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H van der Putten et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 20(16), 6021-6029 (2000-08-10)
The presynaptic protein alpha-synuclein is a prime suspect for contributing to Lewy pathology and clinical aspects of diseases, including Parkinson's disease, dementia with Lewy bodies, and a Lewy body variant of Alzheimer's disease. alpha-Synuclein accumulates in Lewy bodies and Lewy
Y Zhou et al.
Neuroscience, 128(2), 281-291 (2004-09-08)
Maneb, a widely used fungicide, has been associated with Parkinsonism in humans. In experimental models, maneb and its major active element, manganese ethylene-bis-dithiocarbamate (Mn-EBDC) cause selective nigrostriatal neurodegeneration in mice and in rats, respectively. To investigate the mechanisms underlying this
Anne-Sophie Van Rompuy et al.
Molecular neurodegeneration, 10, 23-23 (2015-06-24)
Alpha-synuclein is a key protein in the pathogenesis of Parkinson's disease. Mutations in the parkin gene are the most common cause of early-onset autosomal recessive Parkinson's disease, probably through a loss-of-function mechanism. However, the molecular mechanism by which loss of
A Abeliovich et al.
Neuron, 25(1), 239-252 (2000-03-09)
alpha-Synuclein (alpha-Syn) is a 14 kDa protein of unknown function that has been implicated in the pathophysiology of Parkinson's disease (PD). Here, we show that alpha-Syn-/- mice are viable and fertile, exhibit intact brain architecture, and possess a normal complement
Akihiko Nunomura et al.
Neuroreport, 13(16), 2035-2039 (2002-11-20)
An approach was used to identify the oxidized nucleoside, 8-hydroxyguanosine in brains of dementia with Lewy bodies. Neurons with marked immunoreaction of 8-hydroxyguanosine in the cytoplasm were widely distributed in the hippocampal region and temporal neocortex. Relative intensity measurements of
M C Quilty et al.
Experimental neurology, 182(1), 195-207 (2003-06-25)
Genetic and protein studies have indicated abnormalities in alpha-synuclein in neurodegenerative diseases. However, the developmental localization and cellular role of synuclein isoforms is contentious. We investigated the cellular localization of alpha-, beta-, and gamma-synuclein in developing cultured rat neurons and
Cellular glutathione peroxidase in human brain: cellular distribution, and its potential role in the degradation of Lewy bodies in Parkinson's disease and dementia with Lewy bodies.
John H T Power, Peter C Blumbergs, John H T Power, Peter C Blumbergs
Acta neuropathologica null
P F Durrenberger et al.
Journal of neuroscience research, 87(1), 238-245 (2008-08-20)
DnaJ/Hsp40 chaperones determine the activity of Hsp70s by stabilizing their interaction with substrate proteins. We have predicted, based on the in silico analysis of a brain-derived whole-genome transcriptome data set, an increased expression of DnaJ/Hsp40 homologue, subfamily B, member 6
J K Tiller-Borcich et al.
Journal of neuropathology and experimental neurology, 47(5), 526-535 (1988-09-01)
Cortical Lewy bodies may be difficult to differentiate from Pick bodies by the usual staining methods. This problem is illustrated in a case of progressive dementia with parkinsonian features. Lewy bodies were found, not only in the pigmented nuclei in
Wei Zhang et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 19(6), 533-542 (2005-03-26)
A growing body of evidence indicates that an inflammatory process in the substantia nigra, characterized by activation of resident microglia, likely either initiates or aggravates nigral neurodegeneration in Parkinson's disease (PD). To study the mechanisms by which nigral microglia are
Bernard L Schneider et al.
Human molecular genetics, 16(6), 651-666 (2007-02-21)
Missense mutations and extra copies of the alpha-Synuclein gene result in Parkinson disease (PD). Human stem and progenitor cells can be expanded from embryonic tissues and provide a source of non-transformed neural cells to explore the effects of these pathogenic
Shinji Higashi et al.
Journal of neuropathology and experimental neurology, 70(4), 264-280 (2011-03-18)
There is emerging evidence implicating a role for the autophagy-lysosome pathway in the pathogenesis of Lewy body disease. We investigated potential neuropathologic and biochemical alterations of autophagy-lysosome pathway-related proteins in the brains of patients with dementia with Lewy bodies (DLB)
Fang Cheng et al.
Glycobiology, 32(4), 333-342 (2021-12-24)
In Parkinson's disease (PD), there is accumulation of α-synuclein (SYN) aggregates in neurons, which is promoted by neuroinflammation. The cytokines TNF-α, IL-1β and IL-6 induce accumulation of degradation products of the amyloid precursor protein (APP) combined with heparan sulfate (HS)
Martin Regensburger et al.
Brain structure & function, 223(3), 1357-1368 (2017-11-11)
In the adult mammalian hippocampus, new neurons are constantly added to the dentate gyrus. Adult neurogenesis is impaired in several neurodegenerative mouse models including α-synuclein (a-syn) transgenic mice. Among different a-syn species, a-syn oligomers were reported to be the most
Masahiko Watabe et al.
