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  • 1
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    He− (2014)
    American Physical Society (APS)
    Details
    Publication Date: 2014-05-02
    Description: Author(s): J. A. Salas and K. Varga The energy of the He− ion in a magnetic field is calculated using the stochastic variational method with a deformed correlated Gaussian basis. The energy levels and the stability domains are calculated and the accuracy of the approach is shown by comparison to previous calculations. The structure of... [Phys. Rev. A 89, 052501] Published Thu May 01, 2014
    Keywords: Atomic and molecular structure and dynamics
    Print ISSN: 1050-2947
    Electronic ISSN: 1094-1622
    Topics: Physics
    Published by American Physical Society (APS)
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  • 2
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    Retraction (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-11-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beloqui, Ana -- Guazzaroni, Maria Eugenia -- Pazos, Florencio -- Vieites, Jose M -- Godoy, Marta -- Golyshina, Olga V -- Chernikova, Tatyana N -- Waliczek, Agnes -- Silva-Rocha, Rafael -- Al-Ramahi, Yamal -- La Cono, Violetta -- Mendez, Carmen -- Salas, Jose A -- Solano, Roberto -- Yakimov, Michail M -- Timmis, Kenneth N -- Golyshin, Peter N -- Ferrer, Manuel -- New York, N.Y. -- Science. 2010 Nov 12;330(6006):912. doi: 10.1126/science.330.6006.912-a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21071648" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Reactome array: forging a link between metabolome and genome (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-10-10
    Description: We describe a sensitive metabolite array for genome sequence-independent functional analysis of metabolic phenotypes and networks, the reactomes, of cell populations and communities. The array includes 1676 dye-linked substrate compounds collectively representing central metabolic pathways of all forms of life. Application of cell extracts to the array leads to specific binding of enzymes to cognate substrates, transformation to products, and concomitant activation of the dye signals. Proof of principle was shown by reconstruction of the metabolic maps of model bacteria. Utility of the array for unsequenced organisms was demonstrated by reconstruction of the global metabolisms of three microbial communities derived from acidic volcanic pool, deep-sea brine lake, and hydrocarbon-polluted seawater. Enzymes of interest are captured on nanoparticles coated with cognate metabolites, sequenced, and their functions unequivocally established.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beloqui, Ana -- Guazzaroni, Maria-Eugenia -- Pazos, Florencio -- Vieites, Jose M -- Godoy, Marta -- Golyshina, Olga V -- Chernikova, Tatyana N -- Waliczek, Agnes -- Silva-Rocha, Rafael -- Al-Ramahi, Yamal -- La Cono, Violetta -- Mendez, Carmen -- Salas, Jose A -- Solano, Roberto -- Yakimov, Michail M -- Timmis, Kenneth N -- Golyshin, Peter N -- Ferrer, Manuel -- New York, N.Y. -- Science. 2009 Oct 9;326(5950):252-7. doi: 10.1126/science.1174094.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CSIC, Institute of Catalysis, 28049 Madrid, Spain.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19815770" target="_blank"〉PubMed〈/a〉
    Keywords: Archaea/genetics/metabolism ; Bacteria/genetics/*metabolism ; Bacterial Proteins/metabolism ; Computational Biology ; Ecosystem ; Enzymes/*metabolism ; Enzymes, Immobilized ; Genome, Archaeal ; *Genome, Bacterial ; Hot Springs/microbiology ; *Metabolic Networks and Pathways ; *Metabolome ; Metabolomics/*methods ; Microarray Analysis/*methods ; Nanoparticles ; Pseudomonas putida/genetics/metabolism ; Seawater/microbiology ; Streptomyces coelicolor/genetics/metabolism ; Water Microbiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Three-electron atoms and ions in a magnetic field (2015)
    American Physical Society (APS)
    Details
    Publication Date: 2015-09-04
    Description: Author(s): J. A. Salas, I. Pelaschier, and K. Varga The energies and physical properties of three-electron systems are studied using an explicitly correlated Gaussian basis optimized by the stochastic variational method. The stability of the system as a function of the nuclear charge is analyzed. The role of the Coulomb and magnetic interactions in s… [Phys. Rev. A 92, 033401] Published Wed Sep 02, 2015
    Keywords: Atomic and molecular processes in external fields, including interactions with strong fields and short pulses
    Print ISSN: 1050-2947
    Electronic ISSN: 1094-1622
    Topics: Physics
    Published by American Physical Society (APS)
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  • 5
    Electronic Resource
    Electronic Resource
    Cloning, sequencing and transcriptional analysis of a Streptomyces coelicolor operon containing the rplM and rpsI genes encoding ribosomal proteins ScoL13 and ScoS9 (1997)
