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  • Springer Nature  (25)
  • American Association for the Advancement of Science (AAAS)  (14)
  • 2000-2004  (20)
  • 1995-1999  (12)
  • 1990-1994  (7)
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  • 1
  • 2
    Publication Date: 2003-04-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Munoz-Pinedo, Cristina -- del Pozo, Miguel A -- Galvez, Jose A -- Moreno, Eva M -- Buceta-Fernandez, Javier -- Garcia-Sanchez, Marta -- Valdivielso, Jose M -- Bascones, Elena -- New York, N.Y. -- Science. 2003 Apr 4;300(5616):51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12677039" target="_blank"〉PubMed〈/a〉
    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
    Publication Date: 2001-02-07
    Description: The disulfide reducing enzymes glutathione reductase and thioredoxin reductase are highly conserved among bacteria, fungi, worms, and mammals. These proteins maintain intracellular redox homeostasis to protect the organism from oxidative damage. Here we demonstrate the absence of glutathione reductase in Drosophila melanogaster, identify a new type of thioredoxin reductase, and provide evidence that a thioredoxin system supports GSSG reduction. Our data suggest that antioxidant defense in Drosophila, and probably in related insects, differs fundamentally from that in other organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kanzok, S M -- Fechner, A -- Bauer, H -- Ulschmid, J K -- Muller, H M -- Botella-Munoz, J -- Schneuwly, S -- Schirmer, R -- Becker, K -- New York, N.Y. -- Science. 2001 Jan 26;291(5504):643-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center of Biochemistry, Im Neuenheimer Feld 328, Heidelberg University, D-69120 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11158675" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Binding Sites ; Drosophila melanogaster/*enzymology/genetics/metabolism ; Genes, Insect ; Glutathione/*metabolism ; Glutathione Disulfide/metabolism ; Glutathione Reductase/*metabolism ; Humans ; Kinetics ; Molecular Sequence Data ; Mutation ; NADP/metabolism ; Oxidation-Reduction ; Sequence Alignment ; Species Specificity ; Substrate Specificity ; Thioredoxin-Disulfide Reductase/antagonists & ; inhibitors/chemistry/*genetics/*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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  • 4
    Publication Date: 1999-04-16
    Description: In mammals, ocular photoreceptors mediate an acute inhibition of pineal melatonin by light. The effect of rod and cone loss on this response was assessed by combining the rd mutation with a transgenic ablation of cones (cl) to produce mice lacking both photoreceptor classes. Despite the loss of all known retinal photoreceptors, rd/rd cl mice showed normal suppression of pineal melatonin in response to monochromatic light of wavelength 509 nanometers. These data indicate that mammals have additional ocular photoreceptors that they use in the regulation of temporal physiology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lucas, R J -- Freedman, M S -- Munoz, M -- Garcia-Fernandez, J M -- Foster, R G -- New York, N.Y. -- Science. 1999 Apr 16;284(5413):505-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Sir Alexander Fleming Building, Imperial College of Science, Technology and Medicine, London, SW7 2AZ, UK. r.j.lucas@ic.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10205062" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Clocks/physiology ; Circadian Rhythm/*physiology ; Cryptochromes ; Darkness ; *Drosophila Proteins ; *Eye Proteins ; Flavoproteins/genetics/physiology ; *Light ; Light Signal Transduction ; Melatonin/*metabolism ; Mice ; Mice, Inbred C3H ; Mice, Transgenic ; *Photoreceptor Cells, Invertebrate ; Photoreceptor Cells, Vertebrate/*physiology ; Pineal Gland/*metabolism ; Receptors, G-Protein-Coupled ; Retina/cytology/*physiology ; Retinal Ganglion Cells/physiology ; Retinal Pigments/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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  • 5
    Publication Date: 1999-04-16
