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  • Human tendon elasticity  (1)
  • Key words Non-small-cell lung cancer (NSCLC)  (1)
  • LT  (1)
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Erscheinungszeitraum
  • 1
    ISSN: 1437-7772
    Schlagwort(e): Key words Non-small-cell lung cancer (NSCLC) ; Cisplatin ; Docetaxel
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract Background. This phase II study was designed to determine the toxicity and efficacy of a low dose of docetaxel plus a standard dose of cisplatin for patients with metastatic non-small-cell lung cancer (NSCLC). Methods. Eligibility criteria included metastatic disease (stage IV) of NSCLC and a performance status (PS) of 0-2. Cisplatin 80 mg/m2 was given i.v. on day 1 and docetaxel 60 mg/m2 was given i.v. on day 1. Treatment was repeated every 3 to 4 weeks. Results. Forty-five patients were enrolled in the study, and the median age was 63 years. Forty-two patients (93%) had a PS of 0-1 and 38 (84%) received two to four courses of chemotherapy. The principal toxicity was neutropenia, and grade 3/4 occurred in 36%/49%. Other hematologic toxicities were mild. Of the 45 patients, subsequent chemotherapy was delayed due to toxicities in only 5 patients (11%), and dose modifications were needed in only 3 patients (7%). There were no treatment-related deaths. Non-hematological toxicities were relatively mild. Allergy (2%), skin rash (11%), edema (9%), and neuropathy (9%) occurred infrequently, and all were grade 1 toxicity. Of the 45 patients, 19 showed partial response, giving a response rate of 42%. The median survival time was 43.3 weeks, and the 1-year survival rate of all patients was 38.7%. Conclusion. This cisplatin/docetaxel combination chemotherapy is an active and non-toxic regimen in patients with metastatic NSCLC, a result which suggests that the combination may be suitable for randomized controlled trials.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    European journal of applied physiology 71 (1995), S. 555-557 
    ISSN: 1439-6327
    Schlagwort(e): Human tendon elasticity ; Ultrasonography ; Tibialis anterior muscle ; F-L curve
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract To obtain an insight into tendon elasticity during human movement, a real-time ultrasonography was applied to the contracting tibialis anterior muscle. The insertion point of fascicles onto the aponeurosis was clearly visualized, and its position relative to a fixed marker on the skin moved proximally (Δ1) according to the increasing dorsiflexion force (ΔF) with a fixed ankle joint. Notably, the Δ1 − ΔF relationship in the tendon was found to be quadratic in nature (ΔF = cΔ12; c=1.48 ∼ 2.24, r=0.985 ∼ 0.992, n=9) as has been reported in the isolated tendon, although the ΔF − Δ1 curves were slightly underestimated in comparison with the stiffness constant estimated from tendon architecture. This underestimation might be caused by changes in the height of the foot arch with the application of force.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    ISSN: 1573-7284
    Schlagwort(e): EnterotoxigenicEscherichia coli ; Yibrio cholerae ; LT ; CT
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract It was examined where a protease purified from Vibrio cholerae might nick the heat-labile enterotoxin (LT) A subunit from enterotoxigenicEscherichia coli. LT was digested by the protease and contained a fragment which had the same mobility on SDS-PAGE as that of the Al fragment of LT digested by trypsin. The biological activity of LT by this protease was also identical to that of LT by trypsin. The amino acid sequence of the N-terminus of the A2-like fragment was Thr-Ser-Thr-Gly, which corresponded to the sequence from 193 to 196 of the A subunit. These data suggest that this protease, like trypsin, nicks arginine at position 192 from the N-terminus of the A subunit and that the biological activation of LT by this protease is similar to that by trypsin.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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