The Journal of pharmacology and experimental therapeutics, 311(3), 948-953 (2004-07-29)
Chronic complex I inhibition caused by rotenone induces features of Parkinson's disease in rats, including selective nigrostriatal dopaminergic degeneration and Lewy bodies with alpha-synuclein-positive inclusions. To determine the mechanisms underlying rotenone-induced neuronal death, we used an in vitro model of
Dora Games et al.
The American journal of pathology, 182(3), 940-953 (2013-01-15)
Progressive accumulation of α-synuclein (α-syn) in limbic and striatonigral systems is associated with the neurodegenerative processes in dementia with Lewy bodies (DLB) and Parkinson's disease (PD). The murine Thy-1 (mThy1)-α-syn transgenic (tg) model recapitulates aspects of degenerative processes associated with
TDP-43 pathology in the basal forebrain and hypothalamus of patients with amyotrophic lateral sclerosis.
Cykowski, MD; Takei, H; Schulz, PE; Appel, SH; Powell, SZ
Acta Neuropathologica Communications null
Widespread microRNA dysregulation in multiple system atrophy - disease-related alteration in miR-96.
Kiren Ubhi et al.
The European journal of neuroscience, 39(6), 1026-1041 (2013-12-07)
MicroRNA (miRNA) are short sequences of RNA that function as post-transcriptional regulators by binding to target mRNA transcripts resulting in translational repression. A number of recent studies have identified miRNA as being involved in neurodegenerative disorders including Alzheimer's disease, Parkinson's
Keiichi Inoue et al.
Molecular neurodegeneration, 7, 48-48 (2012-09-25)
Macroautophagy is an evolutionarily conserved mechanism for bulk intracellular degradation of proteins and organelles. Pathological studies have implicated macroautophagy defects in human neurodegenerative disorders of aging including Alzheimer's disease and tauopathies. Neuronal deficiency of macroautophagy throughout mouse embryonic development results
Neuropathology in mice expressing mouse alpha-synuclein.
Rieker, C; Dev, KK; Lehnhoff, K; Barbieri, S; Ksiazek, I; Kauffmann, S; Danner, S; Schell et al.
Testing null
Rosa Vaccaro et al.
The Journal of comparative neurology, 523(7), 1095-1124 (2014-12-10)
Alpha synuclein (α-syn) is a 140 amino acid vertebrate-specific protein, highly expressed in the human nervous system and abnormally accumulated in Parkinson's disease and other neurodegenerative disorders, known as synucleinopathies. The common occurrence of α-syn aggregates suggested a role for
Cocaine abusers have an overexpression of alpha-synuclein in dopamine neurons.
Deborah C Mash, Qinjie Ouyang, John Pablo, Margaret Basile, Sari Izenwasser et al.
The Journal of Neuroscience null
Martí Colom-Cadena et al.
Brain : a journal of neurology, 140(12), 3204-3214 (2017-11-28)
Dementia with Lewy bodies is characterized by the accumulation of Lewy bodies and Lewy neurites in the CNS, both of which are composed mainly of aggregated α-synuclein phosphorylated at Ser129. Although phosphorylated α-synuclein is believed to exert toxic effects at
Glial cytoplasmic inclusions and tissue injury in multiple system atrophy: A quantitative study in white matter (olivopontocerebellar system) and gray matter (nigrostriatal system).
Keisuke Ishizawa,Takashi Komori,Nobutaka Arai,Toshio Mizutani,Takanori Hirose
Neuropathology : Official Journal of the Japanese Society of Neuropathology null
Potential role of ?-synuclein in neurodegeneration: studies in a rat animal model.
George Stoica,Gina Lungu,Nicole L Bjorklund,Giulio Taglialatela,Xing Zhang,Veronica Chiu et al.
Journal of Neurochemistry null
Chronic, low-dose rotenone reproduces Lewy neurites found in early stages of Parkinson's disease, reduces mitochondrial movement and slowly kills differentiated SH-SY5Y neural cells.
Borland, MK; Trimmer, PA; Rubinstein, JD; Keeney, PM; Mohanakumar, K; Liu, L; Bennett, JP
Mol. Neurodegener. null
Mapping the subcellular distribution of ?-synuclein in neurons using genetically encoded probes for correlated light and electron microscopy: implications for Parkinson's disease pathogenesis.
Boassa, D; Berlanga, ML; Yang, MA; Terada, M; Hu, J; Bushong, EA; Hwang, M; Masliah et al.
The Journal of Neuroscience null
Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct.
K A Conway, J C Rochet, R M Bieganski, P T Lansbury
Science (New York, N.Y.) null
A Iwai et al.
Neuron, 14(2), 467-475 (1995-02-01)
Non-A beta component of Alzheimer's disease amyloid (NAC) is the second component in the amyloid from brain tissue of patients affected with Alzheimer's disease. Its precursor protein (NACP) was shown to be a brain-specific protein. In rat brain, NACP was
Masataka Nakamura et al.
American journal of neurodegenerative disease, 3(2), 93-102 (2014-09-19)
Optineurin (OPTN) is a multifunctional protein involved in cellular morphogenesis, vesicle trafficking, maintenance of the Golgi complex, and transcription activation through its interactions with the Rab8, myosin 6 (MYO6), huntingtin. Recently, OPTN immunoreactivity has been reported in intranuclear inclusions in
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