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  • 1
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    Human alpha-defensin 6 promotes mucosal innate immunity through self-assembled peptide nanonets (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-06-23
    Description: Defensins are antimicrobial peptides that contribute broadly to innate immunity, including protection of mucosal tissues. Human alpha-defensin (HD) 6 is highly expressed by secretory Paneth cells of the small intestine. However, in contrast to the other defensins, it lacks appreciable bactericidal activity. Nevertheless, we report here that HD6 affords protection against invasion by enteric bacterial pathogens in vitro and in vivo. After stochastic binding to bacterial surface proteins, HD6 undergoes ordered self-assembly to form fibrils and nanonets that surround and entangle bacteria. This self-assembly mechanism occurs in vivo, requires histidine-27, and is consistent with x-ray crystallography data. These findings support a key role for HD6 in protecting the small intestine against invasion by diverse enteric pathogens and may explain the conservation of HD6 throughout Hominidae evolution.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4332406/" 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/PMC4332406/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chu, Hiutung -- Pazgier, Marzena -- Jung, Grace -- Nuccio, Sean-Paul -- Castillo, Patricia A -- de Jong, Maarten F -- Winter, Maria G -- Winter, Sebastian E -- Wehkamp, Jan -- Shen, Bo -- Salzman, Nita H -- Underwood, Mark A -- Tsolis, Renee M -- Young, Glenn M -- Lu, Wuyuan -- Lehrer, Robert I -- Baumler, Andreas J -- Bevins, Charles L -- AI032738/AI/NIAID NIH HHS/ -- AI040124/AI/NIAID NIH HHS/ -- AI044170/AI/NIAID NIH HHS/ -- AI050843/AI/NIAID NIH HHS/ -- AI057757/AI/NIAID NIH HHS/ -- AI070726/AI/NIAID NIH HHS/ -- AI072732/AI/NIAID NIH HHS/ -- AI073120/AI/NIAID NIH HHS/ -- AI076246/AI/NIAID NIH HHS/ -- AI082320/AI/NIAID NIH HHS/ -- AI088122/AI/NIAID NIH HHS/ -- HD059127/HD/NICHD NIH HHS/ -- R01 AI032738/AI/NIAID NIH HHS/ -- R01 AI050843/AI/NIAID NIH HHS/ -- R01 AI057757/AI/NIAID NIH HHS/ -- R01 AI076246/AI/NIAID NIH HHS/ -- R01 GM099526/GM/NIGMS NIH HHS/ -- T32AI060555/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2012 Jul 27;337(6093):477-81. doi: 10.1126/science.1218831. Epub 2012 Jun 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, School of Medicine, University of California, Davis, CA 95616, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22722251" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/metabolism ; Animals ; Bacterial Proteins/metabolism ; Cell Line ; Humans ; *Immunity, Innate ; *Immunity, Mucosal ; Intestinal Mucosa/immunology/microbiology/ultrastructure ; Intestine, Small/*immunology/microbiology/ultrastructure ; Macromolecular Substances/chemistry/immunology/metabolism ; Mice ; Mice, Transgenic ; Microscopy, Electron, Scanning ; Models, Molecular ; Nanostructures ; Paneth Cells/immunology/metabolism ; Peptides/chemistry/metabolism ; Protein Binding ; Protein Multimerization ; Protein Structure, Quaternary ; Salmonella Infections, Animal/immunology/microbiology ; Salmonella typhimurium/immunology/pathogenicity/ultrastructure ; Yersinia enterocolitica/immunology/pathogenicity ; alpha-Defensins/*chemistry/immunology/*metabolism ; env Gene Products, Human Immunodeficiency Virus/metabolism
    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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  • 2
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    Host-derived nitrate boosts growth of E. coli in the inflamed gut (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-02-09
    Description: Changes in the microbial community structure are observed in individuals with intestinal inflammatory disorders. These changes are often characterized by a depletion of obligate anaerobic bacteria, whereas the relative abundance of facultative anaerobic Enterobacteriaceae increases. The mechanisms by which the host response shapes the microbial community structure, however, remain unknown. We show that nitrate generated as a by-product of the inflammatory response conferred a growth advantage to the commensal bacterium Escherichia coli in the large intestine of mice. Mice deficient in inducible nitric oxide synthase did not support the growth of E. coli by nitrate respiration, suggesting that the nitrate generated during inflammation was host-derived. Thus, the inflammatory host response selectively enhances the growth of commensal Enterobacteriaceae by generating electron acceptors for anaerobic respiration.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4004111/" 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/PMC4004111/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Winter, Sebastian E -- Winter, Maria G -- Xavier, Mariana N -- Thiennimitr, Parameth -- Poon, Victor -- Keestra, A Marijke -- Laughlin, Richard C -- Gomez, Gabriel -- Wu, Jing -- Lawhon, Sara D -- Popova, Ina E -- Parikh, Sanjai J -- Adams, L Garry -- Tsolis, Renee M -- Stewart, Valley J -- Baumler, Andreas J -- AI076246/AI/NIAID NIH HHS/ -- AI088122/AI/NIAID NIH HHS/ -- AI090387/AI/NIAID NIH HHS/ -- R21 AI107393/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2013 Feb 8;339(6120):708-11. doi: 10.1126/science.1232467.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Microbiology and Immunology, School of Medicine, University of California, Davis, One Shields Avenue, Davis, CA, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23393266" target="_blank"〉PubMed〈/a〉
