Relevant bibliographies by topics / Protein 2

Academic literature on the topic 'Protein 2'

Author: Grafiati
Published: 4 June 2021
Last updated: 20 February 2023

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Journal articles on the topic "Protein 2"

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Hayashi, Masahiro, Masahiro Tomita, and Katsutoshi Yoshizato. "Interleukin-2-collagen chimeric protein which liberates interleukin-2 upon collagenolysis." Protein Engineering, Design and Selection 15, no. 5 (May 2002): 429–36. http://dx.doi.org/10.1093/protein/15.5.429.

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Olafsen, T., G. J. Tan, C. w. Cheung, P. J. Yazaki, J. M. Park, J. E. Shively, L. E. Williams, A. A. Raubitschek, M. F. Press, and A. M. Wu. "Characterization of engineered anti-p185HER-2 (scFv-CH3)2 antibody fragments (minibodies) for tumor targeting." Protein Engineering Design and Selection 17, no. 4 (May 4, 2004): 315–23. http://dx.doi.org/10.1093/protein/gzh040.

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Roesler, Keith R., and A. Gururaj Rao. "Conformation and stability of barley chymotrypsin inhibitor-2 (CI-2) mutants containing multiple lysine substitutions." Protein Engineering, Design and Selection 12, no. 11 (November 1999): 967–73. http://dx.doi.org/10.1093/protein/12.11.967.

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McCartney, John E., Mei-Sheng Tai, Robert M. Hudziak, Gregory P. Adams, Louis M. Weiner, Donald Jin, Walter F. Stafford, et al. "Engineering disulfide-linked single-chain Fv dimers [(sFv')2] with improved solution and targeting properties: anti-digoxin 26–10 (sFv')2 and anti-c-erbB-2 741F8 (sFv')2 made by protein folding and bonded through C-terminal cysteinyl peptides." "Protein Engineering, Design and Selection" 8, no. 3 (1995): 301–14. http://dx.doi.org/10.1093/protein/8.3.301.

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Minggu, Renaldo B., Janette M. Rumbajan, and Grace L. A. Turalaki. "Struktur Genom Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2)." JURNAL BIOMEDIK (JBM) 13, no. 2 (March 29, 2021): 233. http://dx.doi.org/10.35790/jbm.13.2.2021.31996.

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Abstract: The genome sequencing as well as the protein structure and function of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is known and helps in structurally characterizing viral proteins, determining evolutionary trajectories, identifying interactions with host proteins and providing biological insights. Knowledge of the structure of the SARS-CoV-2 genome is useful as a means of understanding the disease coronavirus disease 19 (COVID-19). This study aims to determine the genome structure of SARS-CoV-2. This study is a literature review, which was conducted on 23 literatures. This study showed that 23 literatures obtained, as many as in journals suggesting the structure of the genome, there are ORF (open reading frame) / NSP (non-structural protein) and structural protein, namely: S (spike, glycoprotein), E (Envelope), M (Membrane) and N (nucleocapsid) while the remaining 5 literatures do not discuss this structure. The result of this study showed that the genome structure of SARS-CoV-2 consisted of structural proteins, namely; glycoprotein (S), envelope protein (E), membrane protein (M), and nucleocapsid protein (N) and non-structural protein (NSP) encoded by ORF1a and ORF1b via two polyproteins pp1a and pp1b.Keywords: Genome, SARS-CoV-2 Abstrak: Urutan genom serta struktur dan fungsi protein dari severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) telah diketahui dan membantu dalam mengkarakterisasi protein virus secara struktural, menentukan lintasan evolusi, mengidentifikasi interaksi dengan protein inang dan memberikan wawasan biologi. Pengetahuan tentang struktur genom SARS-CoV-2 ini bermanfaat sebagai pengetahuan memahami penyakit coronavirus disease 19 (COVID-19). Penelitian ini bertujuan untuk mengetahui struktur genom SARS-CoV-2. Penelitian ini merupakan penelitian yang bersifat literature review, yang dilakukan terhadap 23 literatur yang memenuhi kriteria inklusi dan eksklusi dari penelitian ini. Penelitian ini menunjukkan bahwa 23 literatur yang didapat, sebanyak pada 18 jurnal mengemukakan tentang struktur genom terdapat ORF (open reading frame)/NSP (Non-Struktural Protein) dan protein struktural yaitu : S (lonjakan, glikoprotein), E (Envelope), M (Membran) dan N (Nukleocapsid) sedangkan sisanya terdapat 5 jurnal tidak membahas struktur tersebut. Hasil penelitian ini menunjukan bahwa struktur genom SARS-CoV-2 terdiri atas protein struktural yaitu; glikoprotein (S), protein amplop (E), protein membran (M), dan protein nuckleokapsid dan protein non-struktural (NSP) yang di kodekan oleh ORF1a dan ORF1b melalui dua poliprotein pp1a dan pp1b.Kata Kunci: Genome, SARS-CoV-2
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Marechal, V., B. Elenbaas, J. Piette, J. C. Nicolas, and A. J. Levine. "The ribosomal L5 protein is associated with mdm-2 and mdm-2-p53 complexes." Molecular and Cellular Biology 14, no. 11 (November 1994): 7414–20. http://dx.doi.org/10.1128/mcb.14.11.7414-7420.1994.

