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  • 1
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    Direct observation of a pressure-induced metal-insulator transition in LiV_{2}O_{4} by optical studies (2011)
    American Physical Society (APS)
    Details
    Publication Date: 2011-12-06
    Description: Author(s): A. Irizawa, S. Suga, G. Isoyama, K. Shimai, K. Sato, K. Iizuka, T. Nanba, A. Higashiya, S. Niitaka, and H. Takagi [Phys. Rev. B 84, 235116] Published Mon Dec 05, 2011
    Keywords: Electronic structure and strongly correlated systems
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
    Published by American Physical Society (APS)
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  • 2
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    Melanopsin (Opn4) requirement for normal light-induced circadian phase shifting (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-14
    Description: The master circadian oscillator in the hypothalamic suprachiasmatic nucleus is entrained to the day/night cycle by retinal photoreceptors. Melanopsin (Opn4), an opsin-based photopigment, is a primary candidate for photoreceptor-mediated entrainment. To investigate the functional role of melanopsin in light resetting of the oscillator, we generated melanopsin-null mice (Opn4-/-). These mice entrain to a light/dark cycle and do not exhibit any overt defect in circadian activity rhythms under constant darkness. However, they display severely attenuated phase resetting in response to brief pulses of monochromatic light, highlighting the critical role of melanopsin in circadian photoentrainment in mammals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Panda, Satchidananda -- Sato, Trey K -- Castrucci, Ana Maria -- Rollag, Mark D -- DeGrip, Willem J -- Hogenesch, John B -- Provencio, Ignacio -- Kay, Steve A -- MH 62405/MH/NIMH NIH HHS/ -- MH51573/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2002 Dec 13;298(5601):2213-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genomics Institute of the Novartis Research Foundation, 10675 John J. Hopkins Drive, San Diego, CA 92121, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12481141" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Clocks/physiology ; Circadian Rhythm/*physiology ; Darkness ; Female ; Gene Targeting ; *Light ; Light Signal Transduction ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Motor Activity ; Retinal Ganglion Cells/physiology ; Rod Opsins/genetics/*physiology ; Suprachiasmatic Nucleus/physiology
    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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  • 3
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    Location, location, location: membrane targeting directed by PX domains (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-01
    Description: Phosphoinositide (PI)-binding domains play critical roles in the intracellular localization of a variety of cell-signaling proteins. The 120-amino acid Phox homology (PX) domain targets proteins to organelle membranes through interactions between two conserved basic motifs within the PX domain and specific PIs. The combination of protein-lipid and protein-protein interactions ensures the proper localization and regulation of PX domain-containing proteins. Upon proper localization, PX domain-containing proteins can then bind to additional proteins and execute their functions in a diverse set of biological pathways, including intracellular protein transport, cell growth and survival, cytoskeletal organization, and neutrophil defense.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sato, T K -- Overduin, M -- Emr, S D -- New York, N.Y. -- Science. 2001 Nov 30;294(5548):1881-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Medicine and Howard Hughes Medical Institute, University of California at San Diego School of Medicine, La Jolla, CA 92093-0668, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11729306" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Animals ; Carrier Proteins/chemistry/metabolism ; Humans ; Intracellular Membranes/*metabolism ; Models, Molecular ; NADPH Oxidase ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphatidylinositols/*metabolism ; Phosphoproteins/*chemistry/*metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Protein Transport ; Signal Transduction ; Structure-Activity Relationship ; src Homology Domains
    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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    Adiponectin and AdipoR1 regulate PGC-1alpha and mitochondria by Ca(2+) and AMPK/SIRT1 (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-04-02
