Luo R

References (8)

Title : Acetylcholinesterase Biosensor Based On Mesoporous Hollow Carbon Spheres\/Core-Shell Magnetic Nanoparticles-Modified Electrode for the Detection of Organophosphorus Pesticides - Luo_2018_Sensors.(Basel)_18_
Author(s) : Luo R , Feng Z , Shen G , Xiu Y , Zhou Y , Niu X , Wang H
Ref : Sensors (Basel) , 18 : , 2018
Abstract : The present study investigated the synthesis of mesoporous hollow carbon spheres (MHCS) and magnetic mesoporous hollow carbon spheres with core-shell structures (Fe(3)O(4)@MHCS). Two acetylcholinesterase sensors (acetylcholinesterase/mesoporous hollow carbon spheres/glassy carbon electrode (AChE/MHCS/GCE) and acetylcholinesterase/core-shell magnetic mesoporous hollow carbon spheres/glassy carbon electrode (AChE/Fe(3)O(4)@MHCS/GCE) based on mesoporous carbon materials were prepared. Under the optimum conditions, using Malathion as the model compound, the developed biosensors showed a wide detection range, low detection limit, good reproducibility, and high stability. The AChE/MHCS/GCE electrochemical sensor response exhibited two good linear ranges at the incubation time of 10 min at the Malathion concentration ranges of 0.01 to 100 ppb and 100 to 600 ppb, with a detection limit of 0.0148 ppb (S/N = 3). The AChE/Fe(3)O(4)@MHCS/GCE electrochemical sensor that was operated with an incubation time of 12 min at the malathion concentration ranges between 0.01(-)50 ppb and 50(-)600 ppb had a detection limit of 0.0182 ppb (S/N = 3). Moreover, the AChE/MHCS/GCE and AChE/Fe(3)O(4)@MHCS/GCE biosensors were effective for the detection of real samples, and were demonstrated to be suitable for the field-testing of organophosphorus pesticide (OP) residues.
ESTHER : Luo_2018_Sensors.(Basel)_18_
PubMedSearch : Luo_2018_Sensors.(Basel)_18_
PubMedID: 30558201

Title : Crystal Structure of StnA for the Biosynthesis of Antitumor Drug Streptonigrin Reveals a Unique Substrate Binding Mode - Qian_2017_Sci.Rep_7_40254
Author(s) : Qian T , Wo J , Zhang Y , Song Q , Feng G , Luo R , Lin S , Wu G , Chen HF
Ref : Sci Rep , 7 :40254 , 2017
Abstract : Streptonigrin methylesterase A (StnA) is one of the tailoring enzymes that modify the aminoquinone skeleton in the biosynthesis pathway of Streptomyces species. Although StnA has no significant sequence homology with the reported alpha/beta-fold hydrolases, it shows typical hydrolytic activity in vivo and in vitro. In order to reveal its functional characteristics, the crystal structures of the selenomethionine substituted StnA (SeMet-StnA) and the complex (S185A mutant) with its substrate were resolved to the resolution of 2.71 A and 2.90 A, respectively. The overall structure of StnA can be described as an alpha-helix cap domain on top of a common alpha/beta hydrolase domain. The substrate methyl ester of 10'-demethoxystreptonigrin binds in a hydrophobic pocket that mainly consists of cap domain residues and is close to the catalytic triad Ser185-His349-Asp308. The transition state is stabilized by an oxyanion hole formed by the backbone amides of Ala102 and Leu186. The substrate binding appears to be dominated by interactions with several specific hydrophobic contacts and hydrogen bonds in the cap domain. The molecular dynamics simulation and site-directed mutagenesis confirmed the important roles of the key interacting residues in the cap domain. Structural alignment and phylogenetic tree analysis indicate that StnA represents a new subfamily of lipolytic enzymes with the specific binding pocket located at the cap domain instead of the interface between the two domains.
ESTHER : Qian_2017_Sci.Rep_7_40254
PubMedSearch : Qian_2017_Sci.Rep_7_40254
PubMedID: 28074848
Gene_locus related to this paper: 9actn-l7pij2

