Relevant bibliographies by topics / Fluorescence spectroscopy. Green fluorescent protein Photochemistry. Proteins Proteins

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Academic literature on the topic 'Fluorescence spectroscopy. Green fluorescent protein Photochemistry. Proteins Proteins'

Author: Grafiati
Published: 4 June 2021
Last updated: 15 February 2022

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Journal articles on the topic "Fluorescence spectroscopy. Green fluorescent protein Photochemistry. Proteins Proteins"

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Bourgeois, Dominique, Aline Regis-Faro, and Virgile Adam. "Photoactivated structural dynamics of fluorescent proteins." Biochemical Society Transactions 40, no. 3 (2012): 531–38. http://dx.doi.org/10.1042/bst20120002.

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Proteins of the GFP (green fluorescent protein) family have revolutionized life sciences because they allow the tagging of biological samples in a non-invasive genetically encoded way. ‘Phototransformable’ fluorescent proteins, in particular, have recently attracted widespread interest, as their fluorescence state can be finely tuned by actinic light, a property central to the development of super-resolution microscopy. Beyond microscopy applications, phototransformable fluorescent proteins are also exquisite tools to investigate fundamental protein dynamics. Using light to trigger processes s
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Toivola, J., K. Ojala, P. O. Michel, M. Vuento, and C. Oker-Blom. "Properties of Baculovirus Particles Displaying GFP Analyzed by Fluorescence Correlation Spectroscopy." Biological Chemistry 383, no. 12 (2002): 1941–46. http://dx.doi.org/10.1515/bc.2002.218.

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Abstract Recombinant baculovirus particles displaying green fluorescent protein (GFP) fused to the major envelope glycoprotein gp64 of the Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV) were characterized by fluorescence correlation spectroscopy (FCS). FCS detected Brownian motion of single, intact recombinant baculovirus display particles with a diffusion coefficient (D) of (2.89±0.74)10 8 cm2s 1 and an apparent hydrodynamic radius of 83.35±21.22 nm. In the presence of sodium dodecyl sulfate (SDS), Triton X-100, and octylglucoside, the diffusion time was reduced to the 0.2 m
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OHSUGI, Y., and MASATAKA KINJO. "ANALYSIS OF MEMBRANE-BINDING PROTEIN MOBILITY IN LIVING CELLS USING TOTAL INTERNAL REFLECTION FLUORESCENCE CORRELATION SPECTROSCOPY." Biophysical Reviews and Letters 01, no. 03 (2006): 293–99. http://dx.doi.org/10.1142/s1793048006000227.

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Total internal reflection fluorescence correlation spectroscopy (TIR-FCS) is an appropriate method for measuring diffusion constants and the number of fluorescent molecules very close to the coverglass surface. Recently, we have reported the application of TIR-FCS to cell biology, measuring membrane-binding farnesylated green fluorescent proteins (EGFP-F) in living cells. In this research, we measured the signal transduction molecule, protein kinase C (PKC), fused with EGFP in living HeLa cells by using TIR-FCS. We observed two different diffusional mobilities of PKCβII-EGFP, three-dimensional
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Hilgers, Fabienne, Nora Lisa Bitzenhofer, Yannic Ackermann, et al. "Genetically Encoded Photosensitizers as Light-Triggered Antimicrobial Agents." International Journal of Molecular Sciences 20, no. 18 (2019): 4608. http://dx.doi.org/10.3390/ijms20184608.

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Diseases caused by multi-drug resistant pathogens have become a global concern. Therefore, new approaches suitable for treating these bacteria are urgently needed. In this study, we analyzed genetically encoded photosensitizers (PS) related to the green fluorescent protein (GFP) or light-oxygen-voltage (LOV) photoreceptors for their exogenous applicability as light-triggered antimicrobial agents. Depending on their specific photophysical properties and photochemistry, these PSs can produce different toxic ROS (reactive oxygen species) such as O2•− and H2O2 via type-I, as well as 1O2 via type-I
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Nomura, Yasutomo, Hirotoshi Tanaka, Lorenz Poellinger, Fumihiro Higashino, and Masataka Kinjo. "Monitoring of in vitro and in vivo translation of green fluorescent protein and its fusion proteins by fluorescence correlation spectroscopy." Cytometry 44, no. 1 (2001): 1–6. http://dx.doi.org/10.1002/1097-0320(20010501)44:1<1::aid-cyto1075>3.0.co;2-0.

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Péresse, Tiphaine, and Arnaud Gautier. "Next-Generation Fluorogen-Based Reporters and Biosensors for Advanced Bioimaging." International Journal of Molecular Sciences 20, no. 24 (2019): 6142. http://dx.doi.org/10.3390/ijms20246142.

