Search Results - (Author, Cooperation:M. A. Davis)

Showing 1 - 14 results of 14, query time: 0.78s Refine Results
  1. 1
    M. A. Davis
    Nature Publishing Group (NPG)
    Published 2011
    Staff View
    Publication Date:
    2011-12-14
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    *Deception ; *Ego ; Humans ; *Rationalization
    Published by:
    http://www.nature.com/

    Latest Papers from Table of Contents or Articles in Press
  2. 2
    Staff View
    Publication Date:
    2011-06-10
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Animals ; Conservation of Natural Resources/*methods ; Ecology/*methods ; *Ecosystem ; Extinction, Biological ; Introduced Species/*statistics & numerical data ; Species Specificity
    Published by:
    http://www.nature.com/

    Latest Papers from Table of Contents or Articles in Press
  3. 3
    A. J. Westphal ; R. M. Stroud ; H. A. Bechtel ; F. E. Brenker ; A. L. Butterworth ; G. J. Flynn ; D. R. Frank ; Z. Gainsforth ; J. K. Hillier ; F. Postberg ; A. S. Simionovici ; V. J. Sterken ; L. R. Nittler ; C. Allen ; D. Anderson ; A. Ansari ; S. Bajt ; R. K. Bastien ; N. Bassim ; J. Bridges ; D. E. Brownlee ; M. Burchell ; M. Burghammer ; H. Changela ; P. Cloetens ; A. M. Davis ; R. Doll ; C. Floss ; E. Grun ; P. R. Heck ; P. Hoppe ; B. Hudson ; J. Huth ; A. Kearsley ; A. J. King ; B. Lai ; J. Leitner ; L. Lemelle ; A. Leonard ; H. Leroux ; R. Lettieri ; W. Marchant ; R. Ogliore ; W. J. Ong ; M. C. Price ; S. A. Sandford ; J. A. Sans Tresseras ; S. Schmitz ; T. Schoonjans ; K. Schreiber ; G. Silversmit ; V. A. Sole ; R. Srama ; F. Stadermann ; T. Stephan ; J. Stodolna ; S. Sutton ; M. Trieloff ; P. Tsou ; T. Tyliszczak ; B. Vekemans ; L. Vincze ; J. Von Korff ; N. Wordsworth ; D. Zevin ; M. E. Zolensky
    American Association for the Advancement of Science (AAAS)
    Published 2014
    Staff View
    Publication Date:
    2014-08-16
    Publisher:
    American Association for the Advancement of Science (AAAS)
    Print ISSN:
    0036-8075
    Electronic ISSN:
    1095-9203
    Topics:
    Biology
    Chemistry and Pharmacology
    Computer Science
    Medicine
    Natural Sciences in General
    Physics
    Published by:
    http://www.aaas.org/

    Latest Papers from Table of Contents or Articles in Press
  4. 4
    P. Jenniskens ; M. D. Fries ; Q. Z. Yin ; M. Zolensky ; A. N. Krot ; S. A. Sandford ; D. Sears ; R. Beauford ; D. S. Ebel ; J. M. Friedrich ; K. Nagashima ; J. Wimpenny ; A. Yamakawa ; K. Nishiizumi ; Y. Hamajima ; M. W. Caffee ; K. C. Welten ; M. Laubenstein ; A. M. Davis ; S. B. Simon ; P. R. Heck ; E. D. Young ; I. E. Kohl ; M. H. Thiemens ; M. H. Nunn ; T. Mikouchi ; K. Hagiya ; K. Ohsumi ; T. A. Cahill ; J. A. Lawton ; D. Barnes ; A. Steele ; P. Rochette ; K. L. Verosub ; J. Gattacceca ; G. Cooper ; D. P. Glavin ; A. S. Burton ; J. P. Dworkin ; J. E. Elsila ; S. Pizzarello ; R. Ogliore ; P. Schmitt-Kopplin ; M. Harir ; N. Hertkorn ; A. Verchovsky ; M. Grady ; K. Nagao ; R. Okazaki ; H. Takechi ; T. Hiroi ; K. Smith ; E. A. Silber ; P. G. Brown ; J. Albers ; D. Klotz ; M. Hankey ; R. Matson ; J. A. Fries ; R. J. Walker ; I. Puchtel ; C. T. Lee ; M. E. Erdman ; G. R. Eppich ; S. Roeske ; Z. Gabelica ; M. Lerche ; M. Nuevo ; B. Girten ; S. P. Worden
    American Association for the Advancement of Science (AAAS)
    Published 2012
    Staff View
    Publication Date:
    2012-12-22
    Publisher:
    American Association for the Advancement of Science (AAAS)
    Print ISSN:
    0036-8075
    Electronic ISSN:
    1095-9203
    Topics:
    Biology
    Chemistry and Pharmacology
    Computer Science
    Medicine
    Natural Sciences in General
    Physics
    Published by:
    http://www.aaas.org/

