Publications by authors named "Yuji Nishimura"

Multiple system atrophy (MSA) is a severe α-synucleinopathy facilitated by glial reactions; the cerebellar variant (MSA-C) preferentially involves olivopontocerebellar fibres with conspicuous demyelination. A lack of aggressive models that preferentially involve olivopontocerebellar tracts in adulthood has hindered our understanding of the mechanisms of demyelination and neuroaxonal loss, and thus the development of effective treatments for MSA. We therefore aimed to develop a rapidly progressive mouse model that recaptures MSA-C pathology.

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Article Synopsis
  • - The main pathological feature of multiple system atrophy (MSA) is the abnormal buildup of phosphorylated α-synuclein in oligodendrocytes, leading to the formation of glial cytoplasmic inclusions (GCIs) and resulting in significant demyelination in specific brain pathways.
  • - Researchers examined changes in glial connexins (Cxs) in the cerebellar fibers of 15 MSA patients and observed three stages of demyelination, noting distinct alterations in Cx32 and Cx47 as the disease progressed.
  • - Findings revealed that while Cx32 largely disappeared from myelin early on and redeployed within oligodendrocytes along with GCIs, astrocytic C
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Blood cells are thought to have emerged as phagocytes in the common ancestor of animals followed by the appearance of novel blood cell lineages such as thrombocytes, erythrocytes, and lymphocytes, during evolution. However, this speculation is not based on genetic evidence and it is still possible to argue that phagocytes in different species have different origins. It also remains to be clarified how the initial blood cells evolved; whether ancient animals have solely developed de novo programs for phagocytes or they have inherited a key program from ancestral unicellular organisms.

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A 20-year-old female was hospitalized due to generalized seizure two weeks after an infection. She reported disorientation, neck stiffness and weakness in her legs. MRI FLAIR images and TWI on her first visit to our hospital showed hyperintense lesions in the bilateral cingulate gyrus and the medial region of the superior frontal gyrus.

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The asymmetric unit of the title coordination polymer, {[Mn(C(6)Cl(2)O(4))(C(10)H(8)N(2))]·2C(2)H(5)OH}(n), consists of one Mn(II) ion, one 2,2'-bipyridine (bpy) ligand, one chloranilate (CA(2-)) ligand and two ethanol solvent mol-ecules. The Mn(II) ion is octa-hedrally coordinated by two N atoms of one bpy ligand and four O atoms of two chloranilate ions. The chloranilate ion serves as a bridging ligand between the Mn(II) ions, leading to an infinite zigzag chain along [101].

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SWIRM is a conserved domain found in several chromatin-associated proteins. Based on their sequences, the SWIRM family members can be classified into three subfamilies, which are represented by Swi3, LSD1, and Ada2. Here we report the SWIRM structure of human MYb-like, Swirm and Mpn domain-containing protein-1 (MYSM1).

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The basic core structure of archaeal membrane lipids is 2,3-di-O-phytanylglyceryl phosphate, which is formed by reduction of 2,3-di-O-geranylgeranylglyceryl phosphate. This reaction is the final committed step in the biosynthesis of archaeal membrane lipids and is catalyzed by digeranylgeranylglycerophospholipid reductase (DGGGPL reductase). The putative DGGGPL reductase gene (Ta0516m) of Thermoplasma acidophilum was cloned and expressed.

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The basic core structure of archaeal membrane lipids is 2,3-di-O-phytanyl-sn-glyceryl phosphate (archaetidic acid), which is formed by the reduction of 2,3-di-O-geranylgeranylglyceryl phosphate. The reductase activity for the key enzyme in membrane lipid biosynthesis, 2,3-digeranylgeranylglycerophospholipid reductase, was detected in a cell free extract of the thermoacidophilic archaeon Thermoplasma acidophilum. The reduction activity was found in the membrane fraction, and FAD and NADH were required for the activity.

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