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1

Southan, Christopher. "Purification and analysis of recombinant proteins." Trends in Biotechnology 10 (1992): 226. http://dx.doi.org/10.1016/0167-7799(92)90226-l.

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Kermasha, S., and I. Alli. "Purification and analysis of recombinant proteins." Food Research International 26, no. 2 (January 1993): 158–59. http://dx.doi.org/10.1016/0963-9969(93)90072-q.

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Kaufman, Randal J. "Mammalian recombinant proteins: Structure, function and immunological analysis." Current Opinion in Biotechnology 1, no. 2 (December 1990): 141–50. http://dx.doi.org/10.1016/0958-1669(90)90023-e.

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Senear, Donald F., Robert A. Mendelson, Deborah B. Stone, Linda A. Luck, Elena Rusinova, and J. B. Alexander Ross. "Quantitative Analysis of Tryptophan Analogue Incorporation in Recombinant Proteins." Analytical Biochemistry 300, no. 1 (January 2002): 77–86. http://dx.doi.org/10.1006/abio.2001.5441.

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Kollárovič, G., D. Majera, K. Luciaková, and P. Baráth. "Expression and purification of recombinant NFI proteins for functional analysis." General Physiology and Biophysics 28, no. 4 (2009): 331–39. http://dx.doi.org/10.4149/gpb_2009_04_331.

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Coutinho, M., K. S. Aulak, and A. E. Davis. "Functional analysis of the serpin domain of C1 inhibitor." Journal of Immunology 153, no. 8 (October 15, 1994): 3648–54. http://dx.doi.org/10.4049/jimmunol.153.8.3648.

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Abstract To analyze the role of the heavily glycosylated amino-terminal domain of C1 inhibitor in protease inhibitory activity, two truncated C1 inhibitor molecules were constructed. The abilities of the recombinant truncated inhibitors to complex with target proteases were compared with that of the wild-type recombinant protein. One recombinant truncated molecule consisted of amino acid residues 76 to 478 (C-serp(76)) and the other of residues 98 to 478 (C-serp(98)). The recombinant proteins were each expressed in similar quantities. The thermal denaturation profiles of the two truncated prot
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Jerlström-Hultqvist, Jon, Britta Stadelmann, Sandra Birkestedt, Ulf Hellman, and Staffan G. Svärd. "Plasmid Vectors for Proteomic Analyses in Giardia: Purification of Virulence Factors and Analysis of the Proteasome." Eukaryotic Cell 11, no. 7 (May 18, 2012): 864–73. http://dx.doi.org/10.1128/ec.00092-12.

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ABSTRACTIn recent years, proteomics has come of age with the development of efficient tools for purification, identification, and characterization of gene products predicted by genome projects. The intestinal protozoanGiardia intestinaliscan be transfected, but there is only a limited set of vectors available, and most of them are not user friendly. This work delineates the construction of a suite of cassette-based expression vectors for use inGiardia. Expression is provided by the strong constitutive ornithine carbamoyltransferase (OCT) promoter, and tagging is possible in both N- and C-termi
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Sims, Andrew H., Manda E. Gent, Karin Lanthaler, Nigel S. Dunn-Coleman, Stephen G. Oliver, and Geoffrey D. Robson. "Transcriptome Analysis of Recombinant Protein Secretion by Aspergillus nidulans and the Unfolded-Protein Response In Vivo." Applied and Environmental Microbiology 71, no. 5 (May 2005): 2737–47. http://dx.doi.org/10.1128/aem.71.5.2737-2747.2005.

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ABSTRACT Filamentous fungi have a high capacity for producing large amounts of secreted proteins, a property that has been exploited for commercial production of recombinant proteins. However, the secretory pathway, which is key to the production of extracellular proteins, is rather poorly characterized in filamentous fungi compared to yeast. We report the effects of recombinant protein secretion on gene expression levels in Aspergillus nidulans by directly comparing a bovine chymosin-producing strain with its parental wild-type strain in continuous culture by using expressed sequence tag micr
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Zeck, Anne, Jörg Thomas Regula, Vincent Larraillet, Björn Mautz, Oliver Popp, Ulrich Göpfert, Frank Wiegeshoff, et al. "Low Level Sequence Variant Analysis of Recombinant Proteins: An Optimized Approach." PLoS ONE 7, no. 7 (July 6, 2012): e40328. http://dx.doi.org/10.1371/journal.pone.0040328.

