Auswahl der wissenschaftlichen Literatur zum Thema „Opdbk“

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Zeitschriftenartikel zum Thema "Opdbk"

1

Morty, Rory E., Vilmos Fülöp und Norma W. Andrews. „Substrate Recognition Properties of Oligopeptidase B from Salmonella enterica Serovar Typhimurium“. Journal of Bacteriology 184, Nr. 12 (15.06.2002): 3329–37. http://dx.doi.org/10.1128/jb.184.12.3329-3337.2002.

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ABSTRACT Oligopeptidase B (OpdB) is a serine peptidase broadly distributed among unicellular eukaryotes, gram-negative bacteria, and spirochetes which has emerged as an important virulence factor and potential therapeutic target in infectious diseases. We report here the cloning and expression of the opdB homologue from Salmonella enterica serovar Typhimurium and demonstrate that it exhibits amidolytic activity exclusively against substrates with basic residues in P1. While similar to its eukaryotic homologues in terms of substrate specificity, Salmonella OpdB differs significantly in catalytic power and inhibition and activation properties. In addition to oligopeptide substrates, restricted proteolysis of histone proteins was observed, although no cleavage was seen at or near residues that had been posttranslationally modified or at defined secondary structures. This supports the idea that the catalytic site of OpdB may be accessible only to unstructured oligopeptides, similar to the closely related prolyl oligopeptidase (POP). Salmonella OpdB was employed as a model enzyme to define determinants of substrate specificity that distinguish OpdB from POP, which hydrolyzes substrates exclusively at proline residues. Using site-directed mutagenesis, nine acidic residues that are conserved in OpdBs but absent from POPs were converted to their corresponding residues in POP. In this manner, we identified a pair of glutamic acid residues, Glu576 and Glu578, that define P1 specificity and direct OpdB cleavage C terminal to basic residues. We have also identified a second pair of residues, Asp460 and Asp462, that may be involved in defining P2 specificity and thus direct preferential cleavage by OpdB after pairs of basic residues.
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2

Tamber, Sandeep, Martina M. Ochs und Robert E. W. Hancock. „Role of the Novel OprD Family of Porins in Nutrient Uptake in Pseudomonas aeruginosa“. Journal of Bacteriology 188, Nr. 1 (01.01.2006): 45–54. http://dx.doi.org/10.1128/jb.188.1.45-54.2006.

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ABSTRACT To circumvent the permeability barrier of its outer membrane, Pseudomonas aeruginosa has evolved a series of specific porins. These channels have binding sites for related classes of molecules that facilitate uptake under nutrient-limited conditions. Here, we report on the identification of a 19-member family of porins similar to the basic-amino-acid-specific porin OprD. The members of this family fell into one of two phylogenetically distinct clusters, one bearing high similarity to OprD and the other bearing most similarity to the putative phenylacetic acid uptake porin PhaK of Pseudomonas putida. Analysis of the genome context, operon arrangement, and regulation of the PhaK-like porin OpdK indicated that it might be involved in vanillate uptake. This result was confirmed by demonstrating that an opdK mutant had a deficiency in the ability to grow on vanillate as a carbon source. To extrapolate these data to other paralogues within this family, the substrate specificities of 6 of the 17 remaining OprD homologues were inferred using an approach similar to that used with opdK. The specificities determined were as follows: OpdP, glycine-glutamate; OpdC, histidine; OpdB, proline; OpdT, tyrosine; OpdH, cis-aconitate; and OpdO, pyroglutamate. Thus, members of the OprD subfamily took up amino acids and related molecules, and those characterized members most similar to PhaK were responsible for the uptake of a diverse array of organic acids. These results imply that there is a functional basis for the phylogenetic clustering of these proteins and provide a framework for studying OprD homologues in other organisms.
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3

KUMAR, SANJAY, G. S. MANOHAR, S. K. GHORUI, S. K. KASHYAP und S. MAHERCHANDANI. „Isolation and molecular characterization of <i>oligopeptidase B</i> gene of <i>Trypanosoma evansi</i> from Indian dromedaries“. Indian Journal of Animal Sciences 84, Nr. 1 (30.01.2014): 3–7. http://dx.doi.org/10.56093/ijans.v84i1.37285.