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Throughout the purification of the mdm-2 or mdm-2-p53 protein complexes, a protein with a molecular weight of 34,000 was observed to copurify with these proteins. Several monoclonal antibodies directed against distinct epitopes in the mdm-2 or p53 protein coimmunoprecipitated this 34,000-molecular-weight protein, which did not react to p53 or mdm-2 polyclonal antisera in a Western immunoblot. The N-terminal amino acid sequence of this 34,000-molecular-weight protein demonstrated that the first 40 amino acids were identical to the ribosomal L5 protein, found in the large rRNA subunit and bound to 5S RNA. Partial peptide maps of the authentic L5 protein and the 34,000-molecular-weight protein were identical. mdm-2-L5 and mdm-2-L5-p53 complexes were shown to bind 5S RNA specifically, presumably through the known specificity of L5 protein for 5S RNA. In 5S RNA-L5-mdm-2-p53 ribonucleoprotein complexes, it was also possible to detect the 5.8S RNA which has been suggested to be covalently linked to a percentage of the p53 protein in a cell. These experiments have identified a unique ribonucleoprotein complex composed of 5S RNA, L5 protein, mdm-2 proteins, p53 protein, and possibly the 5.8S RNA. While the function of such a ribonucleoprotein complex is not yet clear, the identity of its component parts suggests a role for these proteins and RNA species in ribosomal biogenesis, ribosomal transport from the nucleus to the cytoplasm, or translational regulation in the cell.
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Marechal, V., B. Elenbaas, J. Piette, J. C. Nicolas, and A. J. Levine. "The ribosomal L5 protein is associated with mdm-2 and mdm-2-p53 complexes." Molecular and Cellular Biology 14, no. 11 (November 1994): 7414–20. http://dx.doi.org/10.1128/mcb.14.11.7414.

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Throughout the purification of the mdm-2 or mdm-2-p53 protein complexes, a protein with a molecular weight of 34,000 was observed to copurify with these proteins. Several monoclonal antibodies directed against distinct epitopes in the mdm-2 or p53 protein coimmunoprecipitated this 34,000-molecular-weight protein, which did not react to p53 or mdm-2 polyclonal antisera in a Western immunoblot. The N-terminal amino acid sequence of this 34,000-molecular-weight protein demonstrated that the first 40 amino acids were identical to the ribosomal L5 protein, found in the large rRNA subunit and bound to 5S RNA. Partial peptide maps of the authentic L5 protein and the 34,000-molecular-weight protein were identical. mdm-2-L5 and mdm-2-L5-p53 complexes were shown to bind 5S RNA specifically, presumably through the known specificity of L5 protein for 5S RNA. In 5S RNA-L5-mdm-2-p53 ribonucleoprotein complexes, it was also possible to detect the 5.8S RNA which has been suggested to be covalently linked to a percentage of the p53 protein in a cell. These experiments have identified a unique ribonucleoprotein complex composed of 5S RNA, L5 protein, mdm-2 proteins, p53 protein, and possibly the 5.8S RNA. While the function of such a ribonucleoprotein complex is not yet clear, the identity of its component parts suggests a role for these proteins and RNA species in ribosomal biogenesis, ribosomal transport from the nucleus to the cytoplasm, or translational regulation in the cell.
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Rao, B. M., A. T. Girvin, T. Ciardelli, D. A. Lauffenburger, and K. D. Wittrup. "Interleukin-2 mutants with enhanced -receptor subunit binding affinity." Protein Engineering Design and Selection 16, no. 12 (December 1, 2003): 1081–87. http://dx.doi.org/10.1093/protein/gzg111.

