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  • 1
    Online Resource
    Online Resource
    American Society for Microbiology ; 1995
    In:  Journal of Bacteriology Vol. 177, No. 15 ( 1995-08), p. 4571-4574
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 177, No. 15 ( 1995-08), p. 4571-4574
    Abstract: A cell-free system was used to characterize the phosphorylation of Mycoplasma pneumoniae proteins HMW1 and HMW2, which are involved in the adherence of this organism to human tracheal epithelium during infection. The pH and cation requirements for phosphorylation of HMW1 and HMW2 were determined, and the effects of glycolytic intermediates, cyclic AMP, and eukaryotic kinase-phosphatase inhibitors and stimulators on this process were examined. Phosphoamino acid analysis identified serine as the major phosphate acceptor for both HMW1 and HMW2 in this system.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1995
    detail.hit.zdb_id: 1481988-0
    SSG: 12
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  • 2
    Online Resource
    Online Resource
    American Society for Microbiology ; 1994
    In:  Journal of Bacteriology Vol. 176, No. 24 ( 1994-12), p. 7499-7505
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 176, No. 24 ( 1994-12), p. 7499-7505
    Abstract: Attachment to host cells of the respiratory epithelium by Mycoplasma pneumoniae is a complex, multicomponent process, requiring a number of accessory proteins in addition to adhesins directly involved in receptor binding. In this study, protein phosphorylation of the cytadherence-accessory proteins HMW1, HMW2, and HMW4 of M. pneumoniae was examined using biochemical and immunological techniques. The initial indication of protein modification came from Western immunoblot analysis of the two-dimensional polyacrylamide gel electrophoresis (PAGE) profile of M. pneumoniae proteins, revealing multiple spots for both HMW1 and HMW4 that varied in pI but not in size. M. pneumoniae cultured in the presence of H3(32)PO4 exhibited numerous phosphorylated proteins as detected by sodium dodecyl sulfate-PAGE and autoradiography. These included proteins corresponding to HMW1, HMW2, and HMW4 in electrophoretic mobility. The Triton X-100 partitioning characteristics of these phosphorylated proteins was identical to that described previously for HMW1, -2, and -4. Furthermore, these protein bands were absent when a noncytadhering variant deficient in HMW1-5 was examined in the same manner. Finally, the availability of antiserum to HMW1 and -4 enabled us to confirm by radioimmunoprecipitation that HMW1 and HMW4 are phosphoproteins. Phosphoamino acid analysis of acid-hydrolyzed HMW1 and HMW2 identified primarily phosphothreonine and, to a lesser extent, phosphoserine in HMW1 and predominantly phosphoserine, with a trace of phosphothreonine, in HMW2. Neither protein contained phosphotyrosine. HMW1-HMW5 are components of a cytoskeleton-like structure in M. pneumoniae that is thought to function in cell division, changes in cell morphology, gliding motility, and the localization of adhesins in the mycoplasma membrane. Phosphorylation may regulate cytoskeleton dynamics involving these cytadherence-accessory proteins.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1994
    detail.hit.zdb_id: 1481988-0
    SSG: 12
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  • 3
    In: Infection, Genetics and Evolution, Elsevier BV, Vol. 10, No. 7 ( 2010-10), p. 1027-1038
    Type of Medium: Online Resource
    ISSN: 1567-1348
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2010
    detail.hit.zdb_id: 2057622-5
    SSG: 12
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  • 4
    In: Cardiovascular Diabetology, Springer Science and Business Media LLC, Vol. 17, No. 1 ( 2018-12)
    Type of Medium: Online Resource
    ISSN: 1475-2840
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2018
    detail.hit.zdb_id: 2093769-6
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  • 5
    Online Resource
    Online Resource
    Proceedings of the National Academy of Sciences ; 1997
    In:  Proceedings of the National Academy of Sciences Vol. 94, No. 25 ( 1997-12-09), p. 13979-13984
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 94, No. 25 ( 1997-12-09), p. 13979-13984
