Rozprawy doktorskie na temat „FCCUs”
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Whitcombe, Joshua Matthew, i n/a. "Study of Catalyst Particle Emissions From a Fluidized Catalytic Cracker Unit". Griffith University. School of Environmental Engineering, 2003. http://www4.gu.edu.au:8080/adt-root/public/adt-QGU20031003.152200.
Pełny tekst źródłaWhitcombe, Joshua Matthew. "Study of Catalyst Particle Emissions From a Fluidized Catalytic Cracker Unit". Thesis, Griffith University, 2003. http://hdl.handle.net/10072/367301.
Pełny tekst źródłaThesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Environmental Engineering
Faculty of Environmental Sciences
Full Text
Veluswamy, Ganesh Kumar. "Hydrodynamics of industrial scale FCCU stripper". Thesis, Curtin University, 2010. http://hdl.handle.net/20.500.11937/1965.
Pełny tekst źródłaMei, Yu 1969. "An experimental and empirical investigation of the FCC's spectrum auctions". Diss., The University of Arizona, 1998. http://hdl.handle.net/10150/288840.
Pełny tekst źródłaMallory, Donald Paul. "Co-diffusion of particles in biological systems studied using PIE-FCCS". University of Akron / OhioLINK, 2021. http://rave.ohiolink.edu/etdc/view?acc_num=akron1627666937482877.
Pełny tekst źródłaJackson, Penny M. "The effects of the FCC's 2003 revision of the 1996 Telecommunications Act on media ownership groups and voice diversity". Honors in the Major Thesis, University of Central Florida, 2007. http://digital.library.ucf.edu/cdm/ref/collection/ETH/id/1033.
Pełny tekst źródłaBachelors
Sciences
Radio and TV; Broadcast Journalism
Chmyrov, Volodymyr. "Fluorescence fluctuation studies of biomolecular interactions in solutions, biomembranes and live cells". Doctoral thesis, KTH, Experimentell biomolekylär fysik, 2016. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-187708.
Pełny tekst źródłaQC 20160527
定家, 和佳子. "FCCSを用いた生細胞内タンパク質間相互作用の定量". 京都大学 (Kyoto University), 2015. http://hdl.handle.net/2433/199469.
Pełny tekst źródłaRaabe, Isabel. "Visualization of cell-to-cell communication by advanced microscopy techniques". Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2015. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-178404.
Pełny tekst źródłaDéméautis, Claire. "Développement de nouvelles méthodes pour dépasser les limitations rencontrées dans le suivi de biosenseur FRET par microscopie de fluorescence quantitative". Thesis, Rennes 1, 2016. http://www.theses.fr/2016REN1B035/document.
Pełny tekst źródłaFluorescence microscopy has become an invaluable tool in biology. In particular, it allows to follow in time and space the activity of proteins, using genetically encoded FRET biosensors, in live cell imaging. In my thesis work, I have developed new quantitative fluorescence microscopy methods to overcome the limitations encountered in monitoring FRET biosensors. First, I developed a methodology to monitor simultaneously two genetically encoded FRET biosensors by lifetime measures (FLIM) with a single excitation wavelength. Previously, it was not easy to follow two biochemical activities by FRET biosensors in the same live sample by fluorescence microscopy. Two reasons for that: the existence of spectral bleed through in the detection channel of each fluorescent proteins and the use of two excitation wavelengths for the two donors. By combining two fluorescent proteins pairs: mTFP1 / ShadowG and LSSmOrange / mKate2, the “spectral bleed through” artifact became negligible. It became then possible to follow the kinase activity of PKA and ERK proteins simultaneously by FLIM. Using this methodology, we were able to show an activation of the PKA pathway upon stimulation with EGF. Second, I developed a method to monitor FRET biosensor by fluorescence cross-correlation spectroscopy technique (FCCS). Monitoring the activity of certain proteins may be difficult due to their low expression in living sample and their sub-cellular localization. The FCCS methods requires a low concentration of fluorophores and can therefore be adapted to these samples. FRET has a direct effect on the cross-correlation amplitude when it is measured by following the co-diffusion of two fluorescent proteins attached to a same biosensor. An amplitude ratio decrease, of the autocorrelation curves (green or red) on the amplitude of the cross-correlation curve, corresponds to the presence of FRET. We were able to measure this ratio decreases in cells expressing the FRET biosensor Aurora A wild type (FRET) compared to the K162M mutant one (non-FRET). These first results are very promising to monitor the activity of a weakly expressed protein in living cells biosensor using this approach. The improvement of FRET biosensor monitoring, by quantitative fluorescence microscopy methods presented in this work, will help to answer biological questions of interest requiring the measurement of multiplex FRET monitoring or biosensors at low level expression, where conventional techniques are facing these limitations
Pernuš, Agata [Verfasser], i Jörg [Akademischer Betreuer] Langowski. "Imaging mobility and interaction of c-Fos and c-Jun transcription factors in live cells: A SPIM-FCCS study / Agata Pernus ; Betreuer: Jörg Langowski". Heidelberg : Universitätsbibliothek Heidelberg, 2015. http://d-nb.info/1180500849/34.