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Viseux, N., X. Hronowski, J. Delaney, and B. Domon. "Qualitative and Quantitative Analysis of the Glycosylation Pattern of Recombinant Proteins." Analytical Chemistry 73, no. 20 (October 2001): 4755–62. http://dx.doi.org/10.1021/ac015560a.

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Coulot, M., B. Domon, H. Grossenbacher, C. Guenat, W. Maerki, D. R. Müller, and W. J. Richter. "LC-MS and MS/MS in the analysis of recombinant proteins." Journal of Molecular Structure 292 (March 1993): 89–103. http://dx.doi.org/10.1016/0022-2860(93)80092-a.

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Steen, Johanna, Margareta Ramström, Mathias Uhlén, Sophia Hober, and Jenny Ottosson. "Automated sample preparation method for mass spectrometry analysis on recombinant proteins." Journal of Chromatography A 1216, no. 20 (May 2009): 4457–64. http://dx.doi.org/10.1016/j.chroma.2009.03.041.

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Bischoff, Rainer, Dominique Roecklin, and Carolyn Roitsch. "Analysis of recombinant proteins by isoelectric focusing in immobilized pH gradients." Electrophoresis 13, no. 1 (1992): 214–19. http://dx.doi.org/10.1002/elps.1150130144.

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Fei, Dongliang, Yaxi Guo, Qiong Fan, Ming Li, Li Sun, Mingxiao Ma, and Yijing Li. "Codon optimization, expression in Escherichia coli, and immunogenicity analysis of deformed wing virus (DWV) structural protein." PeerJ 8 (March 11, 2020): e8750. http://dx.doi.org/10.7717/peerj.8750.

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Background Deformed wing virus (DWV) is a serious threat to honey bees (Apis mellifera) and is considered a major cause of elevated losses of honey bee colonies. However, lack of information on the immunogenicity of DWV structural proteins has hindered the development of effective biocontrol drugs. Methods We optimized the VP1, VP2 and VP3 codons of DWV surface capsid protein genes on the basis of an Escherichia coli codon bias, and the optimized genes of roVP1, roVP2 and roVP3 were separately expressed in E. coli and purified. Next, the three recombinant proteins of roVP1, roVP2 and roVP3 wer
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Pachner, A. R., D. Dail, L. Li, L. Gurey, S. Feng, E. Hodzic, and S. Barthold. "Humoral Immune Response Associated with Lyme Borreliosis in Nonhuman Primates: Analysis by Immunoblotting and Enzyme-Linked Immunosorbent Assay with Sonicates or Recombinant Proteins." Clinical and Vaccine Immunology 9, no. 6 (November 2002): 1348–55. http://dx.doi.org/10.1128/cdli.9.6.1348-1355.2002.

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ABSTRACT The immune response to Borrelia burgdorferi, the causative agent of Lyme disease, is complex. We studied the immunoglobulin M (IgM) and IgG antibody response to N40Br, a sensu stricto strain, in the rhesus macaque(nonhuman primate [NHP]) model of infection to identify the spirochetal protein targets of specific antibody. Antigens used in enzyme-linked immunosorbent assays were whole-cell sonicates of the spirochete and recombinant proteins of B. burgdorferi. Immunoblotting with a commercially available strip and subsequent quantitative densitometry of the bands were also used. Sera fr
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Shi, Xiaohong, and Richard M. Elliott. "Generation and analysis of recombinant Bunyamwera orthobunyaviruses expressing V5 epitope-tagged L proteins." Journal of General Virology 90, no. 2 (February 1, 2009): 297–306. http://dx.doi.org/10.1099/vir.0.007567-0.

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The L protein of Bunyamwera virus (BUNV; family Bunyaviridae) is an RNA-dependent RNA polymerase, 2238 aa in length, that catalyses transcription and replication of the negative-sense, tripartite RNA genome. To learn more about the molecular interactions of the L protein and to monitor its intracellular distribution we inserted a 14 aa V5 epitope derived from parainfluenza virus type 5, against which high-affinity antibodies are available, into different regions of the protein. Insertion of the epitope at positions 1935 or 2046 resulted in recombinant L proteins that retained functionality in
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Karavaev, VS, E. S. Oleinikova, M. Sh Azaev, and A. B. Beklemishev'. "IMMUNOCHEMICAL ANALYSIS OF RECOMBINANT CHIMERIC POLYPEPTIDE OspCgar+afz OF BORRELIA GARINII AND B. AFZELIIISOLATES." Journal of microbiology, epidemiology and immunobiology, no. 3 (June 28, 2016): 37–44. http://dx.doi.org/10.36233/0372-9311-2016-3-37-44.

