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Auswahl der wissenschaftlichen Literatur zum Thema „Recombinant proteins Analysis“
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Zeitschriftenartikel zum Thema "Recombinant proteins Analysis"
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.
Der volle Inhalt der QuelleKermasha, S., und I. Alli. „Purification and analysis of recombinant proteins“. Food Research International 26, Nr. 2 (Januar 1993): 158–59. http://dx.doi.org/10.1016/0963-9969(93)90072-q.
Der volle Inhalt der QuelleKaufman, Randal J. „Mammalian recombinant proteins: Structure, function and immunological analysis“. Current Opinion in Biotechnology 1, Nr. 2 (Dezember 1990): 141–50. http://dx.doi.org/10.1016/0958-1669(90)90023-e.
Der volle Inhalt der QuelleSenear, Donald F., Robert A. Mendelson, Deborah B. Stone, Linda A. Luck, Elena Rusinova und J. B. Alexander Ross. „Quantitative Analysis of Tryptophan Analogue Incorporation in Recombinant Proteins“. Analytical Biochemistry 300, Nr. 1 (Januar 2002): 77–86. http://dx.doi.org/10.1006/abio.2001.5441.
Der volle Inhalt der QuelleKollárovič, G., D. Majera, K. Luciaková und P. Baráth. „Expression and purification of recombinant NFI proteins for functional analysis“. General Physiology and Biophysics 28, Nr. 4 (2009): 331–39. http://dx.doi.org/10.4149/gpb_2009_04_331.
Der volle Inhalt der QuelleCoutinho, M., K. S. Aulak und A. E. Davis. „Functional analysis of the serpin domain of C1 inhibitor.“ Journal of Immunology 153, Nr. 8 (15.10.1994): 3648–54. http://dx.doi.org/10.4049/jimmunol.153.8.3648.
Der volle Inhalt der QuelleJerlström-Hultqvist, Jon, Britta Stadelmann, Sandra Birkestedt, Ulf Hellman und Staffan G. Svärd. „Plasmid Vectors for Proteomic Analyses in Giardia: Purification of Virulence Factors and Analysis of the Proteasome“. Eukaryotic Cell 11, Nr. 7 (18.05.2012): 864–73. http://dx.doi.org/10.1128/ec.00092-12.
Der volle Inhalt der QuelleSims, Andrew H., Manda E. Gent, Karin Lanthaler, Nigel S. Dunn-Coleman, Stephen G. Oliver und Geoffrey D. Robson. „Transcriptome Analysis of Recombinant Protein Secretion by Aspergillus nidulans and the Unfolded-Protein Response In Vivo“. Applied and Environmental Microbiology 71, Nr. 5 (Mai 2005): 2737–47. http://dx.doi.org/10.1128/aem.71.5.2737-2747.2005.
Der volle Inhalt der QuelleZeck, 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, Nr. 7 (06.07.2012): e40328. http://dx.doi.org/10.1371/journal.pone.0040328.
Der volle Inhalt der QuelleViseux, N., X. Hronowski, J. Delaney und B. Domon. „Qualitative and Quantitative Analysis of the Glycosylation Pattern of Recombinant Proteins“. Analytical Chemistry 73, Nr. 20 (Oktober 2001): 4755–62. http://dx.doi.org/10.1021/ac015560a.
Der volle Inhalt der QuelleDissertationen zum Thema "Recombinant proteins Analysis"
Lee, Jae-Yong. „Expression, purification and interaction analysis of recombinant SRB proteins“. Thesis, Imperial College London, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.407809.
Der volle Inhalt der QuelleKotlarski, Nicholas. „Process-scale renaturation of recombinant proteins from inclusion bodies /“. Title page, contents and summary only, 1998. http://web4.library.adelaide.edu.au/theses/09PH/09phk87.pdf.
Der volle Inhalt der QuelleKepple, Kevin V. „Analysis of the binding mechanisms and cellular targets of peptide inhibitors that block site-specific recombination in vitro /“. Diss., Connect to a 24 p. preview or request complete full text in PDF formate. Access restricted to UC campuses, 2006. http://wwwlib.umi.com/cr/ucsd/fullcit?p3208620.
