Relevant bibliographies by topics / Proteins Escherichia coli

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Proteins Escherichia coli'

Author: Grafiati
Published: 4 June 2021
Last updated: 28 January 2023

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Journal articles on the topic "Proteins Escherichia coli"

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Siegele, Deborah A. "Universal Stress Proteins in Escherichia coli." Journal of Bacteriology 187, no. 18 (2005): 6253–54. http://dx.doi.org/10.1128/jb.187.18.6253-6254.2005.

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Blair, D. F., D. Y. Kim, and H. C. Berg. "Mutant MotB proteins in Escherichia coli." Journal of Bacteriology 173, no. 13 (1991): 4049–55. http://dx.doi.org/10.1128/jb.173.13.4049-4055.1991.

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Tang, Fengyi, and Milton H. Saier. "Transport proteins promoting Escherichia coli pathogenesis." Microbial Pathogenesis 71-72 (June 2014): 41–55. http://dx.doi.org/10.1016/j.micpath.2014.03.008.

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Gill, Stanley C., Stephen E. Weitzel та Peter H. von Hippel. "Escherichia coli σ70 and NusA proteins". Journal of Molecular Biology 220, № 2 (1991): 307–24. http://dx.doi.org/10.1016/0022-2836(91)90015-x.

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Gill, Stanley C., Thomas D. Yager та Peter H. von Hippel. "Escherichia coli σ70 and NusA proteins". Journal of Molecular Biology 220, № 2 (1991): 325–33. http://dx.doi.org/10.1016/0022-2836(91)90016-y.

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Hayat, Seyed Mohammad Gheibi, Najmeh Farahani, Behrouz Golichenari, and Amirhossein Sahebkar. "Recombinant Protein Expression in Escherichia coli (E.coli): What We Need to Know." Current Pharmaceutical Design 24, no. 6 (2018): 718–25. http://dx.doi.org/10.2174/1381612824666180131121940.

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Background: Host, vector, and culture conditions (including cultivation media) are considered among the three main elements contributing to a successful production of recombinant proteins. Accordingly, one of the most common hosts to produce recombinant therapeutic proteins is Escherichia coli. Methodology: A comprehensive literature review was performed to identify important factors affecting production of recombinant proteins in Escherichia coli. Results: Escherichia coli is taken into account as the easiest, quickest, and cheapest host with a fully known genome. Thus, numerous modifications
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Schumann, Wolfgang, and Luis Carlos S. Ferreira. "Production of recombinant proteins in Escherichia coli." Genetics and Molecular Biology 27, no. 3 (2004): 442–53. http://dx.doi.org/10.1590/s1415-47572004000300022.

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BANEYX, FRANÇOIS, and GEORGE GEORGIOU. "Degradation of Secreted Proteins in Escherichia coli." Annals of the New York Academy of Sciences 665, no. 1 Biochemical E (1992): 301–8. http://dx.doi.org/10.1111/j.1749-6632.1992.tb42593.x.

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Weber, Richard F., and Philip M. Silverman. "The Cpx proteins of Escherichia coli K12." Journal of Molecular Biology 203, no. 2 (1988): 467–78. http://dx.doi.org/10.1016/0022-2836(88)90013-7.

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Riley, M. "Genes and proteins of Escherichia coli (GenProtEc)." Nucleic Acids Research 24, no. 1 (1996): 40. http://dx.doi.org/10.1093/nar/24.1.40.

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Dissertations / Theses on the topic "Proteins Escherichia coli"

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Orchard, Lisa Marguerite Denise. "The 1-phosphofructokinase of Escherichia coli." Thesis, University of Cambridge, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.259621.

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Schlegel, Susan. "From protein production to genome evolution in Escherichia coli." Doctoral thesis, Stockholms universitet, Institutionen för biokemi och biofysik, 2013. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-94993.

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The aim of my Ph.D. studies was to improve production yields of membrane- and secretory proteins in the widely used E. coli protein production strain BL21(DE3). In this strain expression of the gene encoding the protein of interest is driven by the powerful T7 RNA polymerase (T7 RNAP) whose gene is located on the chromosome and under control of the strong, IPTG-inducible lacUV5 promoter. Unfortunately, the production of many membrane and secretory proteins is 'toxic' to BL21(DE3), resulting in poor growth and low production yields. To understand this ‘toxicity’, the BL21(DE3) derived mutant st
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Seppälä, Susanna. "Dual-topology membrane proteins in Escherichia coli." Doctoral thesis, Stockholms universitet, Institutionen för biokemi och biofysik, 2011. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-61944.