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Aim. Comparative study of antigenic properties of recombinant proteins OspCgar and OspCafz and recombinant chimeric polypeptide OspCgar+afZ, that contains amino acid sequences of mature immune dominant OspC proteins of West-Siberian isolates of Borrelia garinii (OspCgar) and B. afzelii (OspCafz), and evaluation of possibility of their use as antigens during creation of test-systems for serodiagnostics of Lyme borreliosis (LB) on the territory of Western Siberia. Materials and methods. Recombinant chimeric polypeptide OspCgar+afz and recombinant mature proteins OspCgar and OspCafz, obtained by
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Oulton, Tate, Joshua Obiero, Isabel Rodriguez, Isaac Ssewanyana, Rebecca A. Dabbs, Christine M. Bachman, Bryan Greenhouse, et al. "Plasmodium falciparum serology: A comparison of two protein production methods for analysis of antibody responses by protein microarray." PLOS ONE 17, no. 8 (August 29, 2022): e0273106. http://dx.doi.org/10.1371/journal.pone.0273106.

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The evaluation of protein antigens as putative serologic biomarkers of infection has increasingly shifted to high-throughput, multiplex approaches such as the protein microarray. In vitro transcription/translation (IVTT) systems–a similarly high-throughput protein expression method–are already widely utilised in the production of protein microarrays, though purified recombinant proteins derived from more traditional whole cell based expression systems also play an important role in biomarker characterisation. Here we have performed a side-by-side comparison of antigen-matched protein targets f
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Tu, Chien, Ruey-Yu Chiou, and Meei-Mei Chen. "CLONING, EXPRESSION AND PRELIMINARY ANTIGENICITY ANALYSIS OF STRUCTURAL PROTEINS OF A KOI HERPESVIRUS ISOLATE FROM KOI, CYPRINUS CARPIO IN TAIWAN." Taiwan Veterinary Journal 40, no. 02 (June 2014): 69–75. http://dx.doi.org/10.1142/s1682648514500097.

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The aim of this study was to clone and express the ORF72 and ORF92 genes of koi herpesvirus (KHV) in a prokaryotic system and to examine the antigenicity of recombinant proteins. Phylogenetic analysis revealed that both ORF72 and ORF92 had 100% homology with KHV-J, and 99% homology with those from KHV-U and KHV-I in nucleotides. This suggests that the KHV isolate in Taiwan is more closely related to the Japanese strain (Asian genotype). In the antigenicity analysis, the crude recombinant ORF72 and ORF92 capsid proteins reacted with the positive sera of the survival fish after a KHV outbreak, i
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Grover, J., and P. J. Roughley. "The expression of functional link protein in a baculovirus system: analysis of mutants lacking the A, B and B' domains." Biochemical Journal 300, no. 2 (June 1, 1994): 317–24. http://dx.doi.org/10.1042/bj3000317.

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Functional recombinant human link protein has been produced using a baculovirus expression system. In addition to the intact link protein, three mutant forms have also been expressed. Each mutant bears a deletion equivalent to the protein encoded by one exon in the gene. These deletions represent the A domain, which is thought to be responsible for interaction with aggrecan, and the B or B' domains, which are associated with the interaction with hyaluronate. Such deletions split codons spanning exon boundaries, but maintain the reading frame of the protein and result in the correct amino acid
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Bhandari, Bikash K., Chun Shen Lim, Daniela M. Remus, Augustine Chen, Craig van Dolleweerd, and Paul P. Gardner. "Analysis of 11,430 recombinant protein production experiments reveals that protein yield is tunable by synonymous codon changes of translation initiation sites." PLOS Computational Biology 17, no. 10 (October 5, 2021): e1009461. http://dx.doi.org/10.1371/journal.pcbi.1009461.

