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  • 1
    Publication Date: 2016-03-29
    Description: Circuits in the cerebral cortex consist of thousands of neurons connected by millions of synapses. A precise understanding of these local networks requires relating circuit activity with the underlying network structure. For pyramidal cells in superficial mouse visual cortex (V1), a consensus is emerging that neurons with similar visual response properties excite each other, but the anatomical basis of this recurrent synaptic network is unknown. Here we combined physiological imaging and large-scale electron microscopy to study an excitatory network in V1. We found that layer 2/3 neurons organized into subnetworks defined by anatomical connectivity, with more connections within than between groups. More specifically, we found that pyramidal neurons with similar orientation selectivity preferentially formed synapses with each other, despite the fact that axons and dendrites of all orientation selectivities pass near (〈5 mum) each other with roughly equal probability. Therefore, we predict that mechanisms of functionally specific connectivity take place at the length scale of spines. Neurons with similar orientation tuning formed larger synapses, potentially enhancing the net effect of synaptic specificity. With the ability to study thousands of connections in a single circuit, functional connectomics is proving a powerful method to uncover the organizational logic of cortical networks.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4844839/" 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/PMC4844839/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Wei-Chung Allen -- Bonin, Vincent -- Reed, Michael -- Graham, Brett J -- Hood, Greg -- Glattfelder, Katie -- Reid, R Clay -- P30 EY012196/EY/NEI NIH HHS/ -- P30 EY12196/EY/NEI NIH HHS/ -- P41 GM103712/GM/NIGMS NIH HHS/ -- P41 RR006009/RR/NCRR NIH HHS/ -- P41 RR06009/RR/NCRR NIH HHS/ -- R01 EY010115/EY/NEI NIH HHS/ -- R01 EY10115/EY/NEI NIH HHS/ -- R01 NS075436/NS/NINDS NIH HHS/ -- R21 NS085320/NS/NINDS NIH HHS/ -- England -- Nature. 2016 Apr 21;532(7599):370-4. doi: 10.1038/nature17192. Epub 2016 Mar 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Harvard Medical School, Boston, Massachusetts 02115, USA. ; Neuro-Electronics Research Flanders, a research initiative by imec, Vlaams Instituut voor Biotechnologie (VIB) and Katholieke Universiteit (KU) Leuven, 3001 Leuven, Belgium. ; Biomedical Applications Group, Pittsburgh Supercomputing Center, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA. ; Allen Institute for Brain Science, Seattle, Washington 98103, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/27018655" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/physiology ; Calcium/analysis ; Dendrites/physiology ; Male ; Mice ; Mice, Inbred C57BL ; Photons ; Pyramidal Cells/cytology/physiology ; Synapses/metabolism ; Visual Cortex/*anatomy & histology/cytology/*physiology/ultrastructure ; Visual Pathways/anatomy & histology/*cytology/*physiology/ultrastructure
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2017-06-01
    Description: Outcrops within the Eocene Domengine Formation (central California) provide an exceptional opportunity to observe the relationship between depositional facies and submarine mass failure. The Domengine Formation is interpreted as an assemblage of heterolithic, shallow- to marginal-marine deposits that record progradation and aggradation prior to regional flooding and local collapse of the shelf. Structural analysis of soft-sediment folds and reverse faults within the informally named New Idria mass-transport deposit (MTD) suggests transport toward the west to southwest, which is consistent with paleoflow measurements from cross bedding within the MTD. Depositional facies have a strong influence on the character of soft-sediment deformation (e.g., style and scale of folding and faulting), and major layer-parallel detachment surfaces within and below the New Idria MTD occur where mudstone-dominated or heterolithic units underlie sandstone-dominated units. Conditions favorable to gravitational instability and eventual collapse of the shelf include (1) high sedimentation rates within a rapidly aggrading system; (2) loading of under-compacted, mechanically weak, fine-grained layers by overlying, denser sand bodies; and (3) earthquake seismicity and/or over-steepening of slopes within a tectonically active, convergent margin setting. This study provides a rare detailed glimpse into the collapse of a deltaic stratigraphic sequence, yielding insight into the linkage between marginal marine facies and depositional architecture and the propensity for submarine mass failure of continental shelves.
    Electronic ISSN: 1553-040X
    Topics: Geosciences
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  • 3
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    London : Periodicals Archive Online (PAO)
    Journal of historical geography. 13:1 (1987:Jan.) 3 
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  • 4
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    London : Periodicals Archive Online (PAO)
    Journal of historical geography. 13:1 (1987:Jan.) 61 
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  • 5
    Publication Date: 2014-02-28
    Description: Single-stranded DNA (ssDNA) binding protein (SSB) is an essential protein to protect ssDNA and recruit specific ssDNA-processing proteins. Escherichia coli SSB forms a tetramer at neutral pH, comprising a structurally well-defined ssDNA binding domain (OB-domain) and a disordered C-terminal domain (C-domain) of ~64 amino acid residues. The C-terminal eight-residue segment of SSB (C-peptide) has been shown to interact with the OB-domain, but crystal structures failed to reveal any electron density of the C-peptide. Here we show that SSB forms a monomer at pH 3.4, which is suitable for studies by high-resolution nuclear magnetic resonance (NMR) spectroscopy. The OB-domain retains its 3D structure in the monomer, and the C-peptide is shown by nuclear Overhauser effects and lanthanide-induced pseudocontact shifts to bind to the OB-domain at a site that harbors ssDNA in the crystal structure of the SSB–ssDNA complex. 15 N relaxation data demonstrate high flexibility of the polypeptide segment linking the C-peptide to the OB-domain and somewhat increased flexibility of the C-peptide compared with the OB-domain, suggesting that the C-peptide either retains high mobility in the bound state or is in a fast equilibrium with an unbound state.
    Print ISSN: 0305-1048
    Electronic ISSN: 1362-4962
    Topics: Biology
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  • 6
    Publication Date: 1993-11-01
    Print ISSN: 0016-7398
    Electronic ISSN: 1475-4959
    Topics: Geography
    Published by Wiley
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  • 7
    Publication Date: 2006-02-15
    Description: Frequency stability of carbon dioxide laser design for deep space communication applications
    Keywords: MASERS
    Type: NASA. GODDARD SPACE FLIGHT CENTER THE ASEE-UNIV. OF MD.-CATHOLIC UNIV.-NASA SUMMER FAC. FELLOWSHIP PROGRAM APR. 1968; P 63-76
    Format: text
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