    Description: Circadian rhythms of mammals are entrained by light to follow the daily solar cycle (photoentrainment). To determine whether retinal rods and cones are required for this response, the effects of light on the regulation of circadian wheel-running behavior were examined in mice lacking these photoreceptors. Mice without cones (cl) or without both rods and cones (rdta/cl) showed unattenuated phase-shifting responses to light. Removal of the eyes abolishes this behavior. Thus, neither rods nor cones are required for photoentrainment, and the murine eye contains additional photoreceptors that regulate the circadian clock.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freedman, M S -- Lucas, R J -- Soni, B -- von Schantz, M -- Munoz, M -- David-Gray, Z -- Foster, R -- New York, N.Y. -- Science. 1999 Apr 16;284(5413):502-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Alexander Fleming Building, Imperial College of Science, Technology and Medicine, London, SW7 2AZ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10205061" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Clocks/*physiology ; Circadian Rhythm/*physiology ; *Light ; Mice ; Mice, Transgenic ; Motor Activity ; *Ocular Physiological Phenomena ; Photoreceptor Cells, Vertebrate/*physiology ; Pigments, Biological/physiology ; Retinal Cone Photoreceptor Cells/physiology ; Retinal Pigments/physiology ; Retinal Rod Photoreceptor Cells/physiology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 2000-04-15
    Description: The mechanisms by which hepatitis C virus (HCV) induces chronic infection in the vast majority of infected individuals are unknown. Sequences within the HCV E1 and E2 envelope genes were analyzed during the acute phase of hepatitis C in 12 patients with different clinical outcomes. Acute resolving hepatitis was associated with relative evolutionary stasis of the heterogeneous viral population (quasispecies), whereas progressing hepatitis correlated with genetic evolution of HCV. Consistent with the hypothesis of selective pressure by the host immune system, the sequence changes occurred almost exclusively within the hypervariable region 1 of the E2 gene and were temporally correlated with antibody seroconversion. These data indicate that the evolutionary dynamics of the HCV quasispecies during the acute phase of hepatitis C predict whether the infection will resolve or become chronic.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Farci, P -- Shimoda, A -- Coiana, A -- Diaz, G -- Peddis, G -- Melpolder, J C -- Strazzera, A -- Chien, D Y -- Munoz, S J -- Balestrieri, A -- Purcell, R H -- Alter, H J -- New York, N.Y. -- Science. 2000 Apr 14;288(5464):339-44.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Sciences, University of Cagliari, Via San Giorgio 12, 09124 Cagliari, Italy. farcip@pacs.unica.it〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10764648" target="_blank"〉PubMed〈/a〉
    Keywords: Acute Disease ; Adult ; Aged ; Antibodies, Viral ; Disease Progression ; *Evolution, Molecular ; Female ; Genes, Viral ; Genetic Variation ; Hepacivirus/*genetics/immunology/physiology ; Hepatitis C/immunology/*virology ; Hepatitis C Antibodies/biosynthesis ; Hepatitis C, Chronic/immunology/*virology ; Humans ; Male ; Middle Aged ; Molecular Sequence Data ; Phylogeny ; Prospective Studies ; Selection, Genetic ; Time Factors ; Viral Envelope Proteins/*genetics/immunology ; Virus Replication
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 1999-05-13
    Description: A peat core from a bog in northwest Spain provides a record of the net accumulation of atmospheric mercury since 4000 radiocarbon years before the present. It was found that cold climates promoted an enhanced accumulation and the preservation of mercury with low thermal stability, and warm climates were characterized by a lower accumulation and the predominance of mercury with moderate to high thermal stability. This record can be separated into natural and anthropogenic components. The substantial anthropogenic mercury component began approximately 2500 radiocarbon years before the present, which is near the time of the onset of mercury mining in Spain. Anthropogenic mercury has dominated the deposition record since the Islamic period (8th to 11th centuries A.D.). The results shown here have implications for the global mercury cycle and also imply that the thermal lability of the accumulated mercury can be used not only to quantify the effects of human activity, but also as a new tool for quantitative paleotemperature reconstruction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martinez-Cortizas -- Pontevedra-Pombal -- Garcia-Rodeja -- Novoa-Munoz -- Shotyk -- New York, N.Y. -- Science. 1999 May 7;284(5416):939-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departamento de Edafologia y Quimica Agricola, Facultad de Biologia, Campus Sur s/n, E-15706 Santiago de Compostela, Spain. Geological Institute, University of Bern, Baltzerstrasse 1, CH-3012 Berne, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10320369" target="_blank"〉PubMed〈/a〉
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  • 8
    Publication Date: 2002-12-14