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Cellular life, as we know it, is absolutely dependent on biological membranes; remarkable superstructures made of lipids and proteins. For example, all living cells are surrounded by at least one membrane that protects the cell and holds it together. The proteins that are embedded in the membranes carry out a wide variety of key functions, from nutrient uptake and waste disposal to cellular respiration and communication. In order to function accurately, any integral membrane protein needs to be inserted into the cellular membrane where it belongs, and in that particular membrane it has to atta
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Potamitou, Aristi. "Characterization and function of Escherichia coli glutaredoxins /." Stockholm, 2003. http://diss.kib.ki.se/2003/91-7349-458-5/.

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Fu, Zhibiao. "Studies of protein secretion in escherichia coli /." View abstract or full-text, 2006. http://library.ust.hk/cgi/db/thesis.pl?BICH%202006%20FU.

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Misra, Rajeev. "Studies on the TolC protein of Escherichia coli K-12 and its effect on OmpF expression." Title page, table of contents and abstract only, 1986. http://web4.library.adelaide.edu.au/theses/09PH/09phm678.pdf.

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Handford, Jennifer Iris. "Investigation of conserved, essential proteins in Escherichia coli." Thesis, University of East Anglia, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.441617.

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Yue, Kevin Kin Man. "Assembly of outer membrane proteins in Escherichia coli." Thesis, University of Liverpool, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.257436.

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Martinez, Eric. "Exploitation of NHERF proteins by diarrheagenic Escherichia coli." Thesis, Imperial College London, 2010. http://hdl.handle.net/10044/1/6352.

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Enteropathogenic (EPEC) and enterohaemorrhagic (EHEC) Escherichia coli cause severe disease with symptoms ranging from mild diarrhoea to haemolytic uremic syndrome. During infection of the gut, these bacteria provoke attaching and effacing lesions (A/E lesions), characterised by intimate bacterial attachment and effacement of microvilli from the surface of enterocytes. A type III secretion system (T3SS), encoded by the locus of enterocyte effacement (LEE), allows EPEC and EHEC to inject more than twenty effector proteins into the host cell cytoplasm and to manipulate a large number of cellular
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Thomas, Jeffrey G. "Molecular chaperones and the folding of recombinant proteins in Escherichia coli /." Thesis, Connect to this title online; UW restricted, 1998. http://hdl.handle.net/1773/9881.

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Books on the topic "Proteins Escherichia coli"

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Hengge-Aronis, Regine. Studies of secretion of periplasmic proteins in Escherichia coli. Hartung-Gorre, 1986.

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Karlsson, Jenny. Functional and structural analysis of the membrane domain of proton-translocating Escherichia coli Transhydrogenase. Department of Chemistry, Biochemistry and Physices, Göteborg University, 2006.

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Savery, Nigel Jonathan. High level expression of recombinant proteins from the Escherichia coli nirB promoter. University of Birmingham, 1993.

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Lipscombe, Martin John. Construction and characterisation of "Escherichia coli" heat-labile toxin B-subunit fusion proteins. typescript, 1991.

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Kreutzenbeck, Peter Johannes. Export von Proteinen mit Zwillingsarginin-Signalsequenzen über den Tat-Weg in Escherichia coli. Forschungszentrum Jülich, Zentralbibliothek, 2005.

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Fredriksson, Åsa. On the role of protein oxidation and heat shock proteins in senescence and fitness. Göteborg University, 2006.

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Levente, Emödy, and FEMS Symposium on Genes and Proteins Underlying Microbial Urinary Tract Virulence: Basic Aspects and Applications (1999 : Pécs, Hungary), eds. Genes and proteins underlying microbial urinary tract virulence: Basic aspects and applications. Kluwer Academic/Plenum Publishers, 2000.

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Williams, Jacqueline Claire. Studies on the Escherichia coli transcription activator protein MelR. University of Birmingham, 1994.