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The aim of the study was isolation and molecular characterization of oligopeptidase B (opdB) gene of Trypanosoma evansi of camel. Genomic DNA of T. evansi was used to amplify the opdB gene by polymerase chain reaction then amplicon was cloned in a suitable plasmid vector and finally custom sequenced. The desired amplicon of opdB gene of T. evansi was amplified by PCR using gene specific primers. The amplicon of expected size was purified and then ligated to the pGEM- T Easy vector and ligated mixture was transformed into Escherichia coli JM109 strains for cloning. Screening of recombinants was done by restriction enzyme digestion of plasmid DNA. After confirmation of clone of opdB genes the plasmid DNA was sequenced and coding sequences of opdB gene according to the result obtained was of 2092 bp. Tree topology of opdB gene is based on the Neighbor-Joining method and and maximum parsimony method with 100% bootstrap values and identified opdB gene sequence showed a close homology with other Trypanosoma and Leishmania spp. gene sequences.
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4

Shi, X., B. K. Tay und S. P. Lau. „THE DOUBLE BEND FILTERED CATHODIC ARC TECHNOLOGY AND ITS APPLICATIONS“. International Journal of Modern Physics B 14, Nr. 02n03 (30.01.2000): 136–53. http://dx.doi.org/10.1142/s0217979200000145.

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A new Filtered Cathodic Vacuum Arc coating system with a magnetic macroparticle filter design consisting of an off-plane double-bend (OPDB) filter is described. The transport of the vacuum arc plasma through this OPDB filter is investigated using Langmuir and deposition probes. Films of amorphous hard carbon have been deposited a 90° single bend and the OPDB filter and the macroparticle contents of the films are compared. The experimental results were found to be in good agreement with the simulations results based on an improved drift approximation model. The results demonstrate the OPDB filter has a relatively better transmission efficiency than the 90° single bend filter, lower macroparticle counts and is suitable for preparation of diamond-like carbon coatings with high quality. Some important applications of the ta-C coating produced by using the new FCVA system have been identified and where applicable industrial testing results are presented.
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5

Pothula, Karunakar Reddy, und Ulrich Kleinekathöfer. „Theoretical analysis of ion conductance and gating transitions in the OpdK (OccK1) channel“. Analyst 140, Nr. 14 (2015): 4855–64. http://dx.doi.org/10.1039/c5an00036j.

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6

Fenno, J. Christopher, Si Young Lee, Christopher H. Bayer und Yu Ning. „The opdB Locus Encodes the Trypsin-Like Peptidase Activity of Treponema denticola“. Infection and Immunity 69, Nr. 10 (01.10.2001): 6193–200. http://dx.doi.org/10.1128/iai.69.10.6193-6200.2001.

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ABSTRACT High levels of Treponema denticola in subgingival dental plaque are associated with severe periodontal disease.T. denticola, along with Porphyromonas gingivalis and Bacteroides forsythus, are the only cultivatable oral microorganisms that produce significant amounts of “trypsin-like” peptidase activity. The ability of subgingival plaque to hydrolyzeN-α-benzoyl-dl-arginine-2-naphthylamide (BANA) is associated with high levels of one or more of these organisms. The purpose of this study was to identify the gene encoding trypsin-like activity in T. denticola and thus facilitate molecular-level studies of its potential role in disease. Using published peptide sequences of a T. denticolasurface-associated oligopeptidase with BANA-hydrolyzing activity, we identified the gene, designated opdB, in an apparently noncoding region of the T. denticola genome unannotated contigs (11/2000; http://www.tigr.org ). The opdB gene begins with a TTG start codon and encodes a 685-residue peptide with high homology to the oligopeptidase B family in prokaryotes and eukaryotes. An isogenic T. denticola opdB mutant was constructed by allelic replacement mutagenesis using anermF/AM gene cassette. The mutant lacked BANA-hydrolyzing activity and had a slightly slower growth rate than the parent strain. This mutant will be used in future studies of interactions of T. denticola with host cells and tissue.
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7

Zhang, Yufei, Yuehan Geng, Shengyang Li, Taozhong Shi, Xin Ma, Rimao Hua und Liancheng Fang. „Efficient Knocking Out of the Organophosphorus Insecticides Degradation Gene opdB in Cupriavidus nantongensis X1T via CRISPR/Cas9 with Red System“. International Journal of Molecular Sciences 24, Nr. 6 (22.03.2023): 6003. http://dx.doi.org/10.3390/ijms24066003.

