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  • 1
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    Phosphorylation of the CPC by Cdk1 promotes chromosome bi-orientation (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-08-27
    Description: Successful partition of replicated genomes at cell division requires chromosome attachment to opposite poles of mitotic spindle (bi-orientation). Any defects in this regulation bring about chromosomal instability, which may accelerate tumour progression in humans. To achieve chromosome bi-orientation at prometaphase, the chromosomal passenger complex (CPC), composed of catalytic kinase Aurora B and regulatory components (INCENP, Survivin and Borealin), must be localized to centromeres to phosphorylate kinetochore substrates. Although the CPC dynamically changes the subcellular localization, the regulation of centromere targeting is largely unknown. Here we isolated a fission yeast cyclin B mutant defective specifically in chromosome bi-orientation. Accordingly, we identified Cdk1 (also known as Cdc2)-cyclin-B-dependent phosphorylation of Survivin. Preventing Survivin phosphorylation impairs centromere CPC targeting as well as chromosome bi-orientation, whereas phosphomimetic Survivin suppresses the bi-orientation defect in the cyclin B mutant. Survivin phosphorylation promotes direct binding with shugoshin, which we now define as a conserved centromeric adaptor of the CPC. In human cells, the phosphorylation of Borealin has a comparable role. Thus, our study resolves the conserved mechanisms of CPC targeting to centromeres, highlighting a key role of Cdk1-cyclin B in chromosome bi-orientation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsukahara, Tatsuya -- Tanno, Yuji -- Watanabe, Yoshinori -- England -- Nature. 2010 Oct 7;467(7316):719-23. doi: 10.1038/nature09390. Epub 2010 Aug 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chromosome Dynamics, Institute of Molecular and Cellular Biosciences, University of Tokyo, Yayoi, Tokyo 113-0032, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20739936" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Aurora Kinase B ; Aurora Kinases ; CDC2 Protein Kinase/*metabolism ; Carrier Proteins/genetics/metabolism ; Cell Cycle Proteins/genetics/metabolism ; Cell Line ; Centromere/metabolism ; Chromosomal Proteins, Non-Histone/metabolism ; Chromosomes, Fungal/*metabolism ; Chromosomes, Human/*metabolism ; Cyclin B/genetics/metabolism ; Humans ; Inhibitor of Apoptosis Proteins ; Microtubule-Associated Proteins/metabolism ; Molecular Sequence Data ; Multiprotein Complexes/*chemistry/*metabolism ; Phosphorylation ; Protein Binding ; Protein-Serine-Threonine Kinases/genetics/metabolism ; Schizosaccharomyces/cytology/genetics/metabolism ; Schizosaccharomyces pombe Proteins/genetics/*metabolism ; Substrate Specificity
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    Meikin is a conserved regulator of meiosis-I-specific kinetochore function (2014)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2014-12-24
    Description: The kinetochore is the crucial apparatus regulating chromosome segregation in mitosis and meiosis. Particularly in meiosis I, unlike in mitosis, sister kinetochores are captured by microtubules emanating from the same spindle pole (mono-orientation) and centromeric cohesion mediated by cohesin is protected in the following anaphase. Although meiotic kinetochore factors have been identified only in budding and fission yeasts, these molecules and their functions are thought to have diverged earlier. Therefore, a conserved mechanism for meiotic kinetochore regulation remains elusive. Here we have identified in mouse a meiosis-specific kinetochore factor that we termed MEIKIN, which functions in meiosis I but not in meiosis II or mitosis. MEIKIN plays a crucial role in both mono-orientation and centromeric cohesion protection, partly by stabilizing the localization of the cohesin protector shugoshin. These functions are mediated mainly by the activity of Polo-like kinase PLK1, which is enriched to kinetochores in a MEIKIN-dependent manner. Our integrative analysis indicates that the long-awaited key regulator of meiotic kinetochore function is Meikin, which is conserved from yeasts to humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, Jihye -- Ishiguro, Kei-ichiro -- Nambu, Aya -- Akiyoshi, Bungo -- Yokobayashi, Shihori -- Kagami, Ayano -- Ishiguro, Tadashi -- Pendas, Alberto M -- Takeda, Naoki -- Sakakibara, Yogo -- Kitajima, Tomoya S -- Tanno, Yuji -- Sakuno, Takeshi -- Watanabe, Yoshinori -- England -- Nature. 