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Sebaihia, Mohammed. The effect of chlorpromazine on protein phosphorylation in "Escherichia coli". typescript, 1988.

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Gaston, Kevin Leon. Studies on the cyclic AMP receptor protein of 'Escherichia Coli'. University of Birmingham, 1989.

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Book chapters on the topic "Proteins Escherichia coli"

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Altenbuchner, Josef, and Ralf Mattes. "Escherichia coli." In Production of Recombinant Proteins. Wiley-VCH Verlag GmbH & Co. KGaA, 2005. http://dx.doi.org/10.1002/3527603670.ch2.

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Wick, Kyle L., and Kathleen S. Matthews. "Escherichia coli Repressor Proteins." In Molecular Biology of Chromosome Function. Springer New York, 1989. http://dx.doi.org/10.1007/978-1-4612-3652-8_6.

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Paton, Adrienne W., Hui Wang, and James C. Paton. "BiP (Grp78): A Target for Escherichia coli Subtilase Cytotoxin." In Heat Shock Proteins. Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-6787-4_20.

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Prasadarao, Nemani V. "Escherichia coli K1 Meningitis and Heat Shock Protein, gp96." In Heat Shock Proteins. Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-6787-4_23.

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Nash, Howard A. "The HU and IHF Proteins: Accessory Factors for Complex Protein-DNA Assemblies." In Regulation of Gene Expression in Escherichia coli. Springer US, 1996. http://dx.doi.org/10.1007/978-1-4684-8601-8_8.

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Lossius, I., A. Holck, R. Aasland, L. Haarr, and K. Kleppe. "Proteins Associated with Chromatin from Escherichia coli." In Proceedings in Life Sciences. Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-71266-1_9.

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Hughes, R. K., Z. Wu, D. S. Robinson, and R. Casey. "Production of Pea Seed Lipoxygenases in Escherichia coli." In Plant Proteins from European Crops. Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-662-03720-1_16.

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Yadav, Janardan, Prem Narayan Yadav, Edward Arnold, Swamy Laxminarayan, and Mukund J. Modak. "Molecular modeling of the interactions between Escherichia coli DNA polymerase I and substrates." In Proteins. Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-010-9063-6_49.

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Mergulhão, Filipe J., and Gabriel A. Monteiro. "Periplasmic Targeting of Recombinant Proteins in Escherichia coli." In Protein Targeting Protocols. Humana Press, 2007. http://dx.doi.org/10.1007/978-1-59745-466-7_4.

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Drew, David, Linda Fröderberg, Louise Baars, Joen Luirink, and Jan-Willem de Gier. "Assembly of Inner Membrane Proteins in Escherichia Coli." In Protein Secretion Pathways in Bacteria. Springer Netherlands, 2003. http://dx.doi.org/10.1007/978-94-010-0095-6_4.

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Conference papers on the topic "Proteins Escherichia coli"

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Orjuela-Canon, Alvaro David, Diana C. Rodriguez Burbano, and Oscar Perdomo. "Data Fusion Analysis for Determining Localization of Proteins Associated to Escherichia coli." In 2022 IEEE Colombian Conference on Applications of Computational Intelligence (ColCACI). IEEE, 2022. http://dx.doi.org/10.1109/colcaci56938.2022.9905354.

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Mirzahoseini, Hasan, Samaneh Mafakheri, Somayeh Enayati, and Nahid Mortazavi. "Heterologous proteins expression in Escherichia coli: investigation of the effect of codon usage and expression host optimization." In Proceedings of the III International Conference on Environmental, Industrial and Applied Microbiology (BioMicroWorld2009). WORLD SCIENTIFIC, 2010. http://dx.doi.org/10.1142/9789814322119_0121.

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Jewel, Yead, Prashanta Dutta, and Jin Liu. "Coarse-Grained Molecular Dynamics Simulations of Sugar Transport Across Lactose Permease." In ASME 2015 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2015. http://dx.doi.org/10.1115/imece2015-52337.