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Cupriavidus nantongensis X1T is a type strain of the genus Cupriavidus, that can degrade eight kinds of organophosphorus insecticides (OPs). Conventional genetic manipulations in Cupriavidus species are time-consuming, difficult, and hard to control. The clustered regularly interspaced short palindromic repeat (CRISPR)/associated protein 9 (Cas9) system has emerged as a powerful tool for genome editing applied in prokaryotes and eukaryotes due to its simplicity, efficiency, and accuracy. Here, we combined CRISPR/Cas9 with the Red system to perform seamless genetic manipulation in the X1T strain. Two plasmids, pACasN and pDCRH were constructed. The pACasN plasmid contained Cas9 nuclease and Red recombinase, and the pDCRH plasmid contained the dual single-guide RNA (sgRNA) of organophosphorus hydrolase (OpdB) in the X1T strain. For gene editing, two plasmids were transferred to the X1T strain and a mutant strain in which genetic recombination had taken place, resulting in the targeted deletion of opdB. The incidence of homologous recombination was over 30%. Biodegradation experiments suggested that the opdB gene was responsible for the catabolism of organophosphorus insecticides. This study was the first to use the CRISPR/Cas9 system for gene targeting in the genus Cupriavidus, and it furthered our understanding of the process of degradation of organophosphorus insecticides in the X1T strain.
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8

Cheneke, Belete R., Bert van den Berg und Liviu Movileanu. „Three-State Discrete Kinetics of the OpdK Protein Pore“. Biophysical Journal 100, Nr. 3 (Februar 2011): 336a. http://dx.doi.org/10.1016/j.bpj.2010.12.2037.

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9

Wang, Sheng, Yiran Li, Huorong Li, Feifei Li, Chengjin Tian, Le Su, Yanshan Zhang et al. „Operon“. Proceedings of the VLDB Endowment 15, Nr. 12 (August 2022): 3332–45. http://dx.doi.org/10.14778/3554821.3554826.

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The past decade has witnessed the rapid development of cloud computing and data-centric applications. While these innovations offer numerous attractive features for data processing, they also bring in new issues about the loss of data ownership. Though some encrypted databases have emerged recently, they can not fully address these concerns for the data owner. In this paper, we propose an ownership-preserving database (OPDB), a new paradigm that characterizes different roles' responsibilities from nowadays applications and preserves data ownership throughout the entire application. We build Operon to follow the OPDB paradigm, which utilizes the trusted execution environment (TEE) and introduces a behavior control list (BCL). Different from access controls that merely handle accessibility permissions, BCL further makes data operation behaviors under control. Besides, we make Operon practical for real-world applications, by extending database capabilities towards flexibility, functionality and ease of use. Operon is the first database framework with which the data owner exclusively controls its data across different roles' subsystems. We have successfully integrated Operon with different TEEs, i.e. , Intel SGX and an FPGA-based implementation, and various database services on Alibaba Cloud, i.e. , PolarDB and RDS PostgreSQL. The evaluation shows that Operon achieves 71% - 97% of the performance of plaintext databases under the TPC-C benchmark while preserving the data ownership.
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10

Biswas, Shyamasri, Mohammad M. Mohammad, Liviu Movileanu und Bert van den Berg. „Crystal Structure of the Outer Membrane Protein OpdK from Pseudomonas aeruginosa“. Structure 16, Nr. 7 (Juli 2008): 1027–35. http://dx.doi.org/10.1016/j.str.2008.04.009.

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