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  • History, 21st Century  (67)
  • Protein Structure, Tertiary  (50)
  • Nature Publishing Group (NPG)  (117)
  • Springer Science + Business Media
  • 2015-2019  (117)
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  • 1
    Publication Date: 2015-09-22
    Description: Piezo proteins are evolutionarily conserved and functionally diverse mechanosensitive cation channels. However, the overall structural architecture and gating mechanisms of Piezo channels have remained unknown. Here we determine the cryo-electron microscopy structure of the full-length (2,547 amino acids) mouse Piezo1 (Piezo1) at a resolution of 4.8 A. Piezo1 forms a trimeric propeller-like structure (about 900 kilodalton), with the extracellular domains resembling three distal blades and a central cap. The transmembrane region has 14 apparently resolved segments per subunit. These segments form three peripheral wings and a central pore module that encloses a potential ion-conducting pore. The rather flexible extracellular blade domains are connected to the central intracellular domain by three long beam-like structures. This trimeric architecture suggests that Piezo1 may use its peripheral regions as force sensors to gate the central ion-conducting pore.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ge, Jingpeng -- Li, Wanqiu -- Zhao, Qiancheng -- Li, Ningning -- Chen, Maofei -- Zhi, Peng -- Li, Ruochong -- Gao, Ning -- Xiao, Bailong -- Yang, Maojun -- England -- Nature. 2015 Nov 5;527(7576):64-9. doi: 10.1038/nature15247. Epub 2015 Sep 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences or Medicine, Tsinghua University, Beijing 100084, China. ; Ministry of Education, Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China. ; Department of Pharmacology and Pharmaceutical Sciences, School of Medicine, Tsinghua University, Beijing 100084, China. ; IDG/McGovern Institute for Brain Research, Tsinghua University, Beijing 100084, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26390154" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/metabolism ; *Cryoelectron Microscopy ; Electric Conductivity ; Ion Channel Gating ; Ion Channels/*chemistry/metabolism/*ultrastructure ; Mice ; Models, Molecular ; Pliability ; Protein Multimerization ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism
    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: 2015-07-24
    Description: Bacteria secrete peptides and proteins to communicate, to poison competitors, and to manipulate host cells. Among the various protein-translocation machineries, the peptidase-containing ATP-binding cassette transporters (PCATs) are appealingly simple. Each PCAT contains two peptidase domains that cleave the secretion signal from the substrate, two transmembrane domains that form a translocation pathway, and two nucleotide-binding domains that hydrolyse ATP. In Gram-positive bacteria, PCATs function both as maturation proteases and exporters for quorum-sensing or antimicrobial polypeptides. In Gram-negative bacteria, PCATs interact with two other membrane proteins to form the type 1 secretion system. Here we present crystal structures of PCAT1 from Clostridium thermocellum in two different conformations. These structures, accompanied by biochemical data, show that the translocation pathway is a large alpha-helical barrel sufficient to accommodate small folded proteins. ATP binding alternates access to the transmembrane pathway and also regulates the protease activity, thereby coupling substrate processing to translocation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, David Yin-wei -- Huang, Shuo -- Chen, Jue -- Howard Hughes Medical Institute/ -- England -- Nature. 2015 Jul 23;523(7561):425-30. doi: 10.1038/nature14623.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Laboratory of Membrane Biology and Biophysics, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA [2] Howard Hughes Medical Institute, 1230 York Avenue, New York, New York 10065, USA. ; Howard Hughes Medical Institute, 1230 York Avenue, New York, New York 10065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26201595" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/*chemistry/metabolism ; Adenosine Triphosphate/deficiency/metabolism ; Clostridium thermocellum/*chemistry ; Crystallography, X-Ray ; Models, Molecular ; Peptides/*metabolism/secretion ; Protein Binding ; Protein Multimerization ; Protein Structure, Tertiary ; Structure-Activity Relationship
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    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 3
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    Nature Publishing Group (NPG)
    Publication Date: 2015-05-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉England -- Nature. 2015 May 28;521(7553):394. doi: 10.1038/521394a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26017406" target="_blank"〉PubMed〈/a〉
    Keywords: *Bibliometrics/history ; History, 19th Century ; History, 20th Century ; History, 21st Century ; Research/*history ; Time Factors
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    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 4
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    Nature Publishing Group (NPG)
    Publication Date: 2015-09-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pain, Stephanie -- England -- Nature. 2015 Sep 24;525(7570):S10-1. doi: 10.1038/525S10a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26398731" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Canada ; Cannabinol/history ; *Cannabis/adverse effects/chemistry/classification/genetics ; China ; Dronabinol/adverse effects/history/pharmacology/therapeutic use ; Drug Approval/history ; Drug and Narcotic Control/*history ; Endocannabinoids/history/metabolism ; Herbal Medicine/*history ; History, 16th Century ; History, 17th Century ; History, 19th Century ; History, 20th Century ; History, 21st Century ; History, Ancient ; History, Medieval ; Humans ; Medical Marijuana/adverse effects/history/pharmacology/therapeutic use ; Multiple Sclerosis/drug therapy/physiopathology ; New Orleans ; Phytotherapy/history ; Plant Extracts/therapeutic use ; Plants, Medicinal/adverse effects/chemistry/classification/genetics ; Receptors, Cannabinoid/history/metabolism
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    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 2015-07-15
