Статті в журналах з теми "Escherichia coli Inclusions"
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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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Kushnir, I. M., G. V. Kolodiy, V. I. Kushnir, S. D. Murska, I. S. Semen, and U. Z. Berbeka. "THE INFLUENCE OF POLYHEXAMETHYLENE GUANIDINE SALTS ON THE MICROBIOLOGICAL PARAMETERS OF WATER." Scientific and Technical Bulletin оf State Scientific Research Control Institute of Veterinary Medical Products and Fodder Additives аnd Institute of Animal Biology 22, no. 1 (March 29, 2021): 126–30. http://dx.doi.org/10.36359/scivp.2021-22-1.14.
Park, Youngjin, Mohd Amir F. Abdullah, Milton D. Taylor, Khalidur Rahman, and Michael J. Adang. "Enhancement of Bacillus thuringiensis Cry3Aa and Cry3Bb Toxicities to Coleopteran Larvae by a Toxin-Binding Fragment of an Insect Cadherin." Applied and Environmental Microbiology 75, no. 10 (March 27, 2009): 3086–92. http://dx.doi.org/10.1128/aem.00268-09.
Tam, Jeffrey E., Carolyn H. Davis, and Priscilla B. Wyrick. "Expression of recombinant DNA introduced into Chlamydia trachomatis by electroporation." Canadian Journal of Microbiology 40, no. 7 (July 1, 1994): 583–91. http://dx.doi.org/10.1139/m94-093.
Mifune, Jun, Katrin Grage, and Bernd H. A. Rehm. "Production of Functionalized Biopolyester Granules by Recombinant Lactococcus lactis." Applied and Environmental Microbiology 75, no. 14 (May 22, 2009): 4668–75. http://dx.doi.org/10.1128/aem.00487-09.
Parlane, Natalie A., D. Neil Wedlock, Bryce M. Buddle, and Bernd H. A. Rehm. "Bacterial Polyester Inclusions Engineered To Display Vaccine Candidate Antigens for Use as a Novel Class of Safe and Efficient Vaccine Delivery Agents." Applied and Environmental Microbiology 75, no. 24 (October 16, 2009): 7739–44. http://dx.doi.org/10.1128/aem.01965-09.
Kim, Won-Seok, Jeong Sun-Hyung, Ro-Dong Park, Kil-Yong Kim, and Hari B. Krishnan. "Sinorhizobium fredii USDA257 Releases a 22-kDa Outer Membrane Protein (Omp22) to the Extracellular Milieu When Grown in Calcium-Limiting Conditions." Molecular Plant-Microbe Interactions® 18, no. 8 (August 2005): 808–18. http://dx.doi.org/10.1094/mpmi-18-0808.
Gorbatuk, O. B., U. S. Nikolayev, D. M. Irodov, I. Ya Dubey, and P. V. Gilchuk. "Refolding of ScFv-CBD fusion protein from Escherichia coli inclusion bodies." Biopolymers and Cell 24, no. 1 (January 20, 2008): 51–59. http://dx.doi.org/10.7124/bc.000790.
Steinmann, Björn, Andreas Christmann, Tim Heiseler, Janine Fritz, and Harald Kolmar. "In Vivo Enzyme Immobilization by Inclusion Body Display." Applied and Environmental Microbiology 76, no. 16 (June 25, 2010): 5563–69. http://dx.doi.org/10.1128/aem.00612-10.
Johnson, Dustin L., Chris B. Stone, and James B. Mahony. "Interactions between CdsD, CdsQ, and CdsL, Three Putative Chlamydophila pneumoniae Type III Secretion Proteins." Journal of Bacteriology 190, no. 8 (February 15, 2008): 2972–80. http://dx.doi.org/10.1128/jb.01997-07.
Tzeng, Yih-Ling, Anup K. Datta, Cristy A. Strole, Michael A. Lobritz, Russell W. Carlson, and David S. Stephens. "Translocation and Surface Expression of Lipidated Serogroup B Capsular Polysaccharide in Neisseria meningitidis." Infection and Immunity 73, no. 3 (March 2005): 1491–505. http://dx.doi.org/10.1128/iai.73.3.1491-1505.2005.
Маркелова, Н. Ю., and N. Yu Markelova. "REP-elements of the Escherichia coli Genome and Transcription Signals: Positional and Functional Analysis." Mathematical Biology and Bioinformatics 10, no. 1 (June 24, 2015): 245–59. http://dx.doi.org/10.17537/2015.10.245.
Jürgen, Britta, Antje Breitenstein, Vlada Urlacher, Knut Büttner, Hongying Lin, Michael Hecker, Thomas Schweder, and Peter Neubauer. "Quality control of inclusion bodies in Escherichia coli." Microbial Cell Factories 9, no. 1 (2010): 41. http://dx.doi.org/10.1186/1475-2859-9-41.
