Relevant bibliographies by topics / Protein 1

Academic literature on the topic 'Protein 1'

Author: Grafiati

Published: 4 June 2021

Last updated: 20 February 2023

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Journal articles on the topic "Protein 1"

Brown, Andrew, Gordon Stock, Alpesh A. Patel, Chukwuka Okafor, and Alexander Vaccaro. "Osteogenic Protein-1." BioDrugs 20, no. 4 (2006): 243–51. http://dx.doi.org/10.2165/00063030-200620040-00005.

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Cook, Stephen D., and David C. Rueger. "Osteogenic Protein-1." Clinical Orthopaedics and Related Research 324 (March 1996): 29–38. http://dx.doi.org/10.1097/00003086-199603000-00005.

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Murali, C., and E. H. Creaser. "Protein engineering of alcohol dehydrogenase — 1. Effects of two amino acid changes in the active site of yeast ADH-1." "Protein Engineering, Design and Selection" 1, no. 1 (1986): 55–57. http://dx.doi.org/10.1093/protein/1.1.55.

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Hartigan, Nichola, Laure Garrigue-Antar, and Karl E. Kadler. "Bone Morphogenetic Protein-1 (BMP-1)." Journal of Biological Chemistry 278, no. 20 (March 13, 2003): 18045–49. http://dx.doi.org/10.1074/jbc.m211448200.

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Ammosova, Tatyana, Marina Jerebtsova, Monique Beullens, Bart Lesage, Angela Jackson, Fatah Kashanchi, William Southerland, Victor R. Gordeuk, Mathieu Bollen, and Sergei Nekhai. "Nuclear Targeting of Protein Phosphatase-1 by HIV-1 Tat Protein." Journal of Biological Chemistry 280, no. 43 (August 29, 2005): 36364–71. http://dx.doi.org/10.1074/jbc.m503673200.

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Transcription of human immunodeficiency virus (HIV)-1 genes is activated by HIV-1 Tat protein, which induces phosphorylation of the C-terminal domain of RNA polymerase-II by CDK9/cyclin T1. We previously showed that Tat-induced HIV-1 transcription is regulated by protein phosphatase-1 (PP1). In the present study we demonstrate that Tat interacts with PP1 and that disruption of this interaction prevents induction of HIV-1 transcription. We show that PP1 interacts with Tat in part through the binding of Val36 and Phe38 of Tat to PP1 and that Tat is involved in the nuclear and subnuclear targeting of PP1. The PP1 binding mutant Tat-V36A/F38A displayed a decreased affinity for PP1 and was a poor activator of HIV-1 transcription. Surprisingly, Tat-Q35R mutant that had a higher affinity for PP1 was also a poor activator of HIV-1 transcription, because strong PP1 binding competed out binding of Tat to CDK9/cyclin T1. Our results suggest that Tat might function as a nuclear regulator of PP1 and that interaction of Tat with PP1 is critical for activation of HIV-1 transcription by Tat.

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Miklossy, G., J. Tozser, J. Kadas, R. Ishima, J. M. Louis, and P. Bagossi. "Novel macromolecular inhibitors of human immunodeficiency virus-1 protease." Protein Engineering Design and Selection 21, no. 7 (May 2, 2008): 453–61. http://dx.doi.org/10.1093/protein/gzn022.

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Garcia, Alphonse, Xavier Cayla, Bernard Caudron, Éric Deveaud, Fernando Roncal, and Angelita Rebollo. "New insights in protein phosphorylation: a signature for protein phosphatase 1 interacting proteins." Comptes Rendus Biologies 327, no. 2 (February 2004): 93–97. http://dx.doi.org/10.1016/j.crvi.2004.01.001.

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Popețiu, Romana Olivia, Silviu Daniel Moldovan, Simona Maria Borta, Oana Lucia Amza, and Maria Puşchiță. "Interrelation between chitinase-3-like protein 1 (CHI3L1) – YKL-40, C-reactive protein and spirometry in chronic lung disease." Romanian Journal of Medical Practice 14, no. 4 (December 31, 2019): 393–95. http://dx.doi.org/10.37897/rjmp.2019.4.9.