Der volle Inhalt der QuelleCastilho, Alexandra Marina Machado Ferreira. „Molecular cytogenic analysis of recombinant chromosomes in wheat - Aegilops umbellulata lines“. Thesis, University of East Anglia, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.296341.
Der volle Inhalt der QuelleRauf, Femina. „Chimeric and Recombinant Protein Reagents for Cellular Analysis and Immunoassays“. Diss., The University of Arizona, 2011. http://hdl.handle.net/10150/145441.
Der volle Inhalt der QuelleLarsen, Sasha Ellen Marie. „Characterization of components that increase secretion of recombinant proteins in pichia pastoris“. Scholarly Commons, 2011. https://scholarlycommons.pacific.edu/uop_etds/769.
Der volle Inhalt der QuelleCarre, Heather Emily. „Expression and analysis of recombinant mycoplasma hyponeumoniae proteins as potential subunit vaccine candidates“. Thesis, Royal Veterinary College (University of London), 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.522182.
Der volle Inhalt der QuelleMoore, Shona. „An analysis of the structure and function of malarial Duffy-binding-like protein domains using recombinant fusion proteins“. Thesis, University of Warwick, 2016. http://wrap.warwick.ac.uk/86933/.
Der volle Inhalt der QuellePrasad, Alpana. „Immune function and structural analysis of recombinant bovine conglutinin and human lung surfactant protein-D“. Thesis, University of Oxford, 2000. http://ora.ox.ac.uk/objects/uuid:f9a5ae66-4ed0-4bdf-90eb-c873ca44147d.
Der volle Inhalt der QuelleAlodailah, Sattam Sonitan. „The Generation of Recombinant Zea mays Spastin and Katanin Proteins for In Vitro Analysis“. Thesis, University of North Texas, 2017. https://digital.library.unt.edu/ark:/67531/metadc1062897/.
Der volle Inhalt der QuelleBücher zum Thema "Recombinant proteins Analysis"
1952-, Seetharam Ramnath, und Sharma Satish K. 1951-, Hrsg. Purification and analysis of recombinant proteins. New York: M. Dekker, 1991.
Den vollen Inhalt der Quelle findenW, Thorner Jeremy, Emr Scott und Abelson John, Hrsg. Applications of chimeric genes and hybrid proteins. San Diego, CA: Academic Press, 2000.
Den vollen Inhalt der Quelle findenProtein affinity tags: Methods and protocols. New York: Humana Press, 2014.
Den vollen Inhalt der Quelle findenThomas, Sandra M. Patenting of recombinant proteins: An analysis of tissue plasminogen activator (t-PA) in Europe, United States and Japan. Brighton: University of Sussex, Science Policy Research Unit, 1994.
Den vollen Inhalt der Quelle finden1947-, Stein Stanley, Hrsg. Fundamentals of protein biotechnology. New York: M. Dekker, 1990.
Den vollen Inhalt der Quelle findenHaining, Robert Luddy. Structure/function studies at the active-site region of cyanobacterial ribulose bisphosphate carboxylase/oxygenase by site-directed mutagenesis. 1993.
Den vollen Inhalt der Quelle findenMichaud, Dominique. Recombinant Protease Inhibitors in Plants (Biotechnology Intelligence Unit, 3). Landes Bioscience, 2000.
Den vollen Inhalt der Quelle findenGiannone, Richard J., und Andrew B. Dykstra. Protein Affinity Tags: Methods and Protocols. Springer New York, 2016.
Den vollen Inhalt der Quelle findenBuchteile zum Thema "Recombinant proteins Analysis"
Buntru, Matthias, Simon Vogel, Ricarda Finnern und Stefan Schillberg. „Plant-Based Cell-Free Transcription and Translation of Recombinant Proteins“. In Recombinant Proteins in Plants, 113–24. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2241-4_8.
Der volle Inhalt der QuelleThangaraj, Harry. „Freedom to Operate Analysis of Molecular Farming Projects“. In Recombinant Proteins in Plants, 335–42. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2241-4_18.
Der volle Inhalt der QuelleFitchette-Lainé, Anne-Catherine, Lise-Anne Denmat, Patrice Lerouge und Loïc Faye. „Analysis of N- and O-Glycosylation of Plant Proteins“. In Recombinant Proteins from Plants, 271–90. Totowa, NJ: Humana Press, 1998. http://dx.doi.org/10.1007/978-1-60327-260-5_19.
