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  • 1
    Publication Date: 2014-03-05
    Description: Epithelial folding mediated by apical constriction converts flat epithelial sheets into multilayered, complex tissue structures and is used throughout development in most animals. Little is known, however, about how forces produced near the apical surface of the tissue are transmitted within individual cells to generate the global changes in cell shape that characterize tissue deformation. Here we apply particle tracking velocimetry in gastrulating Drosophila embryos to measure the movement of cytoplasm and plasma membrane during ventral furrow formation. We find that cytoplasmic redistribution during the lengthening phase of ventral furrow formation can be precisely described by viscous flows that quantitatively match the predictions of hydrodynamics. Cell membranes move with the ambient cytoplasm, with little resistance to, or driving force on, the flow. Strikingly, apical constriction produces similar flow patterns in mutant embryos that fail to form cells before gastrulation ('acellular' embryos), such that the global redistribution of cytoplasm mirrors the summed redistribution occurring in individual cells of wild-type embryos. Our results indicate that during the lengthening phase of ventral furrow formation, hydrodynamic behaviour of the cytoplasm provides the predominant mechanism transmitting apically generated forces deep into the tissue and that cell individualization is dispensable.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4111109/" 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/PMC4111109/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉He, Bing -- Doubrovinski, Konstantin -- Polyakov, Oleg -- Wieschaus, Eric -- 5R37HD15587/HD/NICHD NIH HHS/ -- P50 GM 071508/GM/NIGMS NIH HHS/ -- R01 HD015587/HD/NICHD NIH HHS/ -- R37 HD015587/HD/NICHD NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2014 Apr 17;508(7496):392-6. doi: 10.1038/nature13070. Epub 2014 Mar 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544, USA [2]. ; Department of Physics, Princeton University, Princeton, New Jersey 08544, USA. ; 1] Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544, USA [2] Howard Hughes Medical Institute, Princeton University, Princeton, New Jersey 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24590071" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/metabolism ; *Cell Polarity ; *Cell Shape ; Cytoplasm/metabolism ; Drosophila melanogaster/*cytology/*embryology ; Female ; Gastrulation ; Hydrodynamics ; Male ; Mesoderm/cytology/metabolism ; *Morphogenesis ; Movement
    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: 2013-12-18
    Description: Prokaryotic viruses have evolved various mechanisms to transport their genomes across bacterial cell walls. Many bacteriophages use a tail to perform this function, whereas tail-less phages rely on host organelles. However, the tail-less, icosahedral, single-stranded DNA PhiX174-like coliphages do not fall into these well-defined infection processes. For these phages, DNA delivery requires a DNA pilot protein. Here we show that the PhiX174 pilot protein H oligomerizes to form a tube whose function is most probably to deliver the DNA genome across the host's periplasmic space to the cytoplasm. The 2.4 A resolution crystal structure of the in vitro assembled H protein's central domain consists of a 170 A-long alpha-helical barrel. The tube is constructed of ten alpha-helices with their amino termini arrayed in a right-handed super-helical coiled-coil and their carboxy termini arrayed in a left-handed super-helical coiled-coil. Genetic and biochemical studies demonstrate that the tube is essential for infectivity but does not affect in vivo virus assembly. Cryo-electron tomograms show that tubes span the periplasmic space and are present while the genome is being delivered into the host cell's cytoplasm. Both ends of the H protein contain transmembrane domains, which anchor the assembled tubes into the inner and outer cell membranes. The central channel of the H-protein tube is lined with amide and guanidinium side chains. This may be a general property of viral DNA conduits and is likely to be critical for efficient genome translocation into the host.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sun, Lei -- Young, Lindsey N -- Zhang, Xinzheng -- Boudko, Sergei P -- Fokine, Andrei -- Zbornik, Erica -- Roznowski, Aaron P -- Molineux, Ian J -- Rossmann, Michael G -- Fane, Bentley A -- England -- Nature. 2014 Jan 16;505(7483):432-5. doi: 10.1038/nature12816. Epub 2013 Dec 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA [2]. ; 1] School of Plant Sciences and the BIO5 Institute, University of Arizona, Tucson, Arizona 85721, USA [2]. ; 1] Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA [2] The Research Department, Shriner's Hospital for Children, Portland, Oregon 97239, USA. ; Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA. ; School of Plant Sciences and the BIO5 Institute, University of Arizona, Tucson, Arizona 85721, USA. ; Molecular Genetics and Microbiology, Institute for Cell and Molecular Biology, The University of Texas at Austin, Austin, Texas 78712, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24336205" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage phi X 174/*chemistry/*metabolism/ultrastructure ; Biological Transport ; Cryoelectron Microscopy ; Crystallography, X-Ray ; Cytoplasm/metabolism/ultrastructure/virology ; DNA, Viral/*metabolism/ultrastructure ; Escherichia coli/cytology/ultrastructure/*virology ; Genome, Viral ; Models, Molecular ; Periplasm/metabolism/ultrastructure ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Viral Proteins/chemistry/metabolism/ultrastructure ; *Virus Assembly
