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  • Animals  (6)
  • Nature Publishing Group (NPG)  (4)
  • American Association for the Advancement of Science (AAAS)  (2)
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  • Nature Publishing Group (NPG)  (4)
  • American Association for the Advancement of Science (AAAS)  (2)
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  • 1
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    Deletion of Trpm7 disrupts embryonic development and thymopoiesis without altering Mg2+ homeostasis (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-11-01
    Description: The gene transient receptor potential-melastatin-like 7 (Trpm7) encodes a protein that functions as an ion channel and a kinase. TRPM7 has been proposed to be required for cellular Mg2+ homeostasis in vertebrates. Deletion of mouse Trpm7 revealed that it is essential for embryonic development. Tissue-specific deletion of Trpm7 in the T cell lineage disrupted thymopoiesis, which led to a developmental block of thymocytes at the double-negative stage and a progressive depletion of thymic medullary cells. However, deletion of Trpm7 in T cells did not affect acute uptake of Mg2+ or the maintenance of total cellular Mg2+. Trpm7-deficient thymocytes exhibited dysregulated synthesis of many growth factors that are necessary for the differentiation and maintenance of thymic epithelial cells. The thymic medullary cells lost signal transducer and activator of transcription 3 activity, which accounts for their depletion when Trpm7 is disrupted in thymocytes.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2605283/" 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/PMC2605283/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jin, Jie -- Desai, Bimal N -- Navarro, Betsy -- Donovan, Adriana -- Andrews, Nancy C -- Clapham, David E -- T32HL007572-20/HL/NHLBI NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2008 Oct 31;322(5902):756-60. doi: 10.1126/science.1163493.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cardiology, Howard Hughes Medical Institute, Children's Hospital Boston, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18974357" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD44/metabolism ; *Embryonic Development ; Gene Deletion ; Homeostasis ; Intercellular Signaling Peptides and Proteins/genetics/metabolism ; Interleukin-2 Receptor alpha Subunit/metabolism ; *Lymphopoiesis ; Magnesium/*metabolism ; Mice ; Mice, Knockout ; Patch-Clamp Techniques ; STAT3 Transcription Factor/metabolism ; T-Lymphocytes/*cytology/immunology/*metabolism ; TRPM Cation Channels/genetics/*physiology ; Thymus Gland/*cytology
    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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    Allosteric ligands for the pharmacologically dark receptors GPR68 and GPR65 (2015)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2015-11-10
    Description: At least 120 non-olfactory G-protein-coupled receptors in the human genome are 'orphans' for which endogenous ligands are unknown, and many have no selective ligands, hindering the determination of their biological functions and clinical relevance. Among these is GPR68, a proton receptor that lacks small molecule modulators for probing its biology. Using yeast-based screens against GPR68, here we identify the benzodiazepine drug lorazepam as a non-selective GPR68 positive allosteric modulator. More than 3,000 GPR68 homology models were refined to recognize lorazepam in a putative allosteric site. Docking 3.1 million molecules predicted new GPR68 modulators, many of which were confirmed in functional assays. One potent GPR68 modulator, ogerin, suppressed recall in fear conditioning in wild-type but not in GPR68-knockout mice. The same approach led to the discovery of allosteric agonists and negative allosteric modulators for GPR65. Combining physical and structure-based screening may be broadly useful for ligand discovery for understudied and orphan GPCRs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Xi-Ping -- Karpiak, Joel -- Kroeze, Wesley K -- Zhu, Hu -- Chen, Xin -- Moy, Sheryl S -- Saddoris, Kara A -- Nikolova, Viktoriya D -- Farrell, Martilias S -- Wang, Sheng -- Mangano, Thomas J -- Deshpande, Deepak A -- Jiang, Alice -- Penn, Raymond B -- Jin, Jian -- Koller, Beverly H -- Kenakin, Terry -- Shoichet, Brian K -- Roth, Bryan L -- GM59957/GM/NIGMS NIH HHS/ -- GM71896/GM/NIGMS NIH HHS/ -- P01 HL114471/HL/NHLBI NIH HHS/ -- R01 DA017204/DA/NIDA NIH HHS/ -- R01 DA027170/DA/NIDA NIH HHS/ -- U01 MH104974/MH/NIMH NIH HHS/ -- U19MH082441/MH/NIMH NIH HHS/ -- U54 HD079124/HD/NICHD NIH HHS/ -- England -- Nature. 