    Abstract: The genomic sequence of Mycoplasma pneumoniae establish this cell-wall-less prokaryote as among the smallest known microorganisms capable of self-replication. However, this genomic simplicity and corresponding biosynthetic austerity are sharply contrasted by the complex terminal structure found in this species. This tip structure (attachment organelle) directs colonization of the human respiratory mucosa, leading to bronchitis and atypical pneumonia. Furthermore, formation of a second tip structure appears to precede cell division, implying temporal regulation. However, the organization, regulation, and assembly of the attachment organelle in M. pneumoniae are poorly understood, and no counterparts have been identified among the walled bacteria. M. pneumoniae possesses a cytoskeleton-like structure required to localize adhesin proteins to the attachment organelle. The cytadherence-associated proteins HMW1, HMW2, and HMW3 are components of the mycoplasma cytoskeleton, with HMW1 localizing strictly along the filamentous extensions from the cell body and HMW3 being a key structural element of the terminal organelle. Disruptions in hmw2 result in the loss of HMW1 and HMW3. However, the hmw1 and hmw3 genes were transcribed and translated at wild-type levels in hmw2 mutants. HMW1 and HMW3 were relatively stable in the wild-type background over 8 h but disappeared in the mutants over this time period. Evaluation of recombinant HMW1 levels in mycoplasma mutants suggested a requirement for the C-terminal domain of HMW1 for turnover. Finally, an apparent defect in the processing of the precursor for the adhesin protein P1 was noted in the HMW − mutants.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    RVK:
    RVK:
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 1997
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
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  • 6
    Online Resource
    Online Resource
    Elsevier BV ; 2010
    In:  Molecular Phylogenetics and Evolution Vol. 54, No. 2 ( 2010-02), p. 372-385
    In: Molecular Phylogenetics and Evolution, Elsevier BV, Vol. 54, No. 2 ( 2010-02), p. 372-385
    Type of Medium: Online Resource
    ISSN: 1055-7903
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2010
    detail.hit.zdb_id: 1471402-4
    SSG: 12
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  • 7
    Online Resource
    Online Resource
    Canadian Science Publishing ; 2008
    In:  Canadian Journal of Earth Sciences Vol. 45, No. 12 ( 2008-12), p. 1517-1525
    In: Canadian Journal of Earth Sciences, Canadian Science Publishing, Vol. 45, No. 12 ( 2008-12), p. 1517-1525
    Abstract: The 3D acoustic wave equation for a heterogeneous medium is used for the seismic modeling of compressional (P-) wave propagation in complex subsurface structures. A combination of finite difference and finite integral transform methods is employed to obtain a “2.5D” solution to the 3D equation. Such 2.5D approaches are attractive because they result in computational run times that are substantially smaller than those for the 3D finite difference method. The acoustic parameters of the medium are assumed to be constant in one of the three Cartesian spatial dimensions. This assumption is made to reduce the complexity of the problem, but still retain the salient features of the approach. Simple models are used to address the computational issues that arise in the modeling. The conclusions drawn can also be applied to the more general fully inhomogeneous problem. Although similar studies have been carried out by others, the work presented here is new in the sense that (i) it applies to subsurface models that are both vertically and laterally heterogeneous, and (ii) the computational issues that need to be addressed for efficient computations, which are not trivial, are examined in detail, unlike previous works. We find that it is feasible to generate true-amplitude synthetic seismograms using the 2.5D approach, with computational run times, storage requirements, and other factors, being at reduced and acceptable levels.
    Type of Medium: Online Resource
    ISSN: 0008-4077 , 1480-3313
    Language: English
    Publisher: Canadian Science Publishing
    Publication Date: 2008
    detail.hit.zdb_id: 417294-2
    detail.hit.zdb_id: 1491201-6
    SSG: 16,13
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  • 8
    Online Resource
    Online Resource
    Society of Exploration Geophysicists ; 2005
    In:  The Leading Edge Vol. 24, No. 5 ( 2005-05), p. 530-534
    In: The Leading Edge, Society of Exploration Geophysicists, Vol. 24, No. 5 ( 2005-05), p. 530-534
    Type of Medium: Online Resource
    ISSN: 1070-485X , 1938-3789
    Language: English
    Publisher: Society of Exploration Geophysicists
    Publication Date: 2005
    detail.hit.zdb_id: 1221792-X
    detail.hit.zdb_id: 2083479-2
    SSG: 16,13
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