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Relevant bibliographies by topics / FLAG epitope tag

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Journal articles

Academic literature on the topic 'FLAG epitope tag'

Author: Grafiati

Published: 4 June 2021

Last updated: 5 February 2022

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Journal articles on the topic "FLAG epitope tag"

1

Guo, Xin-Yu, Xiao-Dong Gao, and Morihisa Fujita. "Sulfation of a FLAG tag mediated by SLC35B2 and TPST2 affects antibody recognition." PLOS ONE 16, no. 5 (2021): e0250805. http://dx.doi.org/10.1371/journal.pone.0250805.

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A FLAG tag consisting of DYKDDDDK is an epitope tag that is frequently and widely used to detect recombinant proteins of interest. In this study, we performed a CRISPR-based genetic screening to identify factors involved in the detection of a FLAG-tagged misfolded model protein at the cell surface. In the screening, SLC35B2, which encodes 3’-phosphoadenosine-5’-phosphosulfate transporter 1, was identified as the candidate gene. The detection of FLAG-tagged misfolded proteins at the cell surface was significantly increased in SLC35B2-knockout cells. Furthermore, protein tyrosine sulfation media

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2

Zhao, Xinyu, Guoshun Li, and Shufang Liang. "Several Affinity Tags Commonly Used in Chromatographic Purification." Journal of Analytical Methods in Chemistry 2013 (2013): 1–8. http://dx.doi.org/10.1155/2013/581093.

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Affinity tags have become powerful tools from basic biological research to structural and functional proteomics. They were widely used to facilitate the purification and detection of proteins of interest, as well as the separation of protein complexes. Here, we mainly discuss the benefits and drawbacks of several affinity or epitope tags frequently used, including hexahistidine tag, FLAG tag, Strep II tag, streptavidin-binding peptide (SBP) tag, calmodulin-binding peptide (CBP), glutathione S-transferase (GST), maltose-binding protein (MBP), S-tag, HA tag, and c-Myc tag. In some cases, a large

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3

Seago, Julian, Terry Jackson, Claudia Doel, et al. "Characterization of epitope-tagged foot-and-mouth disease virus." Journal of General Virology 93, no. 11 (2012): 2371–81. http://dx.doi.org/10.1099/vir.0.043521-0.

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Foot-and-mouth disease (FMD) is a highly contagious and economically devastating disease of cloven-hoofed animals with an almost-worldwide distribution. Conventional FMD vaccines consisting of chemically inactivated viruses have aided in the eradication of FMD from Europe and remain the main tool for control in endemic countries. Although significant steps have been made to improve the quality of vaccines, such as improved methods of antigen concentration and purification, manufacturing processes are technically demanding and expensive. Consequently, there is large variation in the quality of

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4

Laird, Melissa E., and Ronald C. Desrosiers. "Infectivity and Neutralization of Simian Immunodeficiency Virus with FLAG Epitope Insertion in gp120 Variable Loops." Journal of Virology 81, no. 20 (2007): 10838–48. http://dx.doi.org/10.1128/jvi.00831-07.

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ABSTRACT A FLAG epitope tag was substituted within variable loop 1 (V1), 2 (V2), or 4 (V4) of the gp120 envelope glycoprotein of simian immunodeficiency virus strain 239 (SIV239) to evaluate the extent to which each variable loop may serve as a target for antibody-mediated neutralization. Two sites within each variable loop of SIV239 were chosen for individual epitope tag insertions. FLAG epitope substitutions were also made in the V1, V2, and V4 loops of a neutralization-sensitive derivative of SIV239, SIV316. Of the 10 FLAG-tagged recombinant viruses analyzed, three (SIV239FV1b, SIV239FV2b,

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5

Plemper, Richard K., Anthea L. Hammond, Denis Gerlier, Adele K. Fielding, and Roberto Cattaneo. "Strength of Envelope Protein Interaction Modulates Cytopathicity of Measles Virus." Journal of Virology 76, no. 10 (2002): 5051–61. http://dx.doi.org/10.1128/jvi.76.10.5051-5061.2002.

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ABSTRACT To understand the molecular determinants of measles virus (MV) cytopathicity, we have characterized mutant viruses exhibiting a more-extensive cell-to-cell fusion while maintaining efficient replication to high titers. A virus which is modified by the addition of an 8-amino-acid Flag epitope tag at the cytoplasmic tail of its H (for MV hemagglutinin) envelope glycoprotein replicates efficiently, has an increased cytopathicity, possesses a greater infectivity per particle, and has an altered protein composition compared with that of unmodified MV. The mutant phenotype is not specifical

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6

BLONG, M. Renee, Elliott BEDOWS, and Oksana LOCKRIDGE. "Tetramerization domain of human butyrylcholinesterase is at the C-terminus." Biochemical Journal 327, no. 3 (1997): 747–57. http://dx.doi.org/10.1042/bj3270747.

