Thematische Bibliographien / Escherichia coli Inclusions

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Auswahl der wissenschaftlichen Literatur zum Thema „Escherichia coli Inclusions“

Autor: Grafiati

Veröffentlicht am 4. Juni 2021

Zuletzt aktualisiert am 1. Februar 2022

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Zeitschriftenartikel zum Thema "Escherichia coli Inclusions"

Hänisch, Jan, Marc Wältermann, Horst Robenek, and Alexander Steinbüchel. "The Ralstonia eutropha H16 phasin PhaP1 is targeted to intracellular triacylglycerol inclusions in Rhodococcus opacus PD630 and Mycobacterium smegmatis mc2155, and provides an anchor to target other proteins." Microbiology 152, no. 11 (November 1, 2006): 3271–80. http://dx.doi.org/10.1099/mic.0.28969-0.

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In Ralstonia eutropha, the H16 phasin PhaP1 represents the major phasin that binds to the surface of polyhydroxyalkanoate (PHA) inclusions. In this study, C-terminal fusions of PhaP1 with enhanced green fluorescent protein (eGFP) and with Escherichia coli β-galactosidase (LacZ) were expressed separately in the triacylglycerol (TAG)-accumulating actinomycetes Rhodococcus opacus PD630 and Mycobacterium smegmatis mc2155, employing the M. smegmatis acetamidase (ace) promoter of the Escherichia–Mycobacterium/Rhodococcus shuttle plasmid pJAM2. PhaP1 and the PhaP1 fusion proteins were expressed stabl

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Chen, Shuxiong, Natalie A. Parlane, Jason Lee, D. Neil Wedlock, Bryce M. Buddle, and Bernd H. A. Rehm. "New Skin Test for Detection of Bovine Tuberculosis on the Basis of Antigen-Displaying Polyester Inclusions Produced by Recombinant Escherichia coli." Applied and Environmental Microbiology 80, no. 8 (February 14, 2014): 2526–35. http://dx.doi.org/10.1128/aem.04168-13.

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ABSTRACTThe tuberculin skin test for diagnosing tuberculosis (TB) in cattle lacks specificity if animals are sensitized to environmental mycobacteria, as some antigens in purified protein derivative (PPD) prepared fromMycobacterium bovisare present in nonpathogenic mycobacteria. Three immunodominant TB antigens, ESAT6, CFP10, and Rv3615c, are present in members of the pathogenicMycobacterium tuberculosiscomplex but absent from the majority of environmental mycobacteria. These TB antigens have the potential to enhance skin test specificity. To increase their immunogenicity, these antigens were

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Davis, Katelin L., Liang Cheng, José Ramos-Vara, Melissa D. Sánchez, Rebecca P. Wilkes, and Mario F. Sola. "Malakoplakia in the Urinary Bladder of 4 Puppies." Veterinary Pathology 58, no. 4 (April 23, 2021): 699–704. http://dx.doi.org/10.1177/03009858211009779.

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Malakoplakia in humans most often affects the urinary bladder and is characterized by inflammation with von Hansemann–type macrophages, with or without Michaelis-Gutmann bodies, and is frequently associated with Escherichia coli infection. We describe the microscopic features of malakoplakia in the urinary bladder of 4 puppies. In all cases, the lamina propria of the urinary bladder was markedly expanded by sheets of large, round to polygonal macrophages with intracytoplasmic, periodic acid-Schiff-positive granules and granular inclusions, and rare Prussian blue–positive inclusions. Macrophage

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Wada, Y., H. Kondo, Y. Nakaoka, and M. Kubo. "Gastric Attaching and Effacing Escherichia coli Lesions in a Puppy with Naturally Occurring Enteric Colibacillosis and Concurrent Canine Distemper Virus Infection." Veterinary Pathology 33, no. 6 (November 1996): 717–20. http://dx.doi.org/10.1177/030098589603300615.

