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  • Life and Medical Sciences  (2)
  • Mass spectrometry  (2)
  • RFLP  (2)
  • 1995-1999  (6)
  • 1925-1929
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Year
  • 1
    Electronic Resource
    Electronic Resource
    Mapping of the K+/Na+ discrimination locus Kna1 in wheat (1996)
    Springer
    Theoretical and applied genetics 92 (1996), S. 448-454 
    Details
    ISSN: 1432-2242
    Keywords: Key words  Wheat ; Salt tolerance ; Homoeologous recombination ; QTL ; RFLP ; Genetic marker
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract   In saline environments, bread wheat, Triticum aestivum L. (genomes AABBDD), accumulates less Na+ and more K+ in expanding and young leaves than durum wheat, T. turgidum L. (genomes AABB). Higher K+/Na+ ratios in leaves of bread wheat correlate with its higher salt tolerance. Chromosome 4D from bread wheat was shown in previous work to play an important role in the control of this trait and was recombined with chromosome 4B in the absence of the Ph1 locus. A population of plants disomic for 4D/4B recombined chromosomes in the genetic background of T. turgidum was developed to investigate the genetic control of K+/Na+ discrimination by chromosome 4D. Evidence was obtained that the trait is controlled by a single locus, designated Kna1, in the long arm of chromosome 4D. In the present work, K+/Na+ discrimination was determined for additional families with 4D/4B chromosomes. The concentrations of Na+ and K+/Na+ ratios in the youngest leaf blades clustered in two nonoverlapping classes, and all recombinant families could be unequivocally assigned to Kna1 and kna1 classes. The Kna1 locus scored this way was mapped on a short region in the 4DL arm and was completely linked to Xwg199, Xabc305, Xbcd402, Xpsr567, and Xpsr375; it was also mapped as a quantitative trait. The results of the QTL analysis, based on the K+/Na+ ratios in the young leaves of greenhouse-grown plants and flag leaves of field-grown plants, agreed with the position of Kna1 determined as a qualitative trait. Several aspects of gene introgression by manipulation of the Ph1 locus are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001220050148
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  • 2
    Electronic Resource
    Electronic Resource
    Mapping of the K+/Na+ discrimination locus Kna1 in wheat (1996)
    Springer
    Theoretical and applied genetics 92 (1996), S. 448-454 
    Details
    ISSN: 1432-2242
    Keywords: Wheat ; Salt tolerance ; Homoeologous recombination ; QTL ; RFLP ; Genetic marker
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In saline environments, bread wheat, Triticum aestivum L. (genomes AABBDD), accumulates less Na+ and more K+ in expanding and young leaves than durum wheat, T. turgidum L. (genomes AABB). Higher K+/Na+ ratios in leaves of bread wheat correlate with its higher salt tolerance. Chromosome 4D from bread wheat was shown in previous work to play an important role in the control of this trait and was recombined with chromosome 4B in the absence of the Ph1 locus. A population of plants disomic for 4D/4B recombined chromosomes in the genetic background of T. turgidum was developed to investigate the genetic control of K+/Na+ discrimination by chromosome 4D. Evidence was obtained that the trait is controlled by a single locus, designated Kna1, in the long arm of chromosome 4D. In the present work, K+/Na+ discrimination was determined for additional families with 4D/4B chromosomes. The concentrations of Na+ and K+/Na+ ratios in the youngest leaf blades clustered in two nonoverlapping classes, and all recombinant families could be unequivocally assigned to Kna1 and kna1 classes. The Kna1 locus scored this way was mapped on a short region in the 4DL arm and was completely linked to Xwg199, Xabc305, Xbcd.402, Xpsr567, and Xpsr375; it was also mapped as a quantitative trait. The results of the QTL analysis, based on the K+/Na+ ratios in the young leaves of greenhousegrown plants and flag leaves of field-grown plants, agreed with the position of Knal determined as a qualitative trait. Several aspects of gene introgression by manipulation of the Ph1 locus are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00223692
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  • 3
    Electronic Resource
    Electronic Resource
    Nuclear domain 10 (ND10) associated proteins are also present in nuclear bodies and redistribute to hundreds of nuclear sites after stress (1995)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 59 (1995), S. 498-513 
    Details
    ISSN: 0730-2312
