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Journal articles on the topic 'Protein expression in E'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Mishra, Shashank, K. R. Rathi, Divya Shelly, and Reena Bharadwaj. "Immunohistochemical expression of IDH1R132H in Astrocytictumours and its association with histopathological grade, TP53 and EGFR protein expression." Annals of Pathology and Laboratory Medicine 4, no. 5 (2017): A522—A529. http://dx.doi.org/10.21276/apalm.1458.

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2

Scott, Michael R. D., Darel A. Butler, Dale E. Bredesen, Monika Wälchli, Karen K. Hsiao, and Stanley B. Prusiner. "Prion protein gene expression in cultured cells." "Protein Engineering, Design and Selection" 2, no. 1 (1988): 69–76. http://dx.doi.org/10.1093/protein/2.1.69.

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3

DePalma, Angelo. "Protein Expression Strategies." Genetic Engineering & Biotechnology News 35, no. 2 (2015): 22, 24, 26. http://dx.doi.org/10.1089/gen.35.02.11.

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4

Liszewski, Kathy. "Optimizing Protein Expression." Genetic Engineering & Biotechnology News 36, no. 17 (2016): 26, 30, 32–33. http://dx.doi.org/10.1089/gen.36.17.12.

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5

Daniels, David. "Optimizing Protein Expression." Genetic Engineering & Biotechnology News 32, no. 16 (2012): 1, 29–31. http://dx.doi.org/10.1089/gen.32.16.10.

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6

Kearney, Paul, Heather Butler, Kevin Eng, and Patrice Hugo. "Protein Identification and Peptide Expression Resolver: Harmonizing Protein Identification with Protein Expression Data." Journal of Proteome Research 7, no. 1 (2008): 234–44. http://dx.doi.org/10.1021/pr0705439.

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7

Zabel, Claus, Alexander Andreew, Lei Mao, and Daniela Hartl. "Protein expression overlap: more important than which proteins change in expression?" Expert Review of Proteomics 5, no. 2 (2008): 187–205. http://dx.doi.org/10.1586/14789450.5.2.187.

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8

Koganesawa, Nozomi, Tomoyasu Aizawa, Kazuo Masaki, et al. "Construction of an expression system of insect lysozyme lacking thermal stability: the effect of selection of signal sequence on level of expression in the Pichia pastoris expression system." Protein Engineering, Design and Selection 14, no. 9 (2001): 705–10. http://dx.doi.org/10.1093/protein/14.9.705.

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9

Hsieh, Cheng-Hsilin, San-Yuan Huang, Yu-Ching Wu, et al. "Expression of proteins with dimethylarginines inEscherichia colifor protein-protein interaction studies." Protein Science 16, no. 5 (2007): 919–28. http://dx.doi.org/10.1110/ps.062667407.

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10

Lobb, Leslie, Boguslaw Stec, Evan K. Kantrowitz, et al. "Expression, purification and characterization of recombinant crambin." "Protein Engineering, Design and Selection" 9, no. 12 (1996): 1233–39. http://dx.doi.org/10.1093/protein/9.12.1233.

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11

Nishio, Machiko, Junpei Ohtsuka, Masato Tsurudome, Tetsuya Nosaka, and Daniel Kolakofsky. "Human Parainfluenza Virus Type 2 V Protein Inhibits Genome Replication by Binding to the L Protein: Possible Role in Promoting Viral Fitness." Journal of Virology 82, no. 13 (2008): 6130–38. http://dx.doi.org/10.1128/jvi.02635-07.

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ABSTRACT The human parainfluenza virus type 2 (hPIV2) V protein plays important roles in inhibiting the host interferon response and promoting virus growth, but its role in hPIV2 replication and transcription is not clear. A green fluorescent protein (GFP)-expressing a negative-sense minigenomic construct of hPIV2 has been established by standard technology, with helper plasmids expressing the nucleocapsid protein (NP), phosphoprotein (P), and large RNA polymerase (L) protein, to examine the role of V protein. We found that the simultaneous expression of wild-type V protein in the minigenome s

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12

Zozulya, S. A., V. V. Gurevich, T. A. Zvyaga, et al. "Functional expression in vitro of bovine visual rhodopsin." "Protein Engineering, Design and Selection" 3, no. 5 (1990): 453–58. http://dx.doi.org/10.1093/protein/3.5.453.