    Springer
    Molecular genetics and genomics 257 (1997), S. 91-96 
    Details
    ISSN: 1617-4623
    Keywords: Key words Ribosomal proteins S9/L13 ; Genes rpsI/rplM ; Actinomycetes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The N-terminal amino acid sequences of two peptides derived from a Streptomyces coelicolor ribosomal protein were determined and degenerate oligonucleotide primers derived from these sequences were used as probes for the screening of a chromosomal DNA library of S. coelicolor. Two positive clones were isolated and DNA sequencing of a 1740-bp region of these clones that hybridised with the probes revealed the presence of four genes, two of them incomplete. The deduced products of the two complete genes, rplM and rpsI, showed clear similarities to L13 and S9 ribosomal proteins from various organisms. Promoter-probe and primer extension experiments suggest that the two genes form a single transcriptional unit. The specific rate of synthesis of both proteins was high at early stages of growth but decreased later.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050627
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  • 6
    Electronic Resource
    Electronic Resource
    Analysis of a Streptomyces antibioticus chromosomal region involved in oleandomycin biosynthesis, which encodes two glycosyltransferases responsible for glycosylation of the macrolactone ring (1998)
    Springer
    Molecular genetics and genomics 259 (1998), S. 299-308 
    Details
    ISSN: 1617-4623
    Keywords: Key words Macrolides ; Glycosyltransferase ; Deoxyhexoses ; Actinomycetes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A 6-kb region from the chromosome of Streptomyces antibioticus, an oleandomycin producer, was cloned and sequenced. This region was located between the 3′ end of the gene encoding the third subunit of the oleandomycin type I polyketide synthase and the oleP and oleB genes, which encode a cytochrome P450 monooxygenase and an oleandomycin resistance gene, respectively. Analysis of the nucleotide sequence revealed the presence of five genes encoding a cytochrome P450-like protein (oleP1), two glycosyltransferases (oleG1 and oleG2) involved in the transfer of the two 6-deoxysugars (L-oleandrose and D-desosamine) to the oleandomycin macrolactone ring, a methyltransferase (oleM1), and a gene (oleY) of unknown function. Insertional inactivation of this region by gene disruption generated an oleandomycin non-producing mutant which accumulated a compound that, according to mass spectrometry analysis, could correspond to the oleandomycin macrolactone ring (oleandolide), suggesting that the mutation affects oleandrosyl glycosyltransferase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050816
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  • 7
    Electronic Resource
    Electronic Resource
    Analysis of two chromosomal regions adjacent to genes for a type II polyketide synthase involved in the biosynthesis of the antitumor polyketide mithramycin in Streptomyces argillaceus (1999)
    Springer
    Molecular genetics and genomics 261 (1999), S. 216-225 
    Details
    ISSN: 1617-4623
    Keywords: Key words Oxygenases ; Ketoreductases ; Acyl CoA ligase ; Loading enzyme ; Polyketides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Mithramycin is an aromatic antitumour polyketide synthesized by Streptomyces argillaceus. Two chromosomal regions located upstream and downstream of the locus for the mithramycin type II polyketide synthase were cloned and sequenced. Analysis of the sequence revealed the presence of eight genes encoding three oxygenases (mtmOI, mtmOII and mtmOIII), three reductases (mtmTI, mtmTII and mtmTIII), a cyclase (mtmY) and an acyl CoA ligase (mtmL). The three oxygenase genes were each inactivated by gene replacement. Inactivation of one of them (mtmOII) generated a non-producing mutant, while inactivation of the other two (mtmOI and mtmOIII) did not affect the biosynthesis of mithramycin. The mtmOII gene may code for an oxygenase responsible for the introduction of oxygen atoms at early steps in the biosynthesis of mithramycin leading to 4-demethylpremithramycinone. One of the reductases may be responsible for reductive cleavage of an intermediate from an enzyme and another for the reduction of a keto group in the side-chain of the mithramycin aglycon moiety. A hypothetical biosynthetic pathway showing in particular the involvement of oxygenase MtmOII and of various other gene products in mithramycin biosynthesis is proposed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050960
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  • 8
    Electronic Resource
    Electronic Resource
    An ABC transporter is essential for resistance to the antitumor agent mithramycin in the producerStreptomyces argillaceus (1996)
    Springer
    Molecular genetics and genomics 251 (1996), S. 692-698 
    Details
    ISSN: 1617-4623