    Description: Theory predicts the existence of barrierless protein folding. Without barriers, folding should be noncooperative and the degree of native structure should be coupled to overall protein stability. We investigated the thermal unfolding of the peripheral subunit binding domain from Escherichia coli's 2-oxoglutarate dehydrogenase multienzyme complex (termed BBL) with a combination of spectroscopic techniques and calorimetry. Each technique probed a different feature of protein structure. BBL has a defined three-dimensional structure at low temperatures. However, each technique showed a distinct unfolding transition. Global analysis with a statistical mechanical model identified BBL as a downhill-folding protein. Because of BBL's biological function, we propose that downhill folders may be molecular rheostats, in which effects could be modulated by altering the distribution of an ensemble of structures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Garcia-Mira, Maria M -- Sadqi, Mourad -- Fischer, Niels -- Sanchez-Ruiz, Jose M -- Munoz, Victor -- New York, N.Y. -- Science. 2002 Dec 13;298(5601):2191-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry and Center for Biomolecular Structure and Organization, University of Maryland, College Park, MD 20742, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12481137" target="_blank"〉PubMed〈/a〉
    Keywords: Acyltransferases/*chemistry ; Calorimetry, Differential Scanning ; Circular Dichroism ; Escherichia coli/enzymology ; Fluorescence ; Fluorescence Resonance Energy Transfer ; Hydrogen-Ion Concentration ; Ketoglutarate Dehydrogenase Complex/*chemistry ; Models, Chemical ; Models, Molecular ; Multienzyme Complexes/chemistry ; Nuclear Magnetic Resonance, Biomolecular ; Protein Denaturation ; *Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; Temperature ; Thermodynamics
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  • 9
    Publication Date: 1992-02-28
    Description: Multiple human immunodeficiency virus type-1 sequences from the V3 and V4-V5 regions of the envelope gene were analyzed from three mother-infant pairs. The infants' viral sequences were less diverse than those of their mothers. In two pairs, a proviral form infrequently found in the mother predominated in her infant. A conserved N-linked glycosylation site within the V3 region, present in each mother's sequence set, was absent in all of the infants' sequence sets. These findings demonstrate that a minor subset of maternal virus is transmitted to the infant.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wolinsky, S M -- Wike, C M -- Korber, B T -- Hutto, C -- Parks, W P -- Rosenblum, L L -- Kunstman, K J -- Furtado, M R -- Munoz, J L -- AI-32535/AI/NIAID NIH HHS/ -- HD26619-01/HD/NICHD NIH HHS/ -- P01-25569/PHS HHS/ -- New York, N.Y. -- Science. 1992 Feb 28;255(5048):1134-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Northwestern University Medical School, Chicago, IL 60611.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546316" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/congenital/microbiology/*transmission ; Amino Acid Sequence ; Base Sequence ; Female ; Genotype ; Glycosylation ; HIV Antigens/genetics ; HIV Envelope Protein gp120/genetics/immunology ; HIV-1/*genetics/immunology ; Humans ; Infant ; Maternal-Fetal Exchange ; Molecular Sequence Data ; Oligodeoxyribonucleotides/chemistry ; Polymerase Chain Reaction ; Pregnancy ; Selection, Genetic ; Sequence Alignment
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-03-15
    Description: The superior colliculus contains neurons that cause displacements of the visual axis (gaze shifts). These cells are arranged topographically in a motor map on which the vector (amplitude and direction) of the coded movement varies continuously with location. How this spatial representation becomes a temporal code (frequency and duration) in the motoneurons is unknown. During a gaze shift, a zone of neural activity moved continuously on the map from an initial location, defining the vector of the desired gaze shift, to a final "zero" position containing neurons that were active during fixation. Thus, the spatial-temporal transformation may be accomplished by control of gaze throughout the spatial trajectory of activity on the motor map.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Munoz, D P -- Pelisson, D -- Guitton, D -- New York, N.Y. -- Science. 1991 Mar 15;251(4999):1358-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology and Neurosurgery, McGill University, Montreal, Quebec, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2003221" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cats ; *Eye Movements ; Oculomotor Muscles/innervation/physiology ; Superior Colliculi/*physiology ; Visual Perception/physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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