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13

van Heeke, Gino, and Sheldon M. Schuster. "Expression of human asparagine synthetase in Saccharomyces cerevisiae." "Protein Engineering, Design and Selection" 3, no. 8 (1990): 739–44. http://dx.doi.org/10.1093/protein/3.8.739.

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14

Kuru, Halil İbrahim, Mustafa Buyukozkan, and Oznur Tastan. "PRER: A patient representation with pairwise relative expression of proteins on biological networks." PLOS Computational Biology 17, no. 5 (2021): e1008998. http://dx.doi.org/10.1371/journal.pcbi.1008998.

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Changes in protein and gene expression levels are often used as features in predictive modeling such as survival prediction. A common strategy to aggregate information contained in individual proteins is to integrate the expression levels with the biological networks. In this work, we propose a novel patient representation where we integrate proteins’ expression levels with the protein-protein interaction (PPI) networks: Patient representation with PRER (Pairwise Relative Expressions with Random walks) (PRER). PRER captures the dysregulation patterns of proteins based on the neighborhood of a

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15

Harvie, Marina, Thomas William Jordan, and Anne Camille La Flamme. "Differential Liver Protein Expression during Schistosomiasis." Infection and Immunity 75, no. 2 (2006): 736–44. http://dx.doi.org/10.1128/iai.01048-06.

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ABSTRACT The arrival of eggs in the liver during Schistosoma mansoni infection initiates a protective granulomatous response; however, as the infection progresses, this response results in chronic liver fibrosis. To better understand the impact of schistosomiasis on liver function, we used a proteomic approach to identify proteins whose expression was significantly altered in schistosome-infected mice 8 weeks postinfection. Identification of differentially expressed proteins by mass fingerprinting revealed that schistosome infection markedly reduced the abundance of proteins associated with se

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16

Madsen, Søren. "Recombinant protein expression using microbial expression systems." New Biotechnology 33 (July 2016): S200. http://dx.doi.org/10.1016/j.nbt.2016.06.1411.

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17

Moravec, T., and N. Čeřovská. "The use of legume seed for expression and storage of high value proteins." Czech Journal of Genetics and Plant Breeding 50, No. 2 (2014): 69–76. http://dx.doi.org/10.17221/143/2013-cjgpb.

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There is an ever growing need for the use of recombinant proteins both in medicine and industry; however their widespread use is limited by the lack of production capacity. Transgenic plants offer the possibility to produce and deliver recombinant proteins on a large scale with low production costs and with minimal purification or enrichment requirements. Among crop plants, legumes have great potential as a protein production platform because of their naturally high protein content, nutritional value, independence of N-nutrition, pollen containment, available processing technology, storage sta

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18

Li, E., A. Pedraza, M. Bestagno, S. Mancardi, R. Sanchez, and O. Burrone. "Mammalian cell expression of dimeric small immune proteins (SIP)." Protein Engineering Design and Selection 10, no. 6 (1997): 731–36. http://dx.doi.org/10.1093/protein/10.6.731.

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19

Kasai, Hide, Daita Nadano, Eiko Hidaka, et al. "Differential Expression of Ribosomal Proteins in Human Normal and Neoplastic Colorectum." Journal of Histochemistry & Cytochemistry 51, no. 5 (2003): 567–73. http://dx.doi.org/10.1177/002215540305100502.