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Williams, D. P., K. Parker, P. Bacha, W. Bishai, M. Borowski, F. Genbauffe, T. B. Strom, and J. R. Murphy. "Diphtheria toxin receptor binding domain substitution with interleukin-2: genetic construction and properties of a diphtheria toxin-related interleukin-2 fusion protein." "Protein Engineering, Design and Selection" 1, no. 6 (1987): 493–98. http://dx.doi.org/10.1093/protein/1.6.493.

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Kiyokawa, Tetsuyuki, Diane P. Williams, Catherine E. Snider, Terry B. Strom, and John R. Murphy. "Protein engineering of diphtheria-toxin-related interleukin-2 fusion toxins to increase cytotoxic potency for high-affinity IL-2-receptor-bearing target cells." "Protein Engineering, Design and Selection" 4, no. 4 (1991): 463–68. http://dx.doi.org/10.1093/protein/4.4.463.

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Dissertations / Theses on the topic "Protein 2"

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Gao, Wei, and 高威. "Characterization of protein interactors of Arabidopsis acyl-coenzymea-binding protein 2." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2009. http://hub.hku.hk/bib/B43223837.

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Gao, Wei. "Characterization of protein interactors of Arabidopsis acyl-coenzyme a-binding protein 2." Click to view the E-thesis via HKUTO, 2009. http://sunzi.lib.hku.hk/hkuto/record/B43223837.

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Xu, Ping. "Sensing and analyzing unfolded protein response during heterologous protein production :." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file, 205 p, 2008. http://proquest.umi.com/pqdweb?did=1555621341&sid=2&Fmt=2&clientId=8331&RQT=309&VName=PQD.

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Rowell, Philip Lee. "Protein-protein interactions of the BCL-2 family." Thesis, University of Leeds, 2018. http://etheses.whiterose.ac.uk/20769/.

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The BCL-2 family of proteins are important regulators of mitochondrial apoptosis, comprising both pro- and anti-apoptotic members that interact with one another at the mitochondrial outer membrane to determine cellular fate. Dysregulation of their activities in the cell is implicated in many forms of cancer; the development of molecules able to mimic and modulate their interactions is thus highly desirable and has been the subject of a great deal of research effort. The use of techniques including structure based design and peptidomimetic approaches has produced some notable successes in this area, but few have successfully transitioned from laboratory to clinic, and the search for more and better ways to develop such molecules continues. In this thesis, I present a novel approach to identifying binding partners for BCL-2 proteins, which uses phage display experiments and the production of non-antibody scaffold proteins called Affimers. Five BCL-2 family proteins were selected as targets for study, comprising a good cross section of proand anti-apoptotic members. In the following chapters, I first describe the work undertaken to purify and characterise these target proteins, then detail the work done to identify and purify Affimer binding partners for each of them. Finally, I report on structural studies carried out to explore the mechanism by which BAX, a pro-apoptotic family member, forms death inducing oligomers. Taken together, the results of this project lay the foundations for further structural studies of BAX oligomerisation, and demonstrate that the use of phage display to generate selectively binding non-antibody scaffold proteins can provide useful additions to the existing array of BCL2 family interacting molecules.
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Papadopoulos, Maria. "The prion protein interacts with Bcl-2 and Bax proteins." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape10/PQDD_0026/MQ50849.pdf.

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Schacht, Teresa [Verfasser]. "Neuronal calcium-binding protein 2 (NECAB2): Charakterisierung eines striatalen Ca 2+ -bindenden Proteins / Teresa Schacht." Mainz : Universitätsbibliothek Mainz, 2017. http://d-nb.info/1141937689/34.

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Richards, Susan Diane. "Protein-protein interactions within the 2-oxoacid dehydrogenase complexes." Thesis, University of Glasgow, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.299965.

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Funabashi, Teruki. "Roles of kinesin-2 motor proteins involved in intraciliary protein trafficking." Kyoto University, 2018. http://hdl.handle.net/2433/232321.

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Fang, Lin. "Mechanism of client protein binding by heat shock protein 90 /." view abstract or download file of text, 2006. http://proquest.umi.com/pqdweb?did=1251819301&sid=2&Fmt=2&clientId=11238&RQT=309&VName=PQD.

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Thesis (Ph. D.)--University of Oregon, 2006.
Typescript. Includes vita and abstract. Includes bibliographical references (leaves 115-121). Also available for download via the World Wide Web; free to University of Oregon users.
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Libkind, Marianna. "SiaA: A Heme Protein." Digital Archive @ GSU, 2007. http://digitalarchive.gsu.edu/chemistry_hontheses/2.

