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  • 1
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    Operant reward learning in Aplysia: neuronal correlates and mechanisms (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-06-01
    Description: Operant conditioning is a form of associative learning through which an animal learns about the consequences of its behavior. Here, we report an appetitive operant conditioning procedure in Aplysia that induces long-term memory. Biophysical changes that accompanied the memory were found in an identified neuron (cell B51) that is considered critical for the expression of behavior that was rewarded. Similar cellular changes in B51 were produced by contingent reinforcement of B51 with dopamine in a single-cell analog of the operant procedure. These findings allow for the detailed analysis of the cellular and molecular processes underlying operant conditioning.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brembs, Bjorn -- Lorenzetti, Fred D -- Reyes, Fredy D -- Baxter, Douglas A -- Byrne, John H -- MH 58321/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2002 May 31;296(5573):1706-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology and Anatomy, W. M. Keck Center for the Neurobiology of Learning and Memory, The University of Texas-Houston Medical School, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12040200" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aplysia/*physiology ; Cells, Cultured ; *Conditioning, Operant ; Dopamine/pharmacology/physiology ; Eating ; Electric Stimulation ; Electrophysiology ; Esophagus/innervation ; Feeding Behavior ; Food ; Ganglia, Invertebrate/physiology ; Iontophoresis ; Membrane Potentials ; *Memory ; Nerve Net/physiology ; Neuronal Plasticity ; Neurons/*physiology ; Patch-Clamp Techniques ; Reinforcement (Psychology) ; *Reward
    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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    HU multimerization shift controls nucleoid compaction (2016)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2016-07-30
    Description: Molecular mechanisms controlling functional bacterial chromosome (nucleoid) compaction and organization are surprisingly enigmatic but partly depend on conserved, histone-like proteins HUαα and HUαβ and their interactions that span the nanoscale and mesoscale from protein-DNA complexes to the bacterial chromosome and nucleoid structure. We determined the crystal structures of these chromosome-associated proteins in complex with native duplex DNA. Distinct DNA binding modes of HUαα and HUαβ elucidate fundamental features of bacterial chromosome packing that regulate gene transcription. By combining crystal structures with solution x-ray scattering results, we determined architectures of HU-DNA nucleoproteins in solution under near-physiological conditions. These macromolecular conformations and interactions result in contraction at the cellular level based on in vivo imaging of native unlabeled nucleoid by soft x-ray tomography upon HUβ and ectopic HUα38 expression. Structural characterization of charge-altered HUαα-DNA complexes reveals an HU molecular switch that is suitable for condensing nucleoid and reprogramming noninvasive Escherichia coli into an invasive form. Collective findings suggest that shifts between networking and cooperative and noncooperative DNA-dependent HU multimerization control DNA compaction and supercoiling independently of cellular topoisomerase activity. By integrating x-ray crystal structures, x-ray scattering, mutational tests, and x-ray imaging that span from protein-DNA complexes to the bacterial chromosome and nucleoid structure, we show that defined dynamic HU interaction networks can promote nucleoid reorganization and transcriptional regulation as efficient general microbial mechanisms to help synchronize genetic responses to cell cycle, changing environments, and pathogenesis.
    Electronic ISSN: 2375-2548
    Topics: Natural Sciences in General
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Ab initio structure determination by MicroED [Biophysics and Computational Biology] (2016)
    National Academy of Sciences
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    Publication Date: 2016-10-08
    Description: Electrons, because of their strong interaction with matter, produce high-resolution diffraction patterns from tiny 3D crystals only a few hundred nanometers thick in a frozen-hydrated state. This discovery offers the prospect of facile structure determination of complex biological macromolecules, which cannot be coaxed to form crystals large enough for conventional...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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