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  • Animals  (8)
  • AEROSPACE MEDICINE  (6)
  • 2000-2004  (2)
  • 1990-1994  (3)
  • 1980-1984  (6)
  • 1970-1974  (3)
  • 1960-1964
  • 1955-1959
  • 1940-1944
  • 1935-1939
  • 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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    Prenylated proteins: the structure of the isoprenoid group (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-01-19
    Description: The mevalonate-derived portion of a prenylated protein from Chinese hamster ovary cells has been established as diterpenoid (C20). This group is linked to a carboxyl-terminal cysteine as a thioether. It was removed from the protein by hydrazinolysis followed by Raney nickel desulfurization, and the resulting hydrocarbon fraction was analyzed by gas chromatography-mass spectrometry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rilling, H C -- Breunger, E -- Epstein, W W -- Crain, P F -- GM 29812/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Jan 19;247(4940):318-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Utah, Salt Lake City 84112.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2296720" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cricetinae ; Diterpenes/*metabolism ; Female ; Gas Chromatography-Mass Spectrometry ; Mevalonic Acid/metabolism ; Molecular Structure ; Ovary ; Protein Precursors/metabolism ; *Protein Processing, Post-Translational ; Proteins/*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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    Molecular analysis of protein assembly in muscle development (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-01
    Description: The challenge presented by myofibril assembly in striated muscle is to understand the molecular mechanisms by which its protein components are arranged at each level of organization. Recent advances in the genetics and cell biology of muscle development have shown that in vivo assembly of the myofilaments requires a complex array of structural and associated proteins and that organization of whole sarcomeres occurs initially at the cell membrane. These studies have been complemented by in vitro analyses of the renaturation, polymerization, and three-dimensional structure of the purified proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Epstein, H F -- Fischman, D A -- AR-32147/AR/NIAMS NIH HHS/ -- GM-33223/GM/NIGMS NIH HHS/ -- HL-42267/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Mar 1;251(4997):1039-44.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1998120" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/physiology ; Amino Acid Sequence ; Animals ; Macromolecular Substances ; Molecular Sequence Data ; Morphogenesis ; Muscle Contraction ; *Muscle Development ; Muscle Proteins/*physiology ; Myofibrils/*physiology ; Myosins/physiology ; Polymers ; Sarcolemma/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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  • 4
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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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  • 5
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    Biodiversity questions (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Epstein, P R -- Chikwenhere, G P -- New York, N.Y. -- Science. 1994 Sep 9;265(5178):1510-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8079160" target="_blank"〉PubMed〈/a〉
    Keywords: Africa, Southern ; Animals ; Climate ; *Disease Vectors ; *Pest Control
    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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    Polyene toxicity in renal medulla: injury mediated by transport activity (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-04-06
    Description: Polyene antibiotics such as amphotericin and nystatin increase membrane permeability and thus increase the amount of oxygen consumed in active electrolyte transport. In isolated perfused rat kidneys, the polyenes produced extensive injury to the medullary thick ascending limb, a segment of the nephron with limited oxygen supply. This damage was prevented if reabsorptive transport was inhibited by ouabain. Cell death under these circumstances thus appears to be mediated by increased oxygen demand for transport activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brezis, M -- Rosen, S -- Silva, P -- Spokes, K -- Epstein, F H -- AM18078/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1984 Apr 6;224(4644):66-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6322305" target="_blank"〉PubMed〈/a〉
    Keywords: Amphotericin B/adverse effects ; Animals ; Biological Transport, Active/drug effects ; Cell Membrane Permeability/drug effects ; Furosemide/pharmacology ; Glomerular Filtration Rate/drug effects ; Kidney Medulla/*drug effects/pathology ; Loop of Henle/drug effects ; Nystatin/adverse effects ; Ouabain/pharmacology ; Oxygen Consumption/drug effects ; Polyenes/*adverse effects ; Rats ; Sodium/metabolism ; Sodium-Potassium-Exchanging ATPase/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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  • 7
