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  • 1985-1989  (1)
  • 1975-1979  (4)
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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of clinical periodontology 16 (1989), S. 0 
    ISSN: 1600-051X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract The measurement process of attachment Joss has been criticized in recent years. Problems with clinical interpretation, precision of the measurement, and statistical manipulation of the obtained data, are some of the problems associated with the present methodology. The purpose of the present study was to propose an alternative measurement process which addresses some of the existing problems by estimating the lost attachment surface area (LAS) and the remaining attachment surface area (RAS) from a combination of clinical measurements. The results show that a linear combination of several sources of clinical information can be used to predict RAS and LAS. A diagnostic model for LAS (R2=81.5%) predicts the square root of LAS with information obtained from bucco-lingual attachment level measurements, the radiographic lost attachment area, the gingivitis index and the radiographic tooth length. This model increases the precision of the estimate of LAS by a factor of 1.86 when compared to the estimate of LAS using only attachment level measurements, A diagnostic model for RAS (R2=75.5%) predicts the square root of RAS with the information obtained from the remaining radiographic attachment area, the gingivitis index and the mobility index. Both linear inference models are constructed with measurements of anatomical landmarks to avoid the discrepancy between anatomical and clinical measurements in the produced estimates. It is concluded that modeling of periodontal data provides a simple, inexpensive, and precise diagnostic tool for predicting the lost and the remaining periodontal attachment of single-rooted teeth. Measurement processes of this type could provide a convincing, basis for the evaluation of clinical decisions and research questions.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 144 (1976), S. 59-62 
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The effect on translational fidelity of a particular mutation in the gene coding for protein S5 (rpxE) has been investigated. This mutation has the opposite effect of a restrictive strA mutation; in vivo, it relieves the restriction imposed by strA on the suppression of T4 nonsense mutants and results in hypersensitivity to streptomycin; in vitro, the presence of the altered S5 protein in 30S ribosomes results in increased intrinsic misreading. It is concluded that this mutation, ramC319, acts as a ribosomal ambiguity mutation similar to certain mutations of protein S4 (ramA).
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Strains carrying both the ramA1 and the neaA301 mutations do not exhibit the restriction of informational suppressors normally associated with resistance to neamine. Furthermore, ribosomes from such strains exhibit increased misreading in vitro with respect to particles from the neaA strain. These properties suggest that translational fidelity may be cooperatively controlled by ribosomal proteins S4 and S17, coded by ramA (rpsD) and neaA (rpsQ) genes respectively.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Protein S5 and S12 were isolated from 30S ribosomal subunits of two E. coli mutants highly resistant to the antibiotic neamine, and of the parental strain. Proteinchemical analyses on these proteins led to the following results: a) In protein S5 the arginine residue in peptide T2 of the parental strain is replaced by glycine in one (nea 314) or serine in the other (nea 319) of the two mutants. b) In protein S12 the proline residue in peptide T15 of the parental strain is replaced by leucine in mutant nea 314 and by glutamine in mutant nea 319. Comparison of these results with those obtained in earlier studies on other mutants with altered ribosomal proteins revealed that the amino acid replacements in neamine resistant mutants and in “revertants” from streptomycin dependence occur at the same amino acid positions of proteins S5 and S12. Therefore it is likely that both types of mutants belong to the same class.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 152 (1977), S. 253-257 
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A new photoactivable reagent is described, which allows the formation of RNA-protein crosslinks via disulfide bridges in combination with mercaptobutyrimidate. The reconstituted L24 protein-23S RNA complex from the large subunit of E. coli ribosomes has been used as a model system for the cross-linking. The main advantages of the reagent are the absence of U.V. generated cross-links, since photoactivation is carried out at 360 nm, on one hand and the ease of cleavage of the cross-link by mild reduction (β-mercaptoethanol) on the other.
    Type of Medium: Electronic Resource
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