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  • 1
    Electronic Resource
    Electronic Resource
    Three new mutations in the hepatocyte nuclear factor-1α gene in Japanese subjects with diabetes mellitus: clinical features and functional characterization (1999)
    Springer
    Diabetologia 42 (1999), S. 621-626 
    Details
    ISSN: 1432-0428
    Keywords: Keywords MODY ; HNF-1α ; insulin ; arginine ; mutation.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Aims/hypothesis. Mutations in the hepatocyte nuclear factor-1α gene are a common cause of the type 3 form of maturity-onset diabetes of the young. We examined the clinical features and molecular basis of hepatocyte nuclear factor-1α (HNF-1α) diabetes. Methods. Thirty-seven Japanese subjects with early onset Type II (non-insulin-dependent) diabetes mellitus and 45 with Type I (insulin-dependent) diabetes mellitus were screened for mutations in this gene. Functional properties of mutant HNF-1α were also investigated. Results. Three new mutations [G415R, R272C and A site of the promoter ( + 102G-to-C)] were found. Insulin secretion was impaired in the three subjects. Insulin and glucagon secretory responses to arginine in the subject with the R272C mutation were also diminished. Molecular biological studies indicated that the G415R mutation generated a protein with about 50 % of the activity of wild-type HNF-1α. The R272C mutation had no transactivating or DNA binding activity and acted in a dominant negative manner. The + 102 G-to-C mutation in the A site of the promoter activity was associated with an increase in promoter activity and it had 42–75 % more activity than the wild-type sequence. Conclusion/interpretation. Mutations in the HNF-1α gene may affect the normal islet function by different molecular mechanisms. [Diabetologia (1999) 42: 621–626]
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001250051204
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  • 2
    Electronic Resource
    Electronic Resource
    A novel in vitro effect of the mucosal protective agent sofalcone – inhibition of chemotactic motility in Helicobacter pylori (2000)
    Oxford, UK : Blackwell Science Ltd
    Alimentary pharmacology & therapeutics 14 (2000), S. 0 
    Details
    ISSN: 1365-2036
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background: Motility of Helicobacter pylori is essential for colonization. H. pylori has been shown to exhibit chemotactic activity toward urea and sodium and bicarbonate ions, which are secreted from the gastric epithelia. The importance of urease activity for chemotactic motility of H. pylori in a viscous environment has also been shown. Consequently, application of drugs inhibiting chemotactic motility has been proposed as a strategy for H. pylori eradication. This inhibitory effect can be evaluated through assay of chemotaxis and swarming. Materials and methods: H. pylori CPY3401 and ATCC43504 were grown on brucella agar plates/broth supplemented with 3% horse serum under microaerobic conditions (N2, 85%; O2, 5%; CO2, 10%). For motility assay, H. pylori cells grown on brucella-serum agar were stabbed into motility agar containing 0.35% refined agar in brucella-serum broth and the swarming zone was measured. For the chemotaxis assay, cells were suspended in 10 m m potassium phosphate buffer, pH 7.0, with 3% polyvinyl- pyrrolidone and assayed as described previously. Bacterial swimming in the fluid environment was observed under dark-field microscopy. Results: Numbers of bacteria attracted toward 1 μm flurofamide were reduced with increasing con- centrations of sofalcone (0.2–222 μm). In addition, the size of the swarming zone was reduced in motility agar containing 22 and 222 μm sofalcone. On the other hand, 22 μm sofalcone did not inhibit bacterial growth on day 3. Bacterial swimming speed in brucella broth was slower in the presence of 22 and 222 μm sofalcone than in its absence. Conclusion: Sofalcone was found to inhibit chemotactic motility of H. pylori. This drug may be useful for inhibiting the bacterium's ability to colonize the human stomach.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2036.2000.014s1230.x
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  • 3
    Electronic Resource
    Electronic Resource
    Immunofluorescent study of chromatin proteins in cultured fibroblasts
    Amsterdam : Elsevier
    Experimental Cell Research 86 (1974), S. 59-62 
    Details
    ISSN: 0014-4827
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0014-4827(74)90647-8
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  • 4
    Electronic Resource
    Electronic Resource
    Systemic reaction associated with Iramo scyphopolyp, Stephanoscyphus racemosum Komai (2004)
    Oxford, UK : Blackwell Science Ltd
    Clinical and experimental dermatology 29 (2004), S. 0 
    Details
    ISSN: 1365-2230
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2230.2004.01634.x
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  • 5
    Electronic Resource
    Electronic Resource
    Concept design of a control system for the SUBARU telescope
    Amsterdam : Elsevier
    Nuclear Instruments and Methods in Physics Research Section A: 352 (1994), S. 75-78 
    Details
    ISSN: 0168-9002
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0168-9002(94)91465-6
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  • 6
    Electronic Resource
    Electronic Resource
    Rubbing noise of single crystal ferrite heads
    Amsterdam : Elsevier
    Journal of Magnetism and Magnetic Materials 53 (1986), S. 374-378 
    Details
    ISSN: 0304-8853
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0304-8853(86)90183-6
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  • 7
    Electronic Resource
    Electronic Resource
    Effects of Pre-Strain and Nb Content on Transformation Temperatures in Ti-Ni-Nb Shape Memory Alloy (2005)