    Description: Adiponectin is an anti-diabetic adipokine. Its receptors possess a seven-transmembrane topology with the amino terminus located intracellularly, which is the opposite of G-protein-coupled receptors. Here we provide evidence that adiponectin induces extracellular Ca(2+) influx by adiponectin receptor 1 (AdipoR1), which was necessary for subsequent activation of Ca(2+)/calmodulin-dependent protein kinase kinase beta (CaMKKbeta), AMPK and SIRT1, increased expression and decreased acetylation of peroxisome proliferator-activated receptor gamma coactivator-1alpha (PGC-1alpha), and increased mitochondria in myocytes. Moreover, muscle-specific disruption of AdipoR1 suppressed the adiponectin-mediated increase in intracellular Ca(2+) concentration, and decreased the activation of CaMKK, AMPK and SIRT1 by adiponectin. Suppression of AdipoR1 also resulted in decreased PGC-1alpha expression and deacetylation, decreased mitochondrial content and enzymes, decreased oxidative type I myofibres, and decreased oxidative stress-detoxifying enzymes in skeletal muscle, which were associated with insulin resistance and decreased exercise endurance. Decreased levels of adiponectin and AdipoR1 in obesity may have causal roles in mitochondrial dysfunction and insulin resistance seen in diabetes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Iwabu, Masato -- Yamauchi, Toshimasa -- Okada-Iwabu, Miki -- Sato, Koji -- Nakagawa, Tatsuro -- Funata, Masaaki -- Yamaguchi, Mamiko -- Namiki, Shigeyuki -- Nakayama, Ryo -- Tabata, Mitsuhisa -- Ogata, Hitomi -- Kubota, Naoto -- Takamoto, Iseki -- Hayashi, Yukiko K -- Yamauchi, Naoko -- Waki, Hironori -- Fukayama, Masashi -- Nishino, Ichizo -- Tokuyama, Kumpei -- Ueki, Kohjiro -- Oike, Yuichi -- Ishii, Satoshi -- Hirose, Kenzo -- Shimizu, Takao -- Touhara, Kazushige -- Kadowaki, Takashi -- England -- Nature. 2010 Apr 29;464(7293):1313-9. doi: 10.1038/nature08991. Epub 2010 Mar 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Diabetes and Metabolic Diseases, Graduate School of Medicine, University of Tokyo, Tokyo 113-0033, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20357764" target="_blank"〉PubMed〈/a〉
    Keywords: AMP-Activated Protein Kinases/*metabolism ; Adiponectin/*metabolism ; Animals ; Calcium/*metabolism ; Calcium Signaling ; Calcium-Calmodulin-Dependent Protein Kinase Kinase/metabolism ; Cell Line ; Glucose/metabolism ; Homeostasis ; Insulin/metabolism ; Insulin Resistance ; Mice ; Mitochondria/*metabolism ; Muscle Cells/cytology/metabolism ; Muscle, Skeletal/cytology/metabolism ; Oocytes/metabolism ; Oxidative Stress ; Physical Conditioning, Animal ; Receptors, Adiponectin/deficiency/*metabolism ; Sirtuin 1/*metabolism ; Trans-Activators/*metabolism ; Transcription Factors ; Xenopus laevis
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 5
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    Symmetry change of Co $3d$ orbital associated with the 500-K spin crossover accompanied by insulator-to-metal transition in ${\mathrm{LaCoO}}_{3}$ (2018)
    American Physical Society (APS)
    Details
    Publication Date: 2018-09-27
    Description: Author(s): Y. Kobayashi, Y. Sakurai, N. Tsuji, K. Sato, and K. Asai We have carried out the imaging of the electron momentum density of Co 3 d electrons in LaCoO 3 using x-ray Compton scattering, in order to investigate the electron-orbital states relevant to the spin-crossover phenomenon at around 500 K, where an insulator-metal transition takes place. The electron m... [Phys. Rev. B 98, 115154] Published Wed Sep 26, 2018
    Keywords: Electronic structure and strongly correlated systems
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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  • 6
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    Insect olfactory receptors are heteromeric ligand-gated ion channels (2008)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2008-04-15
    Description: In insects, each olfactory sensory neuron expresses between one and three ligand-binding members of the olfactory receptor (OR) gene family, along with the highly conserved and broadly expressed Or83b co-receptor. The functional insect OR consists of a heteromeric complex of unknown stoichiometry but comprising at least one variable odorant-binding subunit and one constant Or83b family subunit. Insect ORs lack homology to G-protein-coupled chemosensory receptors in vertebrates and possess a distinct seven-transmembrane topology with the amino terminus located intracellularly. Here we provide evidence that heteromeric insect ORs comprise a new class of ligand-activated non-selective cation channels. Heterologous cells expressing silkmoth, fruitfly or mosquito heteromeric OR complexes showed extracellular Ca2+ influx and cation-non-selective ion conductance on stimulation with odorant. Odour-evoked OR currents are independent of known G-protein-coupled second messenger pathways. The fast response kinetics and OR-subunit-dependent K+ ion selectivity of the insect OR complex support the hypothesis that the complex between OR and Or83b itself confers channel activity. Direct evidence for odorant-gated channels was obtained by outside-out patch-clamp recording of Xenopus oocyte and HEK293T cell membranes expressing insect OR complexes. The ligand-gated ion channel formed by an insect OR complex seems to be the basis for a unique strategy that insects have acquired to respond to the olfactory environment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sato, Koji -- Pellegrino, Maurizio -- Nakagawa, Takao -- Nakagawa, Tatsuro -- Vosshall, Leslie B -- Touhara, Kazushige -- England -- Nature. 