Bibliografías temáticas / Proteins – Affinity labeling

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Literatura académica sobre el tema "Proteins – Affinity labeling"

Autor: Grafiati
Publicado: 4 de junio de 2021
Última modificación: 1 de febrero de 2022

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Artículos de revistas sobre el tema "Proteins – Affinity labeling"

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SWEET, FREDERICK, and GARY L. MURDOCK. "Affinity Labeling of Hormone-Specific Proteins*." Endocrine Reviews 8, no. 2 (May 1987): 154–84. http://dx.doi.org/10.1210/edrv-8-2-154.

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Vinkenborg, Jan L., Günter Mayer, and Michael Famulok. "Aptamer-Based Affinity Labeling of Proteins." Angewandte Chemie International Edition 51, no. 36 (August 2, 2012): 9176–80. http://dx.doi.org/10.1002/anie.201204174.

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Löw, Andreas, Heinz G. Faulhammer, and Mathias Sprinzl. "Affinity labeling of GTP-binding proteins in cellular extracts." FEBS Letters 303, no. 1 (May 25, 1992): 64–68. http://dx.doi.org/10.1016/0014-5793(92)80478-y.

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Song, Yinan, Feng Xiong, Jianzhao Peng, Yi Man Eva Fung, Yiran Huang, and Xiaoyu Li. "Introducing aldehyde functionality to proteins using ligand-directed affinity labeling." Chemical Communications 56, no. 45 (2020): 6134–37. http://dx.doi.org/10.1039/d0cc01982h.

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Maldonado, H. M., and P. M. Cala. "Labeling of the Amphiuma erythrocyte K+/H+ exchanger with H2DIDS." American Journal of Physiology-Cell Physiology 267, no. 4 (October 1, 1994): C1002—C1012. http://dx.doi.org/10.1152/ajpcell.1994.267.4.c1002.

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Subsequent to swelling, the Amphiuma red blood cells lose K+, Cl-, and water until normal cell volume is restored. Net solute loss is the result of K+/H+ and Cl-/HCO3- exchangers functionally coupled through changes in pH and therefore HCO3-. Whereas the Cl-/HCO3- exchanger is constitutively active, K+/H+ actively is induced by cell swelling. The constitutive Cl-/HCO3- exchanger is inhibited by low concentrations (< 1 microM) of 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS) or H2DIDS, yet the concentration of H2DIDS > 25 microM irreversibly modifies the K+/H+ exchanger in swoll
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6

Chen, Xi, Fu Li, and Yao-Wen Wu. "Chemical labeling of intracellular proteins via affinity conjugation and strain-promoted cycloadditions in live cells." Chemical Communications 51, no. 92 (2015): 16537–40. http://dx.doi.org/10.1039/c5cc05208d.

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Masselin, Arnaud, Antoine Petrelli, Maxime Donzel, Sylvie Armand, Sylvain Cottaz, and Sébastien Fort. "Unprecedented Affinity Labeling of Carbohydrate-Binding Proteins with s-Triazinyl Glycosides." Bioconjugate Chemistry 30, no. 9 (August 12, 2019): 2332–39. http://dx.doi.org/10.1021/acs.bioconjchem.9b00432.

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Vale, M. G. "Affinity labeling of calmodulin-binding proteins in skeletal muscle sarcoplasmic reticulum." Journal of Biological Chemistry 263, no. 26 (September 1988): 12872–77. http://dx.doi.org/10.1016/s0021-9258(18)37642-7.

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Laudon, Moshe, and Nava Zisapel. "Melatonin binding proteins identified in the rat brain by affinity labeling." FEBS Letters 288, no. 1-2 (August 19, 1991): 105–8. http://dx.doi.org/10.1016/0014-5793(91)81013-x.

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Kuwahara, Daichi, Takahiro Hasumi, Hajime Kaneko, Madoka Unno, Daisuke Takahashi, and Kazunobu Toshima. "A solid-phase affinity labeling method for target-selective isolation and modification of proteins." Chem. Commun. 50, no. 98 (2014): 15601–4. http://dx.doi.org/10.1039/c4cc06783e.