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    Electronic ISSN: 1476-4687
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  • 3
    Publication Date: 2014-11-14
    Description: Films of iron selenide (FeSe) one unit cell thick grown on strontium titanate (SrTiO3 or STO) substrates have recently shown superconducting energy gaps opening at temperatures close to the boiling point of liquid nitrogen (77 kelvin), which is a record for the iron-based superconductors. The gap opening temperature usually sets the superconducting transition temperature Tc, as the gap signals the formation of Cooper pairs, the bound electron states responsible for superconductivity. To understand why Cooper pairs form at such high temperatures, we examine the role of the SrTiO3 substrate. Here we report high-resolution angle-resolved photoemission spectroscopy results that reveal an unexpected characteristic of the single-unit-cell FeSe/SrTiO3 system: shake-off bands suggesting the presence of bosonic modes, most probably oxygen optical phonons in SrTiO3 (refs 5, 6, 7), which couple to the FeSe electrons with only a small momentum transfer. Such interfacial coupling assists superconductivity in most channels, including those mediated by spin fluctuations. Our calculations suggest that this coupling is responsible for raising the superconducting gap opening temperature in single-unit-cell FeSe/SrTiO3.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, J J -- Schmitt, F T -- Moore, R G -- Johnston, S -- Cui, Y-T -- Li, W -- Yi, M -- Liu, Z K -- Hashimoto, M -- Zhang, Y -- Lu, D H -- Devereaux, T P -- Lee, D-H -- Shen, Z-X -- England -- Nature. 2014 Nov 13;515(7526):245-8. doi: 10.1038/nature13894.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Stanford Institute for Materials and Energy Sciences, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA [2] Departments of Physics and Applied Physics, and Geballe Laboratory for Advanced Materials, Stanford University, Stanford, California 94305, USA. ; Stanford Institute for Materials and Energy Sciences, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA. ; 1] Department of Physics and Astronomy, University of British Columbia, Vancouver, British Columbia V6T 1Z1, Canada [2] Quantum Matter Institute, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada [3] Department of Physics and Astronomy, University of Tennessee, Knoxville, Tennessee 37996-1200, USA. ; Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA. ; 1] Stanford Institute for Materials and Energy Sciences, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA [2] Advanced Light Source, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA. ; 1] Department of Physics, University of California at Berkeley, Berkeley, California 94720, USA [2] Material Science Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25391962" target="_blank"〉PubMed〈/a〉
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  • 4
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    Nature Publishing Group (NPG)
    Publication Date: 2014-07-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moskvitch, Katia -- Susman, Edward -- England -- Nature. 2014 Jul 24;511(7510):391. doi: 10.1038/511391a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25056040" target="_blank"〉PubMed〈/a〉
    Keywords: *Acquired Immunodeficiency Syndrome/drug therapy/epidemiology ; *Aircraft ; Anti-HIV Agents ; Australia ; Congresses as Topic ; *Death ; Developing Countries/statistics & numerical data ; Humans ; Netherlands ; *Research Personnel ; Ukraine
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    Electronic ISSN: 1476-4687
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  • 5
    Publication Date: 2014-09-02
    Description: The abundances of elements in stars are critical clues to stars' origins. Observed star-to-star variations in logarithmic abundance within an open star cluster--a gravitationally bound ensemble of stars in the Galactic plane--are typically only about 0.01 to 0.05 over many elements, which is noticeably smaller than the variation of about 0.06 to 0.3 seen in the interstellar medium from which the stars form. It is unknown why star clusters are so homogenous, and whether homogeneity should also prevail in regions of lower star formation efficiency that do not produce bound clusters. Here we report simulations that trace the mixing of chemical elements as star-forming clouds assemble and collapse. We show that turbulent mixing during cloud assembly naturally produces a stellar abundance scatter at least five times smaller than that in the gas, which is sufficient to explain the observed chemical homogeneity of stars. Moreover, mixing occurs very early, so that regions with star formation efficiencies of about 10 per cent are nearly as well mixed as those with formation efficiencies of about 50 per cent. This implies that even regions that do not form bound clusters are likely to be well mixed, and improves the prospects of using 'chemical tagging' to reconstruct (via their unique chemical signatures, or tags) star clusters whose constituent stars have become unbound from one another and spread across the Galactic disk.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feng, Yi -- Krumholz, Mark R -- England -- Nature. 2014 Sep 25;513(7519):523-5. doi: 10.1038/nature13662. Epub 2014 Aug 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Astronomy and Astrophysics, University of California, Santa Cruz, California 95064, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25174709" target="_blank"〉PubMed〈/a〉