2008 Apr 24;452(7190):1002-6. doi: 10.1038/nature06850. Epub 2008 Apr 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Integrated Biosciences, The University of Tokyo, Chiba 277-8562, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18408712" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bombyx ; Calcium/metabolism ; Cell Line ; Culicidae ; Drosophila melanogaster ; Electric Conductivity ; HeLa Cells ; Heterotrimeric GTP-Binding Proteins ; Humans ; Insects/*chemistry ; *Ion Channel Gating ; Kinetics ; Ligands ; Odors/analysis ; Oocytes/metabolism ; Patch-Clamp Techniques ; Protein Subunits/chemistry/metabolism ; Receptors, Odorant/*chemistry/*metabolism ; Smell ; Xenopus laevis
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 7
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    The male mouse pheromone ESP1 enhances female sexual receptive behaviour through a specific vomeronasal receptor (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-07-03
    Description: Various social behaviours in mice are regulated by chemical signals called pheromones that act through the vomeronasal system. Exocrine gland-secreting peptide 1 (ESP1) is a 7-kDa peptide that is released into male tear fluids and stimulates vomeronasal sensory neurons in female mice. Here, we describe the molecular and neural mechanisms that are involved in the decoding of ESP1 signals in the vomeronasal system, which leads to behavioural output in female mice. ESP1 is recognized by a specific vomeronasal receptor, V2Rp5, and the ligand-receptor interaction results in sex-specific signal transmission to the amygdaloid and hypothalamic nuclei via the accessory olfactory bulb. Consequently, ESP1 enhances female sexual receptive behaviour upon male mounting (lordosis), allowing successful copulation. In V2Rp5-deficient mice, ESP1 induces neither neural activation nor sexual behaviour. These findings show that ESP1 is a crucial male pheromone that regulates female reproductive behaviour through a specific receptor in the mouse vomeronasal system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haga, Sachiko -- Hattori, Tatsuya -- Sato, Toru -- Sato, Koji -- Matsuda, Soichiro -- Kobayakawa, Reiko -- Sakano, Hitoshi -- Yoshihara, Yoshihiro -- Kikusui, Takefumi -- Touhara, Kazushige -- England -- Nature. 2010 Jul 1;466(7302):118-22. doi: 10.1038/nature09142.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20596023" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/cytology/metabolism ; Female ; Male ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Neurons/metabolism ; Pheromones/*metabolism ; Proteins/*metabolism ; Proto-Oncogene Proteins c-fos/metabolism ; Receptors, Odorant/deficiency/genetics/*metabolism ; Receptors, Pheromone/deficiency/genetics/*metabolism ; Sexual Behavior, Animal/*physiology ; TRPC Cation Channels/deficiency ; Vomeronasal Organ/cytology/innervation/*metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 8
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    Induction of inflammatory arthropathy resembling rheumatoid arthritis in mice transgenic for HTLV-I (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-30
    Description: Human T cell leukemia virus type-I (HTLV-I) is the etiologic agent of adult T cell leukemia and has also been suggested to be involved in other diseases such as chronic arthritis or myelopathy. To elucidate pathological roles of the virus in disease, transgenic mice were produced that carry the HTLV-I genome. At 2 to 3 months of age, many of the mice developed chronic arthritis resembling rheumatoid arthritis. Synovial and periarticular inflammation with articular erosion caused by invasion of granulation tissues were marked. These observations suggest a possibility that HTLV-I is one of the etiologic agents of chronic arthritis in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Iwakura, Y -- Tosu, M -- Yoshida, E -- Takiguchi, M -- Sato, K -- Kitajima, I -- Nishioka, K -- Yamamoto, K -- Takeda, T -- Hatanaka, M -- New York, N.Y. -- Science. 1991 Aug 30;253(5023):1026-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Medical Science, University of Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1887217" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arthritis, Rheumatoid/*genetics/pathology/physiopathology ; Genes, Viral ; Human T-lymphotropic virus 1/*genetics ; Inflammation ; Joints/pathology ; Mice ; Mice, Inbred Strains ; Mice, Transgenic ; RNA, Messenger/genetics ; Repetitive Sequences, Nucleic Acid ; Viral Envelope Proteins/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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  • 9