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Sugar (one of the critical nutrition elements for all life forms) transport across the cell membranes play essential roles in a wide range of living organism. One of the most important active transport (against the sugar concentration) mechanisms is facilitated by the transmembrane transporter proteins, such as the Escherichia coli lactose permease (LacY) proteins. Active transport of sugar molecules with LacY proteins requires a proton gradient and a sequence of complicated protein conformational changes. However, the exact molecular mechanisms and the protein structural information involved
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"The minimal medium irradiated with terahertz radiation induces proteins of homeostasis of transition metal ions and represses proteins of amino acid metabolism when Escherichia coli cells are cultivated on it." In Bioinformatics of Genome Regulation and Structure/Systems Biology (BGRS/SB-2022) :. Institute of Cytology and Genetics, the Siberian Branch of the Russian Academy of Sciences, 2022. http://dx.doi.org/10.18699/sbb-2022-313.

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Pannekok, H., A. J. Van Zonneveid, C. J. M. de vries, M. E. MacDonald, H. Veerman, and F. Blasi. "FUNCTIONAL PROPERTIES OF DELETION-MUTANTS OF TISSUE-TYPE PLASMINOGEN ACTIVATOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643724.

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Over the past twenty-five years, genetic methods have generated a wealth of information on the regulation and the structure-function relationship of bacterial genes.These methods are based on the introduction of random mutations in a gene to alter its function. Subsequently, genetic techniques cure applied to localize the mutation, while the nature of the impairedfunction could be determined using biochemical methods. Classic examples of this approach is now considered to be the elucidation of the structure and function of genes, constituting the Escherichia coli lactose (lac) and tryptophan (
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Marlon S Thomas. "Protein coated Biosensor for rapid Escherichia coli Detection." In 2011 Louisville, Kentucky, August 7 - August 10, 2011. American Society of Agricultural and Biological Engineers, 2011. http://dx.doi.org/10.13031/2013.37185.

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Di, Y. P., X. Zhang, L. Huleihel, N. Remlinger, and T. W. Gilbert. "Extracellular Matrix Protects Host from Escherichia Coli-Induced Respiratory Infection." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a6162.

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Vu, S. K., A. A. Belloti, C. J. Gabriel, et al. "Modeling ribosome dynamics to optimize heterologous protein production in escherichia coli." In 2014 IEEE Global Conference on Signal and Information Processing (GlobalSIP). IEEE, 2014. http://dx.doi.org/10.1109/globalsip.2014.7032363.

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Vilkhovoy, M., N. Horvath, and J. D. Varner. "Toward genome scale modeling of Escherichia coli cell-free protein synthesis." In IET/SynbiCITE Engineering Biology Conference. Institution of Engineering and Technology, 2016. http://dx.doi.org/10.1049/cp.2016.1253.

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Baldiris, Rosa, and Ricardo Vivas Reyes. "Estudio de proteínas reductoras de cromo en Eschericha coli." In The Fourteen LACCEI International Multi-Conference for Engineering, Education, and Technology: “Engineering Innovations for Global Sustainability”. Latin American and Caribbean Consortium of Engineering Institutions, 2016. http://dx.doi.org/10.18687/laccei2016.1.1.337.

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Reports on the topic "Proteins Escherichia coli"

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Flowers, Ann M. Secretion of Heterologous Proteins from Escherichia coli. Defense Technical Information Center, 2000. http://dx.doi.org/10.21236/ada391190.

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Cheng, S. Repair of psoralen crosslinks in Escherichia coli: In vitro studies with the RecA protein and (A)BC excinuclease. Office of Scientific and Technical Information (OSTI), 1990. http://dx.doi.org/10.2172/7192240.

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Wackett, Lawrence, Raphi Mandelbaum, and Michael Sadowsky. Bacterial Mineralization of Atrazine as a Model for Herbicide Biodegradation: Molecular and Applied Aspects. United States Department of Agriculture, 1999. http://dx.doi.org/10.32747/1999.7695835.bard.

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Atrazine is a broadly used herbicide in agriculture and it was used here as a model to study the biodegradation of herbicides. The bacterium Pseudomonas sp. ADP metabolizes atrazine to carbon dioxide and ammonia and chloride. The genes encoding atrazine catabolism to cyanuric acid were cloned and expressed in Escherichia coli. The genes were designated atzA, atzB and atzC. Each gene was sequenced. The enzyme activities were characterized. AtzA is atrazine chlorohydrolase which takes atrazine to hydroxyatrizine. AtzB is hydroxyatrazine N-ethylaminohydrolase which produces N-isopropylammelide an
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