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  • Molecular Sequence Data  (3)
  • 2010-2014  (1)
  • 2000-2004  (2)
  • 1965-1969
  • 1
    Publication Date: 2002-05-11
    Description: The majority (〉99%) of microorganisms from the environment resist cultivation in the laboratory. Ribosomal RNA analysis suggests that uncultivated organisms are found in nearly every prokaryotic group, and several divisions have no known cultivable representatives. We designed a diffusion chamber that allowed the growth of previously uncultivated microorganisms in a simulated natural environment. Colonies of representative marine organisms were isolated in pure culture. These isolates did not grow on artificial media alone but formed colonies in the presence of other microorganisms. This observation may help explain the nature of microbial uncultivability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaeberlein, T -- Lewis, K -- Epstein, S S -- New York, N.Y. -- Science. 2002 May 10;296(5570):1127-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biology Department, Northeastern University, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004133" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria/classification/cytology/*growth & development/*isolation & purification ; *Bacteriological Techniques ; Colony Count, Microbial ; Culture Media ; DNA, Bacterial/analysis/genetics ; DNA, Ribosomal/analysis/genetics ; Diffusion Chambers, Culture ; Geologic Sediments/*microbiology ; Molecular Sequence Data ; RNA, Ribosomal, 16S/genetics ; *Seawater ; Silicon Dioxide
    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
    Publication Date: 2002-01-26
    Description: The organization of myosin into motile cellular structures requires precise temporal and spatial regulation. Proteins containing a UCS (UNC-45/CRO1/She4p) domain are necessary for the incorporation of myosin into the contractile ring during cytokinesis and into thick filaments during muscle development. We report that the carboxyl-terminal regions of UNC-45 bound and exerted chaperone activity on the myosin head. The amino-terminal tetratricopeptide repeat domain of UNC-45 bound the molecular chaperone Hsp90. Thus, UNC-45 functions both as a molecular chaperone and as an Hsp90 co-chaperone for myosin, which can explain previous findings of altered assembly and decreased accumulation of myosin in UNC-45 mutants of Caenorhabditis elegans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barral, Jose M -- Hutagalung, Alex H -- Brinker, Achim -- Hartl, F Ulrich -- Epstein, Henry F -- New York, N.Y. -- Science. 2002 Jan 25;295(5555):669-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11809970" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Binding Sites ; Caenorhabditis elegans/genetics/*metabolism ; Caenorhabditis elegans Proteins/chemistry/genetics/*metabolism ; Cell Line ; Cloning, Molecular ; HSP70 Heat-Shock Proteins/genetics/metabolism ; HSP90 Heat-Shock Proteins/genetics/metabolism ; Molecular Chaperones/chemistry/genetics/*metabolism ; Molecular Sequence Data ; Myosins/*metabolism ; Peptide Fragments/metabolism ; Protein Binding ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry/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
    Publication Date: 2013-11-01
    Description: The 2002-3 pandemic caused by severe acute respiratory syndrome coronavirus (SARS-CoV) was one of the most significant public health events in recent history. An ongoing outbreak of Middle East respiratory syndrome coronavirus suggests that this group of viruses remains a key threat and that their distribution is wider than previously recognized. Although bats have been suggested to be the natural reservoirs of both viruses, attempts to isolate the progenitor virus of SARS-CoV from bats have been unsuccessful. Diverse SARS-like coronaviruses (SL-CoVs) have now been reported from bats in China, Europe and Africa, but none is considered a direct progenitor of SARS-CoV because of their phylogenetic disparity from this virus and the inability of their spike proteins to use the SARS-CoV cellular receptor molecule, the human angiotensin converting enzyme II (ACE2). Here we report whole-genome sequences of two novel bat coronaviruses from Chinese horseshoe bats (family: Rhinolophidae) in Yunnan, China: RsSHC014 and Rs3367. These viruses are far more closely related to SARS-CoV than any previously identified bat coronaviruses, particularly in the receptor binding domain of the spike protein. Most importantly, we report the first recorded isolation of a live SL-CoV (bat SL-CoV-WIV1) from bat faecal samples in Vero E6 cells, which has typical coronavirus morphology, 99.9% sequence identity to Rs3367 and uses ACE2 from humans, civets and Chinese horseshoe bats for cell entry. Preliminary in vitro testing indicates that WIV1 also has a broad species tropism. Our results provide the strongest evidence to date that Chinese horseshoe bats are natural reservoirs of SARS-CoV, and that intermediate hosts may not be necessary for direct human infection by some bat SL-CoVs. They also highlight the importance of pathogen-discovery programs targeting high-risk wildlife groups in emerging disease hotspots as a strategy for pandemic preparedness.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ge, Xing-Yi -- Li, Jia-Lu -- Yang, Xing-Lou -- Chmura, Aleksei A -- Zhu, Guangjian -- Epstein, Jonathan H -- Mazet, Jonna K -- Hu, Ben -- Zhang, Wei -- Peng, Cheng -- Zhang, Yu-Ji -- Luo, Chu-Ming -- Tan, Bing -- Wang, Ning -- Zhu, Yan -- Crameri, Gary -- Zhang, Shu-Yi -- Wang, Lin-Fa -- Daszak, Peter -- Shi, Zheng-Li -- R01AI079231/AI/NIAID NIH HHS/ -- R01TW005869/TW/FIC NIH HHS/ -- R56TW009502/TW/FIC NIH HHS/ -- England -- Nature. 2013 Nov 28;503(7477):535-8. doi: 10.1038/nature12711. Epub 2013 Oct 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Center for Emerging Infectious Diseases, State Key Laboratory of Virology, Wuhan Institute of Virology of the Chinese Academy of Sciences, Wuhan 430071, China [2].〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24172901" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cercopithecus aethiops ; China ; Chiroptera/*virology ; Disease Reservoirs/virology ; Feces/virology ; Fluorescent Antibody Technique ; Genome, Viral/genetics ; Host Specificity ; Humans ; Molecular Sequence Data ; Pandemics/prevention & control/veterinary ; Peptidyl-Dipeptidase A/genetics/*metabolism ; Real-Time Polymerase Chain Reaction ; Receptors, Virus/genetics/metabolism ; SARS Virus/genetics/*isolation & purification/*metabolism/ultrastructure ; Severe Acute Respiratory Syndrome/prevention & ; control/transmission/veterinary/virology ; Species Specificity ; Spike Glycoprotein, Coronavirus/chemistry/metabolism ; Vero Cells ; Virion/isolation & purification/ultrastructure ; Virus Internalization ; Viverridae/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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