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A puppy suffering from chronic diarrhea was humanely killed at 90 days of age. Numerous Gram-negative bacilli were found adhering to the surface of as well as within epithelial cells from the stomach to the colon. Canine distemper virus inclusions were in the epithelial cytoplasm of the esophageal, gastric, and intestinal mucosa. Typical attaching and effacing ultrastructural lesions were in the stomach, and some bacilli were in the cytoplasm of the epithelial cells, Escherichia coli, isolated from the contents of the small intestine, belonged to serotype 0118: NM and were negative for plasmid

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Aldrich, H. C., S. Elvington, HE Machines, R. Szabady, K. Feder, L. McDowell, and J. M. Shively. "Ultrastructural and Cytochemical Analyses of the Expression of the Thiobacillus Carboxysome Operon in Escherichia Coli." Microscopy and Microanalysis 7, S2 (August 2001): 740–41. http://dx.doi.org/10.1017/s1431927600029779.

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The cytoplasm of the bacterium Thiobacillus neapolitanus contains 117 nm diameter polyhedral inclusions, “carboxysomes” (Fig. 1) that contain ribulose-1,5- bisphosphate carboxylase/oxygenase (RuBisCO). Surrounding the polyhedron are nonmembranous proteinaceous plates devoid of lipid. The carboxysomes are composed of at least 8 major peptides, all coded within the same operon. Six (CsoSIA, CsoSIB, CsoSIC, CsoS2A, CsoS2B, and CsoS3) make up the shell, and two are the large (CbbL) and small subunits (CbbS) of RuBisCO. Using immunogold labeling on ultrathin sections, peptides CsoS2A, CsoS2B, and C

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Blatchford, Paul A., Colin Scott, Nigel French, and Bernd H. A. Rehm. "Immobilization of organophosphohydrolase OpdA from Agrobacterium radiobacter by overproduction at the surface of polyester inclusions inside engineered Escherichia coli." Biotechnology and Bioengineering 109, no. 5 (December 26, 2011): 1101–8. http://dx.doi.org/10.1002/bit.24402.

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Kalscheuer, Rainer, Tim Stöveken, Heinrich Luftmann, Ursula Malkus, Rudolf Reichelt, and Alexander Steinbüchel. "Neutral Lipid Biosynthesis in Engineered Escherichia coli: Jojoba Oil-Like Wax Esters and Fatty Acid Butyl Esters." Applied and Environmental Microbiology 72, no. 2 (February 2006): 1373–79. http://dx.doi.org/10.1128/aem.72.2.1373-1379.2006.

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ABSTRACT Wax esters are esters of long-chain fatty acids and long-chain fatty alcohols which are of considerable commercial importance and are produced on a scale of 3 million tons per year. The oil from the jojoba plant (Simmondsia chinensis) is the main biological source of wax esters. Although it has a multitude of potential applications, the use of jojoba oil is restricted, due to its high price. In this study, we describe the establishment of heterologous wax ester biosynthesis in a recombinant Escherichia coli strain by coexpression of a fatty alcohol-producing bifunctional acyl-coenzyme

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Petrus, Marloes L. C., Lukas A. Kiefer, Pranav Puri, Evert Heemskerk, Michael S. Seaman, Dan H. Barouch, Sagrario Arias, Gilles P. van Wezel, and Menzo Havenga. "A microbial expression system for high-level production of scFv HIV-neutralizing antibody fragments in Escherichia coli." Applied Microbiology and Biotechnology 103, no. 21-22 (October 22, 2019): 8875–88. http://dx.doi.org/10.1007/s00253-019-10145-1.

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Abstract Monoclonal antibodies (mABs) are of great biopharmaceutical importance for the diagnosis and treatment of diseases. However, their production in mammalian expression hosts usually requires extensive production times and is expensive. Escherichia coli has become a new platform for production of functional small antibody fragment variants. In this study, we have used a rhamnose-inducible expression system that allows precise control of protein expression levels. The system was first evaluated for the cytoplasmic production of super folder green fluorescence protein (sfGFP) in various pr

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Carija, Pinheiro, Iglesias, and Ventura. "Computational Assessment of Bacterial Protein Structures Indicates a Selection Against Aggregation." Cells 8, no. 8 (August 8, 2019): 856. http://dx.doi.org/10.3390/cells8080856.

