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Literature DB >> 24072649

Silencing synuclein at the synapse with PLK2.

Brendan D Looyenga¹, Patrik Brundin.

Abstract

Entities: Gene

Mesh：

Substances：

Year: 2013 PMID： 24072649 PMCID： PMC3799359 DOI： 10.1073/pnas.1315622110

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

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21 in total

1. The polo-like protein kinases Fnk and Snk associate with a Ca(2+)- and integrin-binding protein and are regulated dynamically with synaptic plasticity.

Authors: G Kauselmann; M Weiler; P Wulff; S Jessberger; U Konietzko; J Scafidi; U Staubli; J Bereiter-Hahn; K Strebhardt; D Kuhl
Journal: EMBO J Date: 1999-10-15 Impact factor: 11.598

Review 2. Physiology and pathophysiology of the calcium store in the endoplasmic reticulum of neurons.

Authors: Alexei Verkhratsky
Journal: Physiol Rev Date: 2005-01 Impact factor: 37.312

3. Reaction of Lewy bodies with antibodies to phosphorylated and non-phosphorylated neurofilaments.

Authors: L S Forno; L A Sternberger; N H Sternberger; A M Strefling; K Swanson; L F Eng
Journal: Neurosci Lett Date: 1986-03-14 Impact factor: 3.046

4. An antigenic profile of Lewy bodies: immunocytochemical indication for protein phosphorylation and ubiquitination.

Authors: C Bancher; H Lassmann; H Budka; K Jellinger; I Grundke-Iqbal; K Iqbal; G Wiche; F Seitelberger; H M Wisniewski
Journal: J Neuropathol Exp Neurol Date: 1989-01 Impact factor: 3.685

5. Constitutive phosphorylation of the Parkinson's disease associated alpha-synuclein.

Authors: M Okochi; J Walter; A Koyama; S Nakajo; M Baba; T Iwatsubo; L Meijer; P J Kahle; C Haass
Journal: J Biol Chem Date: 2000-01-07 Impact factor: 5.157

6. Synucleins are a novel class of substrates for G protein-coupled receptor kinases.

Authors: A N Pronin; A J Morris; A Surguchov; J L Benovic
Journal: J Biol Chem Date: 2000-08-25 Impact factor: 5.157

7. A new brain-specific 14-kDa protein is a phosphoprotein. Its complete amino acid sequence and evidence for phosphorylation.

Authors: S Nakajo; K Tsukada; K Omata; Y Nakamura; K Nakaya
Journal: Eur J Biochem Date: 1993-11-01

Silencing synuclein at the synapse with PLK2.

1. The polo-like protein kinases Fnk and Snk associate with a Ca(2+)- and integrin-binding protein and are regulated dynamically with synaptic plasticity.

Review 2. Physiology and pathophysiology of the calcium store in the endoplasmic reticulum of neurons.

3. Reaction of Lewy bodies with antibodies to phosphorylated and non-phosphorylated neurofilaments.

4. An antigenic profile of Lewy bodies: immunocytochemical indication for protein phosphorylation and ubiquitination.

5. Constitutive phosphorylation of the Parkinson's disease associated alpha-synuclein.

6. Synucleins are a novel class of substrates for G protein-coupled receptor kinases.

7. A new brain-specific 14-kDa protein is a phosphoprotein. Its complete amino acid sequence and evidence for phosphorylation.

8. Targeted protein degradation and synapse remodeling by an inducible protein kinase.

9. Identification of an early-growth-response gene encoding a novel putative protein kinase.

10. The molecular basis for phosphodependent substrate targeting and regulation of Plks by the Polo-box domain.

1. Polo-like kinase 2 activates an antioxidant pathway to promote the survival of cells with mitochondrial dysfunction.

2. Identification of the PLK2-dependent phosphopeptidome by quantitative proteomics [corrected].

Review 3. Polo-Like Kinase 2: From Principle to Practice.

4. Can the disease course in Parkinson's disease be slowed?