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  • Cell & Developmental Biology  (2)
  • Biochemistry, Immunology  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Detection and location of amphiregulin and Cripto-1 expression in the developing postnatal mouse mammary gland (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 41 (1995), S. 277-286 
    Details
    ISSN: 1040-452X
    Keywords: EGF-like ligands ; Postnatal development ; RT-PCR ; Immunocytochemistry ; Immunoblotting ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Amphiregulin (Ar) and Cripto-1 (Cr-1) are growth promoting peptides that share amino acid sequence homology with epidermal growth factor (EGF). The present study examined Ar and Cr-1 mRNA and protein expression during various stages of C57BL/6 mouse mammary morphogenesis. Reverse transciption-polymerase chain reaction (RT-PCR) was used to detect transcripts for Ar and Cr-1 at all stages of mammary development. Immunocytochemical (ICC) localization demonstrated that in virgin 4-week to mature 12-week-old mouse fourth inguinal mammary gland, Ar and Cr-1 are expressed in the stromal cells, luminal epithelial cells, and myoepithelial cells of the branching ducts. Ar, and to lesser extent Cr-1, were also found in the epithelial cap cells and in the luminal epithelial cells of the advancing terminal end bud (TEB) from virgin 4-week and 6-week-old mice. Western blot analysis demonstrated that both Ar (28 and 26 kDa) and Cr-1 (90, 67, 56, and 21 kDa) proteins are expressed in virgin, 13.5 day midpregnant and in the 14 day lactating mammary gland. In addition, Ar and Cr-1 are associated with developing alveolar structures as determined by ICC. These results imply that together with EGF and transforming growth factor alpha (TGFα), Ar and Cr-1 may play salient roles as modifiers in the morphogenesis and differentiation of the mammary gland. © 1995 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080410302
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Isolation of a clone of F9 teratocarcinoma cells “naturally” resistant to G418 (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 133 (1987), S. 46-54 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Resistance to the neomycin analogue G418 forms the basis of a dominant marker selection system for mammalian (and other) cells transfected with the bacterial neo gene. This system has been particularly effective because of the low incidence of spontaneous conversion to G418 resistance in mammalian cells; no case of resistance to the drug in the absence of the bacterial genes has yet been reported to our knowledge. During the course of transfection experiments, we recently isolated a clone of F9 teratocarcinoma cells which is drug resistant yet has no detectable integrated plasmid sequences, neo RNA transcripts, or aminoglycoside phosphotransferase activity. The G418-resistant clone (F9nr7) did not display enhanced resistance to other cytotoxic drugs tested: colchicine, actinomycin D, cycloheximide, and hygromycin B. Therefore, nr7 cells differ from multidrug-resistant phenotypes previously described. However, this clone is inhibited, relative to control cells, in its response to the differentiation-inducing drugs retinoic acid and dibutyryl cAMP, which suggests that some aspects of general drug metabolism may be altered in these cells.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041330106
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    Paper (German National Licenses)
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  • 3
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    The structural basis of flagellin detection by NAIP5: A strategy to limit pathogen immune evasion (2017)
    American Association for the Advancement of Science (AAAS)
    In: Science
    Details
    Publication Date: 2017-11-17
    Description: Robust innate immune detection of rapidly evolving pathogens is critical for host defense. Nucleotide-binding domain leucine-rich repeat (NLR) proteins function as cytosolic innate immune sensors in plants and animals. However, the structural basis for ligand-induced NLR activation has so far remained unknown. NAIP5 (NLR family, apoptosis inhibitory protein 5) binds the bacterial protein flagellin and assembles with NLRC4 to form a multiprotein complex called an inflammasome. Here we report the cryo–electron microscopy structure of the assembled ~1.4-megadalton flagellin-NAIP5-NLRC4 inflammasome, revealing how a ligand activates an NLR. Six distinct NAIP5 domains contact multiple conserved regions of flagellin, prying NAIP5 into an open and active conformation. We show that innate immune recognition of multiple ligand surfaces is a generalizable strategy that limits pathogen evolution and immune escape.
    Keywords: Biochemistry, Immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Geosciences , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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