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Artículos de revistas 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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1

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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2

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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3

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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4

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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5

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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7

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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8

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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9

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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10

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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11

Cullen, Paul A., Xiaoyi Xu, James Matsunaga, Yolanda Sanchez, Albert I. Ko, David A. Haake, and Ben Adler. "Surfaceome of Leptospira spp." Infection and Immunity 73, no. 8 (August 2005): 4853–63. http://dx.doi.org/10.1128/iai.73.8.4853-4863.2005.

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ABSTRACT The identification of the subset of outer membrane proteins exposed on the surface of a bacterial cell (the surfaceome) is critical to understanding the interactions of bacteria with their environments and greatly narrows the search for protective antigens of extracellular pathogens. The surfaceome of Leptospira was investigated by biotin labeling of viable leptospires, affinity capture of the biotinylated proteins, two-dimensional gel electrophoresis, and mass spectrometry (MS). The leptospiral surfaceome was found to be predominantly made up of a small number of already characterize
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12

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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13

Hayashi, Takahiro, and Itaru Hamachi. "Traceless Affinity Labeling of Endogenous Proteins for Functional Analysis in Living Cells." Accounts of Chemical Research 45, no. 9 (June 8, 2012): 1460–69. http://dx.doi.org/10.1021/ar200334r.

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14

Goshe, Michael B., Josip Blonder, and Richard D. Smith. "Affinity Labeling of Highly Hydrophobic Integral Membrane Proteins for Proteome-Wide Analysis." Journal of Proteome Research 2, no. 2 (April 2003): 153–61. http://dx.doi.org/10.1021/pr0255607.

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15

Zhang, Jianfu, Jianzhao Peng, Yiran Huang, Ling Meng, Qingrong Li, Feng Xiong, and Xiaoyu Li. "Identification of Histone deacetylase (HDAC)‐Associated Proteins with DNA‐Programmed Affinity Labeling." Angewandte Chemie International Edition 59, no. 40 (August 11, 2020): 17525–32. http://dx.doi.org/10.1002/anie.202001205.

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16

Zhang, Jianfu, Jianzhao Peng, Yiran Huang, Ling Meng, Qingrong Li, Feng Xiong, and Xiaoyu Li. "Identification of Histone deacetylase (HDAC)‐Associated Proteins with DNA‐Programmed Affinity Labeling." Angewandte Chemie 132, no. 40 (August 11, 2020): 17678–85. http://dx.doi.org/10.1002/ange.202001205.

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17

Cosma, Antonio. "Affinity Biotinylation: Nonradioactive Method for Specific Selection and Labeling of Cellular Proteins." Analytical Biochemistry 252, no. 1 (October 1997): 10–14. http://dx.doi.org/10.1006/abio.1997.2289.

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18

Weissinger, Ronja, Lisa Heinold, Saira Akram, Ralf-Peter Jansen, and Orit Hermesh. "RNA Proximity Labeling: A New Detection Tool for RNA–Protein Interactions." Molecules 26, no. 8 (April 14, 2021): 2270. http://dx.doi.org/10.3390/molecules26082270.

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Multiple cellular functions are controlled by the interaction of RNAs and proteins. Together with the RNAs they control, RNA interacting proteins form RNA protein complexes, which are considered to serve as the true regulatory units for post-transcriptional gene expression. To understand how RNAs are modified, transported, and regulated therefore requires specific knowledge of their interaction partners. To this end, multiple techniques have been developed to characterize the interaction between RNAs and proteins. In this review, we briefly summarize the common methods to study RNA–protein int
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19

Robinson, M. S., and B. M. Pearse. "Immunofluorescent localization of 100K coated vesicle proteins." Journal of Cell Biology 102, no. 1 (January 1, 1986): 48–54. http://dx.doi.org/10.1083/jcb.102.1.48.

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A family of coated vesicle proteins, with molecular weights of approximately 100,000 and designated 100K, has been implicated in both coat assembly and the attachment of clathrin to the vesicle membrane. These proteins were purified from extracts of bovine brain coated vesicles by gel filtration, hydroxylapatite chromatography, and preparative SDS PAGE. Peptide mapping by limited proteolysis indicated that the polypeptides making up the three major 100K bands have distinct amino acid sequences. When four rats were immunized with total 100K protein, each rat responded differently to the differe
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20

Trinkle-Mulcahy, Laura. "Recent advances in proximity-based labeling methods for interactome mapping." F1000Research 8 (January 31, 2019): 135. http://dx.doi.org/10.12688/f1000research.16903.1.