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Butyrylcholinesterase (BChE) in human serum consists predominantly of tetramers. Recombinant BChE, however, expressed in Chinese hamster ovary (CHO) cells, consists of approx. 55% dimers, 10-30% tetramers and 15-40% monomers. To determine the origin of the monomer species we added the FLAG epitope (epitope tag, amino acid sequence DYKDDDDK) to the C-terminus of the enzyme, and expressed BChE-FLAG in CHO cells. We found that secreted, active monomers had lost their FLAG epitope, suggesting that the monomers were made by proteolysis of dimers or tetramers at the C-terminus. To estimate the numbe

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7

Joyce, Charles W., Gregory S. Shelness, Matthew A. Davis, et al. "ACAT1 and ACAT2 Membrane Topology Segregates a Serine Residue Essential for Activity to Opposite Sides of the Endoplasmic Reticulum Membrane." Molecular Biology of the Cell 11, no. 11 (2000): 3675–87. http://dx.doi.org/10.1091/mbc.11.11.3675.

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A second form of the enzyme acyl-CoA:cholesterol acyltransferase, ACAT2, has been identified. To explore the hypothesis that the two ACAT enzymes have separate functions, the membrane topologies of ACAT1 and ACAT2 were examined. A glycosylation reporter and FLAG epitope tag sequence was appended to a series of ACAT cDNAs truncated after each predicted transmembrane domain. Fusion constructs were assembled into microsomal membranes, in vitro, and topologies were determined based on glycosylation site use and accessibility to exogenous protease. The accessibility of the C-terminal FLAG epitope i

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8

Mazurov, Dmitriy, Alexandra Maslennikova, Dmitriy Komkov, and Anastasia Zotova. "Application of SORTS, a Novel Gene-Edited Cell Selection Method for HIV Study and Therapy." Proceedings 50, no. 1 (2020): 13. http://dx.doi.org/10.3390/proceedings2020050013.

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We have recently developed surface oligopeptide knock-in for rapid target selection (SORTS), a novel method to isolate mammalian cells with gene modifications using FACS-sorting. It relies on CRISPR/Cas9-mediated targeted knock-in of a very short promoterless expression construct (250 bp) comprising a Flag or HA epitope embedded into the smallest GPI-protein CD52, and a polyA signal from the beta-globin. CD52 efficiently delivers the epitope to the cell surface, where it serves as a marker for selection, while polyA terminates transcription and silences target gene expression. Primarily, SORTS

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9

Elvira, Bernat, Jamshed Warsi, Myriam Fezai, Carlos Munoz, and Florian Lang. "SPAK and OSR1 Sensitive Cell Membrane Protein Abundance and Activity of KCNQ1/E1 K+ Channels." Cellular Physiology and Biochemistry 37, no. 5 (2015): 2032–42. http://dx.doi.org/10.1159/000438563.

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Background/Aims: KCNQ1/E1 channels are expressed in diverse tissues and serve a variety of functions including endolymph secretion in the inner ear, cardiac repolarization, epithelial transport and cell volume regulation. Kinases involved in regulation of epithelial transport and cell volume include SPAK (SPS1-related proline/alanine-rich kinase) and OSR1 (oxidative stress-responsive kinase 1), which are under control of WNK (with-no-K[Lys]) kinases. The present study explored whether KCNQ1/E1 channels are regulated by SPAK and/or OSR1. Methods: cRNA encoding KCNQ1/E1 was injected into Xenopus

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10

Kaltwasser, Marcus, Thomas Wiegert, and Wolfgang Schumann. "Construction and Application of Epitope- and Green Fluorescent Protein-Tagging Integration Vectors for Bacillus subtilis." Applied and Environmental Microbiology 68, no. 5 (2002): 2624–28. http://dx.doi.org/10.1128/aem.68.5.2624-2628.2002.

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ABSTRACT Here we describe the construction and application of six new tagging vectors allowing the fusion of two different types of tagging sequences, epitope and localization tags, to any Bacillus subtilis protein. These vectors are based on the backbone of pMUTIN2 and replace the lacZ gene with tagging sequences. Fusion of the tagging sequences occurs by PCR amplification of the 3′ terminal part of the gene of interest (about 300 bp), insertion into the tagging vector in such a way that a fusion protein will be synthesized upon integration of the whole vector via homologous recombination wit

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