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Recombinant protein production is a key process in generating proteins of interest in the pharmaceutical industry and biomedical research. However, about 50% of recombinant proteins fail to be expressed in a variety of host cells. Here we show that the accessibility of translation initiation sites modelled using the mRNA base-unpairing across the Boltzmann’s ensemble significantly outperforms alternative features. This approach accurately predicts the successes or failures of expression experiments, which utilised Escherichia coli cells to express 11,430 recombinant proteins from over 189 dive
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Santos, R. B., A. S. Pires, H. S. Silva, and and R. Abranches. "Assessment of Medicago Based Systems for the Production of Human Proteins: Microscopy Analysis of the Subcellular Deposition Patterns of the Recombinant Product." Microscopy and Microanalysis 18, S5 (August 2012): 11–12. http://dx.doi.org/10.1017/s1431927612012718.

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The use of transgenic plants for the large scale production of recombinant proteins with commercial and therapeutic value has emerged as an alternative to conventional platforms. Plant based systems, including whole plants and plant cell cultures offer many advantages particularly regarding safety and cost effectiveness. In our laboratory we have been using the model plant Medicago truncatula as a system to express recombinant proteins with a variety of applications.
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Guo, Rong, Shiguang Liu, Robert F. Spurney, and L. D. Quarles. "Analysis of recombinant Phex: an endopeptidase in search of a substrate." American Journal of Physiology-Endocrinology and Metabolism 281, no. 4 (October 1, 2001): E837—E847. http://dx.doi.org/10.1152/ajpendo.2001.281.4.e837.

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X-linked hypophosphatemia (XLH) is caused by inactivating mutations of Phex, a phosphate-regulating endopeptidase. Further advances in our knowledge of the pathogenesis of XLH require identification of the biological function of Phex and its physiologically relevant substrates. We evaluated several potential substrates using mouse recombinant wild-type Phex proteins (r Phex-WT) and inactive mutant Phex proteins (r Phex-3′M) lacking the COOH-terminal catalytic domain as controls. By Western blot analysis, we demonstrated that Phex is a membrane-bound 100-kDa glycosylated monomer. Neither casein
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Horvath, C. M., A. Wolven, D. Machadeo, J. Huber, L. Boter, M. Benedetti, B. Hempstead, and M. V. Chao. "Analysis of the trk NGF receptor tyrosine kinase using recombinant fusion proteins." Journal of Cell Science 1993, Supplement 17 (December 1, 1993): 223–28. http://dx.doi.org/10.1242/jcs.1993.supplement_17.31.

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TOTTÉ, PHILIPPE, DECLAN McKEEVER, FRANS JONGEJAN, ANTONY BARBET, SUMAN M. MAHAN, DUNCAN MWANGI, and ALBERT BENSAID. "Analysis of Cellular Responses to Native and Recombinant Proteins of Cowdria ruminantiumaa." Annals of the New York Academy of Sciences 849, no. 1 (June 1998): 155–60. http://dx.doi.org/10.1111/j.1749-6632.1998.tb11045.x.

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Lim, Kwang Suk, Young-Wook Won, Yong Soo Park, and Yong-Hee Kim. "Preparation and functional analysis of recombinant protein transduction domain-metallothionein fusion proteins." Biochimie 92, no. 8 (August 2010): 964–70. http://dx.doi.org/10.1016/j.biochi.2010.04.005.

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Rehbein, Peter, Krishna Saxena, Kai Schlepckow, and Harald Schwalbe. "Protocol for aerosol-free recombinant production and NMR analysis of prion proteins." Journal of Biomolecular NMR 59, no. 2 (April 26, 2014): 111–17. http://dx.doi.org/10.1007/s10858-014-9831-5.

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Kotelnikova, O. V., A. A. Zinchenko, A. A. Vikhrov, A. P. Alliluev, O. V. Serova, E. A. Gordeeva, L. S. Zhigis, et al. "Serological Analysis of Immunogenic Properties of Recombinant Meningococcus IgA1 Protease-Based Proteins." Bulletin of Experimental Biology and Medicine 161, no. 3 (July 2016): 391–94. http://dx.doi.org/10.1007/s10517-016-3422-2.

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Murrell, J. R., R. G. Schoner, J. J. Liepnieks, H. N. Rosen, A. C. Moses, and M. D. Benson. "Production and functional analysis of normal and variant recombinant human transthyretin proteins." Journal of Biological Chemistry 267, no. 23 (August 1992): 16595–600. http://dx.doi.org/10.1016/s0021-9258(18)42044-3.

