, in the tri-snRNP complex.
PAP-1 has been identified by us as a Pim-1-binding protein and has recently been implicated as the defective gene in RP9, one type of autosomal dominant retinitis pigmentosa (adRP). We have thenExpand
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PAP-1, a novel target protein of phosphorylation by pim-1 kinase.
Protooncogene, pim-1, has been reported to be a predisposition for lymphomagenesis along with myc, and its protein product, Pim-1, has been shown to be a serine/threonine protein kinase, whoseExpand
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