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Sansom, Clare E., Jin Wu, and Irene T. Weber. "Molecular mechanics analysis of inhibitor binding to HIV-1 protease." "Protein Engineering, Design and Selection" 5, no. 7 (1992): 659–67. http://dx.doi.org/10.1093/protein/5.7.659.

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Fogolari, F., G. Esposito, P. Viglino, G. Damante, and A. Pastore. "Homology model building of the thyroid transcription factor 1 homeodomain." "Protein Engineering, Design and Selection" 6, no. 5 (1993): 513–19. http://dx.doi.org/10.1093/protein/6.5.513.

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Dissertations / Theses on the topic "Protein 1"

Stylianou, Julianna. "Protein-protein interaction of HSV-1 tegument proteins." Thesis, Imperial College London, 2013. http://hdl.handle.net/10044/1/24663.

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Herpes simplex virus type 1 virions contain a proteinaceous layer between the nucleocapsid and the virus envelope termed the tegument. The mechanism underlying tegumentation remains largely undefined for all herpesviruses, as does the role of many tegument proteins in virus replication. The networks of protein interactions involved in virus assembly have been largely explored and although large-scale studies have been carried out using yeast two hybrid analyses of herpesvirus protein interactions, few of the identified networks have been validated in infected cells. Here, the molecular interactions that occur between the major tegument proteins VP22, VP16 and VP13/14 and a range of glycoproteins and tegument proteins were defined in detail. Two alternative studies were performed from infected cells, however one based on the purification of GFP-tagged proteins and their protein partners proved more successful. These studies validated previous findings and also identified VP13/14, UL21, UL16 and vhs as novel binding partners of VP22, and VP22, UL21, UL16 and vhs as novel binding partners of VP13/14. Thus, these results have led to the identification of two discrete tegument protein complexes in the infected cell: VP22-VP16-VP13/14-vhs and VP22-VP13/14-UL21-UL16. To investigate the nature of the VP22-VP16-VP13/14-vhs complex in more detail, a number of techniques were used and showed that VP22 and VP13/14 both bind directly to the C-terminus of VP16, but were unable to interact with each other. As anticipated from other studies on transfected cell extracts, vhs was shown to be incorporated into this complex by virtue of its direct binding to VP16 during infection, and did not have the capacity to interact directly with VP22. This work has established a defined network of protein-protein interactions encompassing over one third of tegument proteins, and will improve our understanding of the wider protein interaction networks that lead to the assembly of the herpesvirus tegument.

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Tse, Muk-hei. "Investigations on recombinant Arabidopsis acyl-coenzyme A binding protein 1." View the Table of Contents & Abstract, 2005. http://sunzi.lib.hku.hk/hkuto/record/B36427664.

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Lam, Wai Kwan. "Investigation of interaction between solube adenylyl cyclase and p34SEI-1 /." View abstract or full-text, 2010. http://library.ust.hk/cgi/db/thesis.pl?BIOL%202010%20LAM.

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Tse, Muk-hei, and 謝牧熙. "Investigations on recombinant Arabidopsis acyl-coenzyme A binding protein 1." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2005. http://hub.hku.hk/bib/B36427664.

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Bennett, D. H. "Protein phosphatase type 1 binding proteins in Drosophila melanogaster." Thesis, University of Oxford, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.365689.

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Hetti, Arachchilage Madara Dilhani. "Coevolution of epitopes in HIV-1 pre-integration complex proteins: protein-protein interaction insights." Kent State University / OhioLINK, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=kent1530646538935895.

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Niessen, Sherry. "p120e4f-1 : a novel Bmi-1 interacting protein." Thesis, McGill University, 2003. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=80343.

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We demonstrated that the Polycomb Group (Pc-G ) gene Bmi-1 is essential for the self-renewal of both normal and leukemic stem cells. The molecular pathways through which Bmi-1 regulates stem cell function remain undefined. We identified p120E4F-1 as a novel factor, which specifically interacts with Bmi-1 in the cytoplasmic fraction of hemopoietic cells. We observed that the ability of Bmi-1 to extend the proliferative/replicative lifespan of primary fibroblasts correlated with a down-regulation of p120E4F-1 protein levels. This function of Bmi-1 occurred without affecting p120E4F-1 mRNA levels suggestive of a direct interaction between the two proteins. Conversely, p120E4F-1 levels were found to be elevated in Bmi-1-/- progenitors of several types of cerebellar interneurons, providing a molecular basis for the neuronal proliferative defect observed in the Bmi-1 -/- cerebellum. From these studies, we propose that the ability of Bmi-1 to regulate stem/progenitor cell proliferation is in part mediated through the down-regulation of cytoplasmic p120 E4F-1 levels.