2015 Jan 22;517(7535):466-71. doi: 10.1038/nature14097. Epub 2014 Dec 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chromosome Dynamics, Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1Yayoi, Tokyo 113-0032, Japan. ; Instituto de Biologia Molecular y Celular del Cancer (CSIC-USAL), 37007 Salamanca, Spain. ; Center for Animal Resources and Development, Kumamoto University, 2-2-1 Honjo, Kumamoto 860-0811 Japan. ; Laboratory for Chromosome Segregation, RIKEN Center for Developmental Biology, 2-2-3 Minatojima-Minamimachi, Chuo-ku, Kobe 650-0047, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25533956" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Cycle Proteins/metabolism ; Centromere/metabolism ; Chromosomal Proteins, Non-Histone/deficiency/genetics/*metabolism ; *Conserved Sequence ; Female ; Humans ; Infertility/genetics/metabolism ; Kinetochores/*metabolism ; Male ; *Meiosis ; Mice ; Molecular Sequence Data ; Protein-Serine-Threonine Kinases/metabolism ; Proto-Oncogene Proteins/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Schizosaccharomyces pombe Proteins/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
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    Two histone marks establish the inner centromere and chromosome bi-orientation (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-10-12
    Description: For proper partitioning of chromosomes in mitosis, the chromosomal passenger complex (CPC) including Aurora B and survivin must be localized at the center of paired kinetochores, at the site called the inner centromere. It is largely unknown what defines the inner centromere and how the CPC is targeted to this site. Here, we show that the phosphorylation of histone H3-threonine 3 (H3-pT3) mediated by Haspin cooperates with Bub1-mediated histone 2A-serine 121 (H2A-S121) phosphorylation in targeting the CPC to the inner centromere in fission yeast and human cells. H3-pT3 promotes nucleosome binding of survivin, whereas phosphorylated H2A-S121 facilitates the binding of shugoshin, the centromeric CPC adaptor. Haspin colocalizes with cohesin by associating with Pds5, whereas Bub1 localizes at kinetochores. Thus, the inner centromere is defined by intersection of two histone kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamagishi, Yuya -- Honda, Takashi -- Tanno, Yuji -- Watanabe, Yoshinori -- New York, N.Y. -- Science. 2010 Oct 8;330(6001):239-43. doi: 10.1126/science.1194498.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chromosome Dynamics, Institute of Molecular and Cellular Biosciences, University of Tokyo, Yayoi, Tokyo 113-0032, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20929775" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aurora Kinase B ; Aurora Kinases ; Cell Cycle Proteins/metabolism ; Centromere/*metabolism ; Chromatin/metabolism ; Chromosomal Proteins, Non-Histone/metabolism ; Chromosome Segregation ; Chromosomes, Fungal/*physiology ; Chromosomes, Human/*physiology ; HeLa Cells ; Heterochromatin/metabolism ; Histones/*metabolism ; Humans ; Inhibitor of Apoptosis Proteins ; Intracellular Signaling Peptides and Proteins/chemistry/genetics/*metabolism ; Kinetochores/metabolism ; Microtubule-Associated Proteins/metabolism ; Mitosis ; Molecular Sequence Data ; Mutation ; Nucleosomes/metabolism ; Phosphorylation ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Schizosaccharomyces/*genetics/metabolism ; Schizosaccharomyces pombe Proteins/genetics/*metabolism ; Serine/metabolism ; Threonine/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    The inner centromere-shugoshin network prevents chromosomal instability (2015)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2015-09-12
    Description: Chromosomal instability (CIN) is a major trait of cancer cells and a potent driver of tumor progression. However, the molecular mechanisms underlying CIN still remain elusive. We found that a number of CIN(+) cell lines have impairments in the integrity of the conserved inner centromere-shugoshin (ICS) network, which coordinates sister chromatid cohesion and kinetochore-microtubule attachment. These defects are caused mostly by the loss of histone H3 lysine 9 trimethylation at centromeres and sometimes by a reduction in chromatin-associated cohesin; both pathways separately sustain centromeric shugoshin stability. Artificial restoration of the ICS network suppresses chromosome segregation errors in a wide range of CIN(+) cells, including RB- and BRCA1-deficient cells. Thus, dysfunction of the ICS network might be a key mechanism underlying CIN in human tumorigenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tanno, Yuji -- Susumu, Hiroaki -- Kawamura, Miyuki -- Sugimura, Haruhiko -- Honda, Takashi -- Watanabe, Yoshinori -- New York, N.Y. -- Science. 2015 Sep 11;349(6253):1237-40. doi: 10.1126/science.aaa2655.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chromosome Dynamics, Institute of Molecular and Cellular Biosciences, University of Tokyo, Yayoi, Tokyo 113-0032, Japan. ; Laboratory of Chromosome Dynamics, Institute of Molecular and Cellular Biosciences, University of Tokyo, Yayoi, Tokyo 113-0032, Japan. Department of Biological Sciences, Graduate School of Science, University of Tokyo, Yayoi, Tokyo 113-0032, Japan. ; First Department of Pathology, Hamamatsu University School of Medicine, Hamamatsu, Shizuoka 431-3192, Japan. ; Laboratory of Chromosome Dynamics, Institute of Molecular and Cellular Biosciences, University of Tokyo, Yayoi, Tokyo 113-0032, Japan. Department of Biological Sciences, Graduate School of Science, University of Tokyo, Yayoi, Tokyo 113-0032, Japan. ywatanab@iam.u-tokyo.ac.jp.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26359403" target="_blank"〉PubMed〈/a〉
