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  • 1
    Electronic Resource
    Electronic Resource
    Purification and characterization of primer recognition proteins from HeLa cells (1990)
    s.l. : American Chemical Society
    Biochemistry 29 (1990), S. 4767-4773 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00472a004
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  • 2
    Electronic Resource
    Electronic Resource
    Single-stranded DNA-dependent ATPase from HeLa cells that stimulates DNA polymerase .alpha.-primase activity: purification and characterization of the ATPase (1990)
    s.l. : American Chemical Society
    Biochemistry 29 (1990), S. 8753-8759 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00489a036
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of the HeLa Cell DNA Polymerase .alpha.-Associated Ap4A Binding Protein by Photoaffinity Labeling (1994)
    s.l. : American Chemical Society
    Biochemistry 33 (1994), S. 14601-14607 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00252a028
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  • 4
    Electronic Resource
    Electronic Resource
    Uracil DNA-glycosylase/glyceraldehyde-3-phosphate dehydrogenase is an Ap4A binding protein (1995)
    s.l. : American Chemical Society
    Biochemistry 34 (1995), S. 9700-9707 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00030a007
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  • 5
    Electronic Resource
    Electronic Resource
    Diadenosine tetraphosphate binding protein from human HeLa cells: purification and characterization (1992)
    s.l. : American Chemical Society
    Biochemistry 31 (1992), S. 1631-1635 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00121a007
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  • 6
    Electronic Resource
    Electronic Resource
    Role of nitric oxide in the induction of apoptosis by smokeless tobacco extract (1999)
    Springer
    Molecular and cellular biochemistry 200 (1999), S. 51-57 
    Details
    ISSN: 1573-4919
    Keywords: smokeless tobacco ; apoptosis ; nitric oxide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Smokeless tobacco usage is, a growing public health concern in the United States. Lesions of the oral cavity have been clearly linked to smokeless tobacco use. The objective of this study was to determine the biochemical effects of smokeless tobacco extract (STE) exposure upon hamster cheek pouch cell (HCPC-1) cultures. HCPC-1 cells were exposed to a 5 -fold dose-range of STE (0.5, 1.0 and 2.5%) over a time-course of 24-96 h. Following each exposure we measured various biochemical parameters of cell proliferation and cell death. Cell viability, cell cycle progression and S-phase DNA synthesis were measured as markers of cell proliferation. We measured lactate dehydrogenase leakage as a marker of cell membrane damage and cell death due to necrosis. No significant alterations were observed in cell cycle progression and cell proliferation as a result of exposure to STE. LDH measured colorimetrically indicated no significant effect with the lower doses (0.5, 1.0 and 2.5% STE). Apoptosis measured as the A0 peak and by the TUNEL procedure revealed that STE caused significant rates of apoptosis. Maximal apoptosis was noted between 48-96 h. In order to probe the mechanism further we measured the levels of nitrites as an indicator of nitric oxide (NO) in the media. NO levels were significantly elevated at the doses that caused an induction of apoptosis. The results from this study indicate that STE causes a dose-dependent induction of apoptosis and that this is mediated by nitric oxide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006985700851
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  • 7
    Electronic Resource
    Electronic Resource
    Expression of 72 kDa and 92 kDa type IV collagenases from human giant-cell tumor of bone (1995)
    Springer
    Clinical & experimental metastasis 13 (1995), S. 420-426 
    Details
    ISSN: 1573-7276
    Keywords: invasion ; metalloproteinases ; metastasis ; tissue inhibitors of metalloproteinases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Basement membrane forms widespread barriers to tumor invasion. It has been shown that tumor-secreted, basement membrane-degrading enzymes, namely metalloproteinases (MMPs) play an important role in tumor invasion and metastasis. In this study, we determined the enzymatic activity, content, and mRNA of both the 72 kDa (MMP-2) and 92 kDa (MMP-9) MMPs in primary cultures of human giant-cell tumor of bone (GCT)in vitro and in tissue extracts (in vivo). Gelatin zymography showed the presence of lytic bands at Mr 121000, 92000, and 72000, and these enzymatic activities were inhibited by EDTA, an inhibitor of MMPs. Western blots with antibodies specific for MMP-2 and MMP-9 confirmed the presence of MMP-2 and MMP-9 bothin vitro andin vivo, but GCT cells at late passage showed only MMP-2. Northern blots using labeled cDNA probes specific for these molecules revealed the presence of 3.1 kb transcript for MMP-2 and a 2.9 kb transcript for MMP-9. Using specific antibodies to 72 kDa and 92 kDa type IV collagenases, we studied their cellular distribution by immunohistochemical means. Stronger immunoreactivity was found for 92 kDa type IV collagenase than 72 kDa type IV collagenase in the giant cells. It appears, therefore, that MMP-9 may play an important role in the malignant behavior of GCTs and suggests a potential therapeutic role for protease inhibitors in attempting to minimize the invasive behavior of GCTs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00118181