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Proximity-based labeling has emerged as a powerful complementary approach to classic affinity purification of multiprotein complexes in the mapping of protein–protein interactions. Ongoing optimization of enzyme tags and delivery methods has improved both temporal and spatial resolution, and the technique has been successfully employed in numerous small-scale (single complex mapping) and large-scale (network mapping) initiatives. When paired with quantitative proteomic approaches, the ability of these assays to provide snapshots of stable and transient interactions over time greatly facilitate
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21

Braner, M., A. Kollmannsperger, R. Wieneke, and R. Tampé. "‘Traceless’ tracing of proteins – high-affinity trans-splicing directed by a minimal interaction pair." Chemical Science 7, no. 4 (2016): 2646–52. http://dx.doi.org/10.1039/c5sc02936h.

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Using a minimal lock-and-key element the affinity between the intein fragments for N-terminal protein trans-splicing was significantly increased, allowing for site-specific, ‘traceless’ covalent protein labeling in living mammalian cells at nanomolar probe concentrations.
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22

Pfeuffer, Elke, and Thomas Pfeuffer. "Affinity labeling of forskolin-binding proteins comparison between glucose carrier and adenylate cyclase." FEBS Letters 248, no. 1-2 (May 8, 1989): 13–17. http://dx.doi.org/10.1016/0014-5793(89)80422-3.

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23

Tomohiro, Takenori, Hirotsugu Inoguchi, Souta Masuda, and Yasumaru Hatanaka. "Affinity-based fluorogenic labeling of ATP-binding proteins with sequential photoactivatable cross-linkers." Bioorganic & Medicinal Chemistry Letters 23, no. 20 (October 2013): 5605–8. http://dx.doi.org/10.1016/j.bmcl.2013.08.041.

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24

Konziase, Benetode. "Biotinylated probes of artemisinin with labeling affinity toward Trypanosoma brucei brucei target proteins." Analytical Biochemistry 482 (August 2015): 25–31. http://dx.doi.org/10.1016/j.ab.2015.04.020.

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25

Safer, B., R. B. Cohen, S. Garfinkel, and J. A. Thompson. "DNA affinity labeling of adenovirus type 2 upstream promoter sequence-binding factors identifies two distinct proteins." Molecular and Cellular Biology 8, no. 1 (January 1988): 105–13. http://dx.doi.org/10.1128/mcb.8.1.105.

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A rapid affinity labeling procedure with enhanced specificity was developed to identify DNA-binding proteins. 32P was first introduced at unique phosphodiester bonds within the DNA recognition sequence. UV light-dependent cross-linking of pyrimidines to amino acid residues in direct contact at the binding site, followed by micrococcal nuclease digestion, resulted in the transfer of 32P to only those specific protein(s) which recognized the binding sequence. This method was applied to the detection and characterization of proteins that bound to the upstream promoter sequence (-50 to -66) of the
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26

Safer, B., R. B. Cohen, S. Garfinkel, and J. A. Thompson. "DNA affinity labeling of adenovirus type 2 upstream promoter sequence-binding factors identifies two distinct proteins." Molecular and Cellular Biology 8, no. 1 (January 1988): 105–13. http://dx.doi.org/10.1128/mcb.8.1.105-113.1988.

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A rapid affinity labeling procedure with enhanced specificity was developed to identify DNA-binding proteins. 32P was first introduced at unique phosphodiester bonds within the DNA recognition sequence. UV light-dependent cross-linking of pyrimidines to amino acid residues in direct contact at the binding site, followed by micrococcal nuclease digestion, resulted in the transfer of 32P to only those specific protein(s) which recognized the binding sequence. This method was applied to the detection and characterization of proteins that bound to the upstream promoter sequence (-50 to -66) of the
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27

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 (<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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28

Yefidoff, Revital, and Amnon Albeck. "12-Substituted-13,14-dihydroretinols designed for affinity labeling of retinol binding- and processing proteins." Tetrahedron 60, no. 37 (September 2004): 8093–102. http://dx.doi.org/10.1016/j.tet.2004.06.116.

