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Artículos de revistas sobre el tema "Affinity labeling"

Autor: Grafiati
Publicado: 4 de junio de 2021
Última modificación: 25 de febrero de 2023

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1

Ji, Tae H., and Inhae Ji. "Macromolecular affinity labeling." In Vitro Cellular & Developmental Biology 25, no. 8 (August 1989): 676–78. http://dx.doi.org/10.1007/bf02623719.

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2

Martini, C., and A. Lucacchini. "Affinity Labeling of Adenosine A1Binding Sites." Journal of Neurochemistry 49, no. 3 (September 1987): 681–84. http://dx.doi.org/10.1111/j.1471-4159.1987.tb00947.x.

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3

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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4

Shi, Yi Qun, Setsuo Furuyoshi, Ivo Hubacek, and Robert R. Rando. "Affinity labeling of lecithin retinol acyltransferase." Biochemistry 32, no. 12 (March 1993): 3077–80. http://dx.doi.org/10.1021/bi00063a019.

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5

Li, Hong-yu, Ying Liu, Kan Fang, and Koji Nakanishi. "A simple photo-affinity labeling protocol." Chemical Communications, no. 4 (1999): 365–66. http://dx.doi.org/10.1039/a809507h.

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6

SYVERTSEN, Christian, and John S. McKINLEY-McKEE. "Affinity Labeling of Liver Alcohol Dehydrogenase." European Journal of Biochemistry 117, no. 1 (March 3, 2005): 165–70. http://dx.doi.org/10.1111/j.1432-1033.1981.tb06316.x.

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7

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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8

Takaoka, Yousuke, Yuuki Nukadzuka, and Minoru Ueda. "Reactive group-embedded affinity labeling reagent for efficient intracellular protein labeling." Bioorganic & Medicinal Chemistry 25, no. 11 (June 2017): 2888–94. http://dx.doi.org/10.1016/j.bmc.2017.02.059.

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9

Nakanishi, Shuichi, Hiroyuki Tanaka, Kazuhito Hioki, Kohei Yamada, and Munetaka Kunishima. "Labeling study of avidin by modular method for affinity labeling (MoAL)." Bioorganic & Medicinal Chemistry Letters 20, no. 23 (December 2010): 7050–53. http://dx.doi.org/10.1016/j.bmcl.2010.09.109.

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10

Rivera-Monroy, Zuly, Guenther K. Bonn, and András Guttman. "Fluorescent isotope-coded affinity tag 2: Peptide labeling and affinity capture." ELECTROPHORESIS 30, no. 7 (April 2009): 1111–18. http://dx.doi.org/10.1002/elps.200800830.

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11

Perfilov, Maxim M., Alexey S. Gavrikov, Konstantin A. Lukyanov, and Alexander S. Mishin. "Transient Fluorescence Labeling: Low Affinity—High Benefits." International Journal of Molecular Sciences 22, no. 21 (October 30, 2021): 11799. http://dx.doi.org/10.3390/ijms222111799.

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Fluorescent labeling is an established method for visualizing cellular structures and dynamics. The fundamental diffraction limit in image resolution was recently bypassed with the development of super-resolution microscopy. Notably, both localization microscopy and stimulated emission depletion (STED) microscopy impose tight restrictions on the physico-chemical properties of labels. One of them—the requirement for high photostability—can be satisfied by transiently interacting labels: a constant supply of transient labels from a medium replenishes the loss in the signal caused by photobleachi
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12

LINDNER, Anton J., Stephan J. GLASER, Christof K. BIEBRICHER, and Guido R. HARTMANN. "Self-catalysed affinity labeling of Qbeta replicase." European Journal of Biochemistry 202, no. 2 (December 1991): 249–54. http://dx.doi.org/10.1111/j.1432-1033.1991.tb16369.x.

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13

Sharifi, B. G., and T. C. Johnson. "Affinity labeling of the sialoglycopeptide antimitogen receptor." Journal of Biological Chemistry 262, no. 32 (November 1987): 15752–55. http://dx.doi.org/10.1016/s0021-9258(18)47792-7.

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14

Nakatani, Kazuhiko, Souta Horie, and Isao Saito. "Affinity Labeling of a Single Guanine Bulge." Journal of the American Chemical Society 125, no. 30 (July 2003): 8972–73. http://dx.doi.org/10.1021/ja0350740.

