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  • Animals  (3)
  • *Saccharomyces cerevisiae Proteins  (2)
  • American Association for the Advancement of Science (AAAS)  (5)
  • 1990-1994  (5)
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Publisher
  • American Association for the Advancement of Science (AAAS)  (5)
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Year
  • 1
    Publication Date: 1992-02-28
    Description: Many organisms construct structural ceramic (biomineral) composites from seemingly mundane materials; cell-mediated processes control both the nucleation and growth of mineral and the development of composite microarchitecture. Living systems fabricate biocomposites by: (i) confining biomineralization within specific subunit compartments; (ii) producing a specific mineral with defined crystal size and orientation; and (iii) packaging many incremental units together in a moving front process to form fully densified, macroscopic structures. By adapting biological principles, materials scientists are attempting to produce novel materials. To date, neither the elegance of the biomineral assembly mechanisms nor the intricate composite microarchitectures have been duplicated by nonbiological processing. However, substantial progress has been made in the understanding of how biomineralization occurs, and the first steps are now being taken to exploit the basic principles involved.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heuer, A H -- Fink, D J -- Laraia, V J -- Arias, J L -- Calvert, P D -- Kendall, K -- Messing, G L -- Blackwell, J -- Rieke, P C -- Thompson, D H -- New York, N.Y. -- Science. 1992 Feb 28;255(5048):1098-105.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Materials Science and Engineering, Case Western Reserve University, Cleveland, OH 44106.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546311" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bone Matrix ; Calcification, Physiologic ; *Ceramics ; Chickens ; Crystallography
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-08-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mobbs, C V -- Fink, G -- Pfaff, D W -- New York, N.Y. -- Science. 1990 Aug 3;249(4968):566-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2382136" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Brain/enzymology ; Information Systems ; Isoenzymes/*genetics/metabolism ; Type C Phospholipases/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-03-23
    Description: Estrogen and luteinizing hormone-releasing hormone (LH-RH) interact to influence both behavior and gonadotropin release. However, little is known about the biochemical mechanisms that mediate the effects of these hormones or their interactions. The most prominent protein induced by estrogen in the ventromedial hypothalamus has the same amino-terminal sequence as the most prominent protein induced by LH-RH in the pituitary in vitro and in vivo; these proteins comigrate on two-dimensional gels. Furthermore, the hormonal induction may be caused by modification of a constitutive protein with the same molecular weight (70,000) but a slightly more acidic isoelectric point, whose level is inversely related to the level of the induced form after estrogen treatment. Thus estrogen and LH-RH may interact by additively or synergistically inducing this protein, which is called HIP-70.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mobbs, C V -- Fink, G -- Pfaff, D W -- New York, N.Y. -- Science. 1990 Mar 23;247(4949 Pt 1):1477-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology and Behavior, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2181662" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Electrophoresis, Gel, Two-Dimensional ; Estrogens/*pharmacology ; Female ; Gonadotropin-Releasing Hormone/*pharmacology ; Hypothalamus/drug effects/*metabolism ; Molecular Sequence Data ; Nerve Tissue Proteins/*biosynthesis ; Ovariectomy ; Pituitary Gland/drug effects/*metabolism ; *Protein Biosynthesis ; Rats
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 1993-12-10
    Description: Transmission of an external signal from receptors to downstream targets is often mediated by a conserved set of protein kinases that act in sequence (a kinase cascade). In haploid strains of Saccharomyces cerevisiae, a signal initiated by peptide pheromones is transmitted through this kinase cascade to a transcription factor STE12, which is required for the expression of many mating-specific genes. Here it was shown that in diploids some of the same kinases and STE12 are required for filamentous growth, but the pheromone receptors and guanosine triphosphate-binding protein are not required for filament formation. Thus, a similar kinase cascade is activated by different signals in haploids and diploids and mediates different developmental outcomes in the two cell types.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, H -- Styles, C A -- Fink, G R -- GM 35010/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 10;262(5140):1741-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8259520" target="_blank"〉PubMed〈/a〉
    Keywords: Fungal Proteins/*metabolism ; GTP-Binding Proteins/metabolism ; Genes, Fungal ; Mutation ; Peptides/*metabolism/pharmacology ; Phenotype ; Protein Kinases/*metabolism ; Receptors, Mating Factor ; Receptors, Peptide/metabolism ; Saccharomyces cerevisiae/genetics/*growth & development/metabolism ; *Saccharomyces cerevisiae Proteins ; *Signal Transduction ; Transcription Factors/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-12-09
    Description: A Candida albicans gene (CPH1) was cloned that encodes a protein homologous to Saccharomyces cerevisiae Ste12p, a transcription factor that is the target of the pheromone response mitogen-activated protein kinase cascade. CPH1 complements both the mating defect of ste12 haploids and the filamentous growth defect of ste12/ste12 diploids. Candida albicans strains without a functional CPH1 gene (cph1/cph1) show suppressed hyphal formation on solid medium. However, cph1/cph1 strains can still form hyphae in liquid culture and in response to serum. Thus, filamentous growth may be activated in C. albicans by the same signaling kinase cascade that activates Ste12p in S. cerevisiae; however, alternative pathways may exist in C. albicans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, H -- Kohler, J -- Fink, G R -- GM402661/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 9;266(5191):1723-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7992058" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Candida albicans/cytology/genetics/*growth & development ; Cloning, Molecular ; Culture Media ; Fungal Proteins/chemistry/*genetics/physiology ; *Genes, Fungal ; Genetic Complementation Test ; Molecular Sequence Data ; Mutation ; Saccharomyces cerevisiae/cytology/genetics/growth & development ; *Saccharomyces cerevisiae Proteins ; Transcription Factors/chemistry/*genetics/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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