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Nguyen, Khanh Tan, Hung Manh Tran, Anh Tuan Trieu, Van Thi Huynh Nguyen, Hoang M. Nguyen, and Phu Tran Vinh Phu. "PURIFICATION AND ANALYSIS CATALYTIC FUNCTIONS OF RECOMBINANT INFLUENZA VIRAL POLYMERASES." Journal of microbiology, biotechnology and food sciences 11, no. 4 (February 1, 2022): e4954. http://dx.doi.org/10.55251/jmbfs.4954.

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Polymerase of influenza virus is made up of three subunits PB1, PB2, and PA, which are involved in viral genome transcription and replication. Purification of sufficient amounts of viral polymerase is essential to understand the catalytic function of viral polymerase. In this study, we generated a viral polymerase expression system in human embryonic kidney 293T cells (293T cells). The cDNAs for RNA segments 1, 2, and 3, which encode for PB2, PB1, and PA proteins, respectively, were integrated into the mammalian expression plasmids pCAGGS to simultaneously express all viral polymerase proteins
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Jaleel, Zaroug, Shun Zhou, Zaira Martín-Moldes, Lauren M. Baugh, Jonathan Yeh, Nina Dinjaski, Laura T. Brown, Jessica E. Garb, and David L. Kaplan. "Expanding Canonical Spider Silk Properties through a DNA Combinatorial Approach." Materials 13, no. 16 (August 14, 2020): 3596. http://dx.doi.org/10.3390/ma13163596.

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The properties of native spider silk vary within and across species due to the presence of different genes containing conserved repetitive core domains encoding a variety of silk proteins. Previous studies seeking to understand the function and material properties of these domains focused primarily on the analysis of dragline silk proteins, MaSp1 and MaSp2. Our work seeks to broaden the mechanical properties of silk-based biomaterials by establishing two libraries containing genes from the repetitive core region of the native Latrodectus hesperus silk genome (Library A: genes masp1, masp2, tus
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Bakli, Mahfoud, Raul Pascalau, and Laura Smuleac. "Rare Codon Analysis in Rickettsia Affecting Recombinant Protein Expression in Escherichia coli." Advanced Research in Life Sciences 4, no. 1 (January 1, 2020): 30–35. http://dx.doi.org/10.2478/arls-2020-0015.

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Abstract Rickettsia species are important emerging pathogens causing rickettsial diseases, which are important cause death worldwide. The number of recombinant proteins used for diagnostic and therapeutic applications has increased dramatically, which is important in determination of protein function, structure and antigensity. Although E. coli is widely used expression system, the codon bias can hamper protein expression due to the presence of rare codons in gene sequence coding protein of interest. Using bioinformatics tools, rare codon analysis of rickettsial genes was performed and compare
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McBride, Jere W., Lucy M. Ndip, Vsevolod L. Popov, and David H. Walker. "Identification and Functional Analysis of an Immunoreactive DsbA-Like Thio-Disulfide Oxidoreductase of Ehrlichia spp." Infection and Immunity 70, no. 5 (May 2002): 2700–2703. http://dx.doi.org/10.1128/iai.70.5.2700-2703.2002.

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ABSTRACT Novel homologous DsbA-like disulfide bond formation (Dsb) proteins of Ehrlichia chaffeensis and Ehrlichia canis were identified which restored DsbA activity in complemented Escherichia coli dsbA mutants. Recombinant Ehrlichia Dsb (eDsb) proteins were recognized by sera from E. canis-infected dogs but not from E. chaffeensis-infected patients. The eDsb proteins were observed primarily in the periplasm of E. chaffeensis and E. canis.
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Koupriyanov, V. V., L. I. Nikolaeva, A. A. Zykova, P. I. Makhnovskiy, R. Y. Kotlyarov, A. V. Vasilyev, and N. V. Ravin. "IMMUNOGENIC PROPERTIES OF RECOMBINANT MOZAIC PROTEINS BASED ON ANTIGENS NS4A AND NS4B OF HEPATITIS C VIRUS." Problems of Virology, Russian journal 63, no. 3 (June 20, 2018): 138–43. http://dx.doi.org/10.18821/0507-4088-2018-63-3-138-143.