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The protein SiaA (Streptococcal iron acquisition) is involved in heme uptake in the bacterium Streptococcus pyogenes. It is difficult to obtain this protein in its fully holo form (completely loaded with heme). To increase the concentration of heme in the growing cell, we added ä-aminolevulinic acid (ALA) and ferrous sulfate (FeSO4), precursors of heme, to the growth media. Neither increasing the concentration of heme in vivo, nor growth at lower temperature for longer times, increased the production of holoprotein. The classical method of measuring the concentration of heme in a newly discovered heme protein is cumbersome. We have developed an improved method, which gives a solution that is more stable and has a cleaner spectrum. With further development, this new technique may replace the classical assay. Background information on S. pyogenes, SiaA, ABC transporters, heme biosynthesis, and the pyridine hemochrome assay are described.
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Books on the topic "Protein 2"

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Hetz, Claudio, ed. BCL-2 Protein Family. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-6706-0.

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Dan bai zhi nü hai 2: The protein girl 2. Taibei Shi: Shi bao wen hua chu ban qi ye gu fen you xian gong si, 2002.

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Focosi, Daniele. SARS-CoV-2 Spike Protein Convergent Evolution. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-87324-0.

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Kangueane, Pandjassarame, and Christina Nilofer. Protein-Protein and Domain-Domain Interactions. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-10-7347-2.

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Franks, Felix, ed. Protein Biotechnology. Totowa, NJ: Humana Press, 1993. http://dx.doi.org/10.1007/978-1-59259-438-2.

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Brosh,, Robert M., ed. Protein Acetylation. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9434-2.

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Atassi, M. Zouhair, ed. Protein Reviews. Singapore: Springer Singapore, 2017. http://dx.doi.org/10.1007/978-981-10-6922-2.

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Gerrard, Juliet A., and Laura J. Domigan, eds. Protein Nanotechnology. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-4939-9869-2.

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Atassi, M. Zouhair, ed. Protein Reviews. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-67814-2.

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Cieplak, Andrzej Stanisław, ed. Protein Aggregation. New York, NY: Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-2597-2.

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Book chapters on the topic "Protein 2"

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Lin, Shili, Denise Scholtens, and Sujay Datta. "Protein-Protein Interactions." In Bioinformatics Methods, 25–38. Boca Raton: Chapman and Hall/CRC, 2022. http://dx.doi.org/10.1201/9781315153728-2.

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Lai, Lisa A., Chunmei Zhao, Eric E. Zhang, and Gen-Sheng Feng. "The Shp-2 tyrosine phosphatase." In Protein Phosphatases, 275–99. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-540-40035-6_14.

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Dunn, Brandon S., Sharad Awasthi, S. Stephen Yi, and Nidhi Sahni. "CHAPTER 2. Protein–Protein Interaction Networks in Human Disease." In Protein–Protein Interaction Regulators, 25–48. Cambridge: Royal Society of Chemistry, 2020. http://dx.doi.org/10.1039/9781788016544-00025.

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Bonner, Philip L. R. "Protein Structure and Properties." In Protein Purification, 13–30. Second edition. | Boca Raton : Taylor & Francis, 2018. | Series: Basics: Taylor & Francis, 2018. http://dx.doi.org/10.1201/9780429458187-2.

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Corcoran, M. L., M. R. Emmert-Buck, J. L. McClanahan, M. Pelina-Parker, and W. G. Stetler-Stevenson. "TIMP-2 Mediates Cell Surface Binding of MMP-2." In Intracellular Protein Catabolism, 295–304. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-0335-0_36.

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Cheng, Hwee Ming, Kin Kheong Mah, and Kumar Seluakumaran. "Protein Absorption." In Defining Physiology: Principles, Themes, Concepts. Volume 2, 71–73. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-62285-5_20.

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Cheng, Hwee Ming, Kin Kheong Mah, and Kumar Seluakumaran. "Protein Digestion." In Defining Physiology: Principles, Themes, Concepts. Volume 2, 67–69. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-62285-5_19.

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Misra, U. K., and J. Kalita. "Protein energy malnutrition." In Neurological Consequences of Nutritional Disorders, 13–28. First edition. | Boca Raton, FL : Taylor & Francis, 2021.: CRC Press, 2021. http://dx.doi.org/10.1201/9780429316401-2.

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Abola, E. E., U. Weierstall, W. Liu, and V. Cherezov. "Chapter 2. Delivery of GPCR Crystals for Serial Femtosecond Crystallography." In Protein Crystallography, 28–53. Cambridge: Royal Society of Chemistry, 2018. http://dx.doi.org/10.1039/9781788010504-00028.