2015 Nov 26;527(7579):477-83. doi: 10.1038/nature15699. Epub 2015 Nov 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, 27599-7365, USA. ; National Institute of Mental Health Psychoactive Drug Screening Program (NIMH PDSP), School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-7365, USA. ; Department of Pharmaceutical Chemistry, University of California at San Francisco, Byers Hall, 1700 4th Street, San Francisco, California 94158-2550, USA. ; Center for Integrative Chemical Biology and Drug Discovery (CICBDD), University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-7363, USA. ; Division of Chemical Biology and Medicinal Chemistry, Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-7360, USA. ; Department of Psychiatry and Carolina Institute for Developmental Disabilities (CIDD), University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-7146, USA. ; Center for Translational Medicine and Department of Medicine, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA. ; Department of Genetics, School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-7264, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26550826" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation/drug effects ; Allosteric Site ; Animals ; Anti-Anxiety Agents/analysis/chemistry/metabolism/pharmacology ; Benzyl Alcohols/analysis/*chemistry/metabolism/*pharmacology ; Conditioning, Classical ; *Drug Discovery ; Fear ; Female ; HEK293 Cells ; Humans ; Ligands ; Lorazepam/analysis/*chemistry/metabolism/*pharmacology ; Male ; Memory/drug effects ; Mice ; Mice, Knockout ; Models, Molecular ; Receptors, G-Protein-Coupled/agonists/antagonists & ; inhibitors/chemistry/deficiency/*metabolism ; Signal Transduction/drug effects ; Triazines/analysis/*chemistry/metabolism/*pharmacology
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 3
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    Topoisomerase inhibitors unsilence the dormant allele of Ube3a in neurons (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-12-23
    Description: Angelman syndrome is a severe neurodevelopmental disorder caused by deletion or mutation of the maternal allele of the ubiquitin protein ligase E3A (UBE3A). In neurons, the paternal allele of UBE3A is intact but epigenetically silenced, raising the possibility that Angelman syndrome could be treated by activating this silenced allele to restore functional UBE3A protein. Using an unbiased, high-content screen in primary cortical neurons from mice, we identify twelve topoisomerase I inhibitors and four topoisomerase II inhibitors that unsilence the paternal Ube3a allele. These drugs included topotecan, irinotecan, etoposide and dexrazoxane (ICRF-187). At nanomolar concentrations, topotecan upregulated catalytically active UBE3A in neurons from maternal Ube3a-null mice. Topotecan concomitantly downregulated expression of the Ube3a antisense transcript that overlaps the paternal copy of Ube3a. These results indicate that topotecan unsilences Ube3a in cis by reducing transcription of an imprinted antisense RNA. When administered in vivo, topotecan unsilenced the paternal Ube3a allele in several regions of the nervous system, including neurons in the hippocampus, neocortex, striatum, cerebellum and spinal cord. Paternal expression of Ube3a remained elevated in a subset of spinal cord neurons for at least 12 weeks after cessation of topotecan treatment, indicating that transient topoisomerase inhibition can have enduring effects on gene expression. Although potential off-target effects remain to be investigated, our findings suggest a therapeutic strategy for reactivating the functional but dormant allele of Ube3a in patients with Angelman syndrome.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3257422/" 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/PMC3257422/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Hsien-Sung -- Allen, John A -- Mabb, Angela M -- King, Ian F -- Miriyala, Jayalakshmi -- Taylor-Blake, Bonnie -- Sciaky, Noah -- Dutton, J Walter Jr -- Lee, Hyeong-Min -- Chen, Xin -- Jin, Jian -- Bridges, Arlene S -- Zylka, Mark J -- Roth, Bryan L -- Philpot, Benjamin D -- 5F32NS067712/NS/NINDS NIH HHS/ -- 5P30NS045892/NS/NINDS NIH HHS/ -- HHSN-271-2008-00025-C/PHS HHS/ -- P30 HD003110/HD/NICHD NIH HHS/ -- P30 HD003110-45/HD/NICHD NIH HHS/ -- P30HD03110/HD/NICHD NIH HHS/ -- R01EY018323/EY/NEI NIH HHS/ -- R01MH093372/MH/NIMH NIH HHS/ -- R01NS060725/NS/NINDS NIH HHS/ -- R01NS067688/NS/NINDS NIH HHS/ -- T32 HD040127/HD/NICHD NIH HHS/ -- T32 HD040127-10/HD/NICHD NIH HHS/ -- T32HD040127-07/HD/NICHD NIH HHS/ -- England -- Nature. 2011 Dec 21;481(7380):185-9. doi: 10.1038/nature10726.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Molecular Physiology, University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22190039" target="_blank"〉PubMed〈/a〉