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The aim of the study was to investigate immunogenic properties of mosaic recombinant proteins constructed on the data of hepatitis C virus NS4A and NS4B antigens. Four mosaic recombinant proteins, containing the T and B epitopes of the NS4A and NS4B antigens, were created by genetic engineering methods in the E. coli system. To enhance the immune response they were linked in different variations to the nucleotide sequences of murine interleukin-2 (IL-2), the Neisseria meningiditis lipopeptide, and the T helper epitope of the core protein of hepatitis C virus. The immunogenic properties of thes
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Okenu, Daniel M. N., Eleanor M. Riley, Quentin D. Bickle, Philip U. Agomo, Arnoldo Barbosa, Jon R. Daugherty, David E. Lanar, and David J. Conway. "Analysis of Human Antibodies to Erythrocyte Binding Antigen 175 of Plasmodium falciparum." Infection and Immunity 68, no. 10 (October 1, 2000): 5559–66. http://dx.doi.org/10.1128/iai.68.10.5559-5566.2000.

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ABSTRACT Invasion of human erythrocytes by Plasmodium falciparummerozoites is a multistep process. For many strains of the parasite, part of this process requires that the erythrocyte binding antigen 175 (EBA-175) of the merozoite binds to sialic acid residues of glycophorin A on the erythrocyte surface, a receptor-ligand interaction which represents a potential target for inhibition by antibodies. This study characterizes the reactivity of naturally acquired human antibodies with four recombinant proteins representing parts of EBA-175 (region II, regions III to V, and the dimorphic C and F se
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Hamsten, Carl, Georgina Tjipura-Zaire, Laura McAuliffe, Otto J. B. Huebschle, Massimo Scacchia, Roger D. Ayling, and Anja Persson. "Protein-Specific Analysis of Humoral Immune Responses in a Clinical Trial for Vaccines against Contagious Bovine Pleuropneumonia." Clinical and Vaccine Immunology 17, no. 5 (March 31, 2010): 853–61. http://dx.doi.org/10.1128/cvi.00019-10.

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ABSTRACT Specific humoral immune responses in a clinical trial on cattle for vaccines against contagious bovine pleuropneumonia (CBPP) were investigated. The trial included a subunit vaccine consisting of five recombinant putative variable surface proteins of the infectious agent Mycoplasma mycoides subsp. mycoides small colony type (M. mycoides SC) compared to the currently approved attenuated vaccine strain T1/44 and untreated controls. Humoral immune responses to 65 individual recombinant surface proteins of M. mycoides SC were monitored by a recently developed bead-based array assay. Respo
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Deykin, Alexey V., Olesya V. Shcheblykina, Elena E. Povetka, Polina A. Golubinskaya, Vladimir M. Pokrovsky, Liliya V. Korokina, Olesya A. Vanchenko, et al. "Genetically modified animals for use in biopharmacology: from research to production." Research Results in Pharmacology 7, no. 4 (October 29, 2021): 11–27. http://dx.doi.org/10.3897/rrpharmacology.7.76685.

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Introduction: In this review, the analysis of technologies for obtaining biologically active proteins from various sources is carried out, and the comparative analysis of technologies for creating producers of biologically active proteins is presented. Special attention is paid to genetically modified animals as bioreactors for the pharmaceutical industry of a new type. The necessity of improving the technology of development transgenic rabbit producers and creating a platform solution for the production of biological products is substantiated. The advantages of using TrB for the production of
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Mahadevappa, Mamatha, Richard A. DeScenzo, and Roger P. Wise. "Recombination of alleles conferring specific resistance to powdery mildew at the Mla locus in barley." Genome 37, no. 3 (June 1, 1994): 460–68. http://dx.doi.org/10.1139/g94-064.

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In barley (Hordeum vulgare L.), the Mla locus conditions reaction to the powdery mildew fungus Erysiphe graminis f.sp. hordei. Enrichment for genetic recombinants in the Mla region is possible by screening for recombination events between the flanking endosperm storage proteins hordeins C and B. Reciprocal crosses were made between the Franger (C.I. 16151) and Rupee (C.I. 16155) lines carrying the (Mla6 + Mla14) and Mla13 alleles, respectively. Recombinants were identified from F2 segregants by analyzing the extracted hordein polypeptides by sodium dodecyl sulphate – polyacrylamide gel electro
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Fernandes, Luis G. V., Monica L. Vieira, Ivy J. Alves, Zenaide M. de Morais, Silvio A. Vasconcellos, Eliete C. Romero, and Ana L. T. O. Nascimento. "Functional and immunological evaluation of two novel proteins of Leptospira spp." Microbiology 160, no. 1 (January 1, 2014): 149–64. http://dx.doi.org/10.1099/mic.0.072074-0.

