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  • 1
    Electronic Resource
    Electronic Resource
    SPECIFICITY AND VERSATILITY IN TGF-?‚ SIGNALING THROUGH SMADS (2005)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Cell and Developmental Biology 21 (2005), S. 659-693 
    Details
    ISSN: 1081-0706
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Notes: The TGF-?‚ family comprises many structurally related differentiation factors that act through a heteromeric receptor complex at the cell surface and an intracellular signal transducing Smad complex. The receptor complex consists of two type II and two type I transmembrane serine/threonine kinases. Upon phosphorylation by the receptors, Smad complexes translocate into the nucleus, where they cooperate with sequence-specific transcription factors to regulate gene expression. The vertebrate genome encodes many ligands, fewer type II and type I receptors, and only a few Smads. In contrast to the perceived simplicity of the signal transduction mechanism with few Smads, the cellular responses to TGF-?‚ ligands are complex and context dependent. This raises the question of how the specificity of the ligand-induced signaling is achieved. We review the molecular basis for the specificity and versatility of signaling by the many ligands through this conceptually simple signal transduction mechanism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.cellbio.21.022404.142018
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  • 2
    Electronic Resource
    Electronic Resource
    Receptor-associated Mad homologues synergize as effectors of the TGF-β response (1996)
    [s.l.] : Nature Publishing Group
    Nature 383 (1996), S. 168-172 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Several vertebrate Mad homologues have been implicated in BMP-2/4 and activin signalling. MADRl/Smad-1 is phosphorylated following coexpression with type I and type II BMP-2/4 receptors7, andXenopus XMad-1 and XMad-2 induce BMP-2/4-like ventral or activin-like dorsal mesoderm, respectively, in ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/383168a0
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  • 3
    Electronic Resource
    Electronic Resource
    Smad3 and Smad4 cooperate with c-Jun/c-Fos to mediate TGF-β-induced transcription (1998)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 394 (1998), S. 909-913 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Smad proteins transduce signals for transforming growth factor-β (TGF-β)-related factors. Smad proteins activated by receptors for TGF-β form complexes with Smad4. These complexes are translocated into the nucleus and regulate ligand-indu ced gene transcription. 12- ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/29814
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  • 4
    Electronic Resource
    Electronic Resource
    Restoration of shooty morphology of a nontumorous mutant of Nicotiana glauca x N. langsdorffii by cytokinin and the isopentenyltransferase gene (1990)
    Springer
    Plant molecular biology 15 (1990), S. 407-420 
    Details
    ISSN: 1573-5028
    Keywords: cytokinin ; tumor formation ; isopentenyltransferase gene ; Nicotiana ; genetic tumors ; polymerase chain reaction (PCR) ; transformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The shooty morphology of a nontumorous amphidiploid mutant of Nicotiana glauca Grah. x N. langsdorffii Weinm. was restored by cytokinins, whether exogenously applied or endogenously produced by transformation of the mutant with a transfer DNA (T-DNA) cytokinin-biosynthesis gene (isopentenyltransferase; ipt). Auxins alone did not confer this effect. Similar transformation was not achieved for the parental species. In the case of transformation with the ipt gene, selection of the transformed tissues was based on its hormone-independent growth in the presence of the antibiotic kanamycin. Transformed tissues exhibited a shooty morphology, indistinguishable from that of wildtype genetic tumors N. glauca x N. langsdorffii. This altered phenotype was caused by the presence and constitutive expression of the ipt gene. The insertion and expression of this gene in transformed tissues was confirmed by using the polymerase chain reaction (PCR) technique as well as conventional molecular hybridization analysis. Expression of the ipt gene led to an elevated level of cytokinin in the transformed mutant tissues. This evidence supports the notion that genetic tumors are caused, at least in part, by elevated levels of cytokinin in interspecific hybrids.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00019158
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  • 5
    Electronic Resource
    Electronic Resource
    Molecular identification of a soybean protein kinase gene family by using PCR (1992)
    Springer
    Plant molecular biology 18 (1992), S. 581-584 
    Details
    ISSN: 1573-5028
    Keywords: gene family ; polymerase chain reaction ; protein kinases ; signal transduction ; soybean (Glycine max L.)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In this study we report identification of six members of a protein kinase gene family from soybean (Glycine max L.). Two fully degenerate oligonucleotide primers corresponding to two conserved motifs (DLK-PENV and GTHEYLAPE) in the catalytic domains of eukaryotic protein serine/threonine kinases were used in a polymerase chain reaction (PCR) to amplify soybean cDNA. Sequence analysis showed that 28 of the PCR sequences represented six different putative protein serine/threonine kinases. These results not only demonstrate that catalytic domains of protein kinases are highly conserved between plants and other eukaryotes but also suggest that there are multiple genes encoding protein kinases in plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00040673
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  • 6
    Electronic Resource
    Electronic Resource
    Molecular cloning and biochemical characterization of a receptor-like serine/threonine kinase from rice (1994)
    Springer
    Plant molecular biology 26 (1994), S. 791-803 
    Details
    ISSN: 1573-5028
    Keywords: ATP ; GTP ; protein kinase ; receptor ; rice ; signal transduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A receptor-like protein kinase, OsPK10, has been cloned from rice (Oryza sativa). The 2.8 kb cDNA contains an open reading frame capable of encoding a peptide sequence of 824 amino acids. The topological features of the predicted OsPK10 protein include an N-terminal signal peptide, a cysteine-rich extracellular ligand-binding domain, a membrane-spanning segment, and a cytoplasmic domain possessing all the hallmarks of catalytic domains of eukaryotic protein kinases. The cytoplasmic domain was selectively expressed in Escherichia coli and assayed for kinase activity. The results show the protein is capable of autophosphorylation using either ATP or GTP as the phosphate donor. Phosphoamino acid analysis reveals phosphorylation of threonines, consistent with the substrate specificity indicated by sequence motifs in the catalytic core. A single amino acid substitution of Glu for Lys-528 completely abolishes autophosphorylation activity. DNA gel blot analyses suggest that the haploid rice genome contains a single copy of the OsPK10 gene. OsPK10 transcripts appear to be more abundant in shoots than in roots of rice seedlings.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00028849
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