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Relevant bibliographies by topics / SfGFP, superfolder green fluorescent protein

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Journal articles

Academic literature on the topic 'SfGFP, superfolder green fluorescent protein'

Author: Grafiati

Published: 4 June 2021

Last updated: 7 February 2022

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Journal articles on the topic "SfGFP, superfolder green fluorescent protein"

1

Pedelacq, Jean-Denis, and Stéphanie Cabantous. "Development and Applications of Superfolder and Split Fluorescent Protein Detection Systems in Biology." International Journal of Molecular Sciences 20, no. 14 (2019): 3479. http://dx.doi.org/10.3390/ijms20143479.

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Molecular engineering of the green fluorescent protein (GFP) into a robust and stable variant named Superfolder GFP (sfGFP) has revolutionized the field of biosensor development and the use of fluorescent markers in diverse area of biology. sfGFP-based self-associating bipartite split-FP systems have been widely exploited to monitor soluble expression in vitro, localization, and trafficking of proteins in cellulo. A more recent class of split-FP variants, named « tripartite » split-FP, that rely on the self-assembly of three GFP fragments, is particularly well suited for the detection of prote

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2

Olenginski, Gregory M., Juliana Piacentini, Darcy R. Harris, et al. "Structural and spectrophotometric investigation of two unnatural amino-acid altered chromophores in the superfolder green fluorescent protein." Acta Crystallographica Section D Structural Biology 77, no. 8 (2021): 1010–18. http://dx.doi.org/10.1107/s2059798321006525.

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The spectrophotometric properties of the green fluorescent protein (GFP) result from the post-translationally cyclized chromophore composed of three amino acids including a tyrosine at the center of the β-barrel protein. Altering the amino acids in the chromophore or the nearby region has resulted in numerous GFP variants with differing photophysical properties. To further examine the effect of small atomic changes in the chromophore on the structure and photophysical properties of GFP, the hydroxyl group of the chromophore tyrosine was replaced with a nitro or a cyano group. The structures an

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3

Maurici, Nicole, Nicole Savidge, Byung Uk Lee, Scott H. Brewer, and Christine M. Phillips-Piro. "Crystal structures of green fluorescent protein with the unnatural amino acid 4-nitro-L-phenylalanine." Acta Crystallographica Section F Structural Biology Communications 74, no. 10 (2018): 650–55. http://dx.doi.org/10.1107/s2053230x1801169x.

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The X-ray crystal structures of two superfolder green fluorescent protein (sfGFP) constructs containing a genetically incorporated spectroscopic reporter unnatural amino acid, 4-nitro-L-phenylalanine (pNO2F), at two unique sites in the protein have been determined. Amber codon-suppression methodology was used to site-specifically incorporate pNO2F at a solvent-accessible (Asp133) and a partially buried (Asn149) site in sfGFP. The Asp133pNO2F sfGFP construct crystallized with two molecules per asymmetric unit in space group P3221 and the crystal structure was refined to 2.05 Å resolution. Cryst

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4

Lajoie, Patrick, Robyn D. Moir, Ian M. Willis, and Erik L. Snapp. "Kar2p availability defines distinct forms of endoplasmic reticulum stress in living cells." Molecular Biology of the Cell 23, no. 5 (2012): 955–64. http://dx.doi.org/10.1091/mbc.e11-12-0995.

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Accumulation of misfolded secretory proteins in the endoplasmic reticulum (ER) activates the unfolded protein response (UPR) stress pathway. To enhance secretory protein folding and promote adaptation to stress, the UPR upregulates ER chaperone levels, including BiP. Here we describe chromosomal tagging of KAR2, the yeast homologue of BiP, with superfolder green fluorescent protein (sfGFP) to create a multifunctional endogenous reporter of the ER folding environment. Changes in Kar2p-sfGFP fluorescence levels directly correlate with UPR activity and represent a robust reporter for high-through

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5

Jahangir, ZMG Sarwar, and Arleta Helena Marnik. "A study protocol to prepare an RBD protein for vaccine against COVID-19." F1000Research 10 (September 20, 2021): 943. http://dx.doi.org/10.12688/f1000research.54738.1.

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Background: The SARS-CoV-2 pandemic is a global threat to humans and the world’s economy. Effective and safe vaccines against this virus are essential to control and eradicate the pandemic. The currently applied vaccines carry SARS-CoV-2 spike-protein mRNA/cDNA. These vaccines go through several cellular processes in the recipients for producing antigens. On the contrary, the SARS-CoV-2 RBD (receptor binding domain)-protein is an antigen. It will directly stimulate antibody production against SARS-CoV-2. Hence, we propose to produce SARS-CoV-2 RBD-protein as a fast acting, effective and safe v

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6

Ramadani-Muja, Jeta, Benjamin Gottschalk, Katharina Pfeil, et al. "Visualization of Sirtuin 4 Distribution between Mitochondria and the Nucleus, Based on Bimolecular Fluorescence Self-Complementation." Cells 8, no. 12 (2019): 1583. http://dx.doi.org/10.3390/cells8121583.