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This work shows the production and characterization of two novel putative lipoproteins encoded by the genes LIC10645 and LIC10731 identified in the genome sequences of Leptospira interrogans. In silico conservation analysis indicated that the proteins are well conserved among pathogenic leptospiral serovars and species. Recombinant proteins were obtained in Escherichia coli BL21(DE3) Star pLysS strain, purified by metal-affinity chromatography, and used for characterization and immunological evaluations. Recombinant proteins were capable of eliciting a combination of humoral and cellular immun
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Wei, Wenrui, Nengxing Shen, Jie Xiao, Yuanyuan Tao, Yuejun Luo, Christiana Angel, Xiaobin Gu, et al. "Expression Analysis and Serodiagnostic Potential of Microneme Proteins 1 and 3 in Eimeria stiedai." Genes 11, no. 7 (June 29, 2020): 725. http://dx.doi.org/10.3390/genes11070725.

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Eimeria stiedai is an apicomplexan protozoan parasite that invades the liver and bile duct epithelial cells in rabbits and causes severe hepatic coccidiosis, resulting in significant economic losses in the domestic rabbit industry. Hepatic coccidiosis lacks the typical clinical symptoms and there is a lack of effective premortem tools to timely diagnose this disease. Therefore, in the present study we cloned and expressed the two microneme proteins i.e., microneme protein 1 (EsMIC1) and microneme protein 3 (EsMIC3) from E. stiedai and used them as recombinant antigens to develop a serodiagnost
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Bidmeshki Barzoki, Tahereh, Ali Mohammad Ahadi, and Hoda Ayat. "A New Design and Epitopes Analysis for Recombinant Vaccine against Salmonella typhi by In silico Analysis." Trends in Immunotherapy 4, no. 2 (August 24, 2020): 1. http://dx.doi.org/10.24294/ti.v4.i2.891.

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Nowadays, foodborne diseases are one of the main problems of the world that infect humans due to consumption of contaminated water or food. Typhoid fever is one of the major causes of illness and death in the world caused by Salmonella typhi. Vaccination is one of the most effective approaches in order to reduction of the disease risk. The main goal of this study is designing and characterization of antigenic determinants of a fusion protein originated from S.typhi usable as an effective vaccine. In this study, the outer membrane proteins of salmonella have been considered as candidates confer
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Terkawi, Mohamad Alaa, Nguyen Xuan Huyen, Putut Eko Wibowo, Faasoa Junior Seuseu, Mahmoud Aboulaila, Akio Ueno, Youn-Kyoung Goo, Naoaki Yokoyama, Xuenan Xuan, and Ikuo Igarashi. "Spherical Body Protein 4 Is a New Serological Antigen for Global Detection ofBabesia bovisInfection in Cattle." Clinical and Vaccine Immunology 18, no. 2 (December 1, 2010): 337–42. http://dx.doi.org/10.1128/cvi.00388-10.

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ABSTRACTFiveBabesia bovisrecombinant proteins, including merozoite surface antigen 2c (BbMSA-2c), C-terminal rhoptry-associated protein 1 (BbRAP-1/CT), truncated thrombospondin-related anonymous protein (BbTRAP-T), spherical body protein 1 (BbSBP-1), and spherical body protein 4 (BbSBP-4), were evaluated as diagnostic antigens to detect the infection in cattle. The recombinant proteins were highly antigenic when tested with experimentallyB. bovis-infected bovine serum in Western blot analysis. Furthermore, five antisera that had been raised against each of the recombinant proteins reacted spec
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Fenton, Brian, and David Walliker. "Genetic analysis of polymorphic proteins of the human malaria parasite Plasmodium falciparum." Genetical Research 55, no. 2 (April 1990): 81–86. http://dx.doi.org/10.1017/s0016672300025301.

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SummaryFive polymorphic proteins, detected by two-dimensional electrophoresis, were analysed in the parents and progeny of a cross between two clones of the malaria parasite Plasmodium falciparum. The information obtained showed that different forms of each protein were determined by allelic variants of each respective gene. One protein was identified as the parasite enzyme adenosine deaminase. Recombinant parasites were produced at a higher than expected frequency.
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Rakleova, Gorica, Ivanka Tsacheva, Mima Petkova, Ivelyn Pantchev, and Magdalena Tchorbadjieva. "Generation of Recombinant Antibodies against Orchardgrass Acidic nsLTP-Like Proteins." Zeitschrift für Naturforschung C 63, no. 5-6 (June 1, 2008): 395–402. http://dx.doi.org/10.1515/znc-2008-5-614.

