ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

Sie haben 0 gespeicherte Treffer.
Markieren Sie die Treffer und klicken Sie auf "Zur Merkliste hinzufügen", um sie in dieser Liste zu speichern.
feed icon rss

Ihre E-Mail wurde erfolgreich gesendet. Bitte prüfen Sie Ihren Maileingang.

Leider ist ein Fehler beim E-Mail-Versand aufgetreten. Bitte versuchen Sie es erneut.

Vorgang fortführen?

Exportieren
Filter
  • Artikel  (2)
  • *Gene Expression Regulation  (1)
  • Capsid/*chemistry/metabolism  (1)
  • 1990-1994  (2)
  • 1920-1924
  • Science. 252(5010): 1305-8.  (1)
  • Science. 261(5129): 1744-6.  (1)
  • 25
  • Informatik  (2)
  • Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
Sammlung
  • Artikel  (2)
Erscheinungszeitraum
Jahr
Zeitschrift
Thema
  • 1
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1991-05-31
    Beschreibung: Filamentous bacteriophage Pf1 assembles by a membrane-mediated process during which the viral DNA is secreted through the membrane while being encapsulated by the major coat protein. Neutron diffraction studies showed that in the virus most of the coat protein consists of two alpha-helical segments arranged end-to-end with an intervening mobile surface loop. Nuclear magnetic resonance studies of the coat protein in the membrane-bound form have shown that the secondary structure is essentially identical to that in the intact virus. A comparison indicates that during membrane-mediated viral assembly, while the secondary structure of the coat protein is largely conserved, its tertiary structure changes substantially.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nambudripad, R -- Stark, W -- Opella, S J -- Makowski, L -- New York, N.Y. -- Science. 1991 May 31;252(5010):1305-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, Boston University, MA 02215.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925543" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Bacteriophages/chemistry ; Capsid/*chemistry/metabolism ; *Capsid Proteins ; Cell Membrane/*metabolism ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Structure ; Neutrons ; Protein Conformation
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 2
    Publikationsdatum: 1993-09-24
    Beschreibung: Interferon-gamma (IFN-gamma) stimulates transcription of specific genes by inducing tyrosine phosphorylation of a 91-kilodalton cytoplasmic protein (termed STAT for signal transducer and activator of transcription). Stat91 was phosphorylated on a single site (Tyr701), and phosphorylation of this site was required for nuclear translocation, DNA binding, and gene activation. Stat84, a differentially spliced product of the same gene that lacks the 38 carboxyl-terminal amino acids of Stat91, did not activate transcription, although it was phosphorylated and translocated to the nucleus and bound DNA. Thus, Stat91 mediates activation of transcription in response to IFN-gamma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shuai, K -- Stark, G R -- Kerr, I M -- Darnell, J E Jr -- AI32489-02/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 24;261(5129):1744-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rockefeller University, Laboratory of Molecular Cell Biology, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7690989" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Cell Line ; Cell Nucleus/metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; *Gene Expression Regulation ; Humans ; Interferon-gamma/*pharmacology ; Molecular Sequence Data ; Peptide Fragments/chemistry/metabolism ; Phosphotyrosine ; *Signal Transduction ; Transcription Factors/chemistry/*metabolism ; Transcriptional Activation ; Transfection ; Tyrosine/analogs & derivatives/chemistry
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
Schließen ⊗
Diese Webseite nutzt Cookies und das Analyse-Tool Matomo. Weitere Informationen finden Sie hier...