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The aggregation of proteins compromises cell fitness, either because it titrates functional proteins into non-productive inclusions or because it results in the formation of toxic assemblies. Accordingly, computational proteome-wide analyses suggest that prevention of aggregation upon misfolding plays a key role in sequence evolution. Most proteins spend their lifetimes in a folded state; therefore, it is conceivable that, in addition to sequences, protein structures would have also evolved to minimize the risk of aggregation in their natural environments. By exploiting the AGGRESCAN3D structu

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Rybalchenko, O. V., O. G. Orlova, L. B. Zakharova, O. N. Vishnevskaya, and A. G. Markov. "EFFECT OF PROBIOTIC BACTERIA AND LIPOPOLISACCHARIDES ON EPITELIOCYTES TIGHT JUNCTIONS OF RAT JEJUNUM." Journal of microbiology epidemiology immunobiology, no. 6 (December 28, 2017): 80–87. http://dx.doi.org/10.36233/0372-9311-2017-6-80-87.

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Aim. The present study has been undertaken with the main objective the influence of probiotic bacteria Lactobacillus plantarum 8 РАЗ and Escherichia coli M17 and lipopolysaccharide on the ultrastructure of enterocytes tight junctions of mucous membranes of rat jejunum. Materials and methods. The study was carried out on E. coli lipopolysaccharide (Sigma-Aldrich, Germany) and probiotic bacteria L. plantarum 8PA3 and E. coli M17. Male Wistar rats were used. A comparative analysis of the ultrathin structure of enterocytes and tight junctions were carried out by successive incubation of rat jejunu

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Dissertationen zum Thema "Escherichia coli Inclusions"

RODRIGUES, DANIELLA. "Utilização de altas pressões hidrostáticas para o estudo e renaturação de proteínas com estrutura quaternária." reponame:Repositório Institucional do IPEN, 2012. http://repositorio.ipen.br:8080/xmlui/handle/123456789/10161.

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Made available in DSpace on 2014-10-09T12:35:27Z (GMT). No. of bitstreams: 0 Made available in DSpace on 2014-10-09T14:06:25Z (GMT). No. of bitstreams: 0 Dissertação (Mestrado) IPEN/D Instituto de Pesquisas Energeticas e Nucleares - IPEN-CNEN/SP

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Wangsa-Wirawan, Norbertus Djajasantosa. "Physicochemical properties of protein inclusion bodies." Title page, contents and introduction only, 1999. http://web4.library.adelaide.edu.au/theses/09PH/09phw2465.pdf.

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Bibliography: leaves 182-198. Improvements in the current production system of inclusion bodies and the downstream processing sequence are essential to maintain a competitive advantage in the market place. Optimisation of fermentation is considered to improve production yield; then flotation as a possible inclusion body recovery method.

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BALDUINO, KELI N. "Renaturacao em altas pressoes hidrostaticas de proteinas recombinantes agregadas em corpos de inclusao produzidos em Eschirichia coli." reponame:Repositório Institucional do IPEN, 2009. http://repositorio.ipen.br:8080/xmlui/handle/123456789/9457.

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Made available in DSpace on 2014-10-09T12:26:58Z (GMT). No. of bitstreams: 0 Made available in DSpace on 2014-10-09T14:03:47Z (GMT). No. of bitstreams: 0 Dissertacao (Mestrado) IPEN/D Instituto de Pesquisas Energeticas e Nucleares - IPEN-CNEN/SP

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Wong, Heng Ho. "Modelling studies of the interaction between homogenisation, centrifugation and inclusion body dissolution /." Title page, contents and summary only, 1997. http://web4.library.adelaide.edu.au/theses/09PH/09phw8718.pdf.

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Saulou, Claire. "Evaluation des propriétés anti-adhésives et biocides de films nanocomposites avec inclusions d’argent, déposés sur acier inoxydable par procédé plasma." Toulouse, INSA, 2009. http://eprint.insa-toulouse.fr/archive/00000315/.

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Dans le secteur biomédical et l’industrie agro-alimentaire, l’adhésion de microorganismes contaminants aux surfaces engendre de multiples impacts négatifs, à la fois en termes de santé publique, d’hygiène et de sécurité alimentaire. Dans ce contexte, l’objectif de l’étude est de mettre au point un traitement de surface de l’acier inoxydable 316L, afin de prévenir la colonisation microbienne. La modification des surfaces d’acier par traitement chimique ou physique n’a eu aucune incidence sur le détachement de Saccharomyces cerevisiae, évalué in vitro à l’aide d’une chambre à écoulement cisaillé

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Hart, Roger A. Bailey James E. Bailey James E. "Characterization of Vitreoscilla hemoglobin inclusion bodies produced in Escherichia coli /." Diss., Pasadena, Calif. : California Institute of Technology, 1991. http://resolver.caltech.edu/CaltechETD:etd-06272007-152616.