    s.l. ; Stafa-Zurich, Switzerland
    Materials science forum Vol. 475-479 (Jan. 2005), p. 1949-1952 
    Details
    ISSN: 1662-9752
    Source: Scientific.Net: Materials Science & Technology / Trans Tech Publications Archiv 1984-2008
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Ti-Ni-Nb shape memory alloy has a wide transformation hysteresis, and has been used as coupling devices and so on. However systematic researches of the influence of the amount of Nb addition on transformation temperatures are few. The purpose of this work is to clarify the influences of pre-strain and Nb content on transformation temperatures in Ti-Ni-Nb shape memory alloys. The specimens were Ti-Ni-Nb alloys (Ni/Ti=1.0, Nb=0-15at%), annealed at 1223 K for 0.3 ks. The variation of transformation temperatures with pre-strain and Nb content were investigated experimentally. The variation of As, Ms and transformation temperature hysteresis with pre-strain and Nb content will be discussed in relation to the elastic strain energy and the volume fraction of slip-deformed martensite
    Type of Medium: Electronic Resource
    URL: http://www.tib-hannover.de/fulltexts/2011/0528/02/09/transtech_doi~10.4028%252Fwww.scientific.net%252FMSF.475-479.1949.pdf
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  • 8
    Electronic Resource
    Electronic Resource
    Protein substrates and heat shock reduce the DNA-binding ability of Escherichia coli Lon protease (1995)
    Springer
    Applied microbiology and biotechnology 44 (1995), S. 484-488 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  Interaction between the fusion protein MBP-Lon, formed by maltose-binding protein and Lon protease, and the plasmid pBR322 was studied to clarify the DNA-binding behavior of the Lon protease. Since the MBP-Lon fusion protein that was bound to the plasmid was strongly adsorbed by amylose resin, complex formation and dissociation were determined by quantifying the unadsorbed plasmid using agarose gel electrophoresis. The autolysis of MBP-Lon fusion protein was suppressed when the protein was bound to the plasmid. The plasmid was completely dissociated from MBP-Lon fusion protein by the addition of the protein substrates of Lon protease (i.e. α-casein and denatured bovine serum albumin). In addition, at high temperatures, MBP-Lon fusion protein lost its plasmid-binding ability, although it fully retained ATP-dependent protease activity. These results suggest that Lon protease loses DNA-binding ability when cells are exposed to abnormal conditions and the amount of damaged proteins increases. On the other hand, DNA probably plays an important role in controlling the Lon protease activity in cells under normal conditions by entrapping the enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530050586
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  • 9
    Electronic Resource
    Electronic Resource
    Protein substrates and heat shock reduce the DNA-binding ability of Escherichia coli Lon protease (1995)
    Springer
    Applied microbiology and biotechnology 44 (1995), S. 484-488 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Interaction between the fusion protein MBP-Lon, formed by maltose-binding protein and Lon protease, and the plasmid pBR322 was studied to clarify the DNA-binding behavior of the Lon protease. Since the MBP-Lon fusion protein that was bound to the plasmid was strongly adsorbed by amylose resin, complex formation and dissociation were determined by quantifying the unadsorbed plasmid using agarose gel electrophoresis. The autolysis of MBP-Lon fusion protein was suppressed when the protein was bound to the plasmid. The plasmid was completely dissociated from MBP-Lon fusion protein by the addition of the protein substrates of Lon protease (i.e. α-casein and denatured bovine serum albumin). In addition, at high temperatures, MBP-Lon fusion protein lost its plasmid-binding ability, although it fully retained ATP-dependent protease activity. These results suggest that Lon protease loses DNA-binding ability when cells are exposed to abnormal conditions and the amount of damaged proteins increases. On the other hand, DNA probably plays an important role in controlling the Lon protease activity in cells under normal conditions by entrapping the enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00169948
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  • 10
    Electronic Resource
    Electronic Resource
    Overproduction and purification of SulA fusion protein in Escherichia coli and its degradation by Lon protease in vitro (1995)
    Springer
    Applied microbiology and biotechnology 43 (1995), S. 304-309 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  To overproduce extremely unstable SulA protein, which is the cell-division inhibitor of Escherichia coli, we fused the sulA gene to the maltose-binding protein (MBP) fusion vectors with or without the signal sequence (plasmids pMAL-p-SulA and pMAL-c-SulA respectively). The amount of the full-length fusion protein expressed from the plasmid pMAL-p-SulA (pre-MBP-SulA) in E. coli was much larger than that expressed from the plasmid pMAL-c-SulA (MBP-SulA). A major amount of the pre-MBP-SulA fusion protein was expressed in a soluble form and affinity-purified by amylose resin. Since site-specific cleavage of the fusion protein with factor Xa resulted in the precipitation of SulA protein, the pre-MBP-SulA fusion protein was used to study the degradation of SulA protein by E. coli Lon protease in vitro. It was found that only the SulA portion of the fusion protein was degraded by Lon protease in an ATP-dependent manner. This result provides direct evidence that Lon protease plays an important role in the rapid degradation of SulA protein in cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530050407
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