    Keywords: Anaerobiosis ; Animals ; Cattle ; Colitis/*metabolism/*microbiology ; Escherichia coli/genetics/*growth & development/*metabolism ; Ileum/microbiology ; Intestine, Large/*microbiology ; Mice ; Mice, Inbred C57BL ; Mutation ; Nitrates/*metabolism ; Nitric Oxide Synthase Type II/antagonists & inhibitors/deficiency/metabolism
    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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  • 3
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    LZTR1 is a regulator of RAS ubiquitination and signaling (2018)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2018
    Description: 〈p〉In genetic screens aimed at understanding drug resistance mechanisms in chronic myeloid leukemia cells, inactivation of the cullin 3 adapter protein-encoding leucine zipper like transcription regulator 1 (〈i〉LZTR1〈/i〉) gene led to enhanced mitogen-activated protein kinase pathway activity and reduced sensitivity to tyrosine kinase inhibitors. Knockdown of the 〈i〉Drosophila LZTR1〈/i〉 ortholog 〈i〉CG3711〈/i〉 resulted in a RAS-dependent gain of function phenotype. Endogenous human LZTR1 associates with the main RAS isoforms. Inactivation of 〈i〉LZTR1〈/i〉 led to decreased ubiquitination and enhanced plasma membrane localization of endogenous KRAS. We propose that LZTR1 acts as a conserved regulator of RAS ubiquitination and MAPK pathway activation. As 〈i〉LZTR1〈/i〉 disease mutations failed to revert loss-of-function phenotypes, our findings provide a molecular rationale for 〈i〉LZTR1〈/i〉 involvement in a variety of inherited and acquired human disorders.〈/p〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Natural Sciences in General
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  • 4
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    The geography of biodiversity change in marine and terrestrial assemblages (2019)
    American Association for the Advancement of Science (AAAS)
    In: Science
    Details
    Publication Date: 2019
    Description: 〈p〉Human activities are fundamentally altering biodiversity. Projections of declines at the global scale are contrasted by highly variable trends at local scales, suggesting that biodiversity change may be spatially structured. Here, we examined spatial variation in species richness and composition change using more than 50,000 biodiversity time series from 239 studies and found clear geographic variation in biodiversity change. Rapid compositional change is prevalent, with marine biomes exceeding and terrestrial biomes trailing the overall trend. Assemblage richness is not changing on average, although locations exhibiting increasing and decreasing trends of up to about 20% per year were found in some marine studies. At local scales, widespread compositional reorganization is most often decoupled from richness change, and biodiversity change is strongest and most variable in the oceans.〈/p〉
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Unique identities (2019)
    American Association for the Advancement of Science (AAAS)
    In: Science
    Details
    Publication Date: 2019
    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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    Structure of Arp2/3 complex in its activated state and in actin filament branch junctions (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-09-05
    Description: The seven-subunit Arp2/3 complex choreographs the formation of branched actin networks at the leading edge of migrating cells. When activated by Wiskott-Aldrich Syndrome protein (WASp), the Arp2/3 complex initiates actin filament branches from the sides of existing filaments. Electron cryomicroscopy and three-dimensional reconstruction of Acanthamoeba castellanii and Saccharomyces cerevisiae Arp2/3 complexes bound to the WASp carboxy-terminal domain reveal asymmetric, oblate ellipsoids. Image analysis of actin branches indicates that the complex binds the side of the mother filament, and Arp2 and Arp3 (for actin-related protein) are the first two subunits of the daughter filament. Comparison to the actin-free, WASp-activated complexes suggests that branch initiation involves large-scale structural rearrangements within Arp2/3.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Volkmann, N -- Amann, K J -- Stoilova-McPhie, S -- Egile, C -- Winter, D C -- Hazelwood, L -- Heuser, J E -- Li, R -- Pollard, T D -- Hanein, D -- New York, N.Y. -- Science. 2001 Sep 28;293(5539):2456-9. Epub 2001 Aug 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Burnham Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11533442" target="_blank"〉PubMed〈/a〉
    Keywords: Acanthamoeba ; Actin Cytoskeleton/*metabolism/ultrastructure ; Actin-Related Protein 2 ; Actin-Related Protein 3 ; Actins/*chemistry/*metabolism ; Animals ; Cryoelectron Microscopy ; *Cytoskeletal Proteins ; Fourier Analysis ; Image Processing, Computer-Assisted ; Microscopy, Electron ; Models, Molecular ; Proteins/metabolism ; Saccharomyces cerevisiae ; Wiskott-Aldrich Syndrome Protein
    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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  • 7
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    Reshaping human antibodies: grafting an antilysozyme activity (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-03-25