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Lawrence, Charlotte. "Towards a small molecule inhibitor of the HIF-1/HIF-1 protein-protein interaction." Thesis, University of Southampton, 2015. https://eprints.soton.ac.uk/374783/.

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Hypoxia-inducible factor (HIF) is a heterodimeric, oxygen-dependent, transcription factor that regulates the cellular response to hypoxia by directing the expression of multiple genes, such as those involved in angiogenesis and glucose transport. HIF activation has been shown to aid the survival of cancer cells in hypoxic regions; hence it is viewed as a potentially important target for cancer therapy. There are two predominant isoforms of HIF, HIF-1 and HIF-2, formed by heterodimerisation of HIF-1 or HIF-2, respectively, with HIF-1. The dimerisation of the two subunits is necessary for DNA-binding and subsequent activation of transcription. Miranda et al. (2013) have recently identified a six amino acid cyclic peptide inhibitor of HIF dimerisation (cyclo-CLLFVY); the Tat-tagged variant is called P1. This has shown activity within several cell-based assays.1 This project sought to identify which amino acid residues of cyclo-CLLFVY were critical to its activity by synthesising five alanine analogues and testing them in cell and biophysical assays. It was not possible to identify an active motif and it could be concluded that the specific conformation of the intact cyclic peptide is required for activity. The functionality of independently bacterially expressed fragments of HIF-1 and HIF-1 was also validated by an EMSA. The Tavassoli group used these proteins to establish the binding location of the inhibitor to the HIF-1-PAS-B domain (work by A. Tavassoli and A. Male).

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Lubeseder-Martellato, Clara. "The guanylate binding protein-1." Diss., lmu, 2003. http://nbn-resolving.de/urn:nbn:de:bvb:19-11959.

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Sarkar, Mohosin M. "Engineering Proteins with GFP: Study of Protein-Protein Interactions In vivo, Protein Expression and Solubility." The Ohio State University, 2009. http://rave.ohiolink.edu/etdc/view?acc_num=osu1261418776.

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Books on the topic "Protein 1"

Ariga, Hiroyoshi, and Sanae M. M. Iguchi-Ariga, eds. DJ-1/PARK7 Protein. Singapore: Springer Singapore, 2017. http://dx.doi.org/10.1007/978-981-10-6583-5.

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Panchenko, Anna, and Teresa Przytycka, eds. Protein-protein Interactions and Networks. London: Springer London, 2008. http://dx.doi.org/10.1007/978-1-84800-125-1.

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Meyerkord, Cheryl L., and Haian Fu, eds. Protein-Protein Interactions. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2425-7.

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Wendt, Michael D., ed. Protein-Protein Interactions. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-28965-1.

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Pfeil, Wolfgang. Protein Stability and Folding Supplement 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-642-56462-8.

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Canzar, Stefan, and Francisca Rojas Ringeling, eds. Protein-Protein Interaction Networks. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-4939-9873-9.

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Wlodawer, Alexander, Zbigniew Dauter, and Mariusz Jaskolski, eds. Protein Crystallography. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7000-1.

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Gerrard, Juliet A., ed. Protein Nanotechnology. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-354-1.

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Korf, Ulrike, ed. Protein Microarrays. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-286-1.

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Kashina, Anna S., ed. Protein Arginylation. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2935-1.

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Book chapters on the topic "Protein 1"

Dombrádi, Viktor, Endre Kókai, and Ilona Farkas. "Protein phosphatase 1." In Protein Phosphatases, 21–44. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-540-40035-6_2.

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Schreiber, G. "CHAPTER 1. Protein–Protein Interaction Interfaces and their Functional Implications." In Protein–Protein Interaction Regulators, 1–24. Cambridge: Royal Society of Chemistry, 2020. http://dx.doi.org/10.1039/9781788016544-00001.