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Solid-phase affinity labeling of target proteins with the specifically designed chemical tools selectively and effectively furnished the labeled target proteins without the need for tedious manipulations.
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Tesis sobre el tema "Proteins – Affinity labeling"

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Lui, James Kwok Ching. "A fluorescent labelling technique to detect changes in the thiol redox state of proteins following mild oxidative stress." University of Western Australia. School of Biomedical, Biomolecular and Chemical Sciences, 2008. http://theses.library.uwa.edu.au/adt-WU2008.0056.

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There is increasing evidence that hydrogen peroxide (H2O2) can act as a signalling molecule capable of modulating a variety of biochemical and genetic systems. Using Jurkat T-lymphocytes, this study initially investigated the involvement of H2O2 in the activation of a specific signalling protein extracellular signal-regulated protein kinase (ERK). It was found that as a result of H2O2 treatment, mitochondrial complex activities decreased which led to subsequent increase of mitochondrial reactive oxygen species (ROS) production. The increase of ROS resulted in higher cellular H2O2 as well as i
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Song, Zhi-Ning. "Development of novel affinity-guided catalysts for specific labeling of endogenous proteins in living systems." Kyoto University, 2017. http://hdl.handle.net/2433/228238.

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Ciccotosto, Silvana. "The preparation and evaluation of N-acetylneuraminic acid derivatives as probes of sialic acid-recognizing proteins." Monash University, Dept. of Medicinal Chemistry, 2004. http://arrow.monash.edu.au/hdl/1959.1/9649.

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Tran, Hang T. "Photocleavable Linker for Protein Affinity Labeling to Identify the Binding Target of KCN-1." Digital Archive @ GSU, 2010. http://digitalarchive.gsu.edu/chemistry_theses/35.

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KCN-1 is known to reduce tumor growth 6-fold in mice implanted with LN229 glioma cells. Although this inhibitor is effective, the mechanism of action for KCN-1 is not well understood. Based on preliminary studies, KCN-1 reduces tumor growth by disrupting the HIF 1 (hypoxia-induced factor-1) pathway. The binding target of KCN-1 needs to be investigated in order to develop KCN-1 or its analogs for therapeutic applications. In this research, a molecule was designed and synthesized for the identification of the binding target of KCN-1. Specifically, this molecule contains the inhibitor (KCN-1
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Kaminska, Monika. "New activity-based probes to detect matrix metalloproteases." Thesis, Université Paris-Saclay (ComUE), 2018. http://www.theses.fr/2018SACLS538/document.

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Les Métallo Protéases Matricielles (MMP) en tant qu'endopeptidases à zinc ont une large gamme de fonctions biologiques allant du remodelage tissulaire à la modulation de la réponse cellulaire. Une modification de leur activité protéolytique est souvent associée à de nombreux désordres biologiques. In vivo, ces protéases sont soumises à de nombreuses modifications post-traductionnelles. Elles sont sécrétées sous formes latentes à l'extérieur des cellules pour être ensuite transformées en forme fonctionnelles. Ces dernières sont ensuite inhibées par des inhibiteurs endogènes. En raison de leur s
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Cigler, Marko [Verfasser], Kathrin [Akademischer Betreuer] Lang, Kathrin [Gutachter] Lang, and Stephan [Gutachter] Hacker. "Genetically encoding unnatural amino acids: Novel tools for protein labelling and chemical stabilisation of low-affinity protein complexes / Marko Cigler ; Gutachter: Kathrin Lang, Stephan Hacker ; Betreuer: Kathrin Lang." München : Universitätsbibliothek der TU München, 2019. http://d-nb.info/1220322318/34.

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Goulding, Ann Marie. "Biochemical applications of DsRed-monomer utilizing fluorescence and metal-binding affinity." 2011. http://hdl.handle.net/1805/2480.

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Indiana University-Purdue University Indianapolis (IUPUI)<br>The discovery and isolation of naturally occurring fluorescent proteins, FPs, have provided much needed tools for molecular and cellular level studies. Specifically the cloning of green fluorescent protein, GFP, revolutionized the field of biotechnology and biochemical research. Recently, a red fluorescent protein, DsRed, isolated from the Discosoma coral has further expanded the pallet of available fluorescent tools. DsRed shares only 23 % amino acid sequence homology with GFP, however the X-ray crystal structures of the two prot
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Krusemark, Casey J. "Synthetic chemical approaches to proteomics : affinity labeling and protein functional group modification /." 2007. http://www.library.wisc.edu/databases/connect/dissertations.html.