    Keywords: nuclear bodies ; promyelocytic leukemia protein ; herpes simplex virus ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The promyelocytic leukemia protien fused to the retinoic acid receptor in t(15;17) acute promyelocytic leukemia, the primary biliary cirrhosis autoantigen, Sp100, as well as the incompletely charterized protien NDP55, are co-localized in specific immunohistochemically defined nuclear domains (ND10), which are potential equyivalents of ultrastructurally defined nuclear bodies. We investigated whether the distribution of these proteins depends on environmental conditions and whether ND10 correlate with nuclear bodies. Certain nuclear bodies and ND10 react in a similar bodies, which herpes simplex virus infection or heat shock modify both. Redistribution of ND10-associated proteins to hundreds of small sites throughout the chromatin was inducible by stress in the form of heat shock and exposure to Cd++ ions. The change of distribution was rapid and independent of proteins synthesis, and thus not part of the classical heat shock response. The very rapid redistribution of these proteins after heat shock, together with the development of ND10 upon interferon actication, raises the possibility that ND10 represent storage sites of certain matrix proteins readily accessible throughout the chromatin in response to stress or other effectors that induce global nuclear changes. © 1995 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240590410
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  • 4
    Electronic Resource
    Electronic Resource
    Identification of cytokine-regulated proteins in normal and malignant cells by the combination of two-dimensional polyacrylamide gel electrophoresis, mass spectrometry, Edman degradation and immunoblotting and approaches to the analysis of their functional roles (1996)
    Weinheim : Wiley-Blackwell
    Electrophoresis 17 (1996), S. 1655-1670 
    Details
    ISSN: 0173-0835
    Keywords: Protein identification ; Cytokine-regulated proteins ; Mass spectrometry ; Interferon -γ ; Tumor necrosis factor ; Malignancy ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150171103
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  • 5
    Electronic Resource
    Electronic Resource
    Werner syndrome: Entering the helicase era (1996)
    New York, NY : Wiley-Blackwell
    BioEssays 18 (1996), S. 1025-1027 
    Details
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Werner syndrome is a rare autosomal recessive disorder that mimics some of the characteristics of aging. The gene for this disorder has recently been identified as a helicase of the recQ subclass(1). Other phenotypically distinctive disorders caused by different helicase mutations include Bloom syndrome, Cockayne syndrome, xeroderma pigmentosum and trichothiodystrophy. Possible mechanisms by which helicases might produce the variable phenotypes are discussed. These include altered nucleotide excision repair and RNA polymerase II-mediated transcription. The discovery of the helicase defect in Werner syndrome provides a road map for future study of its unique pathogenesis and conceivable, but unproved, relationship to the aging process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bies.950181214
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  • 6
    Electronic Resource
    Electronic Resource
    Immobilized pH gradient two-dimensional gel electrophoresis and mass spectrometric identification of cytokine-regulated proteins in ME-180 cervical carcinoma cells (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 409-417 
    Details
    ISSN: 0173-0835
    Keywords: Cervical carcinoma ; Two-dimensional polyacrylamide gel electrophoresis ; Mass spectrometry ; Immobilized pH gradient ; Cytokine ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Two-dimensional (2-D) polyacrylamide gel electrophoresis combined with mass spectrometry is a powerful combination of technologies that allows high resolution separation of proteins and their rapid identification. Immobilized pH gradient (IPG) first-dimensional gels have several advantages over carrier ampholyte isoelectric focusing, including a high degree of reproducibility, good protein spot resolution, and a selection of pH range. Here we demonstrate the utility and efficacy of combining IPG 2-D gel electrophoresis with mass spectrometry to identify interferon-γ- (IFN) and tumor necrosis factor (TNF)-regulated proteins in ME-180 cervical carcinoma cells. Three cytokine-regulated proteins have been identified, using imidazole-zinc-stained preparative IPG 2-D gels and in-gel tryptic digestion followed by matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry for determination of peptide masses and sequences: (1) triosephosphate isomerase, a glycolytic pathway enzyme, (2) proteasome subunit C3, which is important in protein degradation, and (3) Ran, a GTP-binding protein important in cell cycle regulation, protein import into the nucleus, and RNA export from the nucleus.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150180315
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