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1 Lafora bodies, deposits of abnormally branched, insolubl
2 Lafora disease (LD) is a fatal form of progressive myocl
3 Lafora disease (LD) is a fatal progressive myoclonus epi
4 Lafora disease (LD) is a fatal, congenital, neurodegener
5 Lafora disease (LD) is a genetic and fatal form of neuro
6 Lafora disease (LD) is a progressive myoclonic epilepsy
7 Lafora disease (LD) is a severe teenage-onset neurodegen
8 Lafora disease (LD) is a teenage-onset inherited progres
9 Lafora disease (LD) is an autosomal recessive myoclonus
10 Lafora disease (LD) is an autosomal recessive neurodegen
11 Lafora disease (LD), a fatal genetic form of myoclonic e
12 Lafora disease (progressive myoclonus epilepsy of Lafora
13 Lafora disease is a fatal progressive myoclonus epilepsy
14 Lafora disease is a fatal, progressive myoclonus epileps
15 Lafora disease is a progressive myoclonus epilepsy cause
16 Lafora disease is a progressive myoclonus epilepsy with
17 Lafora disease is a progressive myoclonus epilepsy with
18 Lafora disease is a rare and fatal progressive myoclonus
19 Lafora disease is characterized by accumulation of insol
20 Lafora disease is characterized by the formation of Lafo
21 Lafora disease manifests gradually in previously healthy
22 nimals that, by 3 months of age, accumulated Lafora bodies in the brain and to a lesser extent in hea
27 like in adult polyglucosan body disease and Lafora disease, affects the brain; (ii) that RBCK1 defic
28 like in adult polyglucosan body disease and Lafora disease, has overlong branches; (iii) that unlike
30 ycogen-like polymers (polyglucosan) known as Lafora bodies, which accumulate in neurons, muscle, live
36 recently, it was widely believed that brain Lafora bodies were present exclusively in neurons and th
40 mulations of intracellular inclusions called Lafora bodies and caused by mutations in protein phospha
46 d finally (iv) that unlike laforin-deficient Lafora disease but like malin-deficient Lafora disease,
47 ient Lafora disease but like malin-deficient Lafora disease, RBCK1 deficiency's glycogen hyperphospho
51 cause the fatal neurodegenerative disorder, Lafora disease, characterized by increased glycogen phos
52 ivator protein, nearly completely eliminates Lafora bodies and rescues the neurodegeneration, myoclon
53 disease, the progressive myoclonic epilepsy Lafora disease, excessive phosphorylation of glycogen ha
57 ause up-regulation of laforin cannot explain Lafora body formation, we conclude that malin functions
61 ycogen synthesis in astrocytes-thus impeding Lafora bodies accumulation in this cell type-prevented t
63 fine the role of astrocytic Lafora bodies in Lafora disease pathology, we deleted glycogen synthase s
65 ostasis, the aberrant glycogen metabolism in Lafora disease might disturb whole-body glucose handling
70 tions in the gene encoding laforin result in Lafora disease, a fatal autosomal recessive neurodegener
72 irus (HBV) infection but may also be seen in Lafora's disease (myoclonus epilepsy), cyanamide alcohol
74 structured glycogen accumulates over time in Lafora disease (LD) and precipitates into Lafora bodies
75 e fatal neurodegenerative diseases including Lafora disease and adult polyglucosan body disease (ABPD
76 ding them to precipitate and accumulate into Lafora bodies, which drive a neuroinflammatory response
77 in Lafora disease (LD) and precipitates into Lafora bodies (LBs), leading to neurodegeneration and in
79 ike adult polyglucosan body disease but like Lafora disease, RBCK1 deficiency glycogen is hyperphosph
86 encoding laforin is the predominant cause of Lafora disease, a fatal form of progressive myoclonic ep
87 a disease (progressive myoclonus epilepsy of Lafora type) is an autosomal recessive neurodegenerative
90 cteristic of the disease is the formation of Lafora bodies, insoluble deposits containing abnormal gl
91 disease is characterized by the formation of Lafora bodies, insoluble deposits containing poorly bran
93 ult polyglucosan body disease, both forms of Lafora disease and RBCK1 deficiency, namely overlong bra
95 and resulting cell death is the hallmark of Lafora disease, a progressive and fatal neurodegenerativ
96 n and analysed the pathological hallmarks of Lafora disease, namely glycogen accumulation, Lafora bod
99 also analyzed glycogen from a mouse model of Lafora disease, Epm2a(-/-) mice, which develop Lafora bo
105 esults from multiorgan accumulations, termed Lafora bodies (LB), of abnormally structured aggregation
107 n astrocytes and change the perspective that Lafora disease is caused solely by alterations in neuron
108 present exclusively in neurons and thus that Lafora disease pathology derived from their accumulation
110 oprecipitation assay, we have found that the Lafora disease ubiquitin ligase malin interacts with dis