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Embryogenic and non-embryogenic suspension cultures of orchardgrass (Dactylis glomerata L.) secreted into the culture medium a set of proteins, among which low molecular mass (11/12 kDa) proteins were found. However, only the 11/12 kDa proteins from the embryogenic suspension cultures reacted specifically with an antiserum raised against the carrot EP2 non-specific lipid transfer protein (nsLTP). Two-dimensional (2-D) electrophoretic analysis revealed that the extracellular nsLTP-like proteins from the embryogenic lines were acidic proteins, with pI values ranging between 4.3 and 6.4, and the
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Annweiler, A., S. Zwilling, R. A. Hipskind, and T. Wirth. "Analysis of transcriptional stimulation by recombinant Oct proteins in a cell-free system." Journal of Biological Chemistry 268, no. 4 (February 1993): 2525–34. http://dx.doi.org/10.1016/s0021-9258(18)53807-2.

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Chan, Kun-Wei, Hsien-Hua Hsieh, Hsien-Chi Wang, Ya-Jane Lee, Ming-Hua Sung, Min-Liang Wong, and Wei-Li Hsu. "Identification, expression and antigenic analysis of recombinant hemagglutinin proteins of canine distemper virus." Journal of Virological Methods 155, no. 1 (January 2009): 18–24. http://dx.doi.org/10.1016/j.jviromet.2008.09.024.

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Eaton, Leslie C. "Quantitation of residual Escherichia coli DNA in recombinant biopharmaceutical proteins by hybridization analysis." Journal of Pharmaceutical and Biomedical Analysis 7, no. 5 (January 1989): 633–38. http://dx.doi.org/10.1016/0731-7085(89)80230-4.

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Sako, Yasuhito, Minoru Nakao, Takashi Ikejima, Xian Zhi Piao, Kazuhiro Nakaya, and Akira Ito. "Molecular Characterization and Diagnostic Value ofTaenia solium Low-Molecular-Weight Antigen Genes." Journal of Clinical Microbiology 38, no. 12 (2000): 4439–44. http://dx.doi.org/10.1128/jcm.38.12.4439-4444.2000.

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Neurocysticercosis (NCC) caused by infection with the larvae ofTaenia solium is an important cause of neurological disease worldwide. In order to establish an enzyme-linked immunosorbent assay (ELISA) for this infection using recombinant proteins, we carried out molecular cloning and identified four candidates as diagnostic antigens (designated Ag1, Ag1V1, Ag2, and Ag2V1). Except for Ag2V1, these clones could encode a 7-kDa polypeptide, and Ag2V1 could encode a 10-kDa polypeptide. All of the clones were very similar. Except for Ag2V1, recombinant proteins were successfully expressed using anEs
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Sproles, Ashley E., Anthony Berndt, Francis J. Fields, and Stephen P. Mayfield. "Improved high-throughput screening technique to rapidly isolate Chlamydomonas transformants expressing recombinant proteins." Applied Microbiology and Biotechnology 106, no. 4 (February 2022): 1677–89. http://dx.doi.org/10.1007/s00253-022-11790-9.

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Abstract The single-celled eukaryotic green alga Chlamydomonas reinhardtii has long been a model system for developing genetic tools for algae, and is also considered a potential platform for the production of high-value recombinant proteins. Identifying transformants with high levels of recombinant protein expression has been a challenge in this organism, as random integration of transgenes into the nuclear genome leads to low frequency of cell lines with high gene expression. Here, we describe the design of an optimized vector for the expression of recombinant proteins in Chlamydomonas, that
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Rathore, Jitendra Singh, and Lalit Kumar Gautam. "Expression, Purification, and Functional Analysis of Novel RelE Operon fromX. nematophila." Scientific World Journal 2014 (2014): 1–7. http://dx.doi.org/10.1155/2014/428159.

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Bacterial toxin-antitoxin (TA) complexes induce programmed cell death and also function to relieve cell from stress by various response mechanisms.Escherichia coliRelB-RelE TA complex consists of a RelE toxin functionally counteracted by RelB antitoxin. In the present study, a novel homolog of RelE toxin designated as Xn-relE toxin fromXenorhabdus nematophilapossessing its own antitoxin designated as Xn-relEAT has been identified. Expression and purification of recombinant proteins under native conditions with GST and Ni-NTA chromatography prove the existence of novel TA module. The expression
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