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    Neurotransmitter release from synaptotagmin-deficient clonal variants of PC12 cells (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-06-26
    Description: Synaptotagmin (p65) is an abundant synaptic vesicle protein of neurons and contains regions similar to the regulatory domain of protein kinase C. These domains are thought to be involved in calcium-dependent interaction with membrane phospholipids during exocytosis. To assess the functional role of synaptotagmin, synaptotagmin-deficient clonal variants of PC12 cells were isolated. All of the variant cells released catecholamine and adenosine triphosphate in response to elevated intracellular concentrations of calcium, which suggests that synaptotagmin is not essential for secretion of catecholamine and adenosine triphosphate from PC12 cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shoji-Kasai, Y -- Yoshida, A -- Sato, K -- Hoshino, T -- Ogura, A -- Kondo, S -- Fujimoto, Y -- Kuwahara, R -- Kato, R -- Takahashi, M -- New York, N.Y. -- Science. 1992 Jun 26;256(5065):1821-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Mitsubishi Kasel Institute of Life Sciences, Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1352065" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/secretion ; Animals ; Blotting, Northern ; Blotting, Western ; Calcium/pharmacology ; *Calcium-Binding Proteins ; Cerebellum/metabolism ; Dopamine/secretion ; Ionomycin/pharmacology ; Membrane Glycoproteins/*physiology ; Nerve Tissue Proteins/*physiology ; Neurotransmitter Agents/*secretion ; PC12 Cells ; Prosencephalon/metabolism ; RNA, Messenger/analysis ; Rats ; Synaptotagmin I ; Synaptotagmins
    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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  • 10
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    Two chemoreceptors mediate developmental effects of dauer pheromone in C. elegans (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-10-03
    Description: Intraspecific chemical communication is mediated by signals called pheromones. Caenorhabditis elegans secretes a mixture of small molecules (collectively termed dauer pheromone) that regulates entry into the alternate dauer larval stage and also modulates adult behavior via as yet unknown receptors. Here, we identify two heterotrimeric GTP-binding protein (G protein)-coupled receptors (GPCRs) that mediate dauer formation in response to a subset of dauer pheromone components. The SRBC-64 and SRBC-66 GPCRs are members of the large Caenorhabditis-specific SRBC subfamily and are expressed in the ASK chemosensory neurons, which are required for pheromone-induced dauer formation. Expression of both, but not each receptor alone, confers pheromone-mediated effects on heterologous cells. Identification of dauer pheromone receptors will allow a better understanding of the signaling cascades that transduce the context-dependent effects of ecologically important chemical signals.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4448937/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4448937/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, Kyuhyung -- Sato, Koji -- Shibuya, Mayumi -- Zeiger, Danna M -- Butcher, Rebecca A -- Ragains, Justin R -- Clardy, Jon -- Touhara, Kazushige -- Sengupta, Piali -- F32 GM077943/GM/NIGMS NIH HHS/ -- P30 NS045713/NS/NINDS NIH HHS/ -- P30 NS45713/NS/NINDS NIH HHS/ -- R01 CA024487/CA/NCI NIH HHS/ -- R01 CA24487/CA/NCI NIH HHS/ -- R01 GM056223/GM/NIGMS NIH HHS/ -- R01 GM56223/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2009 Nov 13;326(5955):994-8. doi: 10.1126/science.1176331. Epub 2009 Oct 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and National Center for Behavioral Genomics, Brandeis University, Waltham, MA 02454, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19797623" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/genetics/*growth & development/*physiology ; Caenorhabditis elegans Proteins/genetics/physiology ; Calcium/metabolism ; Cell Line ; Chemoreceptor Cells/metabolism ; Cyclic AMP/metabolism ; Cyclic GMP/metabolism ; GTP-Binding Protein alpha Subunits, Gi-Go/physiology ; Gene Expression Regulation, Developmental ; Genes, Helminth ; Guanylate Cyclase/antagonists & inhibitors/metabolism ; Hexoses/chemistry/physiology ; Humans ; Mutation ; Pheromones/*physiology ; Receptors, G-Protein-Coupled ; Reproduction ; Signal Transduction ; Transfection
    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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