相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of α-synuclein
Katerina E. Paleologou et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2008)
Specificity and regulation of casein kinase-mediated phosphorylation of α-synuclein
Elisa A. Waxman et al.
JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY (2008)
Activity-induced polo-like kinase 2 is required for homeostatic plasticity of hippocampal neurons during epileptiform activity
Daniel P. Seeburg et al.
JOURNAL OF NEUROSCIENCE (2008)
Critical role of CDK5 and Polo-like kinase 2 in homeostatic synaptic plasticity during elevated activity
Daniel P. Seeburg et al.
NEURON (2008)
The phosphorylation state of Ser-129 in human α-synuclein determines neurodegeneration in a rat model of Parkinson disease
Oleg S. Gorbatyuk et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2008)
Casein kinase 2 is the major enzyme in brain that phosphorylates Ser129 of human α-synuclein:: Implication for α-synucleinopathies
Aasami Ishii et al.
FEBS LETTERS (2007)
Pharmacological and functional comparison of the polo-like kinase family: Insight into inhibitor and substrate specificity
Eric F. Johnson et al.
BIOCHEMISTRY (2007)
BI 2536, a potent and selective inhibitor of polo-like kinase 1, inhibits tumor growth in vivo
Martin Steegmaier et al.
CURRENT BIOLOGY (2007)
α2β1 and αVβ1 integrin signaling pathways mediate amyloid-β-induced neurotoxicity
Sarah Wright et al.
NEUROBIOLOGY OF AGING (2007)
Age-dependent cognitive decline and amygdala pathology in alpha-synuclein transgenic mice
Christian Freichel et al.
NEUROBIOLOGY OF AGING (2007)
Phosphorylation of Ser-129 is the dominant pathological modification of α-synuclein in familial and sporadic Lewy body disease
John P. Anderson et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
Identification of rotenone-induced modifications in α-synuclein using affinity pull-down and tandem mass spectrometry
H Mirzaei et al.
ANALYTICAL CHEMISTRY (2006)
α-Synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease
L Chen et al.
NATURE NEUROSCIENCE (2005)
The new mutation, E46K, of α-synuclein causes Parkinson and Lewy body dementia
JJ Zarranz et al.
ANNALS OF NEUROLOGY (2004)
α-synuclein locus duplication as a cause of familial Parkinson's disease
MC Chartier-Harlin et al.
LANCET (2004)
Causal relation between α-synuclein gene duplication and familial Parkinson's disease
P Ibáñez et al.
LANCET (2004)
Neprilysin regulates amyloid beta peptide levels
RA Marr et al.
JOURNAL OF MOLECULAR NEUROSCIENCE (2004)
Targeted protein degradation and synapse remodeling by an inducible protein kinase
DTS Pak et al.
SCIENCE (2003)
α-synuclein locus triplication causes Parkinson's disease
AB Singleton et al.
SCIENCE (2003)
Role of Plk2 (Snk) in mouse development and cell proliferation
S Ma et al.
MOLECULAR AND CELLULAR BIOLOGY (2003)
Hyperphosphorylation and insolubility of α-synuclein in transgenic mouse oligodendrocytes
PJ Kahle et al.
EMBO REPORTS (2002)
α-Synuclein is phosphorylated by members of the Src family of protein-tyrosine kinases
CE Ellis et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2001)
Synucleins are a novel class of substrates for G protein-coupled receptor kinases
AN Pronin et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2000)
Constitutive phosphorylation of the Parkinson's disease associated α-synuclein
M Okochi et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2000)