GLORIA

GEOMAR Library Ocean Research Information Access

X

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
  • American Society for Microbiology  (6)
Materialart
Verlag/Herausgeber
  • American Society for Microbiology  (6)
Person/Organisation
Sprache
Erscheinungszeitraum
FID
Fachgebiete(RVK)
  • 1
    Online-Ressource
    Online-Ressource
    Identification of B-lymphotropic papovavirus-coded proteins
    American Society for Microbiology ; 1983
    In:  Journal of Virology Vol. 45, No. 2 ( 1983-02), p. 872-875
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 45, No. 2 ( 1983-02), p. 872-875
    Kurzfassung: The lymphotropic papovavirus (LPV)-specific mRNAs were translated in vitro in rabbit reticulocyte lysates. The specific products were 84,000-dalton (84K), 41K, 35K, and 26K proteins. Immunoprecipitation with anti-LPV hamster sera and analysis of partially purified LPV virions showed that the last three proteins were the LPV capsid proteins, and we designated the 41K, 35K, and 26K proteins VP1 (major capsid protein), VP2, and VP3, respectively. Several characteristics, such as the small amount of mRNA for the 84K protein at late stages of infection, its absence from partially purified virus preparations, no common tryptic peptides between the 84K and 41K proteins, and the pattern of in vivo phosphorylation, suggest that the 84K protein is not a simple dimer of the 41K protein. Normal human sera and sera from certain leukemic patients positive for antibody to LPV viral antigens immunoprecipitated the 41K protein.
    Materialart: Online-Ressource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/jvi.45.2.872-875.1983
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 1983
    ZDB Id: 1495529-5
    Standort Signatur Einschränkungen Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    Online-Ressource
  • 2
    Online-Ressource
    Online-Ressource
    Phosphorylation of chromatin- and ribosome-associated proteins in cells transformed by adenovirus, murine sarcoma virus, and methylcholanthrene
    American Society for Microbiology ; 1978
    In:  Journal of Virology Vol. 27, No. 3 ( 1978-09), p. 800-808
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 27, No. 3 ( 1978-09), p. 800-808
    Kurzfassung: Endogenous protein phosphorylation in chromatin and ribosomes of monkey, mouse, and rat cells transformed by DNA, RNA tumor viruses, and a chemical carcinogen revealed the association of a protein of approximately 90,000 daltons (90K), which is highly phosphorylated in vitro. Peptide map analysis showed that the 90K proteins associated with these organelles of various transformed cells are similar irrespective of the species of cells and transforming agents. This species of protein could not be detected, or was scarcely detected, by phosphorylation in chromatin and ribosomes of untransformed cells and in revertants of transformed cells. These results suggest that the alteration in the pattern of endogenous protein phosphorylation in these organelles is closely related to the transformed state of cells.
    Materialart: Online-Ressource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/jvi.27.3.800-808.1978
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 1978
    ZDB Id: 1495529-5
    Standort Signatur Einschränkungen Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    Online-Ressource
  • 3
    Online-Ressource
    Online-Ressource
    In vivo evaluation of NM441, a new thiazeto-quinoline derivative
    American Society for Microbiology ; 1991
    In:  Antimicrobial Agents and Chemotherapy Vol. 35, No. 12 ( 1991-12), p. 2496-2499
    Details
    In: Antimicrobial Agents and Chemotherapy, American Society for Microbiology, Vol. 35, No. 12 ( 1991-12), p. 2496-2499
    Kurzfassung: NM441 is a lipophilic prodrug of a new thiazeto-quinoline carboxylic acid derivative NM394, and when it is administered orally it is readily absorbed and hydrolyzed to its parent compound. After oral administration of NM441 at a dose of 20 mg/kg to dogs, the peak concentration of NM394 in plasma was 2.39 micrograms/ml, whereas it was 0.63 micrograms/ml for NM394 administered alone. The in vivo activity of NM441 was compared with those of ciprofloxacin, ofloxacin, and enoxacin in mouse protection studies. NM441 was as effective as ofloxacin and was twice as effective as ciprofloxacin against systemic infection with Staphylococcus aureus. Against infections with streptococci, NM441 was two to three times as effective as ofloxacin and five times as effective as ciprofloxacin. Against infection with Escherichia coli, NM441 was as effective as ciprofloxacin and ofloxacin, but against infections with Klebsiella pneumoniae, Serratia marcescens, and Pseudomonas aeruginosa, NM441 was two to four times as effective as ciprofloxacin and ofloxacin. NM441 was three to seven times as effective as enoxacin in systemic infections. Against urinary tract infections with E. coli, NM441 reduced the number of bacterial CFU per gram of kidney by 1 to 2 log10 more and, with P. aeruginosa, by 1 to 6 log10 more than did ciprofloxacin and ofloxacin. Against respiratory tract infections with K. pneumoniae, NM441 was as effective as ofloxacin and was twice as effective as ciprofloxacin.
    Materialart: Online-Ressource
    ISSN: 0066-4804 , 1098-6596
    URL: Article
    DOI: 10.1128/AAC.35.12.2496
    RVK:
    XA 24552
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 1991
    ZDB Id: 1496156-8
    SSG: 12
    SSG: 15,3
    Standort Signatur Einschränkungen Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    Online-Ressource
  • 4
    Online-Ressource
    Online-Ressource
    Development of enzyme-labeled oligonucleotide probe for detection of mecA gene in methicillin-resistant Staphylococcus aureus