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  • 6
    Publication Date: 2014-04-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moss, Andrew -- Jensen, Eric -- Gusset, Markus -- England -- Nature. 2014 Apr 10;508(7495):186. doi: 10.1038/508186d.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chester Zoo, UK. ; University of Warwick, Coventry, UK. ; World Association of Zoos and Aquariums, Gland, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24717506" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Animals, Zoo ; *Biodiversity ; Conservation of Natural Resources/*trends ; Ecology/*education
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  • 7
    Publication Date: 2014-11-11
    Description: Autophagy is an evolutionarily conserved catabolic process that recycles nutrients upon starvation and maintains cellular energy homeostasis. Its acute regulation by nutrient-sensing signalling pathways is well described, but its longer-term transcriptional regulation is not. The nuclear receptors peroxisome proliferator-activated receptor-alpha (PPARalpha) and farnesoid X receptor (FXR) are activated in the fasted and fed liver, respectively. Here we show that both PPARalpha and FXR regulate hepatic autophagy in mice. Pharmacological activation of PPARalpha reverses the normal suppression of autophagy in the fed state, inducing autophagic lipid degradation, or lipophagy. This response is lost in PPARalpha knockout (Ppara(-/-), also known as Nr1c1(-/-)) mice, which are partially defective in the induction of autophagy by fasting. Pharmacological activation of the bile acid receptor FXR strongly suppresses the induction of autophagy in the fasting state, and this response is absent in FXR knockout (Fxr(-/-), also known as Nr1h4(-/-)) mice, which show a partial defect in suppression of hepatic autophagy in the fed state. PPARalpha and FXR compete for binding to shared sites in autophagic gene promoters, with opposite transcriptional outputs. These results reveal complementary, interlocking mechanisms for regulation of autophagy by nutrient status.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4267857/" 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/PMC4267857/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Jae Man -- Wagner, Martin -- Xiao, Rui -- Kim, Kang Ho -- Feng, Dan -- Lazar, Mitchell A -- Moore, David D -- DK43806/DK/NIDDK NIH HHS/ -- P30 DK019525/DK/NIDDK NIH HHS/ -- P30DX56338-05A2/PHS HHS/ -- P39CA125123-04/CA/NCI NIH HHS/ -- R01 DK049780/DK/NIDDK NIH HHS/ -- R01 DK49780/DK/NIDDK NIH HHS/ -- R37 DK043806/DK/NIDDK NIH HHS/ -- S10RR027783-01A1/RR/NCRR NIH HHS/ -- U54HD-07495-39/HD/NICHD NIH HHS/ -- England -- Nature. 2014 Dec 4;516(7529):112-5. doi: 10.1038/nature13961. Epub 2014 Nov 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas 77030, USA. ; Division of Endocrinology, Diabetes, and Metabolism and the Institute for Diabetes, Obesity, and Metabolism, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, Pennsylvania 19014, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25383539" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autophagy/genetics/*physiology ; Cell Line ; Cells, Cultured ; Fasting/physiology ; Gene Expression Regulation ; Hepatocytes/metabolism ; Liver/cytology/*metabolism/ultrastructure ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Microtubule-Associated Proteins/genetics/metabolism ; PPAR alpha ; Receptors, Cytoplasmic and Nuclear/genetics/*metabolism
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  • 8
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    Nature Publishing Group (NPG)
    Publication Date: 2014-07-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alperin, Juan Pablo -- England -- Nature. 2014 Jul 10;511(7508):155. doi: 10.1038/511155c.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Stanford University, California, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25008513" target="_blank"〉PubMed〈/a〉
    Keywords: *Science
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  • 9
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    Nature Publishing Group (NPG)
    Publication Date: 2014-10-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abbott, Alison -- Callaway, Ewen -- England -- Nature. 2014 Oct 9;514(7521):153. doi: 10.1038/514153a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25297415" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Entorhinal Cortex/*cytology/physiology ; Hippocampus/*cytology/physiology ; Humans ; Models, Neurological ; *Nobel Prize ; Space Perception/*physiology
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  • 10
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    Nature Publishing Group (NPG)
    Publication Date: 2014-11-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ledford, Heidi -- England -- Nature. 2014 Nov 13;515(7526):182-4. doi: 10.1038/515182a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25391943" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antidepressive Agents/pharmacology/therapeutic use ; Biomedical Research/economics/*statistics & numerical data/*trends ; Depression/*epidemiology/genetics/psychology/*therapy ; Depressive Disorder/epidemiology/genetics/psychology/therapy ; Disease Models, Animal ; Humans ; Mice ; *Neoplasms ; Neurosciences/*trends ; Stress, Psychological/epidemiology/etiology/therapy
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