Der volle Inhalt der QuelleTong, Kit I., Masayuki Yamamoto und Toshiyuki Tanaka. „Selective Isotope Labeling of Recombinant Proteins in Escherichia coli“. In Intrinsically Disordered Protein Analysis, 439–48. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-3704-8_30.
Der volle Inhalt der QuelleSominskaya, Irina, und Kaspars Tars. „Immunological Methods for Analysis of Recombinant Proteins“. In Basic Cloning Procedures, 135–44. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-71965-3_7.
Der volle Inhalt der QuelleArakawa, Tsutomu, und John S. Philo. „Biophysical and Biochemical Analysis of Recombinant Proteins“. In Pharmaceutical Biotechnology, 19–45. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-6486-0_2.
Der volle Inhalt der QuelleTolkatchev, Dmitri, Josee Plamondon, Richard Gingras, Zhengding Su und Feng Ni. „Recombinant Production of Intrinsically Disordered Proteins for Biophysical and Structural Characterization“. In Instrumental Analysis of Intrinsically Disordered Proteins, 653–70. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470602614.ch22.
Der volle Inhalt der QuelleMicsonai, András, Éva Bulyáki und József Kardos. „BeStSel: From Secondary Structure Analysis to Protein Fold Prediction by Circular Dichroism Spectroscopy“. In Methods in Molecular Biology, 175–89. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0892-0_11.
Der volle Inhalt der QuelleMattaliano, R. J., J. J. Rosa, C. Foeller, J. P. Woodard und M. J. Bertolini. „Analysis of Recombinant Proteins — Current Trends and Practical Limits in Analytical Stringency“. In Methods in Protein Sequence Analysis · 1986, 79–95. Totowa, NJ: Humana Press, 1987. http://dx.doi.org/10.1007/978-1-59259-480-1_6.
Der volle Inhalt der QuelleChen, Zeya, und Jingjing Huang. „In Vitro Biochemical Analysis of Recombinant Plant Proteins Under Oxidation“. In Methods in Molecular Biology, 143–60. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2469-2_11.
Der volle Inhalt der QuelleKonferenzberichte zum Thema "Recombinant proteins Analysis"
Furis, B. C., M. J. Jorgensem, M. J. Rabiet, A. B. Contor, C. L. Brown, C. B. Shoemaker und B. Furie. „RECOGNITION SITE DIRECTING GAMMA-CARBOXYLATION RESIDES ON THE PROPEPTIDES OF FACTOR IX AND PROTRROMBIN“. In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643992.
Der volle Inhalt der QuelleAshok Kumar, A., Margaret Insley, Jay Gambee, Sharon J. Busby und Kathleen L. Berkner. „SITE SPECIFIC MUTAGENESIS WITHIN THE GLA-DOMAIN OF HUMAN FACTOR IX“. In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644079.
Der volle Inhalt der QuelleHiggins, Deborah L., und William E. Holmes. „CHARACTERIZATION OF RECOMBINANT HUMAN TISSUE-TYPE PLASMINOGEN ACTIVATOR MISSING THE FINGER DOMAIN“. In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643842.
Der volle Inhalt der QuelleAl-Mohannadi, Anjud Khamis, Sara Deola und Ahmed Malki. „Visualization of Factor Viii with Flow-Cytometry as a tool for Novel Gene Therapy Approach in Hemophilia A“. In Qatar University Annual Research Forum & Exhibition. Qatar University Press, 2020. http://dx.doi.org/10.29117/quarfe.2020.0164.
Der volle Inhalt der QuelleBusby, S., K. Berkner, L. Halfpap, J. Gambee und A. Kumar. „ALTERATION OF PROPTIDE SEQUENCE IMPAIRS BIOLOGICAL ACTIVITY OF HUMAN FACTOR VII“. In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643784.
Der volle Inhalt der QuelleJorgensen, M. J., MJ Rabiet, A. B. Cantor, B. Furie, C. L. Brown, C. B. Shoemaker und B. C. Furie. „VITAMIN K-DEPENDENT γ-CARBOXYLATION OF FACTOR IX REQUIRES A RECOGNITION SITE CONTAINED WITHIN THE PROPEPTIDE“. In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643564.
