Search Results - (Author, Cooperation:L. W. Enquist)

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  1. 1
    Staff View
    Publication Date:
    2012-02-02
    Publisher:
    American Association for the Advancement of Science (AAAS)
    Print ISSN:
    0036-8075
    Electronic ISSN:
    1095-9203
    Topics:
    Biology
    Chemistry and Pharmacology
    Computer Science
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Adaptation, Biological ; Advisory Committees ; Animals ; Biological Warfare Agents ; Containment of Biohazards ; Humans ; Influenza A Virus, H5N1 Subtype/*pathogenicity ; Influenza, Human/epidemiology/transmission/*virology ; National Institutes of Health (U.S.) ; Orthomyxoviridae Infections/transmission/*virology ; *Public Health ; *Publishing ; Risk Assessment ; Security Measures ; United States
    Published by:
    Latest Papers from Table of Contents or Articles in Press
  2. 2
    Staff View
    Publication Date:
    2012-02-02
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Animals ; Bioterrorism/prevention & control/*trends ; Humans ; Influenza A Virus, H5N1 Subtype/*genetics/*pathogenicity/physiology ; Influenza, Human/*transmission/*virology ; Public Health ; Risk Assessment ; Zoonoses/transmission/virology
    Published by:
    Latest Papers from Table of Contents or Articles in Press
  3. 3
    Ryan, Patrick ; Robbins, Alan ; Whealy, Mary ; Enquist, L. W.
    Springer
    Published 1993
    Staff View
    ISSN:
    1572-994X
    Keywords:
    Pseudorabies virus ; glycoprotein gIII ; herpesvirus ; signal sequence ; protein export ; hydrophobicity
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Medicine
    Notes:
    Abstract We have described three mutant strains of Pseudorabies virus that contain mutations in the signal sequence coding region of a nonessential envelope glycoprotein, gIII. The alterations disrupt, truncate, or eliminate the hydrophobic core domain of the signal sequence. Each mutant was assayed for its ability to promote the translocation of gIII across the endoplasmic reticulum membrane and the subsequent localization of the mature form of the glycoprotein to the infected cell surface or the virus envelope. Our results confirm and extend findings in other systems that the overall hydrophobicity of the signal sequence core region is a major determinant of translocation efficiency. We were unable to correlate simply the length of the core or the average hydrophobicity of core residues with export efficiency. Because our work involved the use of infectious virus mutants, we were able to identify a virus defect associated with a complete block in gIII export. This defect will facilitate a pseudoreversion analysis of gIII signal sequence function.
    Type of Medium:
    Electronic Resource
    URL:
    Articles: DFG German National Licenses