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29

Fukui, Toshio. "Exploring the Nucleotide-Binding Site in Proteins by Affinity Labeling and Site-Directed Mutagenesis1." Journal of Biochemistry 117, no. 6 (June 1995): 1139–44. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a124834.

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30

Gibson, Kathryn, Yumi Kumagai, and Yasuko Rikihisa. "Proteomic Analysis of Neorickettsia sennetsu Surface-Exposed Proteins and Porin Activity of the Major Surface Protein P51." Journal of Bacteriology 192, no. 22 (September 10, 2010): 5898–905. http://dx.doi.org/10.1128/jb.00632-10.

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ABSTRACT Neorickettsia sennetsu is an obligate intracellular bacterium of monocytes and macrophages and is the etiologic agent of human Sennetsu neorickettsiosis. Neorickettsia proteins expressed in mammalian host cells, including the surface proteins of Neorickettsia spp., have not been defined. In this paper, we isolated surface-exposed proteins from N. sennetsu by biotin surface labeling followed by streptavidin-affinity chromatography. Forty-two of the total of 936 (4.5%) N. sennetsu open reading frames (ORFs) were detected by liquid chromatography-tandem mass spectrometry (LC/MS/MS), incl
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31

Takata, K., and SJ Singer. "Localization of high concentrations of phosphotyrosine-modified proteins in mouse megakaryocytes." Blood 71, no. 3 (March 1, 1988): 818–21. http://dx.doi.org/10.1182/blood.v71.3.818.818.

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Abstract Phosphorylation of tyrosine residues of cellular proteins is a rare event and is considered to be related to the regulation of cellular growth, differentiation, and some forms of neoplastic transformation. Using high-affinity antibodies specific to phosphotyrosine (P-Tyr), we have shown the presence at high concentrations of P-Tyr-modified proteins in mouse bone-marrow megakaryocytes. Immunofluorescence microscopy of semithin frozen sections revealed that P-Tyr labeling was localized in a punctate pattern in the majority of the cytoplasm. The thin outer rim of the cytoplasm and the ce
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32

Takata, K., and SJ Singer. "Localization of high concentrations of phosphotyrosine-modified proteins in mouse megakaryocytes." Blood 71, no. 3 (March 1, 1988): 818–21. http://dx.doi.org/10.1182/blood.v71.3.818.bloodjournal713818.

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Phosphorylation of tyrosine residues of cellular proteins is a rare event and is considered to be related to the regulation of cellular growth, differentiation, and some forms of neoplastic transformation. Using high-affinity antibodies specific to phosphotyrosine (P-Tyr), we have shown the presence at high concentrations of P-Tyr-modified proteins in mouse bone-marrow megakaryocytes. Immunofluorescence microscopy of semithin frozen sections revealed that P-Tyr labeling was localized in a punctate pattern in the majority of the cytoplasm. The thin outer rim of the cytoplasm and the cell membra
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33

Keeble, Anthony H., Paula Turkki, Samuel Stokes, Irsyad N. A. Khairil Anuar, Rolle Rahikainen, Vesa P. Hytönen, and Mark Howarth. "Approaching infinite affinity through engineering of peptide–protein interaction." Proceedings of the National Academy of Sciences 116, no. 52 (December 10, 2019): 26523–33. http://dx.doi.org/10.1073/pnas.1909653116.

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Much of life’s complexity depends upon contacts between proteins with precise affinity and specificity. The successful application of engineered proteins often depends on high-stability binding to their target. In recent years, various approaches have enabled proteins to form irreversible covalent interactions with protein targets. However, the rate of such reactions is a major limitation to their use. Infinite affinity refers to the ideal where such covalent interaction occurs at the diffusion limit. Prototypes of infinite affinity pairs have been achieved using nonnatural reactive groups. Af
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34

LeBel, Denis, та Marlyne Beattie. "Identification of the catalytic subunit of the ATP diphosphohydrolase by photoaffinity labeling of high-affinity ATP-binding sites of pancreatic zymogen granule membranes with 8-azido-[α-32P]ATP". Biochemistry and Cell Biology 64, № 1 (1 січня 1986): 13–20. http://dx.doi.org/10.1139/o86-003.

