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  • 1
    Electronic Resource
    Electronic Resource
    Magnitude and significance of NAD turnover in human cell line D98/AH2 (1976)
    [s.l.] : Nature Publishing Group
    Nature 259 (1976), S. 695-696 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] What is the magnitude in vivo of the reactions which consume NAD? We present here data for D98/AH2, a human cell line derived from HeLa9 which answers this question and which makes possible calculation of the fraction of NAD biosynthesis that compensates for breakdown and the fraction that expands ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/259695a0
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  • 2
    Electronic Resource
    Electronic Resource
    Structure of the proteasome activator REGα (PA28α) (1997)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 390 (1997), S. 639-643 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The specificity of the 20S proteasome, which degrades many intracellular proteins, is regulated by protein complexes that bind to one or both ends of the cylindrical proteasome structure. One of these regulatory complexes, the 11S regulator (known as REG or PA28), stimulates proteasome ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/37670
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  • 3
    Electronic Resource
    Electronic Resource
    Identification of the long ubiquitin extension as ribosomal protein S27a (1989)
    [s.l.] : Nature Publishing Group
    Nature 338 (1989), S. 438-440 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Native CEP80 binds to DEAE resins unless pretreated with RNase and sediments at 100,000g (K.R., unpublished results). Analysis of a rabbit reticulocyte participate preparation on sucrose gradients showed that CEP80 was present in fractions containing SOS monosomes and polysomes (Fig. la). ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/338438a0
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  • 4
    Electronic Resource
    Electronic Resource
    Subunits of the regulatory complex of the 26S protease (1995)
    Springer
    Molecular biology reports 21 (1995), S. 27-34 
    Details
    ISSN: 1573-4978
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00990967
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  • 5
    Electronic Resource
    Electronic Resource
    Effects of nucleotides on assembly of the 26S proteasome and degradation of ubiquitin conjugates (1997)
    Springer
    Molecular biology reports 24 (1997), S. 13-16 
    Details
    ISSN: 1573-4978
    Keywords: 26S proteasome ; regulatory complex ; nucleotide hydrolysis ; ubiquitin-conjugate degradation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have investigated three aspects of nucleotide usage by the 26S proteasome and its regulatory complex (RC). Both particles hydrolyze the four major ribonucleotides, but ATP and CTP have substantially lower K _s for hydrolysis than do GTP and UTP. The K _ for ATP hydrolysis is 15 μm for the 26S proteasome and 30 μm for the regulatory complex. Formation of the 26S proteasome from the RC and the 20S proteasome requires about 5 μm ATP. Although measurable degradation of Ubiquitin(Ub)-lysozyme conjugates occurs in the presence of CTP, GTP, and UTP, the best nucleotide for Ub-conjugate degradation by the 26S proteasome is ATP, with an estimated K _ of 12 μm. In summary, our studies show that micromolar concentrations of ATP are sufficient for several 26S proteasome activities.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006892220996
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  • 6
    Electronic Resource
    Electronic Resource
    Assembly of the regulatory complex of the 26S proteasome (1999)
    Springer
    Molecular biology reports 26 (1999), S. 15-19 
    Details
    ISSN: 1573-4978
    Keywords: ATPase ; protein degradation ; regulatory complex ; 26S proteasome ; ubiquitin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The 19S regulatory complex (RC) of 26S proteasomes is a 900–1000 kDa particle composed of 18 distinct subunits (S1–S15) ranging in molecular mass from 25 to 110 kDa. This particle confers ATP-dependence and polyubiquitin (polyUb) recognition to the 26S proteasome. The symmetry and homogenous structure of the proteasome contrasts sharply with the remarkable complexity of the RC. Despite the fact that the primary sequences of all the subunits are now known, insight has been gained into the function of only eight subunits. The six ATPases within the RC constitute a subfamily (S4-like ATPases) within the AAA superfamily and we have shown that they form specific pairs in vitro[1]. We have now determined that putative coiled-coils within the variable N-terminal regions of these proteins are likely to function as recognition elements that direct the proper placement of the ATPases within the RC. We have also begun mapping putative interactions between non-ATPase subunits and S4-like ATPases. These studies have allowed us to build a model for the specific arrangement of 9 subunits within the human regulatory complex. This model agrees with recent findings by Glickman et al. [2] who have reported that two subcomplexes, termed the base and the lid, form the RC of budding yeast 26S proteasomes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006957802028