    Latest Papers from Table of Contents or Articles in Press
  5. 5
    R. Mitchell ; J. M. Conley ; A. M. Davis ; R. J. Cadigan ; A. W. Dobson ; R. Q. Gladden
    American Association for the Advancement of Science (AAAS)
    Published 2011
    Staff View
    Publication Date:
    2011-04-16
    Publisher:
    American Association for the Advancement of Science (AAAS)
    Print ISSN:
    0036-8075
    Electronic ISSN:
    1095-9203
    Topics:
    Biology
    Chemistry and Pharmacology
    Computer Science
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Biological Specimen Banks/*ethics/legislation & jurisprudence ; Databases, Genetic/*ethics/legislation & jurisprudence ; Genetic Research/*ethics ; Genomics/*ethics ; Humans ; *Informed Consent ; Patents as Topic
    Published by:
    http://www.aaas.org/

    Latest Papers from Table of Contents or Articles in Press
  6. 6
    Afema, J. A., Ahmed, S., Besser, T. E., Jones, L. P., Sischo, W. M., Davis, M. A.
    The American Society for Microbiology (ASM)
    Published 2018
    Staff View
    Publication Date:
    2018-03-06
    Publisher:
    The American Society for Microbiology (ASM)
    Print ISSN:
    0099-2240
    Electronic ISSN:
    1098-5336
    Topics:
    Biology
    Published by:
    http://www.asm.org/

    Latest Papers from Table of Contents or Articles in Press
  7. 7
    Davis, M. A. ; Martin, K. A. ; Austin, S. J.

    Oxford, UK : Blackwell Publishing Ltd
    Published 1992
    Staff View
    ISSN:
    1365-2958
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Biology
    Medicine
    Notes:
    The unit-copy P1 plasmid depends for stability on a plasmld-encoded partition region called par, consisting of the parA and parB genes and the parS site. ParA is absolutely required for partition, but its partition-critical role is not known. Purified ParA protein is shown to possess an ATPase activity in vitro which is specifically stimulated by purified ParB protein and by DNA. ParA is responsible for regulation of expression of parA and parB, and purified ParA has an ATP-dependent, site-specific DNA binding activity which recognizes a sequence that overlaps the parA promoter. The rote of the ATP-dependence of the binding activity, as well as other possible functions of the ATPase activity in partition, is discussed.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1111/j.1365-2958.1992.tb01552.x

    Articles: DFG German National Licenses
  8. 8
    Davis, M. A. ; Radnedge, L. ; Martin, K. A. ; Hayes, F. ; Youngren, B. ; Austin, S. J.

    Oxford BSL : Blackwell Science Ltd
    Published 1996
    Staff View
    ISSN:
    1365-2958
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Biology
    Medicine
    Notes:
    The P1 ParA protein is an ATPase that recognizes the parA promoter region where it acts to autoregulate the P1 parA–parB operon. The ParB protein is essential for plasmid partition and recognizes the cis-acting partition site parS. The regulatory role of ParA is also essential because a controlled level of ParB protein is critical for partition. However, we show that this regulatory activity is not the only role for ParA in partition. Efficient partition can be achieved without autoregulation as long as Par protein levels are kept within a range of low values. The properties of ParA mutants in these conditions showed that ParA is essential for some critical step in the partition process that is independent of par operon regulation. The putative nucleotide-binding site for the ParA ATPase was identified and disrupted by mutation. The resulting mutant was substantially defective for autoregulation and completely inactive for partition in a system in which the need for autoregulation is abolished. Thus, the ParA nucleotide-binding site appears to be necessary both for the repressor activity of ParA and for some essential step in the partition process itself. We propose that the nucleotide-bound form of the enzyme adopts a configuration that favours binding to the operator, but that the ATPase activity of ParA is required for some energetic step in partition of the plasmid copies to daughter cells.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1046/j.1365-2958.1996.721423.x

    Articles: DFG German National Licenses
  9. 9
    Staff View
    ISSN:
    1432-0983
    Keywords:
    Key words Ustilago maydis ; GABA aminotransferase ; Heterologous expression ; Sequence conservation
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Biology
    Notes:
    Abstract  A gene encoding a putative GABA aminotransferase (ugatA) was isolated from the basidiomycete Ustilago maydis via heterologous hybridization to the GABA aminotransferase gene (gatA) of Aspergillus nidulans . The derived amino-acid sequence of ugatA shows strong identity throughout the protein to the GABA aminotransferase enzymes from A. nidulans and Saccharomyces cerevisiae. Northern analysis in U. maydis indicated that the ugatA transcript is inducible by the ω-amino acids GABA and β-alanine, and is not subject to nitrogen catabolite repression. With the use of ugatA promoter-lacZ fusion constructs, it was demonstrated that the removal of sequences located approximately 250 bp 5′ to the translational start site of ugatA (including multiple copies of a 7-bp direct repeat) resulted in the loss of induction by ω-amino acids. While the ugatA gene under the control of the A. nidulans gatA promoter was able to fully complement a gatA - phenotype in A. nidulans, the full-length ugatA gene was not, suggesting a lack of expression from the U. maydis promoter in A. nidulans. A U. maydis strain with a gene disruption at the ugatA locus showed decreased growth on β-alanine as a sole nitrogen source, but was able to grow on GABA as a sole nitrogen source, indicating an alternative pathway for the utilization of GABA in U. maydis.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/s002940050057

