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  • 1
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    A mutant Drosophila insulin receptor homolog that extends life-span and impairs neuroendocrine function (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-04-09
    Description: The Drosophila melanogaster gene insulin-like receptor (InR) is homologous to mammalian insulin receptors as well as to Caenorhabditis elegans daf-2, a signal transducer regulating worm dauer formation and adult longevity. We describe a heteroallelic, hypomorphic genotype of mutant InR, which yields dwarf females with up to an 85% extension of adult longevity and dwarf males with reduced late age-specific mortality. Treatment of the long-lived InR dwarfs with a juvenile hormone analog restores life expectancy toward that of wild-type controls. We conclude that juvenile hormone deficiency, which results from InR signal pathway mutation, is sufficient to extend life-span, and that in flies, insulin-like ligands nonautonomously mediate aging through retardation of growth or activation of specific endocrine tissue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tatar, M -- Kopelman, A -- Epstein, D -- Tu, M P -- Yin, C M -- Garofalo, R S -- R01 AG16632/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2001 Apr 6;292(5514):107-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Brown University, Providence, RI 02912, USA., University of Massachusetts, Amherst, MA 01003, USA. Marc_Tatar@Brown.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11292875" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/*physiology ; Alleles ; Animals ; Carrier Proteins/*genetics/*physiology ; Corpora Allata/*metabolism ; *Drosophila Proteins ; Drosophila melanogaster/genetics/*physiology ; Female ; Fertility ; Genes, Insect ; Genotype ; Insulin/pharmacology ; Juvenile Hormones/metabolism ; Longevity/*physiology ; Male ; Methoprene/pharmacology ; Mutation ; Protein-Tyrosine Kinases/*genetics/*physiology ; *Receptor Protein-Tyrosine Kinases ; Receptor, Insulin/genetics/physiology ; Reproduction ; Signal Transduction ; Superoxide Dismutase/metabolism ; Triglycerides/metabolism ; Vitellogenesis/drug effects
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-26
    Description: The organization of myosin into motile cellular structures requires precise temporal and spatial regulation. Proteins containing a UCS (UNC-45/CRO1/She4p) domain are necessary for the incorporation of myosin into the contractile ring during cytokinesis and into thick filaments during muscle development. We report that the carboxyl-terminal regions of UNC-45 bound and exerted chaperone activity on the myosin head. The amino-terminal tetratricopeptide repeat domain of UNC-45 bound the molecular chaperone Hsp90. Thus, UNC-45 functions both as a molecular chaperone and as an Hsp90 co-chaperone for myosin, which can explain previous findings of altered assembly and decreased accumulation of myosin in UNC-45 mutants of Caenorhabditis elegans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barral, Jose M -- Hutagalung, Alex H -- Brinker, Achim -- Hartl, F Ulrich -- Epstein, Henry F -- New York, N.Y. -- Science. 2002 Jan 25;295(5555):669-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11809970" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Binding Sites ; Caenorhabditis elegans/genetics/*metabolism ; Caenorhabditis elegans Proteins/chemistry/genetics/*metabolism ; Cell Line ; Cloning, Molecular ; HSP70 Heat-Shock Proteins/genetics/metabolism ; HSP90 Heat-Shock Proteins/genetics/metabolism ; Molecular Chaperones/chemistry/genetics/*metabolism ; Molecular Sequence Data ; Myosins/*metabolism ; Peptide Fragments/metabolism ; Protein Binding ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry/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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  • 3
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    Carcinogenic risk estimation (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-05-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Epstein, S S -- Swartz, J B -- New York, N.Y. -- Science. 1988 May 20;240(4855):1043-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Illinois Medical Center, Chicago 60680.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3368788" target="_blank"〉PubMed〈/a〉
    Keywords: Air Pollution ; Animals ; *Carcinogens ; Humans ; Mutagenicity Tests ; Neoplasms/etiology/mortality ; Risk Factors
    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
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    HTLV-III infection in brains of children and adults with AIDS encephalopathy (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-01-11
