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  • 1
    Electronic Resource
    Electronic Resource
    Chichester [u.a.] : Wiley-Blackwell
    International Journal for Numerical Methods in Engineering 26 (1988), S. 1567-1578 
    ISSN: 0029-5981
    Keywords: Engineering ; Engineering General
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Mathematics , Technology
    Notes: It is difficult to analyse a large, complex structure in sufficient detail to obtain accurate results everywhere. One approach is simply to refine the whole structure model in the regions of interest. Another approach is to identify a subregion of the structure and develop a separate refined model of the subregion. It is difficult to assure accuracy in this subregion model because of uncertainties in specifying boundary conditions and loading from the whole structure model solution. In the current literature, three methods other than whole model refinement have been described to deal with this problem. These are called the specified boundary displacement method, the linear constraint method and the zooming method.This paper describes a new approach to this problem of modelling subregions. This approach uses the stiffnesses and forces from the whole model solution at the nodes on the boundary of the sub-region model. Accurate displacement and stress solutions are obtained with this method as it takes into account the interaction between the new stiffness of the subregion and the rest of the structure. This approach is similar to substructuring; however, the equations outside the subregion are discarded rather than condensed out, which results in much less computation effort.Examples of the application of this method to the problem of a plate with a centre hole in tensile loading are presented. The results compared favourably with the results of the same problem solved using other methods, with significant improvement in accuracy over the specified boundary displacement method. Also presented are some results from design modification of the subregion which illustrate the potential of this method for redesign application.
    Additional Material: 13 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 40 (1996), S. 383-397 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Simple collagen-like peptides comprising a repeat Gly-Pro-Hyp sequence are highly platelet-reactive when presented to platelets in triple-helical and polymeric form. This activity is not mediated by the platelet collagen receptor integrin α2β1. This may imply the existence of an intrinsic platelet reactivity associated with the collagen triple helix as such or perhaps that the Gly-Pro-Hyp sequence in collagen serves as a specific cell-recognition site. In our view this basic α2β1-independent reactivity is modulated by the presence in collagen of sequences that may either enhance or diminish the interaction with platelets. Inhibition studies with short linear peptides have allowed the tentative identification of sequences in collagen such as XPGEP(Q)GPX and D(N)GE(Q)X that may promote the activation of platelets and so enhance collagen-platelet interaction. Sequences serving as integrin α2β1-binding sites may also promote platelet reactivity by permitting interaction with the collagen receptor. Using triple-helical peptides based on the sequence of the platelet-reactive collagen type III fragment α1(III)CB4, we have been able to locate an α2β1-binding site in collagen type III within a 30-mer sequence representing residues 508-537 of the α1(III) constituent α-chain. Despite their α2β1-independent platelet reactivity, signalling by the (Gly-Pro-Hyp)n-based peptides shows many features in common with signalling by collagen fibers, including activation of p72SYK and p125FAK the latter of which has until now been considered a specific consequence of ligand binding to α2β1. © 1996 John Wiley & Sons, Inc.
    Additional Material: 10 Ill.
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 4 (1986), S. 277-281 
    ISSN: 0263-6484
    Keywords: Cortisol ; cortisol succinate ; hydrolysis ; cartilage ; synovium ; organ culture ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The pro-drug cortisol succinate is frequently used as a substitute for cortisol in organ cultures. We found, however, that in Dulbecco's modified Eagle's medium the time taken for the ester to undergo 50 per cent hydrolysis (t½) to cortisol was 75 h. When 15 per cent heat-inactivated normal rabbit serum was present t½ decreased to 47 h, but the rate of hydrolysis was not further increased in the presence of porcine articular cartilage or minced synovial tissue. When frozen and thawed synovium was present t½ decreased to 33 h, presumably due to the release of carboxyl-esterases from the disrupted cells. The level of tetrahydrocortisol was low in all of the cultures. The slow hydrolysis of cortisol succinate resulted in the exposure of the tissues to undersirable fluctuations in the concentration of active hormone, which decreased to low levels at each medium change. Thus, in co-cultures of porcine synovium and articular cartilage, cortisol had a greater inhibitory effect than cortisol succinate on the breakdown of cartilage matrix caused by synovial tissue.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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