    Keywords: *Alleles ; Angelman Syndrome/drug therapy/genetics ; Animals ; Cells, Cultured ; Cerebral Cortex/cytology/drug effects/metabolism ; Drug Evaluation, Preclinical ; Fathers ; Female ; Gene Silencing/*drug effects ; Genomic Imprinting/drug effects/genetics ; Male ; Mice ; Mice, Inbred C57BL ; Mothers ; Neurons/*drug effects/*metabolism ; Small Molecule Libraries/administration & dosage/chemistry/pharmacology ; Topoisomerase Inhibitors/administration & ; dosage/analysis/pharmacokinetics/*pharmacology ; Topotecan/administration & dosage/pharmacokinetics/pharmacology ; Ubiquitin-Protein Ligases/deficiency/*genetics
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 4
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    OTUD7B controls non-canonical NF-kappaB activation through deubiquitination of TRAF3 (2013)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2013-01-22
    Description: The non-canonical NF-kappaB pathway forms a major arm of NF-kappaB signalling that mediates important biological functions, including lymphoid organogenesis, B-lymphocyte function, and cell growth and survival. Activation of the non-canonical NF-kappaB pathway involves degradation of an inhibitory protein, TNF receptor-associated factor 3 (TRAF3), but how this signalling event is controlled is still unknown. Here we have identified the deubiquitinase OTUD7B as a pivotal regulator of the non-canonical NF-kappaB pathway. OTUD7B deficiency in mice has no appreciable effect on canonical NF-kappaB activation but causes hyperactivation of non-canonical NF-kappaB. In response to non-canonical NF-kappaB stimuli, OTUD7B binds and deubiquitinates TRAF3, thereby inhibiting TRAF3 proteolysis and preventing aberrant non-canonical NF-kappaB activation. Consequently, the OTUD7B deficiency results in B-cell hyper-responsiveness to antigens, lymphoid follicular hyperplasia in the intestinal mucosa, and elevated host-defence ability against an intestinal bacterial pathogen, Citrobacter rodentium. These findings establish OTUD7B as a crucial regulator of signal-induced non-canonical NF-kappaB activation and indicate a mechanism of immune regulation that involves OTUD7B-mediated deubiquitination and stabilization of TRAF3.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3578967/" 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/PMC3578967/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hu, Hongbo -- Brittain, George C -- Chang, Jae-Hoon -- Puebla-Osorio, Nahum -- Jin, Jin -- Zal, Anna -- Xiao, Yichuan -- Cheng, Xuhong -- Chang, Mikyoung -- Fu, Yang-Xin -- Zal, Tomasz -- Zhu, Chengming -- Sun, Shao-Cong -- AI057555/AI/NIAID NIH HHS/ -- AI064639/AI/NIAID NIH HHS/ -- CA137059/CA/NCI NIH HHS/ -- GM84459/GM/NIGMS NIH HHS/ -- P30 CA016672/CA/NCI NIH HHS/ -- R01 CA137059/CA/NCI NIH HHS/ -- R01 GM084459/GM/NIGMS NIH HHS/ -- T32 CA009598/CA/NCI NIH HHS/ -- T32CA009598/CA/NCI NIH HHS/ -- England -- Nature. 2013 Feb 21;494(7437):371-4. doi: 10.1038/nature11831. Epub 2013 Jan 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, The University of Texas MD Anderson Cancer Center, 7455 Fannin Street, Box 902, Houston, Texas 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23334419" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/immunology/metabolism ; Bacteria/immunology ; Cells, Cultured ; Endopeptidases/deficiency/genetics/*metabolism ; Female ; Fibroblasts ; HEK293 Cells ; Homeostasis ; Humans ; Intestines/immunology ; Male ; Mice ; NF-kappa B/*metabolism ; Proteolysis ; Receptors, Cell Surface/metabolism ; TNF Receptor-Associated Factor 3/*metabolism ; *Ubiquitination
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 5
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    Draft genome of the filarial nematode parasite Brugia malayi (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-09-22
    Description: Parasitic nematodes that cause elephantiasis and river blindness threaten hundreds of millions of people in the developing world. We have sequenced the approximately 90 megabase (Mb) genome of the human filarial parasite Brugia malayi and predict approximately 11,500 protein coding genes in 71 Mb of robustly assembled sequence. Comparative analysis with the free-living, model nematode Caenorhabditis elegans revealed that, despite these genes having maintained little conservation of local synteny during approximately 350 million years of evolution, they largely remain in linkage on chromosomal units. More than 100 conserved operons were identified. Analysis of the predicted proteome provides evidence for adaptations of B. malayi to niches in its human and vector hosts and insights into the molecular basis of a mutualistic relationship with its Wolbachia endosymbiont. These findings offer a foundation for rational drug design.