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15

Matsueda, Rei, Hideaki Umeyama, Rajinder N. Puri, Harlan N. Bradford, and Robert W. Colman. "Potent Affinity Labeling Peptide Inhibitors of Calpain." Chemistry Letters 19, no. 2 (February 1990): 191–94. http://dx.doi.org/10.1246/cl.1990.191.

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16

Rayford, R., D. D. Anthony, R. E. O'Neill, and W. C. Merrick. "Reductive alkylation with oxidized nucleotides. Use in affinity labeling or affinity chromatography." Journal of Biological Chemistry 260, no. 29 (December 1985): 15708–13. http://dx.doi.org/10.1016/s0021-9258(17)36316-0.

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17

Chiba, Kosuke, Yuichi Hashimoto, and Takao Yamaguchi. "Affinity Labeling with 4-Azidophthalimide (AzPI): Relation between Labeling Rate and Fluorescence Intensity." Chemical and Pharmaceutical Bulletin 65, no. 10 (2017): 994–96. http://dx.doi.org/10.1248/cpb.c17-00546.

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18

COLMAN, ROBERTA F., JEROME M. BAILEY, DIANNE L. DeCAMP, YU-CHU HUANG, and SARA H. VOLLMER. "Affinity Labeling of Adenine Nucleotide Sites in Enzymes." Annals of the New York Academy of Sciences 603, no. 1 Biological Ac (December 1990): 417–26. http://dx.doi.org/10.1111/j.1749-6632.1990.tb37690.x.

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19

Takagi, Shiro, Mikihiko Kobayashi, Tadanori Urayama, Itsuko Suzawa, Kazuo Matsuda та Eiji Ichishima. "Affinity Labeling of Muscle Phosphorylasebwith α-Cyclodextrin-Dialdehyde". Agricultural and Biological Chemistry 52, № 11 (листопад 1988): 2709–16. http://dx.doi.org/10.1080/00021369.1988.10869125.

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20

Ray, Rahul, Narasimha Swamy, Paul N. MacDonald, Swapna Ray, Mark R. Haussler, and Michael F. Holick. "Affinity Labeling of the 1,25-Dihydroxyvitamin D Receptor." Journal of Biological Chemistry 271, no. 4 (January 26, 1996): 2012–17. http://dx.doi.org/10.1074/jbc.271.4.2012.

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21

Dominici, P., G. Scholz, F. Kwok, and J. E. Churchich. "Affinity labeling of pyridoxal kinase with adenosine polyphosphopyridoxal." Journal of Biological Chemistry 263, no. 29 (October 1988): 14712–16. http://dx.doi.org/10.1016/s0021-9258(18)68095-0.

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22

Vaughan, Roxanne A., M. Laura Parnas, Jon D. Gaffaney, Margaret J. Lowe, Sara Wirtz, Anh Pham, Brian Reed, Sucharita M. Dutta, Kermit K. Murray, and Joseph B. Justice. "Affinity labeling the dopamine transporter ligand binding site." Journal of Neuroscience Methods 143, no. 1 (April 2005): 33–40. http://dx.doi.org/10.1016/j.jneumeth.2004.09.022.

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23

Yang, Ke, Amy Zuckerman, and Gavril W. Pasternak. "Affinity Labeling Mu Opioid Receptors With Novel Radioligands." Cellular and Molecular Neurobiology 25, no. 3-4 (June 2005): 759–65. http://dx.doi.org/10.1007/s10571-005-3973-7.

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24

NITTA, Yasunori, and Yukihiro ISODA. "Catalytic site of .BETA.-amylase and affinity labeling." Journal of the Japanese Society of Starch Science 36, no. 2 (1989): 77–85. http://dx.doi.org/10.5458/jag1972.36.77.

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25

Wong, Y. S., and J. C. Lagarias. "Affinity labeling of Avena phytochrome with ATP analogs." Proceedings of the National Academy of Sciences 86, no. 10 (May 1, 1989): 3469–73. http://dx.doi.org/10.1073/pnas.86.10.3469.

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26

Volke, Daniela, Mohammed Daghish, Lothar Hennig, Matthias Findeisen, Sabine Giesa, Ramona Oehme, and Peter Welzel. "On Penicillin-Binding Protein 1b Affinity-Labeling Reagents." Helvetica Chimica Acta 86, no. 12 (December 2003): 4214–32. http://dx.doi.org/10.1002/hlca.200390346.