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Photoaffinity labeling has been performed on pancreatic zymogen granule membranes using 8-azido-[α-32P]ATP (8-N3-ATP). Proteins of 92, 67, 53, and 35 kdaltons (kDa) were specifically labeled. ATP (100 μM) inhibited very strongly the labeling with 8-N3-ATP, while ADP was much less potent, AMP and cAMP being inefficient. The apparent constants for 8-N3-ATP binding were in the micromolar concentration range for the four labeled proteins. Without irradiation, 8-N3-ATP was a competitive inhibitor (Ki = 2.66 μM) for the hydrolysis of ATP by the ATP diphosphohydrolase. The optimal conditions for the
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35

Mann, Jasdeep K., Daniel Demonte, Christopher M. Dundas, and Sheldon Park. "Cell labeling and proximity dependent biotinylation with engineered monomeric streptavidin." TECHNOLOGY 04, no. 03 (September 2016): 152–58. http://dx.doi.org/10.1142/s2339547816400057.

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Because streptavidin is a homotetramer, it can bind multiple biotinylated ligands and cause target aggregation. To allow biotin detection without clustering, we previously engineered monomeric streptavidin (mSA) that is structurally similar to a single streptavidin subunit. Introducing the S25H mutation near the binding site increases the biotin dissociation half-life t1/2 to 83 minutes. The slowly dissociating mutant, mSA2, is useful in imaging studies because it allows stable labeling of biotinylated targets. We show that mSA2 conjugated with Alexa 488 binds biotinylated receptors on HEK293
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36

Takata, K., and S. J. Singer. "Phosphotyrosine-modified proteins are concentrated at the membranes of epithelial and endothelial cells during tissue development in chick embryos." Journal of Cell Biology 106, no. 5 (May 1, 1988): 1757–64. http://dx.doi.org/10.1083/jcb.106.5.1757.

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We have used high affinity polyclonal antibodies specific for phosphotyrosine (PTyr) residues to examine the localization in various chick embryonic tissues in situ of PTyr-modified proteins by immunocytochemical methods. During the period from 9 to 21 d of development, most tissues exhibit elevated levels of PTyr-modified proteins as determined by immunoblotting experiments of tissue extracts with the anti-PTyr antibodies (Maher, P. A., and E. B. Pasquale. 1988. J. Cell Biol. 106:1747-1755). By immunofluorescence labeling of semithin frozen sections, the highest concentrations of PTyr immunol
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37

Choi, Woonyoung, Sonya W. Song, and Wei Zhang. "Understanding Cancer through Proteomics." Technology in Cancer Research & Treatment 1, no. 4 (August 2002): 221–30. http://dx.doi.org/10.1177/153303460200100402.

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Proteomics is a rapidly expanding discipline that aims to gain a comprehensive understanding of the expressions, modification, interactions, and regulation of proteins in cells. New high-throughput technologies, such as protein chips and isotope-coded affinity tag peptide labeling, coupled with classic technologies such as two-dimensional gel electrophoresis and mass spectrometry, complement genomic technologies, providing cancer researchers with powerful tools for cancer diagnosis and prognosis and for the identification of targets for therapy.
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38

Kerbler, Sandra M., Roberto Natale, Alisdair R. Fernie, and Youjun Zhang. "From Affinity to Proximity Techniques to Investigate Protein Complexes in Plants." International Journal of Molecular Sciences 22, no. 13 (July 1, 2021): 7101. http://dx.doi.org/10.3390/ijms22137101.

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The study of protein–protein interactions (PPIs) is fundamental in understanding the unique role of proteins within cells and their contribution to complex biological systems. While the toolkit to study PPIs has grown immensely in mammalian and unicellular eukaryote systems over recent years, application of these techniques in plants remains under-utilized. Affinity purification coupled to mass spectrometry (AP-MS) and proximity labeling coupled to mass spectrometry (PL-MS) are two powerful techniques that have significantly enhanced our understanding of PPIs. Relying on the specific binding p
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39

Ross, Gregory M., Brian E. McCarry, and Ram K. Mishra. "Covalent Affinity Labeling of Brain Catecholamine-Absorbing Proteins Using a High-Specific-Activity Substituted Tetrahydronaphthalene." Journal of Neurochemistry 65, no. 6 (November 23, 2002): 2783–89. http://dx.doi.org/10.1046/j.1471-4159.1995.65062783.x.

