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  • 1995-1999  (4)
  • Septum  (2)
  • cardiovascular disease  (1)
  • cyanocarbonyl  (1)
  • Polymer and Materials Science
  • 1
    Electronic Resource
    Electronic Resource
    The cyanocarbonyl group: synthesis and crystal structure of an imidazole carbonyl cyanide, C12N5OH17 (1998)
    Springer
    Journal of chemical crystallography 28 (1998), S. 561-564 
    Details
    ISSN: 1572-8854
    Keywords: Acylcyanide ; cyanocarbonyl ; imidazole ; carbonyl cyanide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract 1-t-Butyl-5-N-(dimethylaminomethylene)aminoimidazole-4-carbonyl cyanide (BUNDAMIC) is the first acyl cyanide to be synthesized from an imidazole-4-carboxylic acid, diethylphosphorocyanidate, and triethylamine and its structure determined by x-ray crystallography. It crystallizes with four molecules in the monoclinic space group C2/m with a = 17.824(2), b = 6.784(2), c = 11.039(2) Å, and β = 96.17(1)°; R = 0.036 over 1086 unique x-ray reflections. The cyanocarbonyl group is nearly linear, C-C≡ N angle 174.4(3)°, with dimensions C≡ N, 1.137(3); C-C 1.493(3); and C=O≡ N 1.224(3) Å. The imidazole ring, in the mirror plane, has a lengthened C4 = C5 bond of 1.421(3) A, and there is a short ring-closing approach, H⋯ O6 =2.07 Å, between the methyleneamino hydrogen and the carbonyl oxygen.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1023200307429
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Isolated post-challenge hyperglycaemia confirmed as a risk factor for mortality (1999)
    Springer
    Diabetologia 42 (1999), S. 1050-1054 
    Details
    ISSN: 1432-0428
    Keywords: Keywords Type II diabetes ; mortality ; cardiovascular disease ; cancer ; population study ; post-challenge hyperglycaemia.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Aims/hypothesis. The aim of this study was to examine the possible link between isolated post-challenge hyperglycaemia (2-h post-challenge plasma glucose ≥ 11.1 mmol/l, and fasting plasma glucose 〈 7.0 mmol/l) and mortality. Methods. The data from three population based longitudinal studies (in Mauritius, Fiji and Nauru) were pooled and mortality rates were determined in 9179 people who were followed for between 5 and 12 years. Results. There were 595 people with previously diagnosed diabetes, and 799 with newly diagnosed diabetes, of whom 243 (31) had isolated post-challenge hyperglycaemia. In comparison with people without diabetes, people with isolated post-challenge hyperglycaemia had an increased risk of all-cause mortality [Cox proportional hazards ratio (95 % CI): 2.7 (1.8–3.9) – men; 2.0 (1.3–3.3) – women], and of cardiovascular mortality [2.3 (1.2–4.2) – men; 2.6 (1.3–5.1) – women]. In addition, men with isolated post-challenge hyperglycaemia had a high risk of cancer death [8.0 (3.6–17.9)]. Conclusion/interpretation. These data show that isolated post-challenge hyperglycaemia, which can only be identified by the 2-h glucose, is common, and at least doubles the mortality risk. This should be considered in the design of screening programmes that use only fasting glucose [Diabetologia (1999) 42: 1050–1054]
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001250051269
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Yeast chitin synthases 1 and 2 consist of a non-homologous and dispensable N-terminal region and of a homologous moiety essential for function (1996)
    Springer
    Molecular genetics and genomics 252 (1996), S. 420-428 
    Details
    ISSN: 1617-4623
    Keywords: Key words Saccharomyces cerevisiae ; Chitin synthases ; Septum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Predicted protein sequences of fungal chitin synthases can be divided into a non-homologous N-terminal region and a C-terminal region that shows significant homology among the various synthases. We have explored the function of these domains by constructing a series of nested deletions, extending from either end, in the CHS1 and CHS2 genes of Saccharomyces cerevisiae. In both cases, most or all of the sequences encoding the non-homologous N-terminal region (one-third of the protein for Chs1p and about one-fourth for Chs2p) could be excised, with little effect on the enzymatic activity in vitro of the corresponding synthase or on its function in vivo. However, further small deletions (20–25 amino acids) into the homologous region were deleterious to enzymatic activity and function, and often led to changes in the zymogenic character of the enzymes. Similarly, relatively small (about 75 amino acids) deletions from the C-terminus resulted in loss of enzymatic activity and function of both synthases. Thus, it appears that all the information necessary for membrane localization, enzymatic activity and function resides in the homologous regions of Chs1p and Chs2p, a situation that may also apply to other chitin synthases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02173007
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Yeast chitin synthases 1 and 2 consist of a non-homologous and dispensable N-terminal region and of a homologous moiety essential for function (1996)
    Springer
    Molecular genetics and genomics 252 (1996), S. 420-428 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Chitin synthases ; Septum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Predicted protein sequences of fungal chitin synthases can be divided into a non-homologous N-terminal region and a C-terminal region that shows significant homology among the various synthases. We have explored the function of these domains by constructing a series of nested deletions, extending from either end, in theCHS1 andCHS2 genes ofSaccharomyces cerevisiae. In both cases, most or all of the sequences encoding the non-homologous N-terminal region (one-third of the protein for Chs1p and about one-fourth for Chs2p) could be excised, with little effect on the enzymatic activity in vitro of the corresponding synthase or on its function in vivo. However, further small deletions (20–25 amino acids) into the homologous region were deleterious to enzymatic activity and function, and often led to changes in the zymogenic character of the enzymes. Similarly, relatively small (about 75 amino acids) deletions from the C-terminus resulted in loss of enzymatic activity and function of both synthases. Thus, it appears that all the information necessary for membrane localization, enzymatic activity and function resides in the homologous regions of Chs1p and Chs2p, a situation that may also apply to other chitin synthases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02173007
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
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