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27

Jiang, Jiangsong, Dexing Zeng, and Shuwei Li. "Photogenerated Quinone Methides as Protein Affinity Labeling Reagents." ChemBioChem 10, no. 4 (February 5, 2009): 635–38. http://dx.doi.org/10.1002/cbic.200800700.

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28

Cheng, Bo, Qi Tang, Che Zhang, and Xing Chen. "Glycan Labeling and Analysis in Cells and In Vivo." Annual Review of Analytical Chemistry 14, no. 1 (June 5, 2021): 363–87. http://dx.doi.org/10.1146/annurev-anchem-091620-091314.

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As one of the major types of biomacromolecules in the cell, glycans play essential functional roles in various biological processes. Compared with proteins and nucleic acids, the analysis of glycans in situ has been more challenging. Herein we review recent advances in the development of methods and strategies for labeling, imaging, and profiling of glycans in cells and in vivo. Cellular glycans can be labeled by affinity-based probes, including lectin and antibody conjugates, direct chemical modification, metabolic glycan labeling, and chemoenzymatic labeling. These methods have been applied
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29

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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30

Attiya, Said, Terrina Dickinson-Laing, John Cesarz, Raymond D. Giese, William E. Lee, David Mah, and D. Jed Harrison. "Affinity protection chromatography for efficient labeling of antibodies for use in affinity capillary electrophoresis." ELECTROPHORESIS 23, no. 5 (March 2002): 750–58. http://dx.doi.org/10.1002/1522-2683(200203)23:5<750::aid-elps750>3.0.co;2-3.

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31

Wong, Franklin C., John Boja, Beng Ho, Michael J. Kuhar, and Dean F. Wong. "Affinity Labeling of Membrane Receptors Using Tissue-Penetrating Radiations." BioMed Research International 2013 (2013): 1–7. http://dx.doi.org/10.1155/2013/503095.

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Photoaffinity labeling, a usefulin vivobiochemical tool, is limited when appliedin vivobecause of the poor tissue penetration by ultraviolet (UV) photons. This study investigates affinity labeling using tissue-penetrating radiation to overcome the tissue attenuation and irreversibly label membrane receptor proteins. Using X-ray (115 kVp) at low doses (&lt;50 cGy or Rad), specific and irreversible binding was found on striatal dopamine transporters with 3 photoaffinity ligands for dopamine transporters, to different extents. Upon X-ray exposure (115 kVp), RTI-38 and RTI-78 ligands showed irreve
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32

Liu, Tianying, Tyler M. Marcinko, and Richard W. Vachet. "Protein–Ligand Affinity Determinations Using Covalent Labeling-Mass Spectrometry." Journal of the American Society for Mass Spectrometry 31, no. 7 (June 5, 2020): 1544–53. http://dx.doi.org/10.1021/jasms.0c00131.

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33

Johanson, R. A., and J. Henkin. "Affinity labeling of dihydrofolate reductase with an antifolate glyoxal." Journal of Biological Chemistry 260, no. 3 (February 1985): 1465–74. http://dx.doi.org/10.1016/s0021-9258(18)89615-6.

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34

Shirasu, Naoto, and Yasuyuki Shimohigashi. "Discriminative disulfide-bonding affinity labeling of opioid receptor subtypes." Journal of Biochemical and Biophysical Methods 49, no. 1-3 (October 2001): 587–606. http://dx.doi.org/10.1016/s0165-022x(01)00222-6.

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35

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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36

Isozaki, Kaname, Hidehiko Fukahori, Takeshi Honda, Naoto Shirasu, Kazushi Okada, Takeru Nose, Kazuyasu Sakaguchi, and Yasuyuki Shimohigashi. "Site-directed affinity-labeling of delta opioid receptors by." International Journal of Peptide Research and Therapeutics 10, no. 5-6 (November 2003): 511–22. http://dx.doi.org/10.1007/s10989-004-2414-7.

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37

Vaz, Alfin D. N., and Guenther Schoellmann. "Affinity labeling of bovine opsin by trans-retinoyl chloromethane." Biochemical and Biophysical Research Communications 160, no. 2 (April 1989): 942–47. http://dx.doi.org/10.1016/0006-291x(89)92526-6.

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38

Swamy, Narasimha, and Rahul Ray. "Affinity Labeling of Rat Serum Vitamin D Binding Protein." Archives of Biochemistry and Biophysics 333, no. 1 (September 1996): 139–44. http://dx.doi.org/10.1006/abbi.1996.0374.