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40

Yang, Yin, Qing-Feng Li, Chan Cao, Feng Huang, and Xun-Cheng Su. "Site-Specific Labeling of Proteins with a Chemically Stable, High-Affinity Tag for Protein Study." Chemistry - A European Journal 19, no. 3 (November 14, 2012): 1097–103. http://dx.doi.org/10.1002/chem.201202495.

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41

Rickard, J. E., and T. E. Kreis. "Identification of a novel nucleotide-sensitive microtubule-binding protein in HeLa cells." Journal of Cell Biology 110, no. 5 (May 1, 1990): 1623–33. http://dx.doi.org/10.1083/jcb.110.5.1623.

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A protein of Mr 170,000 (170K protein) has been identified in HeLa cells, using an antiserum raised against HeLa nucleotide-sensitive microtubule-binding proteins. Affinity-purified antibodies specific for this 170K polypeptide were used for its characterization. In vitro sedimentation of the 170K protein with taxol microtubules polymerized from HeLa high-speed supernatant is enhanced in the presence of an ATP depleting system, but unaffected by the non-hydrolyzable ATP analogue AMP-PNP. In addition, it can be eluted from taxol microtubules by ATP or GTP, as well as NaCl. Thus it shows microtu
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42

Hortin, GL. "Sulfation of tyrosine residues in coagulation factor V." Blood 76, no. 5 (September 1, 1990): 946–52. http://dx.doi.org/10.1182/blood.v76.5.946.946.

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Abstract Sulfation of human coagulation factor V was investigated by biosynthetically labeling the products of HepG2 cells with [35S]sulfate. There was abundant incorporation of the sulfate label into a product identified as factor V by immunoprecipitation, lability to proteases, affinity for the lectin jacalin, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Two or more sites in factor V incorporated sulfate as indicated by labeling of different peptide chains of factor Va. The 150-Kd activation fragment of factor Va incorporated the greatest amounts of sulfate. This fragment o
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43

Hortin, GL. "Sulfation of tyrosine residues in coagulation factor V." Blood 76, no. 5 (September 1, 1990): 946–52. http://dx.doi.org/10.1182/blood.v76.5.946.bloodjournal765946.

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Sulfation of human coagulation factor V was investigated by biosynthetically labeling the products of HepG2 cells with [35S]sulfate. There was abundant incorporation of the sulfate label into a product identified as factor V by immunoprecipitation, lability to proteases, affinity for the lectin jacalin, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Two or more sites in factor V incorporated sulfate as indicated by labeling of different peptide chains of factor Va. The 150-Kd activation fragment of factor Va incorporated the greatest amounts of sulfate. This fragment of factor
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44

Ye, Xian Zhi. "Application of Biological Target Fishing Technology in Drug Discovery." Materials Science Forum 980 (March 2020): 210–19. http://dx.doi.org/10.4028/www.scientific.net/msf.980.210.

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Target fishing, a cutting-edge technology for drug research and development, plays a significant role in drug discovery. Varieties of methods for finding small-molecule drug targets have come into being driven by genomics, proteomics, bioinformatics and other technologies. These new methods are mainly based on the expression of gene or protein and proteins properties, including affinity and stability and so on. A serious challenge for the most widely used small molecule drugs is the discovery and identification of biological (and potential therapeutic) targets. Herein, we enumerate five biolog
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45

Roux, Kyle J., Dae In Kim, Manfred Raida, and Brian Burke. "A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells." Journal of Cell Biology 196, no. 6 (March 12, 2012): 801–10. http://dx.doi.org/10.1083/jcb.201112098.

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We have developed a new technique for proximity-dependent labeling of proteins in eukaryotic cells. Named BioID for proximity-dependent biotin identification, this approach is based on fusion of a promiscuous Escherichia coli biotin protein ligase to a targeting protein. BioID features proximity-dependent biotinylation of proteins that are near-neighbors of the fusion protein. Biotinylated proteins may be isolated by affinity capture and identified by mass spectrometry. We apply BioID to lamin-A (LaA), a well-characterized intermediate filament protein that is a constituent of the nuclear lami
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46

Luo, W., L. R. Latchney, and D. J. Culp. "G protein coupling to M1 and M3muscarinic receptors in sublingual glands." American Journal of Physiology-Cell Physiology 280, no. 4 (April 1, 2001): C884—C896. http://dx.doi.org/10.1152/ajpcell.2001.280.4.c884.