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Benz, Caroline, Eszter Kassa, Elias Tjärnhage, Sara Bergström Lind, and Ylva Ivarsson. "Chapter 1. Identification of Cellular Protein–Protein Interactions." In Inhibitors of Protein–Protein Interactions, 1–39. Cambridge: Royal Society of Chemistry, 2020. http://dx.doi.org/10.1039/9781839160677-00001.

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Connor, John H., Hai Quan, Carey Oliver, and Shirish Shenolikar. "Inhibitor-1, a Regulator of Protein Phosphatase 1 Function." In Protein Phosphatase Protocols, 41–58. Totowa, NJ: Humana Press, 1998. http://dx.doi.org/10.1385/0-89603-468-2:41.

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Murakami, Yota. "Heterochromatin Protein 1." In Encyclopedia of Systems Biology, 884. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-9863-7_1576.

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Lomas, David A., and David H. Perlmutter. "Alpha-1-Antitrypsin Deficiency." In Protein Misfolding Diseases, 403–23. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470572702.ch18.

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Park, Hae Ryoun, Lisa Montoya Cockrell, Yuhong Du, Andrea Kasinski, Jonathan Havel, Jing Zhao, Francisca Reyes-Turcu, Keith D. Wilkinson, and Haian Fu. "Protein–Protein Interactions." In Springer Protocols Handbooks, 463–94. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-60327-375-6_30.

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Howell, Nazlin K. "Protein-Protein Interactions." In Biochemistry of Food Proteins, 35–74. Boston, MA: Springer US, 1992. http://dx.doi.org/10.1007/978-1-4684-9895-0_2.

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Fung, Jia Jun, Karla Blöcher-Juárez, and Anton Khmelinskii. "High-Throughput Analysis of Protein Turnover with Tandem Fluorescent Protein Timers." In Methods in Molecular Biology, 85–100. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-1732-8_6.

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AbstractTandem fluorescent protein timers (tFTs) are versatile reporters of protein dynamics. A tFT consists of two fluorescent proteins with different maturation kinetics and provides a ratiometric readout of protein age, which can be exploited to follow intracellular trafficking, inheritance and turnover of tFT-tagged proteins. Here, we detail a protocol for high-throughput analysis of protein turnover with tFTs in yeast using fluorescence measurements of ordered colony arrays. We describe guidelines on optimization of experimental design with regard to the layout of colony arrays, growth conditions, and instrument choice. Combined with semi-automated genetic crossing using synthetic genetic array (SGA) methodology and high-throughput protein tagging with SWAp-Tag (SWAT) libraries, this approach can be used to compare protein turnover across the proteome and to identify regulators of protein turnover genome-wide.

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Goffin, Vincent, and Paul A. Kelly. "Protein Phosphorylation and Protein-Protein Interactions." In Hormone Signaling, 3–19. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/978-1-4757-3600-7_1.

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Conference papers on the topic "Protein 1"

Luchini, Alessandra, Luisa Paris, Virginia Espina, Kelsey Mitchell, Angela Dailing, and Lance A. Liotta. "Abstract 211: Protein painting identifies PD-1: PDL-1 therapeutic targets at protein-protein interfaces." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-211.

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Swasti, Olivia, Alhadi Bustamam, Dian Lestari, and Wibowo Mangunwardoyo. "Biclustering protein interactions between HIV-1 proteins and humans proteins using LCM-MBC algorithm." In PROCEEDINGS OF THE SYMPOSIUM ON BIOMATHEMATICS (SYMOMATH) 2018. Author(s), 2019. http://dx.doi.org/10.1063/1.5094279.

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Dan Cristea, Paul, Octavian Arsene, Rodica Tuduce, and Dan V. Nicolau. "Protein surface analysis. Part 1: Hydrophobicity densities." In 2011 10th International Symposium on Signals, Circuits and Systems (ISSCS). IEEE, 2011. http://dx.doi.org/10.1109/isscs.2011.5978748.

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"Introduction and Application of Death Protein 1." In 2022 International Conference on Biotechnology, Life Science and Medical Engineering. Clausius Scientific Press, 2022. http://dx.doi.org/10.23977/blsme.2022046.

