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  • 1
    Electronic Resource
    Electronic Resource
    A Monte Carlo model to produce baryons ine + e − annihilation (1982)
    Springer
    The European physical journal 12 (1982), S. 77-79 
    Details
    ISSN: 1434-6052
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract A simple model is described extending the Field-Feynman model to baryon production in quark fragmentation. The model predicts baryon baryon correlations within jets and in opposite jets produced in electron-positron annihilation. Existing data is well described by the model.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01475734
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  • 2
    Electronic Resource
    Electronic Resource
    Isolation and culturing of highly polarized primary epithelial cells from normal human stomach (antrum) as spheroid-like vesicles (1997)
    Springer
    Methods in cell science 19 (1997), S. 169-178 
    Details
    ISSN: 1573-0603
    Keywords: Antrum ; Human gastrointestinal epithelium ; Polarized epithelial cells ; Spheroid-like vesicles ; Tissue culture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A novel procedure is described for the three-dimensional (3-D) in vitro culture and for maintaining of nontransformed gastric epithelial cells from the human antrum mucosa (HAEC). Biopsies obtained from the antrum were cut into small pieces and the tissue fragments were incubated in culture medium containing the appropriate antibiotics. The suspended mucosal fragments generated small, spheroid-like vesicles consisting of predominantly highly prismatic, mucus-producing cells which mimic the in vivo counterparts structurally and functionally. Electron microscopic investigations revealed a number of ultrastructural and morphological features similar to those of normal gastric cells in vivo such as apical microvilli associated with a glycocalyx, tight junctions, desmosomes, membraneous infoldings, mucous droplets, and an irregular basal lamina. In comparison to the two-dimensional (2-D) gastric cell cultures grown on plane supports, the vesicles maintain an intact epithelial organization of individual cells. The prismatic phenotype, the histophysiology as well as the cytoarchitecture of the non-transformed 3-D cultured gastric epithelial cells are comparable to those of the native tissue and therefore represent a suitable model for defined pathogen-host cell interactions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009751913391
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  • 3
    Electronic Resource
    Electronic Resource
    Construction of hermes shuttle vectors: a versatile system useful for genetic complementation of transformable and non-transformableNeisseria mutants (1996)
    Springer
    Molecular genetics and genomics 250 (1996), S. 558-569 
    Details
    ISSN: 1617-4623
    Keywords: Plasmid vector ; Conjugation ; Generalized mutagenesis ; Homologous recombination ; Natural transformation competence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A versatile shuttle system has been developed for genetic complementation with cloned genes of transformable and non-transformableNeisseria mutants. By random insertion of a selectable marker into the conjugativeNeisseria plasmidptetM25.2, a site within this plasmid was identified that is compatible with plasmid replication and with conjugative transfer of plasmid. Regions flanking the permissive insertion site of ptetM25.2 were cloned inEscherichia coli and served as a basis for the construction of the Hermes vectors. Hermes vectors are composed of anE. coli replicon that does not support autonomous replication inNeisseria, e.g. ColE1, p15A, orori fd, fused with a shuttle consisting of a selectable marker and a multiple cloning site flanked by the integration region of ptetM25.2. Complementation of a non-transformableNeisseria strain involves a three-step process: (i) insertion of the desired gene into a Hermes vector; (ii) transformation of Hermes into aNeisseria strain containing ptetM25.2 to create a hybrid ptetM25.2 via gene replacement by the Hermes shuttle cassette; and (iii) conjugative transfer of the hybrid ptetM25.2 into the finalNeisseria recipient. Several applications for the genetic manipulation of pathogenicNeisseriae are described.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02174444
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  • 4
    Electronic Resource
    Electronic Resource
    Kinetics of isomerization for the proline helical forms of two oligoproline redox arrays by circular dichroic spectropolarimetry (1999)
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 61-69 
    Details
    ISSN: 1573-3904
    Keywords: biexponential kinetics ; proline helices ; substituted proline residues
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The kinetics of isomerization of the helical forms of three oligoprolines was determined by far-ultraviolet CD spectropolarimetry and kinetic analysis by singular value decomposition. ZRA (Pro3-X-Pro2-Y-Pro2-Z-Pro3) and ZRA2 (Pro7-X-Pro2-Y-Pro2-Z-Pro7) bear large redox-active substituents on proline residues X, Y, and Z, but P9 (Pro9) does not. All three peptides formed a stable proline-II helix in water. In acetonitrile, both ZRA2 and P9 were converted into a proline-I helical form but ZRA remained predominantly in the proline-II helical form. Evidently, in order to undergo substantial proline II→I isomerization, an oligoproline chain containing large substituents needs to have a segment of consecutive unsubstituted proline residues that is sufficiently long to form a stable proline helix. Biexponential kinetics (A→B, k1 = ∼3.3 × 10-4 s-1; B→C, k2 = ∼0.8 × 10-4 s-1) were observed for the proline II→I isomerization of ZRA2 and P9 in acetonitrile and for the proline I→II isomerization of ZRA2 in water, which provides evidence for the growth and decay of a major kinetic intermediate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008819511721
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  • 5
    Electronic Resource
    Electronic Resource
    Recognition of two initiation codons for the synthesis of phage fd gene 2 protein (1980)
    Springer