Der volle Inhalt der QuelleQuertermous, T., J. M. Schnee, M. S. Runge, G. R. Matsueda, N. W. Hudson, J. G. Seidman und E. Haber. „EXPRESSION OF A RECOMBINANT ANTIBODY-TARGETED THROMBOLYTIC MOLECULE“. In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644616.
Der volle Inhalt der QuelleLeDuc, Philip R., und Michael J. Betenbaugh. „Implementation of a Pharmocokinetic Approach to a Baculovirus System for Analytic Solutions to Virus and Cell Interactions“. In ASME 1997 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 1997. http://dx.doi.org/10.1115/imece1997-0282.
Der volle Inhalt der QuelleGiannelli, B. F. „MOLECULAR GENETICS OF HAEMOPHILIA“. In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643981.
Der volle Inhalt der QuelleZhang, Y., W. McKeand, T. Yuraszeck, W. Seifert, A. Feussner, E. Santagostino und J. Sidhu. „Population Pharmacokinetic Analysis of Recombinant Fusion Protein Linking Coagulation Factor IX with Recombinant Albumin (rIX-FP) in Adult and Pediatric Patients with Severe Hemophilia B“. In 63rd Annual Meeting of the Society of Thrombosis and Haemostasis Research. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1680223.
Der volle Inhalt der QuelleBerichte der Organisationen zum Thema "Recombinant proteins Analysis"
Morrison, Mark, Joshuah Miron, Edward A. Bayer und Raphael Lamed. Molecular Analysis of Cellulosome Organization in Ruminococcus Albus and Fibrobacter Intestinalis for Optimization of Fiber Digestibility in Ruminants. United States Department of Agriculture, März 2004. http://dx.doi.org/10.32747/2004.7586475.bard.
Der volle Inhalt der QuelleFluhr, Robert, und Maor Bar-Peled. Novel Lectin Controls Wound-responses in Arabidopsis. United States Department of Agriculture, Januar 2012. http://dx.doi.org/10.32747/2012.7697123.bard.
Der volle Inhalt der QuelleSadot, Einat, Christopher Staiger und Mohamad Abu-Abied. Studies of Novel Cytoskeletal Regulatory Proteins that are Involved in Abiotic Stress Signaling. United States Department of Agriculture, September 2011. http://dx.doi.org/10.32747/2011.7592652.bard.
Der volle Inhalt der QuelleDolja, Valerian V., Amit Gal-On und Victor Gaba. Suppression of Potyvirus Infection by a Closterovirus Protein. United States Department of Agriculture, März 2002. http://dx.doi.org/10.32747/2002.7580682.bard.
Der volle Inhalt der QuelleEyal, Yoram, und Sheila McCormick. Molecular Mechanisms of Pollen-Pistil Interactions in Interspecific Crossing Barriers in the Tomato Family. United States Department of Agriculture, Mai 2000. http://dx.doi.org/10.32747/2000.7573076.bard.
Der volle Inhalt der QuelleEldar, Avigdor, und Donald L. Evans. Streptococcus iniae Infections in Trout and Tilapia: Host-Pathogen Interactions, the Immune Response Toward the Pathogen and Vaccine Formulation. United States Department of Agriculture, Dezember 2000. http://dx.doi.org/10.32747/2000.7575286.bard.
Der volle Inhalt der QuelleRaghothama, Kashchandra G., Avner Silber und Avraham Levy. Biotechnology approaches to enhance phosphorus acquisition of tomato plants. United States Department of Agriculture, Januar 2006. http://dx.doi.org/10.32747/2006.7586546.bard.
Der volle Inhalt der QuelleFunkenstein, Bruria, und Shaojun (Jim) Du. Interactions Between the GH-IGF axis and Myostatin in Regulating Muscle Growth in Sparus aurata. United States Department of Agriculture, März 2009. http://dx.doi.org/10.32747/2009.7696530.bard.
Der volle Inhalt der QuelleMawassi, Munir, und Valerian Dolja. Role of RNA Silencing Suppression in the Pathogenicity and Host Specificity of the Grapevine Virus A. United States Department of Agriculture, Januar 2010. http://dx.doi.org/10.32747/2010.7592114.bard.
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