    Description: The production of therapeutic human monoclonal antibodies by hybridoma technology has proved difficult, and this has prompted the "humanizing" of mouse monoclonal antibodies by recombinant DNA techniques. It was shown previously that the binding site for a small hapten could be grafted from the heavy-chain variable domain of a mouse antibody to that of a human myeloma protein by transplanting the hypervariable loops. It is now shown that a large binding site for a protein antigen (lysozyme) can also be transplanted from mouse to human heavy chain. The success of such constructions may be facilitated by an induced-fit mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Verhoeyen, M -- Milstein, C -- Winter, G -- New York, N.Y. -- Science. 1988 Mar 25;239(4847):1534-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Laboratory of Molecular Biology, Cambridge, England.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2451287" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antibodies, Monoclonal/genetics/immunology ; Base Sequence ; Binding Sites, Antibody ; Binding, Competitive ; Cloning, Molecular ; DNA, Recombinant ; Epitopes/immunology ; Humans ; Immunoglobulin G/genetics/immunology ; Immunoglobulin Variable Region/genetics ; Mice ; Molecular Sequence Data ; Muramidase/*immunology ; Plasmids ; Recombinant Proteins ; Transfection
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Attenuation of virulence by disruption of the Mycobacterium tuberculosis erp gene (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-23
    Description: The virulence of the mycobacteria that cause tuberculosis depends on their ability to multiply in mammalian hosts. Disruption of the bacterial erp gene, which encodes the exported repetitive protein, impaired multiplication of M. tuberculosis and M. bovis Bacille Calmette-Guerin in cultured macrophages and mice. Reintroduction of erp into the mutants restored their ability to multiply. These results indicate that erp contributes to the virulence of M. tuberculosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berthet, F X -- Lagranderie, M -- Gounon, P -- Laurent-Winter, C -- Ensergueix, D -- Chavarot, P -- Thouron, F -- Maranghi, E -- Pelicic, V -- Portnoi, D -- Marchal, G -- Gicquel, B -- AI 35207/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1998 Oct 23;282(5389):759-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unite de Genetique Mycobacterienne, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9784137" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; BCG Vaccine ; Bacterial Proteins/analysis/genetics/*physiology ; Cell Line ; Genes, Bacterial ; Genetic Complementation Test ; Immunohistochemistry ; Lung/microbiology ; Macrophages/microbiology ; Membrane Proteins/analysis/genetics/*physiology ; Mice ; Mice, Inbred BALB C ; Mutation ; Mycobacterium bovis/genetics/growth & development ; Mycobacterium tuberculosis/genetics/growth & ; development/metabolism/*pathogenicity ; Phagosomes/microbiology ; Recombinant Fusion Proteins ; Tuberculosis/microbiology ; Vaccines, Attenuated ; Virulence/genetics
    Print ISSN: 0036-8075
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  • 9
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    Bat flight generates complex aerodynamic tracks (2007)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2007-05-15
    Description: The flapping flight of animals generates an aerodynamic footprint as a time-varying vortex wake in which the rate of momentum change represents the aerodynamic force. We showed that the wakes of a small bat species differ from those of birds in some important respects. In our bats, each wing generated its own vortex loop. Also, at moderate and high flight speeds, the circulation on the outer (hand) wing and the arm wing differed in sign during the upstroke, resulting in negative lift on the hand wing and positive lift on the arm wing. Our interpretations of the unsteady aerodynamic performance and function of membranous-winged, flapping flight should change modeling strategies for the study of equivalent natural and engineered flying devices.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hedenstrom, A -- Johansson, L C -- Wolf, M -- von Busse, R -- Winter, Y -- Spedding, G R -- New York, N.Y. -- Science. 2007 May 11;316(5826):894-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Theoretical Ecology, Lund University, SE-223 62 Lund, Sweden. anders.hedenstrom@teorekol.lu.se〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17495171" target="_blank"〉PubMed〈/a〉
    Keywords: Air ; Animals ; Biomechanical Phenomena ; Chiroptera/anatomy & histology/*physiology ; *Flight, Animal ; Movement ; Rheology ; Wings, Animal/anatomy & histology/*physiology
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Science-policy interface: beyond assessments (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-08-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hulme, Mike -- Mahony, Martin -- Beck, Silke -- Gorg, Christoph -- Hansjurgens, Bernd -- Hauck, Jennifer -- Nesshover, Carsten -- Paulsch, Axel -- Vandewalle, Marie -- Wittmer, Heidi -- Boschen, Stefan -- Bridgewater, Peter -- Diaw, Mariteuw Chimere -- Fabre, Pierre -- Figueroa, Aurelia -- Heong, Kong Luen -- Korn, Horst -- Leemans, Rik -- Lovbrand, Eva -- Hamid, Mohd Norowi -- Monfreda, Chad -- Pielke, Roger Jr -- Settele, Josef -- Winter, Marten -- Vadrot, Alice B M -- van den Hove, Sybille -- van der Sluijs, Jeroen P -- New York, N.Y. -- Science. 2011 Aug 5;333(6043):697-8. doi: 10.1126/science.333.6043.697.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21817033" target="_blank"〉PubMed〈/a〉
    Keywords: *Biodiversity ; *Ecosystem ; *Policy ; Policy Making
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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