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  • 1
    Electronic Resource
    Electronic Resource
    Temporal Expression of Mouse Glial Fibrillary Acidic Protein mRNA Studied by a Rapid In Situ Hybridization Procedure (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 45 (1985), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: A rapid and sensitive in situ hybridization technique is described for the detection of mRNA sequences in 6–8-μm cryostat sections. The method incorporates the use of α-thio-35S-labelled nucleoside triphosphates for the generation of high-specific-activity DNA probes and a high-stringency washing procedure that virtually eliminates background without unduly compromising histological integrity. Whereas signal resolution is less than that observed using 3H probes, 35S-labelled probes are well-suited for experiments where resolution at the cellular level is required. The method has been applied to a study of the developmental regulation of glial fibrillary acidic protein (GFAP) mRNA expression in developing mouse brain. GFAP-specific sequences are first detectable after the second postnatal day, and thereafter rise to a level that is maintained throughout development and into adulthood. The distribution of GFAP-encoding sequences broadly reflects the known distribution of astrocytes, but the levels of mRNA within these cells vary by a surprisingly large amount depending on their location. For example, in adult animals, the astrocytes of the glial limitans contain an abundance of GFAP-specific mRNA that is higher than corresponding levels in astrocytes in the cerebellar white matter, whereas these cells in turn contain considerably more GFAP-specific mRNA than astrocytes in the gray matter of the cerebrum. Unexpectedly, parallel RNA blot transfer experiments show the existence of some GFAP-encoding mRNA size heterogeneity that is restricted to the first postnatal week.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1985.tb04080.x
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  • 2
    Electronic Resource
    Electronic Resource
    Intragenic Sequences Affect the Expression of the Gene Encoding Glial Fibrillary Acidic Protein (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 57 (1991), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: We show that the expression of the gene encoding glial fibrillary acidic protein (GFAP) gene is affected by at least three as-acting elements. A positive regulatory element that is located between nucleotides -1, 631 and -1, 479 can confer cell type-specific expression on a heterologous gene. A second regulatory element is located between nucleotides -97 and -80. The third is a negative regulatory element that is located within the first intron of the gene. Deletion of this element activates GFAP expression in HeLa cells, and affects promoter function in glioma cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1991.tb03799.x
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  • 3
    Electronic Resource
    Electronic Resource
    Specificity in chaperonin-mediated protein folding (1995)
    [s.l.] : Nature Publishing Group
    Nature 375 (1995), S. 250-253 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] To investigate whether cytosolic chaperonin (c-cpn, the homologue of GroEL in the eukaryotic cytosol5'9"15) cycles its target proteins, we did a dilution experiment, reasoning that dilution should reduce the efficiency with which released non-native forms can be ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/375250a0
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  • 4
    Electronic Resource
    Electronic Resource
    Structural Implications of a cDNA Clone Encoding Mouse Glial Fibrillary Acidic Protein (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 455 (1985), 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.1749-6632.1985.tb50437.x
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  • 5
    Electronic Resource
    Electronic Resource
    Bad chaperone (2002)
    [s.l.] : Nature Publishing Group
    Nature medicine 8 (2002), S. 1202-1203 
    Details
    ISSN: 1546-170X
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] The Human Genome Project has greatly increased the pace of discovery of the causes of genetic disorders. In a recent example of this, eight research groups in six countries have combined to find the genetic lesion that causes a devastating autosomal recessive disease found mainly in people of ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nm1102-1202
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  • 6
    Electronic Resource
    Electronic Resource
    Organization of microtubules in dendrites and axons is determined by a short hydrophobic zipper in microtubule-associated proteins MAP2 and tau (1989)
    [s.l.] : Nature Publishing Group
    Nature 342 (1989), S. 498-505 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Here we report that the microtubule-associated proteins MAP2 and tau share two separable functional domains. One is the microtubule-binding site which serves to nucleate microtubule assembly; the second is a short C-terminal α-helical sequence which can crosslink microtubules by means of a ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/342498a0
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  • 7
    Electronic Resource
    Electronic Resource
    A chaperone with a hydrophilic surface (1999)
    [s.l.] : Nature America Inc.
    Nature structural biology 6 (1999), S. 990-991 
    Details
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] The folding of native tubulin involves at least seven different chaperone proteins: prefoldin, the cytosolic chaperonin CCT and five tubulin-specific chaperone proteins named cofactors A–E. The structure of the yeast homolog of cofactor A, Rbl2p, shows it to be a dimer with largely ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/14870
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  • 8
    Electronic Resource
    Electronic Resource
    Tubulin dimer formation via the release of α- and β-tubulin monomers from multimolecular complexes (1992)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 23 (1992), S. 222-230 
    Details
    ISSN: 0886-1544
    Keywords: native electrophoresis ; tubulin isotypes ; dimerization ; complexes ; GTP binding ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The functional subunit of microtubules is a heterodimer consisting of α- and β-tubulin. An understanding of tubulin dimerization has been hampered because it has not proved possible to purify native tubulin monomers. To study the process whereby tubulin dimers are formed, we made use of tubulins synthesized by in vitro transcription and translation. We present evidence that the in vitro synthesis of different mouse α-tubulin isotypes involves a multimolecular complex. The synthesis of mouse β-tubulin isotypes also involves the formation of multimolecular complexes, though different isotypes behave somewhat differently from one another. The properties of in vitro synthesized α- and β-tubulin multimolecular complexes strongly suggest that they are intermediates in the biosynthesis of tubulin monomers. Upon release, these monomers can exchange with pre-existing tubulin heterodimers. © 1992 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970230306
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