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  • 1
    Electronic Resource
    Electronic Resource
    A Qualitative Assessment of Inner City Elementary School Children's Perceptions of Their Neighborhood (1998)
    Oxford, UK : Blackwell Publishing Ltd
    Public health nursing 15 (1998), S. 0 
    Details
    ISSN: 1525-1446
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract Three hundred seventy-nine youths from an inner city elementary school were surveyed to determine their perceptions of their neighborhood. Using a qualitative, word association format, older students responded to 20 descriptive words (e.g., dirty, safe, quiet, dangerous) while younger youths drew pictures in response to three words (safe, sad, happy). Using content analysis techniques, findings indicated that the youths found neighborhood areas and residents that were perceived as safe, quiet, beautiful, friendly, fun/happy, and helpful. However, safety issues and a dirty, noisy neighborhood also emerged as major themes. Collaborative initiatives focusing on cleaning up the neighborhood and reducing violence are suggested, as are areas of intervention and further research.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1525-1446.1998.tb00336.x
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  • 2
    Electronic Resource
    Electronic Resource
    Chronic Exposure to Adenosine Receptor Agonists and Antagonists Reciprocally Regulates the A1 Adenosine Receptor-Adenylyl Cyclase System in Cerebellar Granule Cells (1996)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 67 (1996), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Chronic treatment with the adenosine receptor antagonist caffeine evokes an up-regulation of A1 adenosine receptors and increased coupling of the receptor to G proteins in rat brain membranes. However, chronic agonist exposure has not been explored. Primary cultures of cerebellar granule cells were exposed chronically to A1 adenosine receptor agonists and antagonists. Exposure to the A1 adenosine receptor agonist N6-cyclopentyladenosine resulted in (1) a time- and concentration-dependent reduction in the density of receptors labeled by 1,3-[3H]dipropyl-8-cyclopentylxanthine, (2) an enhanced ability of guanyl nucleotides to decrease the fraction of A1 adenosine receptor sites displaying high affinity for 2-chloroadenosine, and (3) a functional uncoupling of receptors from adenylyl cyclase (EC 4.6.1.1). The adenosine antagonists caffeine and 8-p-sulfophenyltheophylline produced alterations in A1 adenosine receptor homeostasis that were antipodal to those associated with agonist treatment. Antagonist exposure (1) increased the density of A1 adenosine receptors in cerebellar granule cell membranes, (2) blunted the effect of guanyl nucleotides on receptor coupling to G proteins, and (3) increased the functional coupling of receptors to adenylyl cyclase inhibition. Forskolin treatment of cerebellar granule cells did not affect receptor density, suggesting that cyclic AMP is not involved in the regulation of A1 adenosine receptor expression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1996.67051921.x
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  • 3
    Electronic Resource
    Electronic Resource
    The three-dimensional structure of aquaporin-1 (1997)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 387 (1997), S. 624-627 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The entry and exit of water from cells is a fundamental process of life. Recognition of the high water permeability of red blood cells led to the proposal that specialized water pores exist in the plasma membrane. Expression in Xenopus oocytes and functional studies of an erythrocyte integral ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/42512
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  • 4
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray analysis of ferric enterobactin receptor FepA, an integral membrane protein from Escherichia coli (1998)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 54 (1998), S. 697-699 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Diffraction-quality crystals have been obtained of the integral membrane protein ferric enterobactin receptor (FepA) from the outer membrane of Escherichia coli. Crystals were grown using the zwitterionic detergent lauryldimethylamine oxide (LDAO), the precipitants polyethylene glycol (PEG) 1000 and sodium chloride, and the additive heptane-1,2,3-triol; they have the symmetry of the orthorhomic space group C2221 with a = 112.2, b = 137.2 and c = 135.4 Å and diffract to 2.5 Å resolution. The crystals were flash-cooled and a preliminary data set was collected at 103 K. The crystals are suitable for three-dimensional structure analysis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444997020222
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  • 5
    Electronic Resource
    Electronic Resource
    The progressive party problem: Integer linear programming and constraint programming compared (1996)
    Springer
    Constraints 1 (1996), S. 119-138 
    Details
    ISSN: 1572-9354
    Keywords: combinatorial optimization ; integer linear programming ; constraint programming
    Source: Springer Online Journal Archives 1860-2000
    Topics: Computer Science
    Notes: Abstract Many discrete optimization problems can be formulated as either integer linear programming problems or constraint satisfaction problems. Although ILP methods appear to be more powerful, sometimes constraint programming can solve these problems more quickly. This paper describes a problem in which the difference in performance between the two approaches was particularly marked, since a solution could not be found using ILP. The problem arose in the context of organizing a “progressive party” at a yachting rally. Some yachts were to be designated hosts; the crews of the remaining yachts would then visit the hosts for six successive half-hour periods. A guest crew could not revisit the same host, and two guest crews could not meet more than once. Additional constraints were imposed by the capacities of the host yachts and the crew sizes of the guests. Integer linear programming formulations which included all the constraints resulted in very large models, and despite trying several different strategies, all attempts to find a solution failed. Constraint programming was tried instead and solved the problem very quickly, with a little manual assistance. Reasons for the success of constraint programming in this problem are identified and discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00143880
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  • 6
    Electronic Resource
    Electronic Resource
    Projection map of aquaporin-1 determined by electron crystallography (1995)
    [s.l.] : Nature Publishing Group
    Nature structural biology 2 (1995), S. 730-732 
    Details
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Sir—The plasma membranes of mammalian red cells and renal proximal tubules, the intestinal epithelium of sap-sucking insects, and the vacuolar membranes of plants are highly permeable to water molecules due to the presence of water-selective pores known as the aquaporins (reviewed in refs 1, ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nsb0995-730
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  • 7
    Electronic Resource
    Electronic Resource
    Crystal structure of the outer membrane active transporter FepA from Escherichia coli (1999)
    [s.l.] : Nature America Inc.