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Murdoch, John D. "Contactin-Associated Protein 2." In Encyclopedia of Autism Spectrum Disorders, 796–99. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-1698-3_1321.

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Conference papers on the topic "Protein 2"

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Sasabe, H., T. Furuno, A. Sato, and K. M. Ulmer. "2-dimensional protein crystals for bioelectronics." In Proceedings of the Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 1988. http://dx.doi.org/10.1109/iembs.1988.95316.

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Li, Ming. "(2) Protein structure determination on demand." In 2012 IEEE International Conference on Bioinformatics and Biomedicine (BIBM). IEEE, 2012. http://dx.doi.org/10.1109/bibm.2012.6392662.

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Chen, Tzu-Chi, Kuan-Ting Lin, Yu-Lun Kuo, Pei-Ying Lee, Chun-Houh Chen, Yu-Wen Liu, and Chi-Ying Huang. "Abstract 1976: Systematic identification of protein-protein interactions by Proximity Ligation Assay." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-1976.

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Wilderspin, Andrew F., Edwin Nkansah, Giovanna Zinzalla, F. Anne Stephenson, and David E. Thurston. "Abstract 279: Use of GFP-STAT3βtc for EMSA analysis of protein-protein and protein-DNA interactions in tumorigenic signalling pathways." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-279.

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Ozhimkova, E. V., and I. V. Uschapovsky. "ULTRASONIC EXTRACTION OF PROTEIN COMPLEXES FROM LEGUME SEEDS." In STATE AND DEVELOPMENT PROSPECTS OF AGRIBUSINESS Volume 2. DSTU-Print, 2020. http://dx.doi.org/10.23947/interagro.2020.2.551-553.

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The article presents the basics of resource-saving technology for complex processing of legume seeds with obtaining protein components. The use of low-frequency ultrasound is proposed to intensify the extraction of protein complexes from legume seeds. The conditions of ultrasonic exposure that provide the maximum output of the target components are experimentally selected.
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Melissari, E., M. F. Scully, C. Parker, K. H. Nicolaides, and V. V. Kakkar. "PROTEIN C/PROTEIN S IN THE FOETAL BLOOD. ABSENCE OF BOUND PROTEINS AND C4 BINDING PROTEIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644290.

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Protein C, free and bound protein S and C4 binding protein levels (C4bp), were measured by electroimmunoassay in 7 pregnant women aged 22-29 years at 16-18 weeks of gestation, immediately prior to termination of pregnancy for social reasons. Protein C and protein S levels were also measured in their foetuses from blood taken through the umbilical cord. In this group of pregnant women the mean levels for protein C were 104% of normal adult mean (range 80-128%), for C4bp 100% (52-150%), for free protein S 66% (43-89%). In the foetuses the mean value for protein C was 15.3% (10.5-21%) and for free protein S 36.85% (27-47%) of the normal adult mean. Bound protein S and C4bp levels were zero. Conclusions: (1) free protein S is significantly decreased (< 2SD below the normal adult mean) in women after the first trimester of gestation whereas no change is seen in protein C concentration; (2) C4bp levels are at zero in the foetus as also are the levels of bound protein S; (3) foetal blood protein S level is approximately 2.5 times higher than protein C. Since all other vitamin K-dependent factors have been observed to be in the range of 10-20% of normal at this stage of gestation, our findings may be further proof of a non hepatic (endothelial) source of plasma protein S.
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Gjerris, M., and J. Harfeld. "2. The ethical demand and broiler chickens." In 6th EAAP International Symposium on Energy and Protein Metabolism and Nutrition. The Netherlands: Wageningen Academic Publishers, 2019. http://dx.doi.org/10.3920/978-90-8686-892-6_2.

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Zemskova, Marina Yu, Zanna Beharry, Sandeep Mahajan, and Andrew S. Kraft. "Abstract 1258: Regulation of energy metabolism and protein synthesis by the Pim protein kinases." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-1258.

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Pernazza, Daniele, Kenichiro Doi, Harshani Lawrence, Saïd Sebti, Hong-Gang Wang, and Nicholas Lawrence. "Abstract 1354: New chemical tools for disrupting the Mcl-1/BH3 protein-protein interaction." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-1354.

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Chen, Tzu-Chi, Chia-Hung Liu, Pei-Ying Lee Lee, Kuan-Ting Lin, Yu-Wen Liu, and Chi-Ying Huang. "Abstract 4929: Dissection of protein-protein interaction-mediated cross-talk pathways in hepatocellular carcinoma." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-4929.