    American Society for Microbiology ; 1994
    In:  Journal of Clinical Microbiology Vol. 32, No. 8 ( 1994-08), p. 1866-1869
    Details
    In: Journal of Clinical Microbiology, American Society for Microbiology, Vol. 32, No. 8 ( 1994-08), p. 1866-1869
    Kurzfassung: A DNA hybridization method with an enzyme-labeled oligonucleotide probe (mecA-ELONP) was developed to detect the methicillin-resistant gene (mecA) in methicillin-resistant Staphylococcus aureus. For rapid identification, bacterial colonies were transferred from agar plates directly onto nylon membranes. Lysis of cells, denaturation of DNA, and hybridization were performed on the membranes. These procedures required only 3 h for completion. The results obtained by this test closely corresponded with those obtained by determining the MICs of oxacillin against S. aureus. The results of the mecA-ELONP also correlated well with those of a commercially available PCR test. Thus, mecA-ELONP proved to be a reliable and convenient method for the rapid identification of methicillin-resistant S. aureus, which could be useful in clinical microbiology laboratories.
    Materialart: Online-Ressource
    ISSN: 0095-1137 , 1098-660X
    URL: Article
    DOI: 10.1128/jcm.32.8.1866-1869.1994
    RVK:
    XA 10000
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 1994
    ZDB Id: 1498353-9
    SSG: 12
    Standort Signatur Einschränkungen Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    Online-Ressource
  • 5
    Online-Ressource
    Online-Ressource
    Characterization of N-type and dually permissive cells segregated from mouse fibroblasts whose Fv-1 phenotype could be modified by another independently segregating gene(s)
    American Society for Microbiology ; 1982
    In:  Journal of Virology Vol. 41, No. 1 ( 1982-01), p. 145-152
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 41, No. 1 ( 1982-01), p. 145-152
    Kurzfassung: Though the inbred DDD mouse strain is essentially of the N type, the primary culture of this strain was about 100-fold more sensitive to B-tropic WN1802B virus than were the typical N-type strains (C3H/He, C57L, etc.). After cloning, DDD mouse cells segregated two types of cells, typical N-type cells and cells lacking in Fv-1 restriction. As both types of cells so far tested retained glucose-6-phosphatase-1 coded by a locus closely linked to Fv-1 and genetic cross experiments indicated the presence of a gene(s) modifying the Fv-1 phenotype, variation in Fv-1 restriction could presumably be brought about by genetic changes in a gene(s) other than Fv-1 itself. N-type and dually permissive cell clones were similarly established from the inbred G mouse. Compositions of polypeptides labeled with [35S]methionine in the N-type and dually permissive cells of DDD and G mouse origins were compared by two-dimensional gel electrophoresis. The polypeptide maps of these cells were similar except for a few spots. Among these dissimilar spots, a spot of about 20,000 daltons with a pI of about 5.5 was always present in N-type cells, whereas it was absent in dually permissive cells. In DDD mouse-derived clones, a proportional relation was observed between the intensity of the spot and the restriction to the B-tropic virus.
    Materialart: Online-Ressource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/jvi.41.1.145-152.1982
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 1982
    ZDB Id: 1495529-5
    Standort Signatur Einschränkungen Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    Online-Ressource
  • 6
    Online-Ressource
    Online-Ressource
    Antibodies against a nonapeptide of polyomavirus middle T antigen: cross-reaction with a cellular protein(s)
    American Society for Microbiology ; 1983
    In:  Journal of Virology Vol. 48, No. 3 ( 1983-12), p. 709-720
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 48, No. 3 ( 1983-12), p. 709-720
    Kurzfassung: Antibodies were raised against the sequence Glu-Glu-Glu-Glu-Tyr-Met-Pro-Met -Glu, which represents a part of the middle T antigen of polyomavirus that is considered to be important in inducing the phenotype of transformed cells. The antibodies reacted with native as well as denatured middle T antigens. In addition, the antibodies immunoprecipitated a cellular protein with an apparent molecular weight of 130,000 (130K) from mouse and rat cells. In some cases, a 33K protein was also immunoprecipitated. Immunoprecipitation of middle T antigen as well as 130K and 33K proteins was blocked by the peptide. The antibodies labeled microfilaments of untransformed mouse, rat, human, and chicken cells by immunofluorescence. This labeling was also blocked by the peptide. The labeling pattern and distribution under a variety of conditions were indistinguishable from those of anti-actin antibodies, although no evidence has been obtained to indicate that the anti-peptide antibodies react with actin. The 130K protein migrated in sodium dodecyl sulfate-polyacrylamide gel electrophoresis slightly slower than chicken gizzard vinculin (130K) and slightly faster than myosin light-chain kinase of chicken smooth muscle (130K). Neither of these proteins absorbed the anti-peptide antibodies. The 33K protein does not seem to be tropomyosin (32K to 40K).
    Materialart: Online-Ressource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/jvi.48.3.709-720.1983
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 1983
    ZDB Id: 1495529-5
    Standort Signatur Einschränkungen Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    Online-Ressource
Schließen ⊗
Diese Webseite nutzt Cookies und das Analyse-Tool Matomo. Weitere Informationen finden Sie hier...