HARTLEY, D. L., and J. F. KANE. "Properties of inclusion bodies from recombinant Escherichia coli." Biochemical Society Transactions 16, no. 2 (April 1, 1988): 101–2. http://dx.doi.org/10.1042/bst0160101.
Gilchuk, P. V. "Evaluation of renaturation methods for industrial obtaining of recombinant proteins from Escherichia coli inclusion bodies in biologically active form." Biopolymers and Cell 20, no. 3 (May 20, 2004): 182–92. http://dx.doi.org/10.7124/bc.0006a5.
Simpson, R. J. "Solubilization of Escherichia coli Recombinant Proteins from Inclusion Bodies." Cold Spring Harbor Protocols 2010, no. 9 (September 1, 2010): pdb.prot5485. http://dx.doi.org/10.1101/pdb.prot5485.
Kane, James F., and Donna L. Hartley. "Formation of recombinant protein inclusion bodies in Escherichia coli." Trends in Biotechnology 6, no. 5 (May 1988): 95–101. http://dx.doi.org/10.1016/0167-7799(88)90065-0.
Upadhyay, Vaibhav, Anupam Singh, and Amulya K. Panda. "Purification of recombinant ovalbumin from inclusion bodies of Escherichia coli." Protein Expression and Purification 117 (January 2016): 52–58. http://dx.doi.org/10.1016/j.pep.2015.09.015.
Bowden, Gregory A., Angel M. Paredes, and George Georgiou. "Structure and Morphology of Protein Inclusion Bodies in Escherichia Coli." Nature Biotechnology 9, no. 8 (August 1991): 725–30. http://dx.doi.org/10.1038/nbt0891-725.
Rueda, Fabián, Olivia Cano-Garrido, Uwe Mamat, Kathleen Wilke, Joaquin Seras-Franzoso, Elena García-Fruitós, and Antonio Villaverde. "Production of functional inclusion bodies in endotoxin-free Escherichia coli." Applied Microbiology and Biotechnology 98, no. 22 (August 17, 2014): 9229–38. http://dx.doi.org/10.1007/s00253-014-6008-9.
Carrió, M. Mar, and Antonio Villaverde. "Localization of Chaperones DnaK and GroEL in Bacterial Inclusion Bodies." Journal of Bacteriology 187, no. 10 (May 15, 2005): 3599–601. http://dx.doi.org/10.1128/jb.187.10.3599-3601.2005.
Allam, Ayman B., Leticia Reyes, Nacyra Assad-Garcia, John I. Glass, and Mary B. Brown. "Enhancement of Targeted Homologous Recombination in Mycoplasma mycoides subsp. capri by Inclusion of Heterologous recA." Applied and Environmental Microbiology 76, no. 20 (August 27, 2010): 6951–54. http://dx.doi.org/10.1128/aem.00056-10.
Hart, R. A., U. Rinas, and J. E. Bailey. "Protein composition of Vitreoscilla hemoglobin inclusion bodies produced in Escherichia coli." Journal of Biological Chemistry 265, no. 21 (July 1990): 12728–33. http://dx.doi.org/10.1016/s0021-9258(19)38405-4.
McCaman, M. T. "Fragments of prochymosin produced in Escherichia coli form insoluble inclusion bodies." Journal of Bacteriology 171, no. 2 (1989): 1225–27. http://dx.doi.org/10.1128/jb.171.2.1225-1227.1989.
Carretas-Valdez, Manuel I., Francisco J. Cinco-Moroyoqui, Marina J. Ezquerra-Brauer, Enrique Marquez-Rios, Idania E. Quintero-Reyes, Alonso A. Lopez-Zavala, and Aldo A. Arvizu-Flores. "Refolding and Activation from Bacterial Inclusion Bodies of Trypsin I from Sardine (Sardinops sagax caerulea)." Protein & Peptide Letters 26, no. 3 (March 15, 2019): 170–75. http://dx.doi.org/10.2174/0929866525666181019161114.
Di Lorenzo, Mirella, Aurelio Hidalgo, Michael Haas, and Uwe T. Bornscheuer. "Heterologous Production of Functional Forms of Rhizopus oryzae Lipase in Escherichia coli." Applied and Environmental Microbiology 71, no. 12 (December 2005): 8974–77. http://dx.doi.org/10.1128/aem.71.12.8974-8977.2005.
Lee, Sang-Eun. "Galactooligosaccharide Synthesis by Active β-Galactosidase Inclusion Bodies-Containing Escherichia coli Cells". Journal of Microbiology and Biotechnology 21, № 11 (28 листопада 2011): 1151–58. http://dx.doi.org/10.4014/jmb.1105.05021.