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Reports on the topic "Protein 2"

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Zhou, C. Year 2 Report: Protein Function Prediction Platform. Office of Scientific and Technical Information (OSTI), April 2012. http://dx.doi.org/10.2172/1043635.

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Podack, Eckhard. Secretory Heat Shock Protein - gp96-Ig Chaperoned her-2/New Vaccines. Fort Belvoir, VA: Defense Technical Information Center, July 2001. http://dx.doi.org/10.21236/ada400054.

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Podack, Eckhard. Secretory Heat Shock Protein - gp96-Ig Chaperoned Her-2/new Vaccines. Fort Belvoir, VA: Defense Technical Information Center, July 1999. http://dx.doi.org/10.21236/ada382781.

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Ramesh, Vijaya. Neurofibromatosis 2 Tumor Suppressor Protein, Merlin, in Cellular Signaling to Actin Cytoskeleton. Fort Belvoir, VA: Defense Technical Information Center, October 2000. http://dx.doi.org/10.21236/ada395581.

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Brice, Jeremy. Investment, power and protein in sub-Saharan Africa. Edited by Tara Garnett. TABLE, October 2022. http://dx.doi.org/10.56661/d8817170.

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Abstract:
The place of protein in sub-Saharan Africa’s food system is changing rapidly, raising complex international development, global health and environmental sustainability issues. Despite substantial growth in the region’s livestock agriculture sector, protein consumption per capita remains low, and high levels of undernourishment persist. Meanwhile sub-Saharan Africa’s population is growing and urbanising rapidly, creating expectations that demand for protein will increase rapidly over the coming decades and triggering calls for further investment in the expansion and intensification of the region’s meat and dairy sector. However, growing disquiet over the environmental impacts of further expansion in livestock numbers, and growing sales of alternative protein products in the Global North, has raised questions about the future place of plant-based, insect and lab-grown proteins in African diets and food systems. This report examines financial investment in protein production in sub-Saharan Africa. It begins from the position that investors play an important role in shaping the development of diets and food systems because they are able to mobilise the financial resources required to develop new protein products, infrastructures and value chains, or to prevent their development by withholding investment. It therefore investigates which actors are financing the production in sub-Saharan Africa of: a) animal proteins such as meat, fish, eggs and dairy products; b) ‘protein crops’ such as beans, pulses and legumes; and c) processed ‘alternative proteins’ derived from plants, insects, microbes or animal cells grown in a tissue culture. Through analysing investment by state, philanthropic and private sector organisations – as well as multilateral financial institutions such as development banks – it aims to establish which protein sources and stages of the value chain are financed by different groups of investors and to explore the values and goals which shape their investment decisions. To this end, the report examines four questions: 1. Who is currently investing in protein production in sub-Saharan Africa? 2. What goals do these investors aim to achieve (or what sort of future do they seek to bring about) through making these investments? 3. Which protein sources and protein production systems do they finance? 4. What theory of change links their investment strategy to these goals? In addressing these questions, this report explores what sorts of protein production and provisioning systems different investor groups might be helping to bring into being in sub-Saharan Africa. It also considers what alternative possibilities might be marginalised due to a lack of investment. It thus seeks to understand whose priorities, preferences and visions for the future of food might be informing the changing place of protein in the region’s diets, economies and food systems.
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Adhami, Vaqar M. Association Between Microtubule Associated Protein -2 and the EGRF Signaling in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, September 2005. http://dx.doi.org/10.21236/ada445117.

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Adhami, Vaqar M. Association between Microtubule Associated Protein -2 and the EGRF Signaling in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, September 2006. http://dx.doi.org/10.21236/ada466580.

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Carpen, Olli. Novel Molecular Interactions and Biological Functions of the Neurofibromatosis 2 Tumor Suppressor Protein, Merlin. Fort Belvoir, VA: Defense Technical Information Center, August 2008. http://dx.doi.org/10.21236/ada482967.

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Dutton, P. Leslie. Modular Designed Protein Constructions for Solar Generated H2 From Water (Final Report). Office of Scientific and Technical Information (OSTI), February 2015. http://dx.doi.org/10.2172/1170276.

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Ramamoorthy, Sivapriya. Role of PY Motif Containing Protein, WBP-2 in ER, PR Signaling and Breast Tumorigenesis. Fort Belvoir, VA: Defense Technical Information Center, September 2009. http://dx.doi.org/10.21236/ada534171.

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