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  • 2000-2004  (2)
  • 1970-1974  (2)
  • 1925-1929
  • Analytical Chemistry and Spectroscopy  (1)
  • Biochemistry and Biotechnology  (1)
  • DNA Methylation  (1)
  • G2/M arrest  (1)
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Material
Years
  • 2000-2004  (2)
  • 1970-1974  (2)
  • 1925-1929
  • 1980-1984  (3)
Year
Keywords
  • 1
    Electronic Resource
    Electronic Resource
    Activation of MAD 2 checkprotein and persistence of cyclin B1/CDC 2 activity associate with paclitaxel-induced apoptosis in human nasopharyngeal carcinoma cells (2000)
    Springer
    Apoptosis 5 (2000), S. 235-241 
    Details
    ISSN: 1573-675X
    Keywords: apoptosis ; cyclin B1/CDC 2 ; G2/M arrest ; MAD 2 ; paclitaxel
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Paclitaxel (Taxol™) is a microtubule-interfering agent that induced persistent and transient G2/M arrest before apoptosis in human nasopharyngeal carcinoma (NPC) cells at high and low concentrations, respectively. In this study, we intended to explore the underlying molecular events and found that cellular cyclin B1/CDC 2 kinase activity was increased and persisted for 〉6 h upon paclitaxel treatment both at high and low concentrations. Furthermore, activation of MAD 2 checkprotein could account for the loss of cyclin B1 ubiquitination and the persistence of cyclin B1/CDC 2 activation in the cases. To investigate the involvement of cyclin B1 and MAD 2 activation in paclitaxel-induced apoptosis, we introduced affinity-purified anti-cyclin B1 and MAD 2 antibodies into NPC cells by electroporation before the further paclitaxel treatment. The antibodies against cyclin B1 and MAD 2 indeed attenuated paclitaxel-induced cytotoxicity and DNA fragmentation. Our study suggests that activation of cyclin B1/CDC 2 and MAD 2 were the M-phase events required for paclitaxel-induced apoptosis in NPC cells. The dys-regulated cyclin B1/CDC 2 activation could enhance the prometaphase progression, but activation of MAD 2 rendered cells inable to exit from the metaphase. Under this circumstance, cells were probably going to “mitotic catastrophe” and ultimately, destined to apoptosis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009652412399
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Inactivation of p16INK4a in Primary Tumors and Cell Lines of Head and Neck Squamous Cell Carcinoma (2000)
    Springer
    Molecules and cells 10 (2000), S. 557-565 
    Details
    ISSN: 0219-1032
    Keywords: DNA Methylation ; Head and Neck Squamous Cell Carcinoma ; p16INK4a
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Inactivation of the p16INK4a gene by mutation and deletion is common in head and neck squamous cell carcinoma (HNSCC). The present study demonstrates that hypermethylation of the 5′ CpG islands can serve as an alternative mechanism for the inactivation of the p16INK4a gene in this tumor. We studied 11 HNSCC cell lines and 17 oral squamous cell carcinoma (OSCC) primary tumors for p16INK4a gene status by protein/mRNA and DNA genetic/epigenetic analyses to determine the incidence of its inactivation. Our study indicates that: (1) inactivation of p16 protein is frequent in HNSCC cell lines (6/11, 54.5%) and OSCC primary tumors (15/17, 88.2%), (2) inactivation of p16INK4a protein is commonly associated with the presence of gene alteration such as mutation, homozygous deletion and especially aberrant methylation, and (3) genomic sequencing of bisulfite-modified DNA shows that the carcinoma develops a heterogeneous pattern of hypermethylation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s10059-000-0557-8
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Effectiveness factor calculations for immobilized enzyme catalysts (1973)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 15 (1973), S. 879-888 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The steady state, nonlinear diffusion equations which describe reactions in constrained enzyme solutions are of great interest in many biological and engineering applications. As in other types of nonlinear differential equations, exact analytical solutions do not exist except in some simplified cases. In this paper, a general procedure is presented for solving numerically for the substrate concentration profile and effectiveness factor utilizing the transformation method suggested by Na and Na. Design correlations for enzyme solutions constrained within spherical membranes are included. The use of a unique definition of the Thiele Modulus in these charts permits the clear illustration of the effects of substrate concentration and external mass transfer resistances on the overall effectiveness factor for the catalyst particle.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260150505
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Identification of an atypical constitutent of a clandestine opiate (1974)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 1 (1974), S. 350-351 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: An unusual morphine analog was extracted and separated from an opium-like sample. The high resolution mass spectrum of the unknown substance confirmed the empirical formula as C17H18O2NCl. Mass spectra and retention factor values in thin-layer chromatography of both unknown and authentic standards were compared, which lead to the identification of the unknown as β-chloromorphide.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200010511
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    Paper (German National Licenses)
    Fulltext
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