    Keywords: Streptomyces ; ABC transporters ; ATP-binding protein ; Secretion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Mithramycin is an antitumor antibiotic synthesized byStreptomyces argillaceus. This producer strain is highly resistant in vivo to mithramycin (MIC 100 µg/ml) but sensitive to the related drugs chromomycin and olivomycin (MIC 10 µg/ml). From a genomic library ofS. argillaceus DNA two cosmid clones were isolated which confer a high level of resistance to mithramycin onS. albus. The resistance genes were mapped by subcloning to a 3.9-kbPstI-PvuII fragment. DNA sequence analysis of this fragment revealed one incomplete and three complete open reading frames. Subcloning experiments demonstrated that resistance to mithramycin is mediated by the genesmtrA andmtrB. ThemtrA gene can potentially encode an ATP-binding protein of the ABC transporter superfamily, containing one nucleotide-binding domain and showing similarity with other ABC transporters involved in resistance to daunorubicin, oleandomycin and tetronasin in their respective producer strains. ThemtrB gene codes for an integral membrane protein with six putative transmembrane helices. A mithramycin-sensitive mutant was generated in a gene replacement experiment by disrupting themtrA gene, thus demonstrating that the system encoded by themtrAB genes is essential for conferring resistance to mithramycin inS. argillaceus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02174118
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  • 9
    Electronic Resource
    Electronic Resource
    An ABC transporter is essential for resistance to the antitumor agent mithramycin in the producer Streptomyces argillaceus (1996)
    Springer
    Molecular genetics and genomics 251 (1996), S. 692-698 
    Details
    ISSN: 1617-4623
    Keywords: Key words Streptomyces ; ABC transporters ; ATP-binding protein ; Secretion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Mithramycin is an antitumor antibiotic synthesized by Streptomyces argillaceus. This producer strain is highly resistant in vivo to mithramycin (MIC 100 μg/ml) but sensitive to the related drugs chromomycin and olivomycin (MIC 10 μg/ml). From a genomic library of S. argillaceus DNA two cosmid clones were isolated which confer a high level of resistance to mithramycin on S. albus. The resistance genes were mapped by subcloning to a 3.9-kb PstI-PvuII fragment. DNA sequence analysis of this fragment revealed one incomplete and three complete open reading frames. Subcloning experiments demonstrated that resistance to mithramycin is mediated by the genes mtrA and mtrB. The mtrA gene can potentially encode an ATP-binding protein of the ABC transporter superfamily, containing one nucleotide-binding domain and showing similarity with other ABC transporters involved in resistance to daunorubicin, oleandomycin and tetronasin in their respective producer strains. The mtrB gene codes for an integral membrane protein with six putative transmembrane helices. A mithramycin-sensitive mutant was generated in a gene replacement experiment by disrupting the mtrA gene, thus demonstrating that the system encoded by the mtrAB genes is essential for conferring resistance to mithramycin in S. argillaceus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02174118
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  • 10
    Electronic Resource
    Electronic Resource
    Characterization of two glycosyltransferases involved in early glycosylation steps during biosynthesis of the antitumor polyketide mithramycin by Streptomyces argillaceus (2000)
    Springer
    Molecular genetics and genomics 262 (2000), S. 991-1000 
    Details
    ISSN: 1617-4623
    Keywords: Key words Antitumor ; Polyketides ; Streptomycetes ; Aureolic acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A 2580-bp region of the chromosome of Streptomyces argillaceus, the producer of the antitumor polyketide mithramycin, was sequenced. Analysis of the nucleotide sequence revealed the presence of two genes (mtmGIII and mtmGIV ) encoding proteins that showed a high degree of similarity to glycosyltransferases involved in the biosynthesis of various antibiotics and antitumor drugs. Independent insertional inactivation of both genes produced mutants that did not synthesize mithramycin but accumulated several mithramycin intermediates. Both mutants accumulated premithramycinone, a non-glycosylated intermediate in mithramycin biosynthesis. The mutant affected in the mtmGIII gene also accumulated premithramycin A1, which contains premithramycinone as the aglycon unit and a D-olivose attached at C-12a-O. These experiments demonstrate that the glycosyltransferases MtmGIV and MtmGIII catalyze the first two glycosylation steps in mithramycin biosynthesis. A model is proposed for the glycosylation steps in mithramycin biosynthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00008667
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