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2613796/" 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/PMC2613796/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ghedin, Elodie -- Wang, Shiliang -- Spiro, David -- Caler, Elisabet -- Zhao, Qi -- Crabtree, Jonathan -- Allen, Jonathan E -- Delcher, Arthur L -- Guiliano, David B -- Miranda-Saavedra, Diego -- Angiuoli, Samuel V -- Creasy, Todd -- Amedeo, Paolo -- Haas, Brian -- El-Sayed, Najib M -- Wortman, Jennifer R -- Feldblyum, Tamara -- Tallon, Luke -- Schatz, Michael -- Shumway, Martin -- Koo, Hean -- Salzberg, Steven L -- Schobel, Seth -- Pertea, Mihaela -- Pop, Mihai -- White, Owen -- Barton, Geoffrey J -- Carlow, Clotilde K S -- Crawford, Michael J -- Daub, Jennifer -- Dimmic, Matthew W -- Estes, Chris F -- Foster, Jeremy M -- Ganatra, Mehul -- Gregory, William F -- Johnson, Nicholas M -- Jin, Jinming -- Komuniecki, Richard -- Korf, Ian -- Kumar, Sanjay -- Laney, Sandra -- Li, Ben-Wen -- Li, Wen -- Lindblom, Tim H -- Lustigman, Sara -- Ma, Dong -- Maina, Claude V -- Martin, David M A -- McCarter, James P -- McReynolds, Larry -- Mitreva, Makedonka -- Nutman, Thomas B -- Parkinson, John -- Peregrin-Alvarez, Jose M -- Poole, Catherine -- Ren, Qinghu -- Saunders, Lori -- Sluder, Ann E -- Smith, Katherine -- Stanke, Mario -- Unnasch, Thomas R -- Ware, Jenna -- Wei, Aguan D -- Weil, Gary -- Williams, Deryck J -- Zhang, Yinhua -- Williams, Steven A -- Fraser-Liggett, Claire -- Slatko, Barton -- Blaxter, Mark L -- Scott, Alan L -- R01 AI048562/AI/NIAID NIH HHS/ -- R01 AI048562-09/AI/NIAID NIH HHS/ -- R01 LM006845/LM/NLM NIH HHS/ -- R01 LM006845-08/LM/NLM NIH HHS/ -- R01 LM007938/LM/NLM NIH HHS/ -- R01 LM007938-04/LM/NLM NIH HHS/ -- R15 ES013128/ES/NIEHS NIH HHS/ -- R15 ES013128-01/ES/NIEHS NIH HHS/ -- U01 AI048828/AI/NIAID NIH HHS/ -- U01-AI50903/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2007 Sep 21;317(5845):1756-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Infectious Diseases, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, USA. GhedinE@dom.pitt.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17885136" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brugia malayi/*genetics/physiology ; Caenorhabditis/genetics ; Drosophila melanogaster/genetics ; Drug Resistance/genetics ; Filariasis/parasitology ; *Genome, Helminth ; Humans ; Molecular Sequence Data
    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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    Principles underlying sensory map topography in primary visual cortex (2016)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2016-04-28
    Description: The primary visual cortex contains a detailed map of the visual scene, which is represented according to multiple stimulus dimensions including spatial location, ocular dominance and stimulus orientation. The maps for spatial location and ocular dominance arise from the spatial arrangement of thalamic afferent axons in the cortex. However, the origins of the other maps remain unclear. Here we show that the cortical maps for orientation, direction and retinal disparity in the cat (Felis catus) are all strongly related to the organization of the map for spatial location of light (ON) and dark (OFF) stimuli, an organization that we show is OFF-dominated, OFF-centric and runs orthogonal to ocular dominance columns. Because this ON-OFF organization originates from the clustering of ON and OFF thalamic afferents in the visual cortex, we conclude that all main features of visual cortical topography, including orientation, direction and retinal disparity, follow a common organizing principle that arranges thalamic axons with similar retinotopy and ON-OFF polarity in neighbouring cortical regions.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4860131/" 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/PMC4860131/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kremkow, Jens -- Jin, Jianzhong -- Wang, Yushi -- Alonso, Jose M -- EY005253/EY/NEI NIH HHS/ -- R01 EY005253/EY/NEI NIH HHS/ -- R01 EY020679/EY/NEI NIH HHS/ -- England -- Nature. 2016 May 5;533(7601):52-7. doi: 10.1038/nature17936. Epub 2016 Apr 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate Center for Vision Research, State University of New York, College of Optometry, 33 West 42nd Street, New York, New York 10036, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/27120164" target="_blank"〉PubMed〈/a〉
    Keywords: Afferent Pathways/radiation effects ; Animals ; Axons/physiology ; *Brain Mapping ; Cats ; Darkness ; Dominance, Ocular/physiology ; Light ; Macaca mulatta ; Male ; Models, Neurological ; Orientation/physiology/radiation effects ; Photic Stimulation ; Retina/physiology/radiation effects ; Space Perception/*physiology/radiation effects ; Thalamus/physiology/radiation effects ; Visual Cortex/*physiology/radiation effects ; Visual Fields/*physiology
    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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