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Olbrich, Richard. "The characterisation and recovery of protein inclusion bodies from recombinant Escherichia-coli." Thesis, University College London (University of London), 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.324583.

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Garcia, i. Fruitós Elena. "Regulation of recombinant proteína solubility and conformational quality in Escherichia coli." Doctoral thesis, Universitat Autònoma de Barcelona, 2008. http://hdl.handle.net/10803/3923.

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All the processes that take place in a cell require one or more proteins, meaning that they are essential components of life. Proteins are macromolecules consisting of amino acid units, all of them being constructed with combinations of only 20 amino acids. The primary structure of a protein molecule is determined by the sequence of amino acids connected by peptide bonds forming a polypeptide chain. Once the amino acid chain is synthesized, the protein folds by a physical process that might be eventually assisted by other proteins, reaching its characteristic three‐dimensional structure

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Mikkola, Isak. "Does SCP-2 promote the expression of foreign proteins in Escherichia coli?" Thesis, Linköpings universitet, Biologi, 2016. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-129802.

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Expression of foreign proteins in host organisms usually results in the development of insoluble, inactive proteins. Further, these proteins have a tendency to form aggregates termed inclusion bodies. However, the formation of inclusion bodies can be avoided by fusing the gene encoding the foreign protein to a highly soluble protein. In this report Sterol Carrier Protein-2 (SCP-2) is reviewed as a possible solubility tag. The experiment was carried out by fusing SCP-2 to one of two i nsoluble proteins, Green fluorescent protein (GFP) or a form of chloramphenicol acetyl transferase (CAT∆9). The

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Hedhammar, My. "Strategies for facilitated production of recombinant proteins in escherichia coli." Doctoral thesis, KTH, School of Biotechnology (BIO), 2005. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-471.

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The successful genomic era has resulted in a great demand for efficient production and purification of proteins. The main objective of the work described in this thesis was to develop methods to facilitate recovery of target proteins after recombinant production in Escherichia coli.A positively charged purification tag, Zbasic, has previously been constructed by protein design of a compact three-helix bundle domain, Z. The charged domain was investigated for general use as a fusion partner. All target proteins investigated could be selectively captured by ion-exchange chro

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Bücher zum Thema "Escherichia coli Inclusions"

Henderson, Ian. Solving the inclusion body problem: A case study : high level expression of TEM-1 [beta]-lactamase in Escherichia coli. [s.l.]: typescript, 1993.

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Buchteile zum Thema "Escherichia coli Inclusions"

Garcìa-Fruitòs, Elena, Nuria Gonzàlez-Montalbàn, Mònica Martìnez-Alonso, Ursula Rinas, and Antonio Villaverde. "Systems-Level Analysis of Protein Quality in Inclusion Body-Forming Escherichia coli Cells." In Systems Biology and Biotechnology of Escherichia coli, 295–326. Dordrecht: Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-1-4020-9394-4_15.

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Williamson, Richard A. "Refolding of TIMP-2 from Escherichia coli Inclusion Bodies." In Methods in Molecular Biology, 111–21. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60327-299-5_7.

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Mouillac, Bernard, and Jean-Louis Banères. "Mammalian Membrane Receptors Expression as Inclusion Bodies in Escherichia coli." In Methods in Molecular Biology, 39–48. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60761-344-2_3.

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Panda, Amulya K. "Bioprocessing of Therapeutic Proteins from the Inclusion Bodies of Escherichia coli." In Biotechnology in India II, 43–93. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/3-540-36466-8_3.

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Lee, Wen-Chien, and Shao-Yen Hsu. "Over-Expression of Functionally Active Inclusion Bodies of Enzymes in Recombinant Escherichia coli." In Emerging Areas in Bioengineering, 21–33. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2018. http://dx.doi.org/10.1002/9783527803293.ch2.

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Burgess, Richard R. "[12] Purification of overproduced Escherichia coli RNA polymerase σ factors by solubilizing inclusion bodies and refolding from Sarkosyl." In Methods in Enzymology, 145–49. Elsevier, 1996. http://dx.doi.org/10.1016/s0076-6879(96)73014-8.

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