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Ribosomal proteins are a major component of ribosomes and play critical roles in protein biosynthesis. Recently it has been shown that the ribosomal proteins also function during various cellular processes that are independent of protein biosynthesis therefore called extraribosomal functions. In this study we have, for the first time, determined the expression profile of 12 ribosomal proteins (Sa, S8, S11, S12, S18, S24, L7, L13a, L18, L28, L32, and L35a) in normal epithelia of human colorectal mucosa using immunohistochemistry (IHC) and then compared their expression patterns with those of co

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20

Shea, Jill E., Kelly C. Hewitt, and Courtney L. Scaife. "Effect of altering fibroblast integrin associated protein expression on the growth and protein expression of pancreas cancer cells." Journal of Clinical Oncology 31, no. 4_suppl (2013): 251. http://dx.doi.org/10.1200/jco.2013.31.4_suppl.251.

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251 Background: The lack of success of current treatments for pancreatic ductal adenocarcinoma (PDA) may be due in part to the presence of the dense surrounding stromal response and the interactions between the stroma and cancer cells. We have shown that integrin associated proteins, in particular PINCH, are expressed to a higher degree in the stroma adjacent to the tumor cells and PINCH expression is positively correlated with poorer PDA patient outcomes. We hypothesize that decreasing PINCH protein expression in the tumor associated stroma will decrease the growth and expression of growth pr

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21

Telesca, Donatello, Peter Müller, Steven M. Kornblau, Marc A. Suchard, and Yuan Ji. "Modeling Protein Expression and Protein Signaling Pathways." Journal of the American Statistical Association 107, no. 500 (2012): 1372–84. http://dx.doi.org/10.1080/01621459.2012.706121.

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22

Shang, Yonglei, Devin Tesar, and Isidro Hötzel. "Modular protein expression by RNAtrans-splicing enables flexible expression of antibody formats in mammalian cells from a dual-host phage display vector." Protein Engineering Design and Selection 28, no. 10 (2015): 437–44. http://dx.doi.org/10.1093/protein/gzv018.

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23

Zhangazin, S. B., and R. M. Ualiyeva. "Plant protein expression system." BULLETIN of the L.N. Gumilyov Eurasian National University. BIOSCIENCE Series 125, no. 4 (2018): 49–58. http://dx.doi.org/10.32523/2616-7034-2018-125-4-49-58.

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24

Cole, Philip A. "Chaperone-assisted protein expression." Structure 4, no. 3 (1996): 239–42. http://dx.doi.org/10.1016/s0969-2126(96)00028-7.

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25

Stein, M.D.,, Richard A. "Recombinant Protein Expression Advances." Genetic Engineering & Biotechnology News 31, no. 16 (2011): 34–36. http://dx.doi.org/10.1089/gen.31.16.14.

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26

Birch,, John R. "Protein Expression Technology Review." Genetic Engineering & Biotechnology News 31, no. 17 (2011): 50–51. http://dx.doi.org/10.1089/gen.31.17.12.

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27

DePalma, Angelo. "Advances in Protein Expression." Genetic Engineering & Biotechnology News 34, no. 1 (2014): 24–25. http://dx.doi.org/10.1089/gen.34.01.14.

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28

Heifetz, P. "Protein expression in plastids." Current Opinion in Plant Biology 4, no. 2 (2001): 157–61. http://dx.doi.org/10.1016/s1369-5266(00)00153-9.

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29

Dutton, Gail. "Fine-Tuning Protein Expression." Genetic Engineering & Biotechnology News 34, no. 19 (2014): 10. http://dx.doi.org/10.1089/gen.34.19.05.

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30

Doranz, Benjamin J., and Soma S. R. Banik. "Optimizing Membrane Protein Expression." Genetic Engineering & Biotechnology News 35, no. 15 (2015): 20–21. http://dx.doi.org/10.1089/gen.35.15.09.

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31

DePalma, Angelo. "Protein Expression Systems Proliferate." Genetic Engineering & Biotechnology News 36, no. 2 (2016): 1, 20–22. http://dx.doi.org/10.1089/gen.36.02.02.

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32

Růčková, Eva, Petr Müller, and Bořivoj Vojtěšek. "Protein Expression and Purification." Klinicka onkologie 27, Suppl 1 (2014): S92—S98. http://dx.doi.org/10.14735/amko20141s92.

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33

Vogel, C. "Protein Expression Under Pressure." Science 342, no. 6162 (2013): 1052–53. http://dx.doi.org/10.1126/science.1247833.

