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  • Books
  • Articles  (2)
  • Other Sources
  • 71.55  (1)
  • Mammalian endoplasmic reticulum  (1)
  • Springer  (2)
  • American Association for the Advancement of Science
  • 1990-1994  (2)
  • Physics  (2)
  • Chemistry and Pharmacology  (1)
Collection
  • Books
  • Articles  (2)
  • Other Sources
Publisher
  • Springer  (2)
  • American Association for the Advancement of Science
Years
  • 1990-1994  (2)
Year
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Applied physics 54 (1992), S. 40-46 
    ISSN: 1432-0630
    Keywords: 61.40 ; 71.55 ; 82.60
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract Amorphous (a-) semiconductors like a-Si:H and the chalcogenide glasses possess a general tendency to establish an overall equilibrium between the electronic system and the lattice with its dopant and defect sites. In the present paper the chemical interactions which establish these equilibria within the bulk of the a-semiconductor lattices are compared to chemical interactions in liquid electrolytes, particularly to those in H2O. These considerations reveal close similarities between autocompensation doping in a-semiconductors and acid/base reactions in H2O. The effects of light and field-effect induced defect formation, on the other hand, are shown to be related to the phenomenon of electrolysis in H2O. The consideration of these analogies further emphasizes the roles of charge-carrier localization and that of H-diffusion in promoting dopant and defect equilibration reactions in a-semiconductors.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-6881
    Keywords: Mammalian endoplasmic reticulum ; prepromelittin ; prepropeptide GLa ; preprocecropin A ; M13 procoat protein ; protein transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract There are at least two different mechanisms for the transport of secretory proteins into the mammalian endoplasmic reticulum. Both mechanisms depend on the presence of a signal peptide on the respective precursor protein and involve a signal peptide receptor on the cis-side and signal peptidase on the trans-side of the membrane. Furthermore, both mechanisms involve a membrane component with a cytoplasmically exposed sulfhydryl. The decisive feature of the precursor protein with respect to which of the two mechanisms is used is the chain length of the polypeptide. The critical size seems to be around 70 amino acid residues (including the signal peptide). The one mechanism is used by precursor proteins larger than about 70 amino acid residues and involves two cytosolic ribonucleoparticles and their receptors on the microsomal surface. The other one is used by small precursor proteins and relies on the mature part within the precursor molecule and a cytosolic ATPase.
    Type of Medium: Electronic Resource
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