    Description: Unexplained debilitating dementia or encephalopathy occurs frequently in adults and children with the acquired immune deficiency syndrome (AIDS). Brains from 15 individuals with AIDS and encephalopathy were examined by Southern analysis and in situ hybridization for the presence of human T-cell leukemia (lymphotropic) virus type III (HTLV-III), the virus believed to be the causative agent of AIDS. HTLV-III DNA was detected in the brains of five patients, and viral-specific RNA was detected in four of these. In view of these findings and the recent demonstration of morphologic and genetic relatedness between HTLV-III and visna virus, a lentivirus that causes a chronic degenerative neurologic disease in sheep, HTLV-III should be evaluated further as a possible cause of AIDS encephalopathy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shaw, G M -- Harper, M E -- Hahn, B H -- Epstein, L G -- Gajdusek, D C -- Price, R W -- Navia, B A -- Petito, C K -- O'Hara, C J -- Groopman, J E -- New York, N.Y. -- Science. 1985 Jan 11;227(4683):177-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2981429" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/microbiology ; Adult ; Antibodies, Viral/analysis ; Brain Diseases/*microbiology ; Cerebral Cortex/analysis/*microbiology ; Child ; Deltaretrovirus/*isolation & purification ; Dementia/microbiology ; Female ; Humans ; Infant ; Male ; Middle Aged ; Nucleic Acid Hybridization ; RNA, Viral/analysis
    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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    Individual tumors of multifocal EB virus-induced malignant lymphomas in tamarins arise from different B-cell clones (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-10
    Description: Cotton-top tamarins were inoculated with sufficient Epstein-Barr virus to induce multiple tumors in each animal within 14 to 21 days. The tumors consisted of large-cell lymphomas that contained multiple copies of the Epstein-Barr virus genome and generated Epstein-Barr virus-carrying cell lines showing no detectable consistent chromosomal abnormality. Hybridization of tumor DNA with immunoglobulin gene probes revealed that each lymphoma was oligo- or monoclonal in origin and that individual tumors from the same animal arose from different B-cell clones. Thus the virus induced multiple transformation events in tamarins in vivo to cause malignant tumors resembling the Epstein-Barr virus-associated lymphomas of patients with organ transplants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cleary, M L -- Epstein, M A -- Finerty, S -- Dorfman, R F -- Bornkamm, G W -- Kirkwood, J K -- Morgan, A J -- Sklar, J -- CA 34233/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 10;228(4700):722-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2986287" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/*microbiology ; Burkitt Lymphoma/genetics/*microbiology ; Cell Line ; DNA, Neoplasm/genetics ; Heart Transplantation ; Herpesvirus 4, Human ; Humans ; Neoplasms, Experimental/genetics/microbiology ; Nucleic Acid Hybridization ; Saguinus
    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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  • 6
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    Structure-activity studies of interleukin-2 (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-10-17
    Description: The critical role of interleukin-2 (IL-2) in immune response heightens the need to know its structure in order to understand its activity. New computer-assisted predictive methods for the assignment of secondary structure together with a method to predict the tertiary structure of a protein from data on its primary sequence and secondary structure were applied to IL-2. This method generated four topological families of structures, of which the most plausible is a right-handed fourfold alpha-helical bundle. Members of this family were shown to be compatible with existing structural data on disulfide bridges and monoclonal antibody binding for IL-2. Experimental estimates of secondary structure from circular dichroism and site-directed mutagenesis data support the model. A region likely to be important in IL-2 binding to its receptor was identified as residues Leu36, Met38, Leu40, Phe42, Phe44, and Met46.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, F E -- Kosen, P A -- Kuntz, I D -- Epstein, L B -- Ciardelli, T L -- Smith, K A -- CA27903/CA/NCI NIH HHS/ -- GM34197/GM/NIGMS NIH HHS/ -- MOJ JD17001/PHS HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Oct 17;234(4774):349-52.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3489989" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Computer Simulation ; Humans ; *Interleukin-2/genetics/physiology ; Mice ; Models, Molecular ; Structure-Activity Relationship
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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