    Description: Surface polysaccharides are important for bacterial interactions with multicellular organisms, and some are virulence factors in pathogens. In the legume-rhizobium symbiosis, bacterial exopolysaccharides (EPS) are essential for the development of infected root nodules. We have identified a gene in Lotus japonicus, Epr3, encoding a receptor-like kinase that controls this infection. We show that epr3 mutants are defective in perception of purified EPS, and that EPR3 binds EPS directly and distinguishes compatible and incompatible EPS in bacterial competition studies. Expression of Epr3 in epidermal cells within the susceptible root zone shows that the protein is involved in bacterial entry, while rhizobial and plant mutant studies suggest that Epr3 regulates bacterial passage through the plant's epidermal cell layer. Finally, we show that Epr3 expression is inducible and dependent on host perception of bacterial nodulation (Nod) factors. Plant-bacterial compatibility and bacterial access to legume roots is thus regulated by a two-stage mechanism involving sequential receptor-mediated recognition of Nod factor and EPS signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawaharada, Y -- Kelly, S -- Nielsen, M Wibroe -- Hjuler, C T -- Gysel, K -- Muszynski, A -- Carlson, R W -- Thygesen, M B -- Sandal, N -- Asmussen, M H -- Vinther, M -- Andersen, S U -- Krusell, L -- Thirup, S -- Jensen, K J -- Ronson, C W -- Blaise, M -- Radutoiu, S -- Stougaard, J -- England -- Nature. 2015 Jul 16;523(7560):308-12. doi: 10.1038/nature14611. Epub 2015 Jul 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Centre for Carbohydrate Recognition and Signalling. Aarhus University, Aarhus 8000 C, Denmark [2] Department of Molecular Biology and Genetics, Aarhus University, Aarhus 8000 C, Denmark. ; 1] Centre for Carbohydrate Recognition and Signalling. Aarhus University, Aarhus 8000 C, Denmark [2] Department of Molecular Biology and Genetics, Aarhus University, Aarhus 8000 C, Denmark [3] Department of Microbiology and Immunology, University of Otago, Dunedin 9054, New Zealand. ; 1] Centre for Carbohydrate Recognition and Signalling. Aarhus University, Aarhus 8000 C, Denmark [2] Department of Chemistry, University of Copenhagen, Frederiksberg 1871 C, Denmark. ; Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602, USA. ; 1] Centre for Carbohydrate Recognition and Signalling. Aarhus University, Aarhus 8000 C, Denmark [2] Department of Microbiology and Immunology, University of Otago, Dunedin 9054, New Zealand.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26153863" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Carbohydrate Sequence ; Lipopolysaccharides/chemistry/*metabolism ; Lotus/genetics/*metabolism/*microbiology ; Molecular Sequence Data ; Mutation/genetics ; Phenotype ; Plant Epidermis/metabolism/microbiology ; Plant Proteins/chemistry/genetics/*metabolism ; Plant Root Nodulation ; Protein Kinases/chemistry/genetics/metabolism ; Protein Structure, Tertiary ; Receptors, Cell Surface/chemistry/genetics/*metabolism ; Rhizobium/*metabolism ; Root Nodules, Plant/metabolism/microbiology ; Signal Transduction ; Species Specificity ; Suppression, Genetic/genetics ; *Symbiosis
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  • 6
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    Nature Publishing Group (NPG)
    Publication Date: 2015-04-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Livio, Mario -- England -- Nature. 2015 Apr 16;520(7547):287-9. doi: 10.1038/520287a.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Space Telescope Science Institute (STScI) in Baltimore, Maryland, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25877188" target="_blank"〉PubMed〈/a〉
    Keywords: Astronomy/economics/education/*history/trends ; Exobiology/trends ; History, 20th Century ; History, 21st Century ; Planets ; Telescopes/economics/*history/trends
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    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 2015-09-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, Rebekah R -- Deletic, Ana -- Wong, Tony H F -- England -- Nature. 2015 Sep 17;525(7569):315-7. doi: 10.1038/525315a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26381970" target="_blank"〉PubMed〈/a〉
    Keywords: Biophysics ; Career Mobility ; *Conservation of Natural Resources/history ; *Cooperative Behavior ; History, 21st Century ; Humanities ; *Interdisciplinary Communication ; Policy Making ; Research/history/manpower/*organization & administration ; *Research Design ; Research Personnel/*organization & administration ; Social Sciences ; Water Supply
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  • 8
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    Nature Publishing Group (NPG)
    Publication Date: 2015-05-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mandavilli, Apoorva -- England -- Nature. 2015 May 14;521(7551):148-50. doi: 10.1038/521148a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25971493" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Science Disciplines/manpower/*organization & ; administration/standards/trends ; Biotechnology/organization & administration/standards ; History, 20th Century ; History, 21st Century ; India ; Personnel Selection ; *Research Personnel
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  • 9
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    Nature Publishing Group (NPG)
    Publication Date: 2015-12-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grafton, Anthony -- England -- Nature. 2015 Dec 3;528(7580):40. doi: 10.1038/528040a.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Princeton University in Princeton, New Jersey, USA. He collaborated extensively with Lisa Jardine.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26632582" target="_blank"〉PubMed〈/a〉
    Keywords: Female ; Great Britain ; History, 15th Century ; History, 16th Century ; History, 17th Century ; History, 20th Century ; History, 21st Century ; Humans ; Knowledge ; Literature, Modern/*history ; Male ; Mitochondrial Replacement Therapy ; Science/*history ; Teaching/history ; Writing
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  • 10
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    Nature Publishing Group (NPG)
    Publication Date: 2015-05-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DeWeerdt, Sarah -- England -- Nature. 2015 May 21;521(7552):S50-1. doi: 10.1038/521S50a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25992671" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Beekeeping/*history ; Bees/classification/genetics/*physiology ; Colony Collapse/history ; Diet/*history/veterinary ; Genome, Insect/genetics ; History, 16th Century ; History, 17th Century ; History, 19th Century ; History, 20th Century ; History, 21st Century ; History, Ancient ; Honey/*history/supply & distribution ; Humans ; Phylogeny ; Primates ; Social Behavior
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    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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