Search Results - (Author, Cooperation:B. Beckerman)

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  1. 1
    K. Zhao ; B. S. Tseng ; B. Beckerman ; F. Jin ; M. L. Gibiansky ; J. J. Harrison ; E. Luijten ; M. R. Parsek ; G. C. Wong
    Nature Publishing Group (NPG)
    Published 2013
    Staff View
    Publication Date:
    2013-05-10
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Algorithms ; Bacterial Adhesion/physiology ; Biofilms/*growth & development ; Cell Tracking ; Feedback, Physiological ; Fluorescent Dyes ; Polysaccharides, Bacterial/*metabolism ; Pseudomonas aeruginosa/*cytology/*growth & development ; Staining and Labeling
    Published by:
    http://www.nature.com/

    Latest Papers from Table of Contents or Articles in Press
  2. 2
    YAMADA, T. ; KLUVE-BECKERMAN, B. ; LIEPNIEKS, J. J. ; BENSON, M. D.

    Oxford, UK : Blackwell Publishing Ltd
    Published 1995
    Staff View
    ISSN:
    1365-3083
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Medicine
    Notes:
    The effects of acid proteases on degradation of serum amyloid A protein (SAA) were investigated in vitro. Human recombinant SAA1 (rSAA1), when incubated with human spleen extracts at pH 3.2, was degraded in the amino-terminal portion of the molecule. This reaction was inhibited by an acid protease inhibitor, pepstatin. The degraded SAA molecules lacking nine or more amino-terminal residues, when exposed to in vitro fibril-forming conditions, failed to form Congo red positive precipitates and did not show amyloid fibril-like structure by electron microscopy. This suggests that the amino-terminal portion of SAA is essential for fibril formation. Cathepsin D, one of the lysosomal enzymes, also initiated degradation of rSAAl at the amino-terminus. Cathepsin D immunoreactivity was detected in marginal areas of amyloid deposits in spleens from patients with reactive amyloidosis. These findings suggest that cathepsin D or similar acid proteases may be involved in SAA catabolism and may protect against amyloid formation.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1111/j.1365-3083.1995.tb03609.x

    Articles: DFG German National Licenses
  3. 3
    Kluve–beckerman, B. ; Manaloor, J. ; Liepnieks, J. J.

    Oxford, UK : Blackwell Science Ltd
    Published 2001
    Staff View
    ISSN:
    1365-3083
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Medicine
    Notes:
    Murine serum amyloid A1.1 (SAA1.1) has been conjugated with the fluorophore Texas Red (TxR), and its interaction with peritoneal macrophages has been visualized by scanning confocal microscopy. Binding of TxR–SAA to cell surfaces was inhibited by an excess of unlabelled SAA indicating the involvement of saturable receptors. Internalized TxR–SAA was seen initially as small punctate signals which in some cells evolved into a fine fluorescent network, a pattern typical of tubular endosomes. Colocalization of TxR–SAA with Cy5-labelled low density lipoprotein (LDL) but not with Oregon Green-labelled transferrin suggested that SAA trafficked through endosomes and lysosomes for degradation rather than through recycling compartments. Consistent with this catabolic pathway, macrophages loaded with TxR–SAA lost fluorescence within several days after being shifted to a fluorophore-free medium. In sharp contrast to this, cells maintained under amyloid-forming conditions, i.e. in the presence of unlabelled SAA and amyloid-enhancing factor (AEF) before and after treatment with TxR–SAA, remained brightly fluorescent over the course of 5 days. Immunocytochemistry verified the accumulation of SAA within macrophages. These findings support the hypothesis that a decreased catabolism of internalized SAA plays a role in AA amyloid pathogenesis.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1046/j.1365-3083.2001.00879.x

    Articles: DFG German National Licenses
  4. 4
    Staff View
    ISSN:
    0925-4439
    Keywords:
    Amyloid fibril ; Isotype ; Recombinant ; Serum amyloid A
    Source:
    Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Physics
    Type of Medium:
    Electronic Resource
    URL:
    http://linkinghub.elsevier.com/retrieve/pii/0925-4439(94)90044-2

    Articles: DFG German National Licenses
  5. 5
    Staff View
    ISSN:
    0925-4439
    Keywords:
    Amyloid ; Baculovirus ; Serum amyloid A
    Source:
    Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Physics
    Type of Medium:
    Electronic Resource
    URL:
    http://linkinghub.elsevier.com/retrieve/pii/0925-4439(93)90073-A

    Articles: DFG German National Licenses
  6. 6
    Staff View
    ISSN:
    0888-7543
    Source:
    Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics:
    Biology
    Medicine
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1006/geno.1993.1050

    Articles: DFG German National Licenses
  7. 7
    Staff View
    ISSN:
    0006-291X
    Source:
    Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics:
    Biology
    Chemistry and Pharmacology
    Physics
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1016/0006-291X(85)91956-4

    Articles: DFG German National Licenses
  8. 8
    Staff View
    ISSN:
    0006-291X
    Source:
    Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics:
    Biology
    Chemistry and Pharmacology
    Physics
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1016/0006-291X(86)90352-9

    Articles: DFG German National Licenses
  9. 9
    Staff View
    ISSN:
    0006-291X
    Source:
    Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics:
    Biology
    Chemistry and Pharmacology
    Physics
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1016/0006-291X(91)92051-K

    Articles: DFG German National Licenses
  10. 10
    Staff View
    ISSN:
    0305-0491
    Source:
    Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics:
    Biology
    Chemistry and Pharmacology
    Type of Medium:
    Electronic Resource
    URL:
    http://linkinghub.elsevier.com/retrieve/pii/0305-0491(89)90030-8

    Articles: DFG German National Licenses
  11. 11
    YAMADA, T. ; LIEPNIEKS, J. J. ; KLUVE-BECKERMAN, B. ; BENSON, M. D.

    Oxford, UK : Blackwell Publishing Ltd
    Published 1995
    Staff View
    ISSN:
    1365-3083
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Medicine
    Notes:
    Amyloid A protein (AA), the chief constituent of reactive amyloid deposits, is derived from serum amyloid A (SAA) and most commonly corresponds to the amino-terminal 76 residues (AA76). Digestion of recombinant human SAAl with a lysosomal thiol protease, cathepsin B. and analysis of the products by SDS-PAGE and amino-terminal sequencing revealed that AA76 was generated as a minor and transient degradation product. Digestion with neutrophil eiastase generated intermediates different from AA76. This finding suggests that cathepsin B may play an important role in amyloid fibrilogenesis by converting SAA to AA.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1111/j.1365-3083.1995.tb03538.x

    Articles: DFG German National Licenses