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Libros sobre el tema "Proteins – Affinity labeling"

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Protein affinity tags: Methods and protocols. New York: Humana Press, 2014.

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Viktorovich, Vlasov Valentin, ed. Affinity modification of biopolymers. Boca Raton, Fla: CRC Press, 1989.

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3

1949-, Müller S. C., ed. Synthetic peptides as antigens. Amsterdam: Elsevier, 1999.

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4

1940-, Creighton Thomas E., ed. Protein function: A practical approach. Oxford: IRL Press, 1989.

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1940-, Creighton Thomas E., ed. Protein function: A practical approach. 2nd ed. Oxford: IRL Press at Oxford University Press, 1997.

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Creighton, Thomas E. Protein Structure and Protein Function: A Practical Approach 2 Volume Set (Practical Approach Series, 175). Oxford University Press, USA, 1997.

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Protein Structure and Protein Function: A Practical Approach 2 Volume Set (The Practical Approach Series , No 174&175). 2nd ed. Oxford University Press, USA, 1997.

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Capítulos de libros sobre el tema "Proteins – Affinity labeling"

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Tamura, Tomonori, and Itaru Hamachi. "Labeling Proteins by Affinity-Guided DMAP Chemistry." In Site-Specific Protein Labeling, 229–42. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-2272-7_16.

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Colman, Roberta F. "Advances in Affinity Labeling of Purine Nucleotide Sites in Dehydrogenases." In Proteins, 569–80. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1787-6_57.

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Misono, Kunio S. "Atrial Natriuretic Factor Receptor in Adrenal Plasma Membrane: Identification by Photo-Affinity Labeling." In Proteins, 641–48. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1787-6_64.

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Peter, Marcus E., and Mathias Sprinzl. "Affinity Labeling of the GDP/GTP Binding Site in Thermus Thermophilus Elongation Factor Tu." In The Guanine — Nucleotide Binding Proteins, 99–110. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4757-2037-2_10.

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Chen, Xi, Fu Li, and Yao-Wen Wu. "Affinity Conjugation for Rapid and Covalent Labeling of Proteins in Live Cells." In Methods in Molecular Biology, 191–202. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9537-0_15.

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Landgraf, Peter, Elmer R. Antileo, Erin M. Schuman, and Daniela C. Dieterich. "BONCAT: Metabolic Labeling, Click Chemistry, and Affinity Purification of Newly Synthesized Proteomes." In Site-Specific Protein Labeling, 199–215. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-2272-7_14.

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Singer, S. J. "Affinity Labelling of Protein Active Sites." In Ciba Foundation Symposium - Molecular Properties of Drug Receptors, 229–46. Chichester, UK: John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470719763.ch11.

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Jonák, Jiří, Karel Karas, and Ivan Rychlík. "Characterization of Elongation Factor Tu from Bacillus Subtilis Modified by Affinity Labelling." In The Guanine — Nucleotide Binding Proteins, 111–19. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4757-2037-2_11.

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Xiao, Zhen, and Timothy D. Veenstra. "Comparison of Protein Expression by Isotope-Coded Affinity Tag Labeling." In Methods in Molecular Biology™, 181–92. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-117-8_10.

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Ji, Tae H., Ryuichiro Nishimura, and Inhae Ji. "Chapter 11 Affinity Labeling of Binding Proteins for the Study of Endocytic Pathways." In Methods in Cell Biology, 277–304. Elsevier, 1989. http://dx.doi.org/10.1016/s0091-679x(08)61176-0.

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Actas de conferencias sobre el tema "Proteins – Affinity labeling"

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Kruithof, E. KO, W. D. Schleuning, and F. Bachman. "PLASMINOGEN ACTIVATOR INHIBITOR BIOCHEMICAL AND CLINICAL ASPECTS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644764.

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Plasminogen activator (PAs) are enzymes that convert the zymogen plasminogen into the trypsin-like protease plasmin, which degrades extracellular matrix proteins and fibrin in the course of fibrinolysis, embryogenesis, tissue remodeling and in tumor metastasis. Plasminogen activator inhibitors (PAIs) are important modulators of PA activity. Several proteins have been identified which inhibit at fast rates urokinase (u-PA) and tissue-type PA (t-PA). In the order of inhibition rate constants these are: a) PAI-1, present in human plasma and platelet extracts and purified from human endothelial ce
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