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  • 1
    Electronic Resource
    Electronic Resource
    Identification and typing of members of the protein-tyrosine phosphatase gene family expressed in mouse brain (1992)
    Springer
    Molecular biology reports 16 (1992), S. 241-248 
    Details
    ISSN: 1573-4978
    Keywords: mouse brain ; protein evolution ; protein-tyrosine phosphatases ; signal transduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Protein-tyrosine phosphatases (PTPases) form a novel and important class of cell regulatory proteins. We evaluated the expression of PTPases in mouse brain by polymerase chain amplification of cDNA segments that encode the catalytic domains of these enzymes. Degenerate primer pairs devised on the basis of conserved protein motifs were used to generate a series of distinct PCR-derived clones. In this way, murine homologues of the human PTPases LRP, PTPβ, PTPδ, PTPɛ and LAR were obtained. Corresponding regions in their catalytic domains were used to reveal the evolutionary relationships between all currently known mammalian PTPase protein family members. Phylogenetic reconstruction displayed considerable differences in mutation rates for closely related PTPases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00419663
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  • 2
    Electronic Resource
    Electronic Resource
    Rapid assessment of protein-tyrosine phosphatase expression levels by RT-PCR with degenerate primers (1994)
    Springer
    Molecular biology reports 19 (1994), S. 105-108 
    Details
    ISSN: 1573-4978
    Keywords: expression ; polymerase chain reaction ; protein-tyrosine phosphatases ; reverse transcription ; signal transduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Using degenerate oligodeoxynucleotide primers we previously obtained cDNA fragments from ten different murine protein-tyrosine phosphatases (PTPases). Employing this same primer set, a method was developed to assess the expression levels of these PTPase family members in a fast and simple way. RT-PCR products of several cell types and tissue samples were used as probes on dot-blots containing the ten different PTPase fragments in equimolar amounts. Hybridization intensities at the various dots reflect the relative expression levels of the corresponding PTPases in the starting material. In this way expression of PTPases during mouse brain development could be monitored. Expression of PTPδ was found to be absent in embryonic stem cells but high in fetal and adult brain. PTPɛ expression is shown to gradually increase in brain during maturation. Our method is generally applicable to gene families of which the transcripts can be detected with a single degenerate primer pair and is especially useful in situations where only limited amounts of RNA can be obtained.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00997155
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  • 3
    Electronic Resource
    Electronic Resource
    Receptor-like protein tyrosine phosphatases: alike and yet so different (1997)
    Springer
    Molecular biology reports 24 (1997), S. 247-262 
    Details
    ISSN: 1573-4978
    Keywords: cell adhesion ; development ; differentiation ; receptors ; signal transduction ; tyrosine phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Reversible phosphorylation on tyrosine residues is an extremely rapid and powerful posttranslational modification that is used in signalling pathways for the regulation of cell growth and differentiation. Over the past several years an impressive number of receptor-like protein tyrosine phosphatase (RPTPase) family members have been identified by molecular cloning, and undoubtedly many more will follow. This review provides an overview of the molecular data that are available for the currently identified RPTPases and discusses their possible biological implications.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006870016238
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  • 4
    Electronic Resource
    Electronic Resource
    Tissue- and cell-specific distribution of creatine kinase B: A new and highly specific monoclonal antibody for use in immunohistochemistry (1995)
    Springer
    Cell & tissue research 280 (1995), S. 435-446 
    Details
    ISSN: 1432-0878
    Keywords: Creatine kinase ; B-subunit ; Monoclonal antibody ; Immunohistochemistry ; Immuno-electron microscopy ; Western blot ; Mouse (C57BL/6) ; Rabbit (New Zealand White)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract A synthetic 17-mer peptide corresponding to an unique sequence in the amino-terminal region of human creatine kinase B was used to raise a new and highly B-subunit-specific monoclonal antibody, CK-BYK/21E10. We show here that the monoclonal antibody is suitable for immunohistochemistry of unfixed frozen sections as well as formaldehyde- or Bouin-fixed, paraffin-embedded sections of human, rabbit, and mouse tissues. Moreover, in the study of cell- and tissue-specific distribution patterns, parallel Western blot analysis and immunoelectron microscopy is possible using this antibody. Our analyses demonstrate that creatine kinase B expression is restricted to a specific subset of cell types in various tissues. In brain, the B-subunit was found only in neurocytes, but not in glia cells. High expression was also observed in inner segments of photoreceptor cells and the outer plexiform layer of the retina, in the parietal cells of the stomach and in gut enterocytes, gallbladder and epithelial cells of the urogenital system. The possible roles of the creatine kinase/phosphocreatine-ATP system in these tissues are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307817
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  • 5
    Electronic Resource
    Electronic Resource
    Tissue- and cell-specific distribution of creatine kinase B: A new and highly specific monoclonal antibody for use in immunohistochemistry (1995)
    Springer
    Cell & tissue research 280 (1995), S. 435-446 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Creatine kinase ; B-subunit ; Monoclonal antibody ; Immunohistochemistry ; Immuno-electron microscopy ; Western blot ; Mouse (C57BL/6) ; Rabbit (New Zealand White)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. A synthetic 17-mer peptide corresponding to an unique sequence in the amino-terminal region of human creatine kinase B was used to raise a new and highly B-subunit-specific monoclonal antibody, CK-BYK/21E10. We show here that the monoclonal antibody is suitable for immunohistochemistry of unfixed frozen sections as well as formaldehyde- or Bouin-fixed, paraffin-embedded sections of human, rabbit, and mouse tissues. Moreover, in the study of cell- and tissue-specific distribution patterns, parallel Western blot analysis and immuno-electron microscopy is possible using this antibody. Our analyses demonstrate that creatine kinase B expression is restricted to a specific subset of cell types in various tissues. In brain, the B-subunit was found only in neurocytes, but not in glia cells. High expression was also observed in inner segments of photoreceptor cells and the outer plexiform layer of the retina, in the parietal cells of the stomach and in gut enterocytes, gallbladder and epithelial cells of the urogenital system. The possible roles of the creatine kinase/phosphocreatine-ATP system in these tissues are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307817
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  • 6
    Electronic Resource
    Electronic Resource
    Molecular cloning of a mouse epithelial protein-tyrosine phosphatase with similarities to submembranous proteins (1995)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 59 (1995), S. 418-430 
    Details
    ISSN: 0730-2312
    Keywords: gene expression ; mouse embryo ; signal transduction ; band 4.1 ; discs-large homologous region ; membrane skeleton ; cytoskeleton ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Protein-tyrosine phosphatases (PTPases) form an important class of cell regulatory proteins. We have isolated overlapping cDNA clones that together comprise an 8 kb transcript encoding a novel murine PTPase which is expressed in various organs. Sequence analysis revealed an open reading frame of 2,460 amino acid residues. The predicted protein, PTP-BL, is a large non-transmembrane PTPase that exhibits 80% homology with PTP-BAS, a recently described human PTPase. PTP-BL shares some intriguing sequence homologies with submembranous proteins. It contains a band 4.1-like motif also present in the tumor suppressors neurofibromatosis 2 and expanded, five 80 amino acid repeats also present in the disc-large tumor suppressor, and a single catalytic phosphatase domain. No obvious homologies to other proteins were found for the N-terminal region of the protein other than human PTP-BAS. RNA in situ hybridization experiments show that the PTP-BL gene is expressed in epithelial cells, predominantly in kidney, lung, and skin. These data suggest a cell cortical localization for PTP-BL in epithelial cells and a possible role in the morphology and motility of epithelial tissues. © 1995 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240590403
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