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34

Diller, Kenneth R. "STRESS PROTEIN EXPRESSION KINETICS." Annual Review of Biomedical Engineering 8, no. 1 (2006): 403–24. http://dx.doi.org/10.1146/annurev.bioeng.7.060804.100449.

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35

Oberholzer, Thomas, Knud H. Nierhaus, and Pier Luigi Luisi. "Protein Expression in Liposomes." Biochemical and Biophysical Research Communications 261, no. 2 (1999): 238–41. http://dx.doi.org/10.1006/bbrc.1999.0404.

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36

Short, Kevin R. "Exercise Stimulated Protein Expression." Medicine & Science in Sports & Exercise 38, Supplement (2006): 78. http://dx.doi.org/10.1249/00005768-200605001-00844.

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37

Ratner, Mark. "Protein Expression in Yeast." Nature Biotechnology 7, no. 11 (1989): 1129–33. http://dx.doi.org/10.1038/nbt1189-1129.

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38

Alkebsi, Lobna, Hiroshi Handa, Kenichi Tahara, et al. "Differences in Expression Patterns of DNMTs and TSG Proteins in Lymphoid Tissue Section Play an Important Role in Their Association." Blood 126, no. 23 (2015): 2657. http://dx.doi.org/10.1182/blood.v126.23.2657.2657.

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Abstract In situ, patterns of expression of DNMTs (DNA methytransferases) in normal reactive tonsillar tissue have been examined. Difference in pattering of expression of DNMTs and TSG (Tumor suppressor genes) proteins in lymphoid tissue section is an important question in relation to their association with each other as well as relationship to mRNA gene expression level. In order to examine this issue, we examined DNMTs and TSG proteins expression by immunohistochemistry in sections of paraffin-embedded specimens obtained from 33 subjects of lymphoma and 16 subjects of Non-malignant tissues a

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39

Ataka, Kenichi, Joachim Heberle, Axel Baumann, et al. "2P103 Direct monitoring of membrane protein folding process during in-vitro expression by Surface Enhanced IR spectroscopy(03. Membrane proteins,Poster)." Seibutsu Butsuri 53, supplement1-2 (2013): S176. http://dx.doi.org/10.2142/biophys.53.s176_1.

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40

Schuster, M., A. Einhauer, E. Wasserbauer, et al. "Protein expression in yeast; comparison of two expression strategies regarding protein maturation." Journal of Biotechnology 84, no. 3 (2000): 237–48. http://dx.doi.org/10.1016/s0168-1656(00)00355-2.

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41

Lesley, Scott A., Jim Graziano, Charles Y. Cho, Mark W. Knuth, and Heath E. Klock. "Gene expression response to misfolded protein as a screen for soluble recombinant protein." Protein Engineering, Design and Selection 15, no. 2 (2002): 153–60. http://dx.doi.org/10.1093/protein/15.2.153.

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42

Rucker, P., F. M. Torti, and S. V. Torti. "Recombinant ferritin: modulation of subunit stoichiometry in bacterial expression systems." Protein Engineering Design and Selection 10, no. 8 (1997): 967–73. http://dx.doi.org/10.1093/protein/10.8.967.

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43

Rokeach, Luis A., Jeanne A. Haselby, and Sallie O. Hoch. "High-level bacterial expression, purification and characterization of human calreticulin." "Protein Engineering, Design and Selection" 4, no. 8 (1991): 981–87. http://dx.doi.org/10.1093/protein/4.8.981.

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44

Dudgeon, K., R. Rouet, and D. Christ. "Rapid prediction of expression and refolding yields using phage display." Protein Engineering Design and Selection 26, no. 10 (2013): 671–74. http://dx.doi.org/10.1093/protein/gzt019.

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45

Ayala, Gustavo, Anna Frolov, Deyali Chatterjee, Dandan He, Susan Hilsenbeck, and Michael Ittmann. "Expression of ERG protein in prostate cancer: variability and biological correlates." Endocrine-Related Cancer 22, no. 3 (2015): 277–87. http://dx.doi.org/10.1530/erc-14-0586.