    Nature structural biology 6 (1999), S. 56-63 
    Details
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Integral outer membrane receptors for iron chelates and vitamin B 12 carry out specific ligand transport against a concentration gradient. Energy for active transport is obtained from the proton–motive force of the inner membrane through physical interaction with ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/4931
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  • 8
    Electronic Resource
    Electronic Resource
    Specific Detection of Xylella fastidiosa Pierce's Disease Strains (1999)
    Springer
    Current microbiology 39 (1999), S. 85-88 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Pierce's disease (PD, Xylella fastidiosa) of grapevine is the primary pathogen limiting vinifera grape production in Florida and other regions of the southeastern United States. Quick and accurate detection of PD strains is essential for PD studies and control. A unique random amplified polymorphic DNA (PD1-1-2) was isolated from a PD strain from Florida. Fragment PD1-1-2 was cloned, sequenced, and found to be 1005 bp in length. PCR primers were designed to utilize these sequence data for PD strain detection. One primer set (XF176f–XF954r) amplified a 779-bp DNA fragment from 34 PD strains including seven pathotypes of X. fastidiosa, but not from strains of Xanthomonas campestris pv. campestris, Xan. vesicatoria or Escherichia coli. A second primer set (XF176f and XF686r) amplified a 511-bp fragment specific to 98 PD strains, but not from strains of citrus variegated chlorosis, mulberry leaf scorch, oak leaf scorch, periwinkle wilt, phony peach, or plum leaf scald. Sequence analysis indicated that RAPD fragment PD1-1-2 contains a Ser-tRNA gene. The PD-specific region includes a TaqI restriction site (TCGA) and is 150 bp downstream of the Ser-tRNA gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002849900423
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  • 9
    Electronic Resource
    Electronic Resource
    Role of the pro-α2(I) COOH-terminal region in assembly of type I collagen: Disruption of two intramolecular disulfide bonds in pro-α2(I) blocks assembly of type I collagen (1998)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 71 (1998), S. 233-242 
    Details
    ISSN: 0730-2312
    Keywords: assembly of type I collagen ; COOH-terminal propeptide ; pesin-resistant heterotrimers ; disulfide bonds ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Collagen biosynthesis is a complex process that begins with the association of three procollagen chains. A series of conserved intra- and interchain disulfide bonds in the carboxyl-terminal region of the procollagen chains, or C-propeptide, has been hypothesized to play an important role in the nucleation and alignment of the chains. We tested this hypothesis by analyzing the ability of normal and cysteine-mutated pro-α2(I) chains to assemble into type I collagen heterotrimers when expressed in a cell line (D2) that produces only endogenous pro-α1(I). Pro-α2(I) chains containing single or double cysteine mutations that disrupted individual intra- or interchain disulfide bonds were able to form pepsin resistant type I collagen with pro-α1(I), indicating that individual disulfide bonds were not critical for assembly of the pro-α2(I) chain with pro-α1(I). Pro-α2(I) chains containing a triple cysteine mutation that disrupted both intrachain disulfide bonds were not able to form pepsin resistant type I collagen with pro-α1(I). Therefore, disruption of both pro-α2(I) intrachain disulfide bonds prevented the production and secretion of type I collagen heterotrimers. Although none of the individual disulfide bonds is essential for assembly of the procollagen chains, the presence of at least one intrachain disulfide bond may be necessary as a structural requirement for chain association or to stabilize the protein to prevent intracellular degradation. J.Cell. Biochem. 71:233-242, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Role of the pro-α2(I) COOH-terminal region in assembly of type I collagen: Truncation of the last 10 amino acid residues of pro-α2(I) chain prevents assembly of type I collagen heterotrimer (1998)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 71 (1998), S. 216-232 
    Details
    ISSN: 0730-2312
    Keywords: assembly of type I collagen ; COOH-terminal propeptide ; pepsin-resistant heterotrimers ; interspecies collagen molecule ; thermal stability ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Procollagen (Type I) contains a noncollagenous COOH-terminal propeptide (C-propeptide) hypothesized to be important in directing chain association and alignment during assembly. We previously expressed human pro-α2(I) cDNA in rat liver epithelial cells, W8, that produce only pro-α1(I) trimer collagen (Lim et al. [1994] MatrixBiol. 14: 21-30). In the resulting cell lines, α2(I) assembled with α1(I) forming heterotrimers. Using this cell system, we investigated the importance of the COOH-terminal propeptide sequence of the pro-α2(I) chain for normal assembly of type I collagen. Full-length human pro-α2(I) cDNA was cloned into expression vectors with a premature stop signal eliminating the final 10 amino acids. No triple-helical molecules containing α2(I) were detected in transfected W8 cells, although pro-α2(I) mRNA was detected. Additional protein analysis demonstrated that these cells synthesize small amounts of truncated pro-α2(I) chains detected by immunoprecipitation with a pro-α2(I) antibody. In addition, since the human-rat collagen was less thermostable than normal intraspecies collagen, wild-type and C-terminal truncated mouse cDNAs were expressed in mouse D2 cells, which produced only type I trimers. Results from both systems were consistent, suggesting that the last 10 amino acid residues of the pro-α2(I) chain are important for formation of stable type I collagen. J. Cell. Biochem. 71:216-232, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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