    Molecular genetics and genomics 180 (1980), S. 489-494 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Bacteriophage fd gene 2 protein was specifically labeled with radioactive amino acids and was isolated from membranous cell structures as an apparently homogenous protein. Amino acid sequence analysis revealed that the protein was initiated at two distinct AUG codons close to the ribosome binding site. The two resulting translation products were found to begin with a deformylated methionine residue. Initiation at the first signal was used for 90% of the chains and at the second signal for 10% of the sequenced molecules. The use of one or the other chain start may influence functions of gene 2 protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00268051
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  • 6
    Electronic Resource
    Electronic Resource
    Tyrosine Phosphorylation of Moesin in Arachidonic Acid–Stimulated Human Platelets (1998)
    Springer
    Journal of thrombosis and thrombolysis 6 (1998), S. 117-124 
    Details
    ISSN: 1573-742X
    Keywords: moesin ; ezrin ; tyrosine phosphorylation ; arachidonic acid ; platelets
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Moesin, a member of the ezrin/radixin/moesin (ERM) family of cytoskeletal proteins, has been implicated in dynamic membrane-based processes such as the formation and stabilization of filopodia. Ezrin is known to be a substrate of tyrosine kinases in activated T cells and epithelial growth factor–stimulated A431 cells. For the closely related 77-kD protein moesin, which shares 72% identity with ezrin on the basis of their amino acid sequences, a reversible phosphorylation on tyrosine residues has not yet been described. Because our scanning electron microscopy studies revealed the appearance of multiple, up to 3 μm long filopodia on the surface of activated human platelets, we investigated the participation of moesin in dynamic shape changes on platelet stimulation with arachidonic acid. Antimoesin immunoprecipitates obtained under denaturing conditions from lysates of resting platelets contained only low amounts of tyrosine-phosphorylated moesin. In lysates of arachidonic acid–stimulated platelets, the level of tyrosine phosphorylation was significantly increased. This activation-dependent phosphorylation of moesin was verified by probing antiphosphotyrosine immunoprecipitates from unstimulated and stimulated platelets with antimoesin antibodies. Tyrosine-phosphorylated moesin was detectable only in the presence of the tyrosine phosphatase inhibitor vanadate, suggesting that a coordinated balance between kinase and phosphatase activities controls the steady-state level of moesin phosphorylation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008845421381
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  • 7
    Electronic Resource
    Electronic Resource
    Cloning and characterization of the Neisseria gonorrhoeae MS11 folC gene (1996)
    Springer
    Molecular genetics and genomics 250 (1996), S. 277-285 
    Details
    ISSN: 1617-4623
    Keywords: Key words Gonococcus ; Folic acid ; Dihydrofolate synthetase ; Folylpolyglutamate synthetase ; One-carbon metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  The gene coding for folylpoly-(γ)-glutamate synthetase (FPGS)-dihydrofolate synthetase (DHFS) of Neisseria gonorrhoeae (Ngo) has been cloned by functional complementation of an Escherichia coli folC mutant (SF4). The sequence encodes a 224-residue protein of 46.4 kDa. It shows 46% identity to the E. coli FPGS-DHFS and 29% identity to the FPGS of Lactobacillus casei. Sequence comparisons between the three genes reveal regions of high homology, including ATP binding sites required for bifunctionality, all of which may be important for FPGS activity. In contrast to L. casei FPGS, the E. coli and Ngo enzymes share some additional regions which may be essential for DHFS activity. The products of Ngo folC and flanking genes were monitored by T7 promoter expression. Interestingly, deletion of the upstream folI gene, which encodes a 16.5 kDa protein, abolishes the capacity of folC to complement E. coli SF4 to the wild-type phenotype. The ability to complement can be restored by folI provided in trans. Unlike folC mutants, gonococcal folI mutants are viable and display no apparent phenotype. Thus, in contrast to E. coli, Ngo folC is expressed at a sufficiently high level from its own promoter, in the absence of FolI. This study provides the first insights into the genetic complexity of one-carbon metabolism in Ngo.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02174385
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  • 8
    Electronic Resource
    Electronic Resource
    Kinetics of isomerization for the proline helical forms of two oligoproline redox arrays by circular dichroic spectropolarimetry (1999)
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 61-69 
    Details
    ISSN: 1573-3904
    Keywords: biexponential kinetics ; proline helices ; substituted proline residues
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The kinetics of isomerization of the helical forms of three oligoprolines was determined by far-ultraviolet CD spectropolarimetry and kinetic analysis by singular value decomposition. ZRA (Pro3-X-Pro2-Y-Pro2-Z-Pro3) and ZRA2 (Pro7-X-Pro2-Y-Pro2-Z-Pro7) bear large redox-active substituents on proline residues X, Y, and Z, but P9 (Pro9) does not. All three peptides formed a stable proline-II helix in water. In acetonitrile, both ZRA2 and P9 were converted into a proline-I helical form but ZRA remained predominantly in the proline-II helical form. Evidently, in order to undergo substantial proline II→I isomerization, an oligoproline chain containing large substituents needs to have a segment of consecutive unsubstituted proline residues that is sufficiently long to form a stable proline helix. Biexponential kinetics (A→B, k1=∼3.3×10−4s−1; B→C, k2=∼0.8×10−4s−1) were observed for the proline II→I isomerization of ZRA2 and P9 in acetonitrile and for the proline I→II isomerization of ZRA2 in water, which provides evidence for the growth and decay of a major kinetic intermediate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02443619
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