Einloggen

Thematische Bibliographien / Affinity labeling / Zeitschriftenartikel

Um die anderen Arten von Veröffentlichungen zu diesem Thema anzuzeigen, folgen Sie diesem Link: Affinity labeling.

Zeitschriftenartikel zum Thema „Affinity labeling“

Autor: Grafiati

Veröffentlicht am 4. Juni 2021

Zuletzt aktualisiert am 25. Februar 2023

Geben Sie eine Quelle nach APA, MLA, Chicago, Harvard und anderen Zitierweisen an

Wählen Sie eine Art der Quelle aus:

Machen Sie sich mit Top-50 Zeitschriftenartikel für die Forschung zum Thema "Affinity labeling" bekannt.

Neben jedem Werk im Literaturverzeichnis ist die Option "Zur Bibliographie hinzufügen" verfügbar. Nutzen Sie sie, wird Ihre bibliographische Angabe des gewählten Werkes nach der nötigen Zitierweise (APA, MLA, Harvard, Chicago, Vancouver usw.) automatisch gestaltet.

Sie können auch den vollen Text der wissenschaftlichen Publikation im PDF-Format herunterladen und eine Online-Annotation der Arbeit lesen, wenn die relevanten Parameter in den Metadaten verfügbar sind.

Sehen Sie die Zeitschriftenartikel für verschiedene Spezialgebieten durch und erstellen Sie Ihre Bibliographie auf korrekte Weise.

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

Annotation:

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 photobleaching. Moreover, exchangeable tags are less likely to hinder the intrinsic dynamics and cellular functions of labeled molecules. Low-affinity labels may be used both for fixed and living cells in a range of nanoscopy modalities. Nevertheless, the design of optimal labeling and imaging protocols with these novel tags remains tricky. In this review, we highlight the pros and cons of a wide variety of transiently interacting labels. We further discuss the state of the art and future perspectives of low-affinity labeling methods.

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

Annotation:

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 to label glycans with fluorophores, which enables the visualization and tracking of glycans in cells, tissues, and living organisms. Alternatively, labeling glycans with affinity tags has enabled the enrichment of glycoproteins for glycoproteomic profiling. Built on the glycan labeling methods, strategies enabling cell-selective and tissue-specific glycan labeling and protein-specific glycan imaging have been developed. With these methods and strategies, researchers are now better poised than ever to dissect the biological function of glycans in physiological or pathological contexts.

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

Annotation:

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 swollen cells. We exploited the volume-dependent irreversible low-affinity reaction between H2DIDS and the K+/H+ to identify the protein(s) associated with K+/H+ exchange activity. Labeling of the membrane proteins of intact cells with 3H2DIDS results in high-affinity labeling of a broad 100-kDa band, thought to be the anion exchanger. Additional swelling-dependent low-affinity labeling at 110 kDa suggests the possibility of a volume-induced population of anion exchangers. Finally, the correlation between volume-sensitive K+/H+ modification and low-affinity labeling suggests that transport activity is associated with a protein of approximately 85 kDa. Although a 55-kDa protein is also labeled, it is a less likely candidate, since label incorporation and transport modification are less well correlated than that of the 85- and 110-kDa proteins.

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

Annotation:

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 (<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 irreversible and specific binding to the dopamine transporter similar to those seen with UV exposure under other conditions. Similarly, gamma rays at higher energy (662 keV) also affect irreversible binding of photoreactive ligands to peripheral benzodiazepine receptors (by PK14105) and to the dopamine (D2) membrane receptors (by azidoclebopride), respectively. This study reports that X-ray and gamma rays induced affinity labeling of membrane receptors in a manner similar to UV with photoreactive ligands of the dopamine transporter, D2 dopamine receptor (D2R), and peripheral benzodiazepine receptor (PBDZR). It may provide specific noninvasive irreversible block or stimulation of a receptor using tissue-penetrating radiation targeting selected anatomic sites.

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

Annotation:

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 considerable loss of labeling over isolated wheat coleoptile walls treated for removal of pectin, after incubation with the AGL-gold complex, strongly suggested an affinity of AGL for pectic substances. A series of cytochemical controls, including sugar inhibition tests, has proven the specificity of the technique and the high affinity of AGL towards galacturonic acids. The potential value of this new lectin for ultrastructural studies on cell wall pectic substances in plant biology and pathology is demonstrated.

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

Annotation:

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 intense and specific labeling, whereas protein A-gold yielded intense and specific labeling, whereas protein A-gold was very variable; it either gave weaker signals or failed to reveal any specific site or, as with one monoclonal, both protein G and protein A gave similar results. The higher affinity and versatility of protein G over protein A, established by the immunochemical approach, was confirmed by immunocytochemistry. Because of its enhanced reactivity with monoclonal antibodies and its broader affinity for polyclonal antibodies, protein G-gold complex appears to be a better and more versatile probe for high-resolution immunocytochemistry.

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

Annotation:

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.

APA, Harvard, Vancouver, ISO und andere Zitierweisen

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.

Der volle Inhalt der Quelle

APA, Harvard, Vancouver, ISO und andere Zitierweisen

Wir bieten Rabatte auf alle Premium-Pläne für Autoren, deren Werke in thematische Literatursammlungen aufgenommen wurden. Kontaktieren Sie uns, um einen einzigartigen Promo-Code zu erhalten!