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  • 1
    Electronic Resource
    Electronic Resource
    Hemophilic arthropathy of the knee joint: static and dynamic Gd-DTPA — enhanced MRI (1995)
    Springer
    European radiology 5 (1995), S. 547-552 
    Details
    ISSN: 1432-1084
    Keywords: Hemophilia ; Knee joint ; Synovial proliferation ; MR studies ; Gadolinium ; Contrast enhancement
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A total of 17 patients with hemophilic arthropathy of the knee joint were studied with static and dynamic MRI before and after an IV bolus injection of Gadolinium-DTPA (Gd-DTPA; 0.1 mmol/kg body weight). The T1-weighted spin-echo (SE) and gradient-echo (fast-field echo [FFE]) sequences were applied. The FFE sequences of eight consecutive scans carried out over a time interval of 160 s were used in order to determine the time to signal intensity (SI) curves of the synovial proliferations surrounding soft tissue, bone marrow, and joint effusion. After the administration of a contrast agent, synovial proliferations exhibited an increase on FFE and SE images of 47.7 % (SD ± 14.3 %) and 37.4 % (SD ± 11.2 %), respectively, whereas muscle and fatty tissue, tendons, bone marrow, and joint effusion revealed only a minor increase in SI. The gradient of SI (ratio SI/time) of pannus was 39.6 %/min (SD ± 7.7 %/min) and differed significantly (P 〈 0.001) from that of bone marrow, fatty tissue, muscle tissue, tendons, and joint effusion (P 〈 0.05). In contrast to synovial proliferations in rheumatoid arthritis, no differentiation between various pannus vascularities based on the degree of enhancement was possible. The Gd-DTPA-enhanced MRI studies delineate and quantify the synovial proliferations in hemophilic arthropathy. Dynamic studies in hemophilic arthropathy do not provide qualitative assessment of the inflammatory process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00208351
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  • 2
    Electronic Resource
    Electronic Resource
    Analysis of chimeric UmuC proteins: identification of regions inSalmonella typhimurium UmuC important for mutagenic activity (1996)
    Springer
    Molecular genetics and genomics 251 (1996), S. 121-129 
    Details
    ISSN: 1617-4623
    Keywords: Escherichia coli ; Salmonella typhimurium ; SOS mutagenesis ; Chimeric proteins ; UmuC
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract UnlikeEscherichia coli, the closely related bacteriumSalmonella typhimurium is relatively unresponsive to the mutagenic effects of DNA-damaging agents. Previous experiments have suggested that these phenotypic differences might result from reduced activity of theS. typhimurium UmuC protein. To investigate this possibility, we have taken advantage of the high degree of homology between the UmuC proteins ofE. coli andS. typhimurium and have constructed a series of plasmid-encoded chimeric proteins. The possibility that the phenotypic differences might be due to differential expression of the respective UmuC proteins was eliminated by constructing chimeric proteins that retained the first 25 N-terminal amino acids of either of the UmuC proteins (and presumably the same translational signals), but substituting the remaining 397 C-terminal amino acids with the corresponding segments from the reciprocal operon. Constructs expressing mostlyE. coli UmuC were moderately proficient for mutagenesis whereas those expressing mostlyS. typhimurium UmuC exhibited much lower frequencies of mutation, indicating that the activity of the UmuC protein ofS. typhimurium is indeed curtailed. The regions responsible for this phenotype were more precisely localized by introducing smaller segments of theS. typhimurium UmuC protein into the UmuC protein ofE. coli. While some regions could be interchanged with few or no phenotypic effects, substitution of residues 212–395 and 396–422 ofE. coli UmuC with those fromS. typhimurium resulted in reduced mutability, while substitution of residues 26–59 caused a dramatic loss of activity. We suggest, therefore, that the primary cause for the poor mutability ofS. typhimurium can be attributed to mutations located within residues 26–59 of theS. typhimurium UmuC protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02172909
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    Paper (German National Licenses)
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