    Articles: DFG German National Licenses
  10. 10
    Macheda, Maria L. ; Hynes, Michael J. ; Davis, M. A.
    Springer
    Published 1999
    Staff View
    ISSN:
    1432-0983
    Keywords:
    Key wordsAspergillus nidulans ; Ammonium assimilation ; Glutamate synthase ; Gene inactivation ; Glutamate dehydrogenase
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Biology
    Notes:
    Abstract Mutants of Aspergillus nidulans lacking NADP-glutamate dehydrogenase activity grow more poorly than wild-type strains on ammonium as a sole nitrogen source. The leaky growth of these mutants is indicative of an alternative pathway of ammonium assimilation and glutamate biosynthesis. We have PCR-amplified a portion of the A. nidulans gene encoding glutamate synthase and used this sequence to inactivate the genomic copy. This gene, designated gltA, was found to be dispensable for growth on ammonium in the presence of NADP-glutamate dehydrogenase activity. However, a strain carrying the gltA inactivation together with an NADP-glutamate dehydrogenase structural gene mutation (gdhA) was unable to grow on ammonium or on nitrogen sources metabolized via ammonium. The gltA gene was located to linkage group V of the A. nidulans genetic map.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/s002940050421

    Articles: DFG German National Licenses
  11. 11
    Staff View
    ISSN:
    1617-4623
    Keywords:
    Aspergillus ; HAP3 ; CCAAT ; Gene regulation ; DNA binding
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Biology
    Notes:
    lacZ reporter gene and this effect is particularly evident under conditions of carbon limitation. Nuclear extracts prepared from thehapC deletion mutant show no CCAAT binding activity to theamdS orgatA promoters, indicating thathapC may encode a component of the complex binding at this sequence.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/BF02172369

    Articles: DFG German National Licenses
  12. 12
    Staff View
    ISSN:
    1617-4623
    Keywords:
    Key wordsAspergillus ; CCAAT ; HapC ; Hap complex ; DNA binding
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Biology
    Notes:
    Abstract The Aspergillus nidulans hapC gene was expressed as a fusion protein with MalE or glutathione-S-transferase (GST) in Escherichia coli, and used for the purification of HapC and the preparation of anti-HapC antiserum. The CCAAT-binding factor AnCP/AnCF contains a component with an approximate molecular mass of 32 kDa that cross-reacts with the antibody. The MalE-HapC fusion protein was able to replace authentic HapC in AnCP when incubated under appropriate conditions. Furthermore, reconstitution experiments with recombinant HapC, yHAP2 and yHAP5 polypeptides showed that all three polypeptides were required for the assembly of a complex capable of binding to CCAAT-containing taaG2 promoter DNA. The relationship between AnCP/AnCF and the Saccharomyces cerevisiae HAP complex is discussed.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/s004380050664

    Articles: DFG German National Licenses
  13. 13
    Staff View
    ISSN:
    1617-4623
    Keywords:
    Key words Acetate metabolism  ;  facB  ;  Zn(II)2Cys6 (C6 zinc) binuclear cluster  ;  Aspergillus  ;  Gene regulation
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Biology
    Notes:
    Abstract Genetic studies have indicated that the facB gene of Aspergillus nidulans is a major regulatory gene involved in acetamide and acetate utilisation. Sequencing of the facB gene revealed that it encodes a protein that contains an N-terminal GAL4-like Zn(II)2Cys6 (or C6 zinc) binuclear cluster for DNA binding, leucine zipper-like heptad repeat motifs and central and C-terminal acidic α-helical regions, consistent with a function as a DNA-binding transcriptional activator. The Zn(II)2Cys6 cluster shows strong similarity with those of the Saccharomyces cerevisiae carbon metabolism regulatory proteins CAT8 and SIP4. A significant level of similarity with CAT8 is found throughout the length of the protein, suggesting at least partial functional homology. The facB genes of Aspergillus oryzae and Aspergillus niger were also sequenced and found to be highly conserved. Deletion of the facB gene confirmed that it is required for growth on acetate as a sole carbon source. Functional dissection using deletion and fusion constructs and in vitro mutagenesis indicated that the Zn(II)2Cys6 cluster and the C-terminal end of the protein are required for function.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/s004380050444

    Articles: DFG German National Licenses
  14. 14
    Thayer, W. J. ; Davis, M. A.

    Hoboken, NJ : Wiley-Blackwell
    Published 1981
    Staff View
    ISSN:
    0730-6679
    Keywords:
    Chemistry ; Polymer and Materials Science
    Source:
    Wiley InterScience Backfile Collection 1832-2000
    Topics:
    Chemistry and Pharmacology
    Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Additional Material:
    15 Ill.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1002/adv.1981.060010307

    Articles: DFG German National Licenses