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Ma, Liang, Meixiang Xu, and Andres F. Oberhauser. "Nanoscale Analysis of the Effect of Pathogenic Mutations on Polycystin-1." In ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASMEDC, 2010. http://dx.doi.org/10.1115/nemb2010-13093.

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The activity of proteins and their complexes often involves the conversion of chemical energy (stored or supplied) into mechanical work through conformational changes. Mechanical forces are also crucial for the regulation of the structure and function of cells and tissues. Thus, the shape of eukaryotic cells is the result of cycles of mechano-sensing, mechano-transduction, and mechano-response. Recently developed single-molecule atomic force microscopy (AFM) techniques can be used to manipulate single molecules, both in real time and under physiological conditions, and are ideally suited to directly quantify the forces involved in both intra- and intermolecular protein interactions. In combination with molecular biology and computer simulations, these techniques have been applied to characterize the unfolding and refolding reactions in a variety of proteins, such as titin (an elastic mechano-sensing protein found in muscle) and polycystin-1 (PC1, a mechanosensor found in the kidney).

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Barnes, Bradley, Maryam Karimloo, Andrew Schoenrock, Daniel Burnside, Edana Cassol, Alex Wong, Frank Dehne, Ashkan Golshani, and James R. Green. "Predicting novel protein-protein interactions between the HIV-1 virus and homo sapiens." In 2016 IEEE EMBS International Student Conference (ISC). IEEE, 2016. http://dx.doi.org/10.1109/embsisc.2016.7508598.

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GUARRACINO, M. R., A. NEBBIA, A. CHINCHULUUN, and P. M. PARDALOS. "PROTEIN-PROTEIN INTERACTIONS PREDICTION USING 1-NEAREST NEIGHBORS CLASSIFICATION ALGORITHM AND FEATURE SELECTION." In International Symposium on Mathematical and Computational Biology. WORLD SCIENTIFIC, 2010. http://dx.doi.org/10.1142/9789814304900_0018.

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Tuszynski, George, Vicki L. Rothman, Mohammed Gutu, and Frank Chang. "Abstract 3183: The role of G-protein coupled receptor-associated sorting protein 1 (GASP-1) in breast cancer progression." 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.am2011-3183.

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Hasegawa, Hirotsugu, Naoki Inui, Takafumi Suda, Dai Hashimoto, Tomoyuki Fujisawa, Noriyuki Enomoto, Yutaro Nakamura, and Kingo Chida. "Multidrug Resistance Protein 1 And Multidrug Resistance-Associated Protein 1 Expression In Young And Aged Murine Lung Dendritic Cells." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a2842.

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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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Reports on the topic "Protein 1"

Disis, Mary L. Immunity to HER-1/neu Protein. Fort Belvoir, VA: Defense Technical Information Center, October 1999. http://dx.doi.org/10.21236/ada390484.

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Disis, Mary L. Immunity to HER-1/neu Protein. Fort Belvoir, VA: Defense Technical Information Center, October 2000. http://dx.doi.org/10.21236/ada391420.

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Clarke, Robert. X-Box Binding Protein-1 in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, August 2005. http://dx.doi.org/10.21236/ada446755.

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Clarke, Robert R. X-Box Binding Protein-1 in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, August 2004. http://dx.doi.org/10.21236/ada433869.

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Clarke, Robert R. X-Box Binding Protein-1 in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, August 2003. http://dx.doi.org/10.21236/ada421992.

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Clarke, Robert. X-Box Binding Protein-1 in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, August 2006. http://dx.doi.org/10.21236/ada460787.

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Weiss, Shimon. Biochemical and Physiological Characterization: Development & Apply Optical Methods for Charaterizing Biochemical Protein-Protein Interactions in MR-1. Office of Scientific and Technical Information (OSTI), August 2006. http://dx.doi.org/10.2172/890585.

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Rivera, Charlene. Role of Nonreceptor Protein Kinase Ack 1 in Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, May 2011. http://dx.doi.org/10.21236/ada545693.

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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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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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Weiss, Shimon, and Xavier Michalet. Single-Molecule Methods for the Large-Scale Characterization of Expression Levels and Protein-Protein Interactions in Shewanella Oneidensis MR-1. Office of Scientific and Technical Information (OSTI), October 2008. http://dx.doi.org/10.2172/1010284.

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