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Our ability to observe biochemical events with high spatial and temporal resolution is essential for understanding the functioning of living systems. Intrinsically fluorescent proteins such as the green fluorescent protein (GFP) have revolutionized the way biologists study cells and organisms. The fluorescence toolbox has been recently extended with new fluorescent reporters composed of a genetically encoded tag that binds endogenously present or exogenously applied fluorogenic chromophores (so-called fluorogens) and activates their fluorescence. This review presents the toolbox of fluorogen-b
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Osa-Andrews, Bremansu, Kee Tan, Angelina Sampson, and Surtaj Iram. "Development of Novel Intramolecular FRET-Based ABC Transporter Biosensors to Identify New Substrates and Modulators." Pharmaceutics 10, no. 4 (2018): 186. http://dx.doi.org/10.3390/pharmaceutics10040186.

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Multidrug resistance protein 1 (MRP1) can efflux a wide variety of molecules including toxic chemicals, drugs, and their derivatives out of cells. Substrates of MRP1 include anti-cancer agents, antibiotics, anti-virals, anti-human immunodeficiency virus (HIV), and many other drugs. To identify novel substrates and modulators of MRP1 by exploiting intramolecular fluorescence resonance energy transfer (FRET), we genetically engineered six different two-color MRP1 proteins by changing green fluorescent protein (GFP) insertion sites, while keeping the red fluorescent protein (RFP) at the C-termina
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Smoyer, Christine J., Santharam S. Katta, Jennifer M. Gardner, et al. "Analysis of membrane proteins localizing to the inner nuclear envelope in living cells." Journal of Cell Biology 215, no. 4 (2016): 575–90. http://dx.doi.org/10.1083/jcb.201607043.

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Understanding the protein composition of the inner nuclear membrane (INM) is fundamental to elucidating its role in normal nuclear function and in disease; however, few tools exist to examine the INM in living cells, and the INM-specific proteome remains poorly characterized. Here, we adapted split green fluorescent protein (split-GFP) to systematically localize known and predicted integral membrane proteins in Saccharomyces cerevisiae to the INM as opposed to the outer nuclear membrane. Our data suggest that components of the endoplasmic reticulum (ER) as well as other organelles are able to
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Knol, Jaco C., Ruchira Engel, Mieke Blaauw, Antonie J. W. G. Visser та Peter J. M. van Haastert. "The Phosducin-Like Protein PhLP1 Is Essential for Gβγ Dimer Formation in Dictyostelium discoideum". Molecular and Cellular Biology 25, № 18 (2005): 8393–400. http://dx.doi.org/10.1128/mcb.25.18.8393-8400.2005.

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ABSTRACT Phosducin proteins are known to inhibit G protein-mediated signaling by sequestering Gβγ subunits. However, Dictyostelium discoideum cells lacking the phosducin-like protein PhLP1 display defective rather than enhanced G protein signaling. Here we show that green fluorescent protein (GFP)-tagged Gβ (GFP-Gβ) and GFP-Gγ subunits exhibit drastically reduced steady-state levels and are absent from the plasma membrane in phlp1 − cells. Triton X-114 partitioning suggests that lipid attachment to GFP-Gγ occurs in wild-type cells but not in phlp1 − and gβ − cells. Moreover, Gβγ dimers could n
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KRETZSCHMAR, Antje K., Michaela C. DINGER, Christian HENZE, Katja BROCKE-HEIDRICH, and Friedemann HORN. "Analysis of Stat3 (signal transducer and activator of transcription 3) dimerization by fluorescence resonance energy transfer in living cells." Biochemical Journal 377, no. 2 (2004): 289–97. http://dx.doi.org/10.1042/bj20030708.

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Signal transducer and activator of transcription 3 (Stat3) dimerization is commonly thought to be triggered by its tyrosine phosphorylation in response to interleukin-6 (IL-6) or other cytokines. Accumulating evidence from in vitro studies, however, suggests that cytoplasmic Stat3 may be associated with high-molecular-mass protein complexes and/or dimerize prior to its activation. To directly study Stat3 dimerization and subcellular localization upon cytokine stimulation, we used live-cell fluorescence spectroscopy and imaging microscopy combined with fluorescence resonance energy transfer (FR
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Dissertations / Theses on the topic "Fluorescence spectroscopy. Green fluorescent protein Photochemistry. Proteins Proteins"

1

Shu, Xiaokun. "Photophysics of emission color in flourescent proteins /." view abstract or download file of text, 2007. http://proquest.umi.com/pqdweb?did=1400969251&sid=1&Fmt=2&clientId=11238&RQT=309&VName=PQD.

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Thesis (Ph. D.)--University of Oregon, 2007.<br>Typescript. Includes vita and abstract. Includes bibliographical references (leaves 176-185). Also available for download via the World Wide Web; free to University of Oregon users.
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Henderson, Julius Nathan. "Crystallographic and spectroscopic studies of photoswitching in fluorescent proteins /." view abstract or download file of text, 2007. http://proquest.umi.com/pqdweb?did=1417810431&sid=5&Fmt=2&clientId=11238&RQT=309&VName=PQD.

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Thesis (Ph. D.)--University of Oregon, 2007.<br>Typescript. Includes vita and abstract. Includes bibliographical references (leaves 143-151). Also available for download via the World Wide Web; free to University of Oregon users.
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