    Keywords: BRCA1 Protein/genetics ; Carcinogenesis/genetics/*metabolism ; Cell Cycle Proteins/genetics/*metabolism ; Centromere/genetics/*metabolism ; Chromatids/metabolism ; Chromatin/metabolism ; *Chromosomal Instability ; Chromosomal Proteins, Non-Histone/metabolism ; *Chromosome Segregation ; HeLa Cells ; Histones/metabolism ; Humans ; Kinetochores/metabolism ; Lysine/metabolism ; Methylation ; Microtubules/metabolism ; Retinoblastoma Protein/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 5
    Electronic Resource
    Electronic Resource
    Distinct clustering of point mutations in mitochondrial DNA among patients with mitochondrial encephalomyopathies and with Parkinson's disease
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 176 (1991), S. 938-946 
    Details
    ISSN: 0006-291X
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0006-291X(05)80276-1
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  • 6
    Electronic Resource
    Electronic Resource
    Quantitation of mitochondrial DNA carrying tRNA^L^y^s mutation in MERRF patients
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 179 (1991), S. 880-885 
    Details
    ISSN: 0006-291X
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0006-291X(91)91900-W
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  • 7
    Electronic Resource
    Electronic Resource
    Distinct clustering of point mutations in mitochondrial DNA among patients with mitochondrial encephalomyopathies and with Parkinson's disease
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 176 (1991), S. 938-946 
    Details
    ISSN: 0006-291X
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0006-291X(05)80276-1
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  • 8
    Electronic Resource
    Electronic Resource
    Direct formation of ferrite films in wet process (1985)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 57 (1985), S. 3795-3797 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: We have prepared a polycrystalline Co-ferrite film by the electroless ferrite-plating technique of our invention [J. Appl. Phys. 55, 2614 (1984)] in an aqueous solution at 70 °C on substrates of organic compounds (polyethylene terephthalate, polymethyl methacrylate, polycarbonate, Teflon), a stainless steel, and a polyester fiber. We used no intermediate layer, which we needed previously to enhance the adhesion of the ferrite film to the surface. By exposing the organic substrates to an rf-excited air plasma, the wettability of the surface improved, which enhanced the adhesion of the film to the substrate. Here we have measured the adhesion by a cross-cut test. The plasma forms hydrophilic groups such as -OH and -COOH, which improve the wettability. The OH group adsorbs the metal ions in the reaction solution, initiating the ferrite film formation. The glass shows a strong adhesion to the film even when it is not exposed to the plasma, because the glass has the OH group on the surface inherently. The stainless steel does not enhance the adhesion by the plasma treatment because the plasma forms no OH group on the metal surface. The adhesion power higher than ∼10 kg/cm2 has been obtained between the Co-ferrite film and the glass (not plasma treated), the polyethylene terephthalate (plasma treated) and the Teflon (plasma treated).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.334922
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  • 9
    Electronic Resource
    Electronic Resource
    On the reactivity of recoil tritium with organic compounds (1988)
    Springer
    Journal of radioanalytical and nuclear chemistry 128 (1988), S. 181-188 
    Details
    ISSN: 1588-2780
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Energy, Environment Protection, Nuclear Power Engineering
    Notes: Abstract The reactivity of recoil tritium in the T-for-H substitution was studied in mixtures of benzene, hexane, cyclohexane or cyclohexane-d12 with lithium carbonate which were irradiated in a reactor. The relative rates per C−H bond of hexane and cyclohexane to benzene were somewhat less than one third. The H/D isotope effect in cyclohexane was given as 1.14.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02166647
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  • 10
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    Retraction (2017)
    American Association for the Advancement of Science (AAAS)
    In: Science
    Details
    Publication Date: 2017-09-08
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Geosciences , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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