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Rat sublingual gland M1 and M3 muscarinic receptors each directly activate exocrine secretion. To investigate the functional role of coreceptor expression, we determined receptor-G protein coupling. Although membrane proteins of 40 and 41 kDa are ADP-ribosylated by pertussis toxin (PTX), and 44 kDa proteins by cholera toxin (CTX), both carbachol-stimulated high-affinity GTPase activity and the GTP-induced shift in agonist binding are insensitive to CTX or PTX. Carbachol enhances photoaffinity labeling ([α-32P]GTP-azidoaniline) of only 42-kDa proteins that are subsequently tractable to immunopr
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47

Pearson, R. K., E. M. Hadac, and L. J. Miller. "Structural analysis of a distinct subtype of CCK receptor on human gastric smooth muscle tumors." American Journal of Physiology-Gastrointestinal and Liver Physiology 256, no. 6 (June 1, 1989): G1005—G1010. http://dx.doi.org/10.1152/ajpgi.1989.256.6.g1005.

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Human gastric smooth muscle tumors (leiomyosarcomas) have been shown to express cholecystokinin (CCK) binding sites that are functionally similar to physiologically important receptors present on their cells of origin. In this work, we have applied affinity-labeling techniques using 125I-D-Tyr-Gly-[Nle28,31]CCK-(26-33) to attempt to define the ligand-binding subunit of this receptor, and we have used the receptor antagonist L364,718 and deglycosylating enzymes to compare this molecule with well-defined CCK receptors on the classical peripheral targets (pancreas and gallbladder) of this hormone
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48

Haas, M., P. B. Dunham, and B. Forbush. "[3H]bumetanide binding to mouse kidney membranes: identification of corresponding membrane proteins." American Journal of Physiology-Cell Physiology 260, no. 4 (April 1, 1991): C791—C804. http://dx.doi.org/10.1152/ajpcell.1991.260.4.c791.

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Crude plasma membranes from whole mouse kidneys have two classes of [3H]bumetanide binding sites. High-affinity sites (K1/2 approximately equal to 0.04 microM; Bmax = 1-2 pmol/mg protein) are similar to those identified on dog kidney membranes (B. Forbush and H.C. Palfrey. J. Biol. Chem. 258: 11787-11792, 1983) both with respect to affinity and in that Na, K, and Cl are required for [3H]bumetanide binding. Low-affinity sites (K1/2 approximately equal to 1 microM; Bmax = 7-14 pmol/mg) are unaffected by removal of these ions; such sites are not seen with dog kidney. When mouse kidney membranes a
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49

Thibonnier, M., T. Goraya, and L. Berti-Mattera. "G protein coupling of human platelet V1 vascular vasopressin receptors." American Journal of Physiology-Cell Physiology 264, no. 5 (May 1, 1993): C1336—C1344. http://dx.doi.org/10.1152/ajpcell.1993.264.5.c1336.

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We used several approaches to identify the G protein coupled to V1 vascular arginine vasopressin (AVP) receptors of human platelets. In purified platelet membranes, high-affinity specific binding of [3H]AVP but not that of the V1 vascular antagonist [3H]d(CH2)5Tyr(Me)AVP was modulated by guanosine 5'-O-(3-thiotriphosphate) or sodium fluoride both in the presence and absence of MgCl2. AVP failed to modify the [alpha-32P]GTP labeling pattern or the cytosolic translocation of the 24- to 27-kDa GTP-binding proteins. AVP-stimulated GTPase activity of platelet membranes was blocked by antibodies spe
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50

Kalkhof, Stefan, Stefan Schildbach, Conny Blumert, Friedemann Horn, Martin von Bergen, and Dirk Labudde. "PIPINO: A Software Package to Facilitate the Identification of Protein-Protein Interactions from Affinity Purification Mass Spectrometry Data." BioMed Research International 2016 (2016): 1–13. http://dx.doi.org/10.1155/2016/2891918.

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The functionality of most proteins is regulated by protein-protein interactions. Hence, the comprehensive characterization of the interactome is the next milestone on the path to understand the biochemistry of the cell. A powerful method to detect protein-protein interactions is a combination of coimmunoprecipitation or affinity purification with quantitative mass spectrometry. Nevertheless, both methods tend to precipitate a high number of background proteins due to nonspecific interactions. To address this challenge the software Protein-Protein-Interaction-Optimizer (PIPINO) was developed to
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