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Mitochondrial sirtuins (Sirts) control important cellular processes related to stress. Despite their regulatory importance, however, the dynamics and subcellular distributions of Sirts remain debatable. Here, we investigate the subcellular localization of sirtuin 4 (Sirt4), a sirtuin variant with a mitochondrial targeting sequence (MTS), by expressing Sirt4 fused to the superfolder green fluorescent protein (Sirt4-sfGFP) in HeLa and pancreatic β-cells. Super resolution fluorescence microscopy revealed the trapping of Sirt4-sfGFP to the outer mitochondrial membrane (OMM), possibly due to slow m

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7

Gao, Wei, Ning Bu, and Yuan Lu. "Efficient Incorporation of Unnatural Amino Acids into Proteins with a Robust Cell-Free System." Methods and Protocols 2, no. 1 (2019): 16. http://dx.doi.org/10.3390/mps2010016.

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Unnatural proteins are crucial biomacromolecules and have been widely applied in fundamental science, novel biopolymer materials, enzymes, and therapeutics. Cell-free protein synthesis (CFPS) system can serve as a robust platform to synthesize unnatural proteins by highly effective site-specific incorporation of unnatural amino acids (UNAAs), without the limitations of cell membrane permeability and the toxicity of unnatural components. Here, we describe a quick and simple method to synthesize unnatural proteins in CFPS system based on Escherichia coli crude extract, with unnatural orthogonal

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8

Subach, Oksana M., and Fedor V. Subach. "GAF-CaMP3–sfGFP, An Enhanced Version of the Near-Infrared Genetically Encoded Positive Phytochrome-Based Calcium Indicator for the Visualization of Neuronal Activity." International Journal of Molecular Sciences 21, no. 18 (2020): 6883. http://dx.doi.org/10.3390/ijms21186883.

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The first generation of near-infrared, genetically encoded calcium indicators (NIR-GECIs) was developed from bacterial phytochrome-based fluorescent proteins that utilize biliverdin (BV) as the chromophore moiety. However, NIR-GECIs have some main drawbacks such as either an inverted response to calcium ions (in the case of NIR-GECO1) or a limited dynamic range and a lack of data about their application in neurons (in the case of GAF-CaMP2–superfolder green fluorescent protein (sfGFP)). Here, we developed an enhanced version of the GAF-CaMP2–sfGFP indicator, named GAF-CaMP3–sfGFP. The GAF-CaMP

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9

Dippel, Andrew B., Gregory M. Olenginski, Nicole Maurici, Melanie T. Liskov, Scott H. Brewer, and Christine M. Phillips-Piro. "Probing the effectiveness of spectroscopic reporter unnatural amino acids: a structural study." Acta Crystallographica Section D Structural Biology 72, no. 1 (2016): 121–30. http://dx.doi.org/10.1107/s2059798315022858.

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The X-ray crystal structures of superfolder green fluorescent protein (sfGFP) containing the spectroscopic reporter unnatural amino acids (UAAs) 4-cyano-L-phenylalanine (pCNF) or 4-ethynyl-L-phenylalanine (pCCF) at two unique sites in the protein have been determined. These UAAs were genetically incorporated into sfGFP in a solvent-exposed loop region and/or a partially buried site on the β-barrel of the protein. The crystal structures containing the UAAs at these two sites permit the structural implications of UAA incorporation for the native protein structure to be assessed with high resolut

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10

Khmelinskii, Anton, Matthias Meurer, Chi-Ting Ho, et al. "Incomplete proteasomal degradation of green fluorescent proteins in the context of tandem fluorescent protein timers." Molecular Biology of the Cell 27, no. 2 (2016): 360–70. http://dx.doi.org/10.1091/mbc.e15-07-0525.

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Tandem fluorescent protein timers (tFTs) report on protein age through time-dependent change in color, which can be exploited to study protein turnover and trafficking. Each tFT, composed of two fluorescent proteins (FPs) that differ in maturation kinetics, is suited to follow protein dynamics within a specific time range determined by the maturation rates of both FPs. So far, tFTs have been constructed by combining slower-maturing red fluorescent proteins (redFPs) with the faster-maturing superfolder green fluorescent protein (sfGFP). Toward a comprehensive characterization of tFTs, we compar

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