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  • 1
    Electronic Resource
    Electronic Resource
    Detection of the Microtubule Cytoskeleton of the Coccidian Toxoplasma gondii and the Hemoflagellate Leishmania donovani by Monoclonal Antibodies Specific for β-Tubulin (1985)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 32 (1985), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Seven monoclonal antibodies specific for mammalian β-tubulin demonstrate the microtubule cytoskeleton of Toxoplasma gondii and Leishmania donovani by indirect immunofluorescence microscopy. Immunoblots of T. gondii and L. donovani proteins separated by SDS polyacrylamide gel electrophoresis confirm the specificity of the monoclonal antibodies for tubulin. Differential staining of flagellar and subpellicular microtubule populations was not seen in L. donovani with these antibodies. All seven antibodies also detected the subpellicular microtubules of T. gondii, but the polar ring and conoid of this organism was not visualized by any of them. This technique provides a rapid and specific way to assess microtubular organization in whole organisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.1985.tb03115.x
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  • 2
    Electronic Resource
    Electronic Resource
    Differential Localization of MAP-2 and Tau in Mammalian Neurons in Situ (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 466 (1986), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1986.tb38392.x
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  • 3
    Electronic Resource
    Electronic Resource
    DIRECTIONALITY AND RATE OF ASSEMBLY OF CHICK BRAIN TUBULIN ONTO PIECES OF NEUROTUBULES, FLAGELLAR AXONEMES, AND BASAL BODIES (1975)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 253 (1975), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1975.tb19198.x
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  • 4
    Electronic Resource
    Electronic Resource
    The Cytomatrix Regulates “Resolute” Transport in Erythrophores (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 466 (1986), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1986.tb38475.x
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  • 5
    Electronic Resource
    Electronic Resource
    Tau as a nucleolar protein in human nonneural cells in vitro and in vivo (1996)
    Springer
    Chromosoma 105 (1996), S. 20-30 
    Details
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The Tau-1 monoclonal antibody was localized to the nucleolus of interphase cells and the nucleolar organizing regions (NORs) of acrocentric chromosomes in cultured human cells. Putative nucleolar and NOR tau was found in HeLa cells and lymphoblasts as well as in nontransformed fibroblasts and lymphocytes. To confirm the presence of tau in the nuclei of these nonneural cells, immunoblotting analysis was performed on isolated nuclei from lymphoblasts. Several tau bands were noted on the blot of the nuclear extract suggesting the presence of multiple tau isoforms. Tau-1 immunostaining demonstrated variable staining intensities between individual acrocentric chromosomes in all cells tested. In cultured peripheral lymphocytes, these staining patterns were the same from one chromosome spread to the next within an individual. This consistency of Tau-1 staining and its variability among NORs was reminiscent of staining patterns obtained using the silver-NOR procedure. Comparisons of Tau-1 immunostaining with silver staining of chromosome spreads from human lymphocytes demonstrated that Tau-1 did not immunostain all of the NORs that were silver stained. The intensity of Tau-1 fluorescence in nucleoli was further shown to be increased in phytohemagglutinin-stimulated lymphocytes, indicating an upregulation of nuclear tau when cells reentered the cell cycle. These results contribute to a growing body of evidence defining tau as a multifunctional protein that may be involved in ribosomal biogenesis and/or rRNA transcription in the nucleus of all cells as well as microtubule-stabilizing functions in the neuronal cytoplasm.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004120050155
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  • 6
    Electronic Resource
    Electronic Resource
    Evidence that MAP-2 may be involved in pigment granule transport in squirrel fish erythrophores (1987)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 7 (1987), S. 221-234 
    Details
    ISSN: 0886-1544
    Keywords: α-cytomatrix ; monoclonal antibodies ; immnuolabeling ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We have demonstrated the presence of MAP-2 in squirrel fish erythrophores using SDS-PAGE, immunobolt, and immunoprecipitation techniques. The monoclonal antibodies used (AP-9, -13, -14) were raised against distinct antigenic sites on Chinese hamster brain MAP-2. Immunoprecipitation studies demonstrated that all three antibodies bind a 300 K protein found in crude cell extracts and in partially purified MAP fractions isolated from erythrophores of the squirrel fish Holocentrus rufus. Immunofluorescent studies confirmed that the 300 K protein was present in cultured erythrophores. Studies of cells induced to aggregate and disperse their pigment granules revealed that the 300 K protein comigrated with the pigment, suggesting that the 300 K protein may constitute part of the “α-cytomatrix” involved in pigment translocations.