Morreale, G. "Continuous processing of fusion protein expressed as an Escherichia coli inclusion body." Journal of Chromatography B 786, no. 1-2 (March 25, 2003): 237–46. http://dx.doi.org/10.1016/s1570-0232(02)00718-3.
Lipničanová, Sabina, Daniela Chmelová, Andrej Godány, Miroslav Ondrejovič, and Stanislav Miertuš. "Purification of viral neuraminidase from inclusion bodies produced by recombinant Escherichia coli." Journal of Biotechnology 316 (June 2020): 27–34. http://dx.doi.org/10.1016/j.jbiotec.2020.04.005.
Hwang, Soon Ook. "Effect of inclusion bodies on the buoyant density of recombinant Escherichia coli." Biotechnology Techniques 10, no. 3 (March 1996): 157–60. http://dx.doi.org/10.1007/bf00158938.
Ni, He, Peng-Cheng Guo, Wei-Ling Jiang, Xiao-Min Fan, Xiang-Yu Luo, and Hai-Hang Li. "Expression of nattokinase in Escherichia coli and renaturation of its inclusion body." Journal of Biotechnology 231 (August 2016): 65–71. http://dx.doi.org/10.1016/j.jbiotec.2016.05.034.
Xia, Xiao-Xia, Ya-Ling Shen, and Dong-Zhi Wei. "Purification and Characterization of Recombinant sTRAIL Expressed in Escherichia coli." Acta Biochimica et Biophysica Sinica 36, no. 2 (February 1, 2004): 118–22. http://dx.doi.org/10.1093/abbs/36.2.118.
Dolgikh, V. V., I. V. Senderskiy, G. V. Tetz, and V. V. Tetz. "Optimization of the Protocol for the Isolation and Refolding of the Extracellular Domain of HER2 Expressed in Escherichia coli." Acta Naturae 6, no. 2 (June 15, 2014): 106–9. http://dx.doi.org/10.32607/20758251-2014-6-2-106-109.
Awofisayo-Okuyelu, Adedoyin, Julii Brainard, Ian Hall, and Noel McCarthy. "Incubation Period of Shiga Toxin–Producing Escherichia coli." Epidemiologic Reviews 41, no. 1 (2019): 121–29. http://dx.doi.org/10.1093/epirev/mxz001.
Alimuddin, Alimuddin, Indra Lesmana, Agus Oman Sudrajat, Odang Carman, and Irvan Faizal. "PRODUCTION AND BIOACTIVITY POTENTIAL OF THREE RECOMBINANT GROWTH HORMONES OF FARMED FISH." Indonesian Aquaculture Journal 5, no. 1 (June 30, 2010): 11. http://dx.doi.org/10.15578/iaj.5.1.2010.11-17.
Fan, Gaofu, Zhiguo Yu, Jie Tang, Ruomeng Dai та Zhenguo Xu. "Preparation of gallic acid-hydroxypropyl-β-cyclodextrin inclusion compound and study on its effect mechanism on Escherichia coli in vitro". Materials Express 11, № 5 (1 травня 2021): 655–62. http://dx.doi.org/10.1166/mex.2021.1968.
McCusker, Emily, та Anne Skaja Robinson. "Refolding of G protein α subunits from inclusion bodies expressed in Escherichia coli". Protein Expression and Purification 58, № 2 (квітень 2008): 342–55. http://dx.doi.org/10.1016/j.pep.2007.11.015.
Huang, Liurong, Haile Ma, Yunliang Li, and Shuxiang Li. "Antihypertensive activity of recombinant peptide IYPR expressed in Escherichia coli as inclusion bodies." Protein Expression and Purification 83, no. 1 (May 2012): 15–20. http://dx.doi.org/10.1016/j.pep.2012.02.004.
Valax, Pascal, and George Georgiou. "Molecular characterization of .beta.-lactamase inclusion bodies produced in Escherichia coli. 1. Composition." Biotechnology Progress 9, no. 5 (September 1993): 539–47. http://dx.doi.org/10.1021/bp00023a014.
Georgiou, G., J. N. Telford, M. L. Shuler, and D. B. Wilson. "Localization of inclusion bodies in Escherichia coli overproducing beta-lactamase or alkaline phosphatase." Applied and Environmental Microbiology 52, no. 5 (1986): 1157–61. http://dx.doi.org/10.1128/aem.52.5.1157-1161.1986.
Sinacola, Jessica R., and Anne S. Robinson. "Rapid refolding and polishing of single-chain antibodies from Escherichia coli inclusion bodies." Protein Expression and Purification 26, no. 2 (November 2002): 301–8. http://dx.doi.org/10.1016/s1046-5928(02)00538-7.