Title : First Draft Genome Sequence of the Pathogenic Fungus Lomentospora prolificans (Formerly Scedosporium prolificans) - Luo_2017_G3.(Bethesda)_7_3831
Author(s) : Luo R , Zimin A , Workman R , Fan Y , Pertea G , Grossman N , Wear MP , Jia B , Miller H , Casadevall A , Timp W , Zhang SX , Salzberg SL
Ref : G3 (Bethesda) , 7 :3831 , 2017
Abstract : Here we describe the sequencing and assembly of the pathogenic fungus Lomentospora prolificans using a combination of short, highly accurate Illumina reads and additional coverage in very long Oxford Nanopore reads. The resulting assembly is highly contiguous, containing a total of 37,627,092 bp with over 98% of the sequence in just 26 scaffolds. Annotation identified 8896 protein-coding genes. Pulsed-field gel analysis suggests that this organism contains at least 7 and possibly 11 chromosomes, the two longest of which have sizes corresponding closely to the sizes of the longest scaffolds, at 6.6 and 5.7 Mb.
ESTHER : Luo_2017_G3.(Bethesda)_7_3831
PubMedSearch : Luo_2017_G3.(Bethesda)_7_3831
PubMedID: 28963165
Gene_locus related to this paper: 9pezi-a0a2n3nij3 , 9pezi-a0a2n3mzq9 , 9pezi-a0a2n3n7y4

Title : Separation and purification of bioactive botrallin and TMC-264 by a combination of HSCCC and semi-preparative HPLC from endophytic fungus Hyalodendriella sp. Ponipodef12 - Mao_2014_World.J.Microbiol.Biotechnol_30_2533
Author(s) : Mao Z , Luo R , Luo H , Tian J , Liu H , Yue Y , Wang M , Peng Y , Zhou L
Ref : World J Microbiol Biotechnol , 30 :2533 , 2014
Abstract : Two dibenzo-alpha-pyrones, botrallin (1) and TMC-264 (2) were preparatively separated from crude ethyl acetate extract of the endophytic fungus Hyalodendriella sp. Ponipodef12, which was isolated from the hybrid 'Neva' of Populus deltoides Marsh x P. nigra L. using a combination of high-speed counter-current chromatography (HSCCC) and semi-preparative HPLC. Botrallin (1) with 74.73 % of purity and TMC-264 (2) with 82.29 % of purity were obtained through HSCCC by employing a solvent system containing n-hexane-ethyl acetate-methanol-water at a volume ratio of 1.2:1.0:0.9:1.0. It was the first time for TMC-264 (2) to be isolated from this fungus. TMC-264 (2) showed strong antimicrobial and antinematodal activity, and botrallin (1) exhibited moderate inhibitory activity on acetylcholinesterase.
ESTHER : Mao_2014_World.J.Microbiol.Biotechnol_30_2533
PubMedSearch : Mao_2014_World.J.Microbiol.Biotechnol_30_2533
PubMedID: 24898177

Title : Genome sequence of Mycoplasma iowae strain 695, an unusual pathogen causing deaths in turkeys - Wei_2012_J.Bacteriol_194_547
Author(s) : Wei S , Guo Z , Li T , Zhang T , Li X , Zhou Z , Li Z , Liu M , Luo R , Bi D , Chen H , Zhou R , Jin H
Ref : Journal of Bacteriology , 194 :547 , 2012
Abstract : Mycoplasma iowae is associated mainly with reduced hatchability in turkeys and is well known for the unusual ability of phenotypic variation in the Mycoplasma surface components as well as a relative resistance to heat, bile salts, and many antimicrobials. A subset of unique genes and a gene cluster responsible for these characteristics could be identified from the genome. Here, we report the first genome sequence of this species.
ESTHER : Wei_2012_J.Bacteriol_194_547
PubMedSearch : Wei_2012_J.Bacteriol_194_547
PubMedID: 22207750