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Prostate cancer is the second leading cause of cancer-related death of men in the USA. TheTMPRSS2/ERG (T/E)fusion gene is present in approximately 50% of prostate cancers and promotes tumor progressionin vivo. The presence of theT/Efusion gene is strongly associated with the expression of ERG protein, but emerging evidence indicates a significant interfocal and intrafocal variability in the levels of ERG protein expression. We therefore analyzed ERG protein expression by image analysis to objectively quantitate the extent of such heterogeneity, and confirmed significant interfocal and intrafoc

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46

Salvatore, Mirella, Christopher F. Basler, Jean-Patrick Parisien, et al. "Effects of Influenza A Virus NS1 Protein on Protein Expression: the NS1 Protein Enhances Translation and Is Not Required for Shutoff of Host Protein Synthesis." Journal of Virology 76, no. 3 (2002): 1206–12. http://dx.doi.org/10.1128/jvi.76.3.1206-1212.2002.

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ABSTRACT The influenza A virus NS1 protein, a virus-encoded alpha/beta interferon (IFN-α/β) antagonist, appears to be a key regulator of protein expression in infected cells. We now show that NS1 protein expression results in enhancement of reporter gene activity from transfected plasmids. This effect appears to be mediated at the translational level, and it is reminiscent of the activity of the adenoviral virus-associated I (VAI) RNA, a known inhibitor of the antiviral, IFN-induced, PKR protein. To study the effects of the NS1 protein on viral and cellular protein synthesis during influenza A

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47

Degani, O. "Cochliobolus heterostrophus T-toxin gene expression modulation via G protein and MAPK pathways." Plant Protection Science 51, No. 2 (2016): 53–60. http://dx.doi.org/10.17221/67/2014-pps.

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48

Saito, Kousuke, Keith Meyer, Rebecca Warner, Arnab Basu, Ratna B. Ray, and Ranjit Ray. "Hepatitis C Virus Core Protein Inhibits Tumor Necrosis Factor Alpha-Mediated Apoptosis by a Protective Effect Involving Cellular FLICE Inhibitory Protein." Journal of Virology 80, no. 9 (2006): 4372–79. http://dx.doi.org/10.1128/jvi.80.9.4372-4379.2006.

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ABSTRACT We have previously shown that hepatitis C virus (HCV) core protein modulates multiple cellular processes, including those that inhibit tumor necrosis factor alpha (TNF-α)-mediated apoptosis. In this study, we have investigated the signaling mechanism for inhibition of TNF-α-mediated apoptosis in human hepatoma (HepG2) cells expressing core protein alone or in context with other HCV proteins. Activation of caspase-3 and the cleavage of DNA repair enzyme poly(ADP-ribose) polymerase were inhibited upon TNF-α exposure in HCV core protein-expressing HepG2 cells. In vivo protein-protein int

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49

Lin, Bo, Hailing Meng, Hui Bing, Dongting Zhangsun, and Sulan Luo. "Efficient Expression of Acetylcholine-Binding Protein fromAplysia californicain Bac-to-Bac System." BioMed Research International 2014 (2014): 1–9. http://dx.doi.org/10.1155/2014/691480.

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The Bac-to-Bac baculovirus expression system can efficiently produce recombinant proteins, but the system may have to be optimized to achieve high-level expression for different candidate proteins. We reported here the efficient expression of acetylcholine-binding proteins from sea haresAplysia californica(Ac-AChBP) and a convenient method to monitor protein expression level in this expression system. Three key factors affecting expression of Ac-AChBP were optimized for maximizing the yield, which included the cell density, volume of the infecting baculovirus inoculums, and the culturing time

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50

Ducancel, FrÉdÉric, Jean-Claude Boulain, Odile TrÉmeau, and AndrÉ MÉnez. "Direct expression in E.coli of a functionally active protein A–snake toxin fusion protein." "Protein Engineering, Design and Selection" 3, no. 2 (1989): 139–43. http://dx.doi.org/10.1093/protein/3.2.139.

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