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  • BioMed Central  (30)
  • Nature Publishing Group
  • 2010-2014  (27)
  • 2005-2009  (5)
  • 1930-1934  (4)
  • 1
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    Thermodynamic analysis of DNA binding by a Bacillus single stranded DNA binding protein (2012)
    BioMed Central
    Details
    Publication Date: 2012-06-15
    Description: Background: Single-stranded DNA binding proteins (SSB) are essential for DNA replication, repair, and recombination in all organisms. SSB works in concert with a variety of DNA metabolizing enzymes such as DNA polymerase. Results: We have cloned and purified SSB from Bacillus anthracis (SSBBA). In the absence of DNA, at concentrations [less than or equal to]100 mug/ml, SSBBA did not form a stable tetramer and appeared to resemble bacteriophage T4 gene 32 protein. Fluorescence anisotropy studies demonstrated that SSBBA bound ssDNA with high affinity comparable to other prokaryotic SSBs. Thermodynamic analysis indicated both hydrophobic and ionic contributions to ssDNA binding. FRET analysis of oligo(dT)70 binding suggested that SSBBA forms a tetrameric assembly upon ssDNA binding. This report provides evidence of a bacterial SSB that utilizes a novel mechanism for DNA binding through the formation of a transient tetrameric structure. Conclusions: Unlike other prokaryotic SSB proteins, SSBBA from Bacillus anthracis appeared to be monomeric at concentrations [less than or equal to]100 mug/ml as determined by SE-HPLC. SSBBA retained its ability to bind ssDNA with very high affinity, comparable to SSB proteins which are tetrameric. In the presence of a long ssDNA template, SSBBA appears to form a transient tetrameric structure. Its unique structure appears to be due to the cumulative effect of multiple key amino acid changes in its sequence during evolution, leading to perturbation of stable dimer and tetramer formation. The structural features of SSBBA could promote facile assembly and disassembly of the protein-DNA complex required in processes such as DNA replication.
    Electronic ISSN: 1471-2091
    Topics: Chemistry and Pharmacology
    Published by BioMed Central
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  • 2
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    Thermodynamic analysis of DNA binding by a Bacillus single stranded DNA binding protein (2012)
    BioMed Central
    Details
    Publication Date: 2012-01-01
    Electronic ISSN: 1471-2091
    Topics: Chemistry and Pharmacology
    Published by BioMed Central
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  • 3
    Electronic Resource
    Electronic Resource
    On the design and analysis of gene expression studies in human populations (2007)
    [s.l.] : Nature Publishing Group
    Nature genetics 39 (2007), S. 807-808 
    Details
    ISSN: 1546-1718
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] To the Editor: In a recent Nature Genetics Letter entitled “Common genetic variants account for differences in gene expression among ethnic groups,” Spielman et al. estimate the number of genes differentially expressed between individuals of European (CEU) and Asian (ASN) ancestry and ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/ng0707-807
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Structural insight into OprD substrate specificity (2007)
    [s.l.] : Nature Publishing Group
    Nature structural & molecular biology 14 (2007), S. 1108-1109 
    Details
    ISSN: 1545-9985
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] OprD proteins form a large family of substrate-specific outer-membrane channels in Gram-negative bacteria. We report here the X-ray crystal structure of OprD from Pseudomonas aeruginosa, which reveals a monomeric 18-stranded β-barrel characterized by a very narrow pore constriction, with a ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nsmb1304
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  • 5
    Electronic Resource
    Electronic Resource
    Synthesis of Munjisthin. (1930)
    [s.l.] : Nature Publishing Group
    Nature 126 (1930), S. 761-761 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] MUNJISTHIN, a dihydroxyanthraquinone carboxylio acid occurring in Rubia tinctorum, Rubia sikkimensis, and Rubia munjistha, has been synthesised by us in the following way : 2 chloro-6-methoxy toluene (Ullmann and Pan-chaud; Annalen, 350, 108; 1906) is condensed with phthalic anhydride in ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/126761a0
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  • 6
    Electronic Resource
    Electronic Resource
    Synthesis of Munjisthin. (1931)
    [s.l.] : Nature Publishing Group
    Nature 127 (1931), S. 166-166 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A MISTAKE in nomenclature has, through our inadvertence, crept into our communication on the “Synthesis of Munjisthin”, published in NATURE of Nov. 15, 1930, page 761, which we hasten to rectify. In line 6, par. 2, instead of " 2 - chloro - 3 methyl -4 methoxy ", read " 1 - chloro - 2 ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/127166e0