Title : The oyster genome reveals stress adaptation and complexity of shell formation - Zhang_2012_Nature_490_49
Author(s) : Zhang G , Fang X , Guo X , Li L , Luo R , Xu F , Yang P , Zhang L , Wang X , Qi H , Xiong Z , Que H , Xie Y , Holland PW , Paps J , Zhu Y , Wu F , Chen Y , Wang J , Peng C , Meng J , Yang L , Liu J , Wen B , Zhang N , Huang Z , Zhu Q , Feng Y , Mount A , Hedgecock D , Xu Z , Liu Y , Domazet-Loso T , Du Y , Sun X , Zhang S , Liu B , Cheng P , Jiang X , Li J , Fan D , Wang W , Fu W , Wang T , Wang B , Zhang J , Peng Z , Li Y , Li N , Chen M , He Y , Tan F , Song X , Zheng Q , Huang R , Yang H , Du X , Chen L , Yang M , Gaffney PM , Wang S , Luo L , She Z , Ming Y , Huang W , Huang B , Zhang Y , Qu T , Ni P , Miao G , Wang Q , Steinberg CE , Wang H , Qian L , Liu X , Yin Y
Ref : Nature , 490 :49 , 2012
Abstract : The Pacific oyster Crassostrea gigas belongs to one of the most species-rich but genomically poorly explored phyla, the Mollusca. Here we report the sequencing and assembly of the oyster genome using short reads and a fosmid-pooling strategy, along with transcriptomes of development and stress response and the proteome of the shell. The oyster genome is highly polymorphic and rich in repetitive sequences, with some transposable elements still actively shaping variation. Transcriptome studies reveal an extensive set of genes responding to environmental stress. The expansion of genes coding for heat shock protein 70 and inhibitors of apoptosis is probably central to the oyster's adaptation to sessile life in the highly stressful intertidal zone. Our analyses also show that shell formation in molluscs is more complex than currently understood and involves extensive participation of cells and their exosomes. The oyster genome sequence fills a void in our understanding of the Lophotrochozoa.
ESTHER : Zhang_2012_Nature_490_49
PubMedSearch : Zhang_2012_Nature_490_49
PubMedID: 22992520
Gene_locus related to this paper: cragi-k1qzk7 , cragi-k1rad0 , cragi-k1p6v9 , cragi-k1pa46 , cragi-k1pga2 , cragi-k1pp63 , cragi-k1pwa8 , cragi-k1q0b1.1 , cragi-k1q0b1.2 , cragi-k1q1h2 , cragi-k1q2z6 , cragi-k1qaj8 , cragi-k1qaw5 , cragi-k1qhl5 , cragi-k1qly1 , cragi-k1qqb1.1 , cragi-k1qqb1.2 , cragi-k1qs61 , cragi-k1qs99 , cragi-k1qwl6 , cragi-k1r068 , cragi-k1r0n3.1 , cragi-k1r0n3.2 , cragi-k1r0r4 , cragi-k1r1i9 , cragi-k1r8q9 , cragi-k1rgi1 , cragi-k1rig4 , cragi-k1s0a7.1 , cragi-k1s0a7.2 , cragi-k1s0a7.3 , cragi-k1q6q0 , cragi-k1rru1 , cragi-k1qfi4 , cragi-k1qvm5 , cragi-k1qq58 , cragi-k1qdc0 , cragi-k1r754 , cragi-k1pje5 , cragi-k1qca6 , cragi-k1qdt5 , cragi-k1qkz7 , cragi-k1rgd2 , cragi-k1puh6 , cragi-k1raz4 , cragi-k1qqj4 , cragi-k1rbs1

Title : Complete genome sequence of Mycoplasma hyopneumoniae strain 168 - Liu_2011_J.Bacteriol_193_1016
Author(s) : Liu W , Feng Z , Fang L , Zhou Z , Li Q , Li S , Luo R , Wang L , Chen H , Shao G , Xiao S
Ref : Journal of Bacteriology , 193 :1016 , 2011
Abstract : Mycoplasma hyopneumoniae strain 168, a pathogenic strain prevalent in China, was isolated in 1974. Although this strain has been widespread for a long time, the genome sequence had not been determined. Here, we announce the complete genome sequence of M. hyopneumoniae strain 168.
ESTHER : Liu_2011_J.Bacteriol_193_1016
PubMedSearch : Liu_2011_J.Bacteriol_193_1016
PubMedID: 21148737

Title : Complete genome sequence of Mycoplasma hyorhinis strain HUB-1 - Liu_2010_J.Bacteriol_192_5844
Author(s) : Liu W , Fang L , Li S , Li Q , Zhou Z , Feng Z , Luo R , Shao G , Wang L , Chen H , Xiao S
Ref : Journal of Bacteriology , 192 :5844 , 2010
Abstract : Mycoplasma hyorhinis is generally considered a swine pathogen yet is most commonly found infecting laboratory cell lines. An increasing body of evidence suggests that chronic infections with M. hyorhinis may cause oncogenic transformation. Here, we announce the complete genome sequence of M. hyorhinis strain HUB-1.
ESTHER : Liu_2010_J.Bacteriol_192_5844
PubMedSearch : Liu_2010_J.Bacteriol_192_5844
PubMedID: 20802032