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39

Konziase, Benetode. "Synthesis of biotinylated probes of artemisinin for affinity labeling." Data in Brief 4 (September 2015): 66–74. http://dx.doi.org/10.1016/j.dib.2015.04.017.

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40

Amini, Frank, Thomas Kodadek, and Kathlynn C. Brown. "Protein Affinity Labeling Mediated by Genetically Encoded Peptide Tags." Angewandte Chemie 114, no. 2 (January 18, 2002): 366–69. http://dx.doi.org/10.1002/1521-3757(20020118)114:2<366::aid-ange366>3.0.co;2-6.

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41

FABRY, M., and D. BRANDENBURG. "ChemInform Abstract: Photoreactive Biotinylated Peptide Ligands for Affinity Labeling." ChemInform 28, no. 15 (August 4, 2010): no. http://dx.doi.org/10.1002/chin.199715315.

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42

Benhamou, N., N. Gilboa-Garber, J. Trudel, and A. Asselin. "A new lectin-gold complex for ultrastructural localization of galacturonic acids." Journal of Histochemistry & Cytochemistry 36, no. 11 (November 1988): 1403–11. http://dx.doi.org/10.1177/36.11.3049790.

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We report the development of a cytochemical affinity technique for detection of galacturonic acids at the ultrastructural level. The highly purified gonad lectin from Aplysia depilans (AGL) was tagged with colloidal gold particles and used for labeling carbohydrates in resin-embedded sections of various plant and fungal tissues. Patterns of AGL binding sites were compared to those obtained with a D-galactose-specific lectin, Ricinus communis agglutinin I. Differences in labeling patterns were noted, indicating that the lectins exhibited differential carbohydrate binding. In addition, the consi
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43

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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44

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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45

Bendayan, M., and S. Garzon. "Protein G-gold complex: comparative evaluation with protein A-gold for high-resolution immunocytochemistry." Journal of Histochemistry & Cytochemistry 36, no. 6 (June 1988): 597–607. http://dx.doi.org/10.1177/36.6.2452843.

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We combined the protein G-gold complex with several polyclonal and monoclonal antibodies for localization of various antigenic sites. The labelings were compared with those obtained using the protein A-gold complex. The results from either the immunodot experiment or immunoelectron microscopy have demonstrated that, for rabbit and guinea pig antibodies, both protein G-gold and protein A-gold complexes label several different specific antibodies with similar efficiency. However, with antibodies raised in goats or in mice, and particularly with mouse monoclonal antibodies, protein G-gold yielded
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46

Saha, Subham, Thilo Hetzke, Thomas F. Prisner, and Snorri Th Sigurdsson. "Noncovalent spin-labeling of RNA: the aptamer approach." Chemical Communications 54, no. 83 (2018): 11749–52. http://dx.doi.org/10.1039/c8cc05597a.

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47

Van Obberghen-Schilling, Ellen, та Jacques Pouysségur. "Affinity labeling of high-affinity α-thrombin binding sites on the surface of hamster fibroblasts". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 847, № 3 (грудень 1985): 335–43. http://dx.doi.org/10.1016/0167-4889(85)90039-4.

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48

Koshi, Yoichiro, Eiji Nakata, and Itaru Hamachi. "Lectin Functionalization by Post-Photo Affinity Labeling Modification (P-PALM)." Trends in Glycoscience and Glycotechnology 19, no. 107 (2007): 121–31. http://dx.doi.org/10.4052/tigg.19.121.

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49

Palma, Susana I. C. J., Alexandra R. Fernandes, and Ana C. A. Roque. "An affinity triggered MRI nanoprobe for pH-dependent cell labeling." RSC Advances 6, no. 114 (2016): 113503–12. http://dx.doi.org/10.1039/c6ra17217b.

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The pH-sensitive affinity pair composed by neutravidin and iminobiotin was used to develop a multilayered Magnetic Resonance Imaging (MRI) nanoprobe responsive to the acidic pH of tumor microenvironment.
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50

TAKAGI, Shiro, Mikihiko KOBAYASHI, Tadanori URAYAMA, Itsuko SUZAWA, Kazuo MATSUDA, and Eiji ICHISHIMA. "Affinity labeling of muscle phosphorylase b with .ALPHA.-cyclodextrin-dialdehyde." Agricultural and Biological Chemistry 52, no. 11 (1988): 2709–16. http://dx.doi.org/10.1271/bbb1961.52.2709.

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