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  • 7
    Electronic Resource
    Electronic Resource
    Kinetics of human chromosome loss from 3T3-human hybrid cells (1978)
    Springer
    Somatic cell and molecular genetics 4 (1978), S. 661-676 
    Details
    ISSN: 1572-9931
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Human chromosomes were lost from populations of 3T3-HeLa and 3T3-diploid human fibroblast (HF) hybrids with similar firstorder kinetics. Whereas loss began immediately in 3T3-HF hybrids, there was a lag of 5–10 cell divisions before chromosome loss began in 3T3-HeLa hybrids. Human chromosome loss was not affected by aminopterin selection, the use of polyethylene glycol rather than Sendai virus as fusagen, or by the presence of one or two 3T3 genomes. However, when cell division was retarded by growing 3T3-HF hybrids in low serum or at low temperatures, fewer human chromosomes were lost. This suggests that cell cycle traverse is important in chromosome loss. The distribution of human chromosomes among hybrid metaphases indicated that gradual chromosome loss occurred in all hybrids rather than extensive loss from a portion of the hybrids. During the period of chromosome loss, increased numbers of individual asynchronously condensed human chromosomes were randomly distributed among hybrid metaphases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01543157
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  • 8
    Electronic Resource
    Electronic Resource
    The distribution of pyridine nucleotides between nucleus and cytoplasm (1974)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 84 (1974), S. 481-485 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Following enucleation of a portion of human culture cells containing 3H-pyridine nucleotides, autoradiography revealed no difference in the grain density over enucleated and whole cells. These results provide evidence that the concentration of pydine nucleotides does not differ by more than threefold between nucleus and cytoplasm and probably does not vary at all.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1040840316
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  • 9
    Electronic Resource
    Electronic Resource
    Studies on the intranuclear distribution of human and mouse genomes and formation of human-mouse hybrid cells (1976)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 88 (1976), S. 167-179 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Autoradiographic examination of early hybrid cells formed by the fusion of 3H-thymidine labeled D98/AH2 cells and 3T3-4E cells revealed that human and mouse chromosomes are often separated within metaphase and interphase nuclei. Although the marked separation of human and mouse chromosomes progressively disappeared with succeeding cell division, the occurrence of sectored nuclei in 16-cell hybrid colonies and the labeling pattern of human chromosomes within separated metaphases indicate that separation of human and mouse chromosomes may persist through several mitoses.Fusion of 3H-thymidine labeled D98/AH2 cells and 3T3-4E cells was coupled with aminopterin selection to study other aspects of hybrid cell formation. Hybrid cells arose from heterokaryons by cell division. Nuclear fusion may have occurred in two out of several thousand heterokaryons examined. However, these could reflect the close apposition of adjacent nuclei. A large fraction (〉 0.5) of D98/3T3 heterokaryons underwent at least one cell division. However, the number of hybrid colonies containing more than eight cells at ten days following fusion was about 0.03 of the total number of heterokaryons. Many hybrid colonies arrested growth before the 8-cell stage, and the cells in such colonies exhibited nuclear abnormalities.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1040880206
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  • 10
    Electronic Resource
    Electronic Resource
    Degradation of proteins microinjected into cultured mammalian cells (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 100 (1979), S. 175-185 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Iodinated proteins were degraded after injection into HeLa cells at first-order rates with half-lives varying from three hours for the trout nonhistone chromosomal protein, HMG-T, to 60 hours for whale myoglobin. Fluoresceinated-bovine serum albumin (fl-BSA) was degraded almost twice as fast as unmodified BSA. The rate of degradation of 125I-BSA was very similar in eight cell lines of mouse, human, monkey and rat origin. Microinjected proteins were analyzed on SDS-acrylamide gels after injection, and for BSA and immunoglobin G, all remaining intracellular 125I migrated at the molecular weight of the injected proteins. By contrast, more than 80% of the extracellular 125I chromatographed as iodotyrosine. With the exception of fl-BSA, which exhibited perinuclear accumulation in approximately one-half of the injected cells, autoradiography showed that throughout the period of study the injected proteins remained dispersed in the cytoplasm.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041000118
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