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  • 7
    Electronic Resource
    Electronic Resource
    Freshwater Biological Research in the Indian Empire. (1930)
    [s.l.] : Nature Publishing Group
    Nature 125 (1930), S. 670-670 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] I HAVE read with deep interest the article by Prof. F. E. Fritsch under the title of “Research in Freshwater Biology and the Functions of a Freshwater Biological Station”, published in NATURE of Feb. 15 (vol. 125, p. 241). Work in this line is imperative in the Indian Empire. Algological ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/125670a0
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  • 8
    Electronic Resource
    Electronic Resource
    Photo-Oxidation of Nitrite to Nitrate (1934)
    [s.l.] : Nature Publishing Group
    Nature 133 (1934), S. 213-214 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] THERE is considerable difference of opinion regarding the possibility of the oxidation of nitrites by oxygen to nitrates. Berzelius reported that when aqueous solutions of alkali nitrites are boiled in air, they absorb oxygen with the formation of nitrates. G. Lunge and E. Frémy, J. ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/133213b0
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  • 9
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    A novel GPR40 agonist, CNX-011-67, suppresses glucagon secretion in pancreatic islets under chronic glucolipotoxic conditions in vitro (2014)
    BioMed Central
    Details
    Publication Date: 2014-09-04
    Description: Background: Elevated glucose concentrations lead to increased insulin secretion and suppression of glucagon secretion. In fact, insulin is a physiological inhibitor of glucagon secretion. Type 2 diabetes mellitus (T2DM) patients have defects in insulin secretion. In addition to this, lack of suppression of glucagon secretion under elevated glucose concentrations is also observed in T2DM patients. We have earlier shown that GPR40 activation by CNX-011-67 stimulates glucose stimulated insulin secretion (GSIS). Here we extended our studies to examine the impact of GPR40 activation by CNX-011-67 on glucagon secretion from intact islets under both normal and glucolipotoxic conditions.FindingsGlucagon secretion from intact rat islets was suppressed under elevated glucose concentration. Activation of GPR40 by CNX-011-67 further suppressed glucagon secretion. Culturing islets under chronic glucolipotoxic (GL) conditions, we have observed increased high glucose mediated glucagon secretion and content which were reduced with GPR40 activation by CNX-011-67. Interestingly, expression of pre-proglucagon gene (GCG) remained unchanged under glucolipotoxicity in the presence or absence of GPR40 activation. Conclusion: Activation of GPR40 by CNX-011-67 can reduce glucagon secretion from pancreatic islets.
    Electronic ISSN: 1756-0500
    Topics: Biology , Medicine
    Published by BioMed Central
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  • 10
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    Molecular cloning and in-silico characterization of high temperature stress responsive pAPX gene isolated from heat tolerant Indian wheat cv. Raj 3765 (2014)
    BioMed Central
    Details
    Publication Date: 2014-10-11
    Description: Background: Heat stress leads to accelerated production of reactive oxygen species (ROS) which causes a huge amount of oxidative damage to the cellular components of plants. A large number of heat stress related genes as HSPs, catalases, peroxidases are overexpressed at the time of stress. A potent stress responsive gene peroxisomal ascorbate peroxidase (TapAPX) obtained from heat stress (42[degree sign]C) responsive subtractive cDNA library from a thermo tolerant wheat cv. Raj3765 at anthesis stage was cloned, characterized and its role was validated under heat stress by proteomics and in-silico studies.. In the present study we report the characterization at molecular and in-silico level of peroxisomal TapAPX gene isolated from heat tolerant wheat cultivar of India. Results: qPCR studies of TapAPX gene displayed up to 203 fold level of expression at 42[degree sign]C heat stress exposure. A full length cDNA of 876 bp obtained by RACE deduced a protein of 292 amino acid residues which gives a complete 3D structure of pAPX by homology modeling. TapAPX cDNA was cloned in expression vector pET28 (a+) and the recombinant protein over-expressed in E. coli BL21 showed highest homology with APX protein as deduced by peptide mass fingerprinting. Conclusions: TapAPX gene from wheat cv Raj3765 has a distinct role in conferring thermo tolerance to the plants and thus can be used in crop improvement programmes for development of crops tolerant to high temperature.
    Electronic ISSN: 1756-0500
    Topics: Biology , Medicine
    Published by BioMed Central
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