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  • Anti-Pr cold agglutinins  (1)
  • Thermodynamics  (1)
  • 1995-1999  (1)
  • 1980-1984  (1)
  • 1955-1959
  • 1945-1949
  • 1935-1939
Collection
Keywords
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  • 1995-1999  (1)
  • 1980-1984  (1)
  • 1955-1959
  • 1945-1949
  • 1935-1939
Year
  • 1
    Electronic Resource
    Electronic Resource
    Structure and function of viroids (1983)
    Springer
    European biophysics journal 9 (1983), S. 145-170 
    Details
    ISSN: 1432-1017
    Keywords: Viroids ; Thermodynamics ; Kinetics ; Hydrodynamics ; Function
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract Viroids are an independent class of plant pathogens which are distinguished from viruses by the absence of a protein coat and by their unusually small size. They are single-stranded circular RNAs composed of about 360 nucleotide residues. Sequence analysis and physicochemical studies of the potato spindle tuber viroid (PSTV) have shown that, as a result of intra-molecular base pairing, viroids form a unique rod-like secondary structure which is characterized by a serial arrangement of double-helical sections and internal loops. There is no indication for an additional tertiary structure because all parts of the molecule are freely accessible to ligand interaction. During the denaturation all of the native base pairs of viroids are dissociated in one highly cooperative transition, and in the same process very stable hairpins which are not present in the native structure are newly formed. Most of the properties of the structure and structural transitions of PSTV have been found also in citrus exocortis viroid, chrysanthemum stunt viroid and four different viroid-like RNAs associated with the cadang-cadang disease. The close similarity between these viroids is more expressed in the overall structure and in thermodynamic and functional domains than in the primary sequence. The stiffness of all viroids can be described by an unique persistence length of 300 å. Characteristically, regions of premelting, regions of stable hairpins, and the sequence UACUACCCGGUGG which is opposite to one of the stable hairpins, are the most conservative sequences in the molecules. Current hypotheses about the function of viroids are discussed on the basis of their structural and thermodynamic features. The suggestion that viroid RNA has features similar to DNA has been supported by the finding that they are replicated in vitro by the DNA-dependent RNA polymerase II of the host plant. The highly conserved sequence in viroids mentioned above corresponds very closely to a segment at the 5′-end of the small nuclear RNA U1 of eukaryotes. Because this segment is discussed in recent models, to be involved in the splicing process, a hypothesis is proposed in which viroids interfere with the splicing process leading to a pathogenic misregulation of mRNA processing.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00537813
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Anti-Pr cold agglutinins recognize immunodominant α2,3- or α2,6-sialyl groups on glycophorins (1995)
    Springer
    Glycoconjugate journal 12 (1995), S. 714-720 
    Details
    ISSN: 1573-4986
    Keywords: Anti-Pr cold agglutinins ; sialidase ; sialyltransferase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Anti-Pr cold agglutinins (CAs) with the subspecificities anti-Pr1h,-Pr1d, -Pr2, -Pr3h, -Pr3d, -PrM and anti-Sa CAs recognize immunodominantN-acetylneuraminic acid (NeuN Ac) groups of tetra and/or trisaccharides (O-glycans) of glycophorin. These O-glycans are sialylated in α2,3- and/or α2,6-linkages. Sa and most Pr antigens have been inactivated by α2,3-specific sialidases. Antigenicity was reconstituted on desialylated glycophorin by α2,3-specific Galβ1,3GalN Ac-sialyltransferase indicating that α2,3-linked NeuN Ac groups are the immunodominant components of Sa and most Pr antigens. Some Pr antigens were resistant to α2,3-specific sialidase and were not reconstituted by α2,3-specific Galβ1,3GalN Ac-sialyltransferase, which indicates that α2,6-linked NeuN Ac group represents an immunodominant component of some Pr antigens.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731269
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