    Additional Material: 20 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970070305
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  • 7
    Electronic Resource
    Electronic Resource
    Phosphorylation determines two distinct species of tau in the central nervous system (1987)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 8 (1987), S. 210-226 
    Details
    ISSN: 0886-1544
    Keywords: tau antibodies ; immunohistochemistry ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The monoclonal antibody, Tau-1, which had previously been used to localize tau to the axonal compartment in brain has been reutilized for light and electron microscopic immunohistochemistry following phosphatase treatment of tissue. We report here that a significant quantity of tau in the central nervous system is phosphorylated in situ at or near the Tau-1 epitope, preventing the binding of the Tau-1 antibody. Upon removal of this/these phosphate group(s), however, Tau-1 was observed in the somatodendritic compartment of neurons as well as in axons. Furthermore, intense staining was also observed in astrocytes and in perineuronal glial cells. This immunoreactivity was present along the lengths of microtubules and on ribosomes (polysomes). Treatment of immunoblots of extracts of whole cerebral cortex with phosphatase confirmed the immunohistochemical results in that a 50-65% increase in Tau-1 binding to the tau region of the blot was noted. Moreover, a novel monoclonal antibody, Tau-2, was also used in these experiments. This antibody binds only to tau and localizes along microtubulesin axons, somata, dendrites, and astrocytes and on ribosomes (polysomes) without phosphatase pretreatment.
    Additional Material: 13 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970080303
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  • 8
    Electronic Resource
    Electronic Resource
    Identification and characterization of a novel mammalian intermediate filament-associated protein (1990)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 17 (1990), S. 19-33 
    Details
    ISSN: 0886-1544
    Keywords: HeLa cells ; microtubule-associated proteins ; MAPIA ; vimentin filaments ; cytokeratin filaments ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A novel monoclonal antibody, designated M1.4, recognizes the high molecular weight microtubule-associated protein MAPIA (ca. Mr 380 kD) in both bovine and rat brain. In HeLa cells, however, M1.4 binds to a 240 kD polypeptide on immunoblots and co-localizes with both vimentin and cytokeratin filaments using double-label immunofluorescence microscopy. Immunoelectron microscopy indicates that the 240 kD polypeptide localizes along bundled intermediate filaments in a periodic manner. Two-dimensional electrophoretic analysis indicates that the 240 kD polypeptide has a basic pI of 7.7. When HeLa cell intermediate filaments are isolated using standard non-ionic detergent/high-salt conditions the 240 kD polypeptide does not sediment with the intermediate filaments, unlike the established intermediate filament-associated protein plectin. Immunoblot analysis with M1.4 shows the 240 kD polypeptide is expressed in a number of mammalian cell lines. Additionally, double-label immunofluorescence shows the 240 kD polypeptide to associate with vimentin filaments in African Green Monkey kidney (CV-1) and JC neuroblastoma cells. Due to its unique biochemical and biological characteristics, the 240 kD polypeptide is clearly a novel intermediate filament-associated protein for which we have proposed the designation gyronemin (Gr.gyros: around: nemin: filament).
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970170105
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  • 9
    Electronic Resource
    Electronic Resource
    Actin-binding protein is a component of bovine erythrocytes (1993)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 24 (1993), S. 100-108 
    Details
    ISSN: 0886-1544
    Keywords: actin-binding protein ; filamin ; erythrocytes ; membrane skeleton ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Actin-binding protein (ABP) is a well-characterized polypeptide capable of crosslinking filamentous actin. To date, this polypeptide has been shown to exist in a number of tissues and cultured cell lines. This report shows that by using a panel of three monoclonal antibodies for immunoblotting and immunofluorescence analysis, that ABP is present in bovine erythrocytes. Moreover, the data obtained suggest that this protein is a component of the erythrocyte membrane skeleton. Additionally, bovine erythrocyte ABP is shown to possess both an apparent molecular weight and an isoelectric point identical to that of bovine smooth muscle filamin, implying that these two polypeptides are identical. © 1993 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970240203
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  • 10
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    Tau as a nucleolar protein in human nonneural cells in vitro and in vivo (1996)
    Springer
    Details
    Publication Date: 1996-07-01
    Print ISSN: 0009-5915
    Electronic ISSN: 1432-0886
    Topics: Biology , Medicine
    Published by Springer
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