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  • 8
    Electronic Resource
    Electronic Resource
    Characterization of the HeLa cell single-stranded DNA-dependent ATPase/DNA helicase II (1995)
    Springer
    Molecular and cellular biochemistry 146 (1995), S. 121-126 
    Details
    ISSN: 1573-4919
    Keywords: Ku antigen ; ssDNA-dependent ATPase ; DNA helicase II ; DNA repair ; DNA replication
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract A single-stranded DNA-dependent ATPase activity, consisting of two subunits of 83 kDa (p90) and 68 kDa (p70), was previously purified from HeLa cells (Vishwanatha, J.K. and Baril, E.F. (1990) Biochem 29, 8753–8759). Homology of the two subunits of single-stranded DNA-dependent ATPase with the human Ku protein (Caoet al. (1994) Biochem 33, 8548–8557) and identity of the Ku protein as the human DNA helicase II (Tutejaet al. (1994) EMBO J. 13, 4991–5001) have been reported recently. Using antisera raised against the subunits of the HDH II, we confirm that the Hela single-stranded DNA-dependent ATPase is the HDH II. Similar to the activity reported for Ku protein, ssDNA-dependent ATPase binds to double-stranded DNA and the DNA-protein complex detected by gel mobility shift assay consists of both the ATPase subunits. The p90 subunit is predominantly nuclear and is easily dissociated from chromatin. The p70 is distributed in cytosol and nucleus, and a fraction of the nuclear p70 protein is found to be associated with the nuclear matrix. Both the p90 and p70 subunits of the ATPase are present in G1 and S phase of the cell cycle and are rapidly degraded in the G2/M phase of the cell cycle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00944604
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  • 9
    Electronic Resource
    Electronic Resource
    Specific down-regulation of annexin II expression in human cells interferes with cell proliferation (1999)
    Springer
    Molecular and cellular biochemistry 199 (1999), S. 139-147 
    Details
    ISSN: 1573-4919
    Keywords: annexin II ; DNA synthesis ; antisense ; Simian Virus 40 ; cell proliferation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The protein-tyrosine kinase substrate annexin II is a growth regulated gene whose expression is increased in several human cancers. While the precise function of this protein is not understood, annexin II is proposed to be involved in multiple physiological activities, including DNA synthesis and cell proliferation. Targeted disruption of the annexin II gene affects calcium signaling, tyrosine phosphorylation and apoptosis, indicating the important physiological role of this protein. We used a transient co-transfection assay to regulate annexin II expression in human HeLa, 293 and 293T cells, and measured the effects of annexin II down regulation on DNA synthesis and proliferation. Transfection of cells with an antisense annexin II vector results in inhibition of cell division and proliferation, with concomitant reduction in annexin II message and protein levels. Cellular DNA synthesis is significantly reduced in antisense transfected cells. Replication extracts made from antisense transfected cells have significantly reduced efficiency to support SV40 in vitro DNA replication, while the extracts made from sense transfected cells are fully capable of replication. Our results indicate an important role of annexin II in cellular DNA synthesis and cell proliferation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006942128672
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  • 10
    Electronic Resource
    Electronic Resource
    Effect of regulated expression of the fragile histidine traid gene on cell cycle and proliferation (2000)
    Springer
    Molecular and cellular biochemistry 204 (2000), S. 83-88 
    Details
    ISSN: 1573-4919
    Keywords: FHIT ; cell cycle ; ecdysone ; tumor suppressor ; apoptosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The mechanism of tumor suppressor action of the fragile histidine triad (FHIT) gene is unknown. Disruption of cell cycle regulation leads to the tumor formation and many tumor suppressor genes suppress tumorigenesis through their effect on cell cycle regulation. We examined the expression of FHIT during the cell cycle, and determined whether overexpression of FHIT affects cell cycle kinetics and apoptosis. The FHIT cDNA was cloned into the ecdysone-inducible expression vector in both the sense and antisense orientations. Overexpression of the sense or antisense construct did not affect cell proliferation, cell cycle distribution or apoptosis in human 293T cells. Analysis of the FHIT expression in 293T cells collected at various cell cycle phases showed that the expression of FHIT is not under cell cycle regulation. These results indicate that the tumor suppressor activity of the FHIT gene may be independent of an effect on the cell cycle and apoptosis mechanisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007068823848
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