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    Hydrogen isotope ratios of mouse tissues are influenced by a variety of factors other than diet (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-12-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DeNiro, M J -- Epstein, S -- New York, N.Y. -- Science. 1981 Dec 18;214(4527):1374-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7313700" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Deuterium/*metabolism ; *Diet ; Hydrogen/*metabolism ; Mice ; Water/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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  • 8
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    Role of nitrogen dioxide in the biosynthesis of nitraosamines in mice (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-03-28
    Description: Groups of three to four mice were gavaged with aqueous solutions of 2 milligrams of morpholine, after which they were exposed to nitrogen dioxide in inhalation chambers at concentrations of 0.2 to 50 parts per million for up to 4 hours. At sequential intervals during the exposure, mice were frozen and pulverized in liquid nitrogen, and the mice powder was extracted with ice-cold 35 percent aqueous methanol and dichloromethane; organic-phase concentrates were analyzed for N-nitrosomorpholine with a thermal energy analyzer interfaced to a gas chromatograph. The N-nitrosomorpholine yields, ranging up to about 2.3 micrograms per mouse, were time-dependent relative to the duration of exposure to nitrogen dioxide and dose-dependent relative to the concentrations of nitrogen dioxide; control levels (in mice that were gavaged with morpholine or distilled water and then exposed to air instead of nitrogen dioxide) were less than 5 nanograms per mouse. These preliminary studies demonstrate the in vivo nitrosating potential of nitrogen oxides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Iqbal, Z M -- Dahl, K -- Epstein, S S -- New York, N.Y. -- Science. 1980 Mar 28;207(4438):1475-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7361099" target="_blank"〉PubMed〈/a〉
    Keywords: Amines/metabolism ; Animals ; Ascorbic Acid/pharmacology ; Biotransformation ; Dose-Response Relationship, Drug ; Mice ; Morpholines/*metabolism ; Nitrogen Dioxide/antagonists & inhibitors/*metabolism ; Nitrosamines/*metabolism ; Time Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 9
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    Effect of prolonged space flight on cardiac function and dimensions (1974)
    In:  CASI
    Details
    Publication Date: 2016-06-07
    Description: Echocardiographic studies were performed preflight 5 days before launch and on recovery day and 1, 2, 4, 11, 31 and 68 days postflight. From these echocardiograms measurements were made. From these primary measurements, left ventricular end-diastolic volume, end-systolic volume, stroke volume, and mass were derived using the accepted assumptions. Findings in the Scientist Pilot and Pilot resemble those seen in trained distance runners. Wall thickness measurements were normal in all three crewmembers preflight. Postflight basal studies were unchanged in the Commander on recovery day through 68 days postflight in both the Scientist Pilot and Pilot, however, the left ventricular end-diastolic volume, stroke volume, and mass were decreased slightly. Left ventricular function curves were constructed for the Commander and Pilot by plotting stroke volume versus end-diastolic volume. In both astronauts, preflight and postflight data fell on the same straight line demonstrating that no deterioration in cardiac function had occurred. These data indicate that the cardiovascular system adapts well to prolonged weightlessness and suggest that alterations in cardiac dimensions and function are unlikely to limit man's future in space.
    Keywords: AEROSPACE MEDICINE
    Type: NASA. Johnson Space Center Proc. of the Skylab Life Sci. Symp., Vol. 2; p 711-721
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    NASA TECHNICAL REPORTS
  • 10
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    Effects of water immersion on plasma catecholamines in normal humans (1983)
    In:  Other Sources
    Details
    Publication Date: 2019-06-28
    Description: An investigation was conducted in order to determine whether water immersion to the neck (NI) alters plasma catecholamines in normal humans. Eight normal subjects were studied during a seated control study (C) and during 4 hr of NI, and the levels of norepinephrine (NE) and epinephrine (E) as determined by radioenzymatic assay were measured hourly. Results show that despite the induction of a marked natriuresis and diuresis indicating significant central hypervolemia, NI failed to alter plasma NE or E levels compared with those of either C or the corresponding prestudy 1.5 hr. In addition, the diuresis and natriuresis was found to vary independently of NE. These results indicate that the response of the sympathetic nervous system to acute volume alteration may differ from the reported response to chronic volume expansion.
    Keywords: AEROSPACE MEDICINE
    Type: Journal of Applied Physiology: Respiratory, Environmental and Exercise Physiology (ISSN 0161-7567); 54; Jan. 198
    Format: text
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    NASA TECHNICAL REPORTS
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