Pełny tekst źródłaKIM, SOYEON. "INVESTIGATING THE MOLECULAR INTERACTION OF ERBB RECEPTOR TYROSINE KINASES USING FLUORESCENCE CROSS CORRELATION SPECTROSCOPY". University of Akron / OhioLINK, 2021. http://rave.ohiolink.edu/etdc/view?acc_num=akron1632756640189756.
Pełny tekst źródłaStaroske, Wolfgang. "In Vitro and In Vivo Applications of Fluorescence Cross-Correlation Spectroscopy". Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2010. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-62329.
Pełny tekst źródłaFluoreszenz-Korrelations-Spektroskopie (FCS) analysiert die Fluktuationen im Fluoreszenzsignal eines kleinen angeregten Volumens, um Informationen über die Konzentration, die Bewegung und die Interaktionen der markierten Moleküle zu erhalten. Die Fluoreszenz-Kreuzkorrelations-Spektroskopie (FCCS) erhöht die Genauigkeit bei der Messung von Fließgeschwindigkeiten und Bindungskonstanten im Vergleich zur Standard-FCS. Die Miniaturisierung der Biomedizin und Chemie hat sich rapide entwickelt, angetrieben von der Vision eines kompletten Labors auf einem Chip und dem Einsatz dieses in der medizinischen Therapie, zum Beispiel als implantierter Medikamentenspender. Ein Schlüsselelement zur Erfüllung dieser Vision ist der Transport von kleinsten Flüssigkeitsmengen in diesen miniaturisierten Systemen. Der Transport von Flüssigkeiten mittels des elektrohydrodynamischen Prinzips umgeht viele Nachteile von anderen Systemen, allerdings zeigt eine solche Pumpe ein kompliziertes Strömungsbild in der aktiven Region, welches sich mit herkömmlichen Methoden wie Teilchenverfolgung nicht vermessen ließ. Hier wurde Zwei-Fokus-FCCS (2f-FCCS) genutzt, um das Strömungsbild in der Pumpe zu vermessen. Die hohe Genauigkeit der 2f-FCCS bei der Bestimmung von Fließgeschwindigkeiten auch mit kleinen fluoreszierenden Teilchen ermöglichte die Messung der Fließgeschwindigkeiten, aufgrund der auf das Lösungsmittel wirkenden elektrohydrodynamischen Kräfte, unter Ausschluss der auf größere Teilchen wirkenden dielektrophoretischen Kräfte. Die Analyse der Daten ergab, dass das Strömungsbild aus zwei entgegengesetzt rotierenden unterschiedlich großen Wirbeln besteht. Dieses Strömungsbild erklärt die komplizierten Teilchenbewegungsbahnen und die Anreicherung der Teilchen in klar abgegrenzten Bereichen über den Mikroelektroden. Im zweiten Teil dieser Arbeit wurde der RNAi-Mechanismus in lebenden Zellen mittels Zwei-Farben-FCCS untersucht. RNA Interferenz (RNAi) ist ein evolutionär erhaltener Geninaktivierungsmechanismus, der kurze doppelsträngige RNA Moleküle, so genannte kurze interferierende RNAs (siRNAs), als Effektormoleküle nutzt. Die Spezifi tät und Einfachheit der RNAi hat ihr ein weites Feld in der medikamentösen Therapie geöffnet. Zur Erweiterung dieses Feldes ist es nötig die Stabilität der siRNAs im Körper mittels chemischer Modi fikationen zu erhöhen. Einige dieser Modifikationen hemmen aber den RNAi-Mechanismus. Die hier vorgestellten FCCS Experimente sind sehr gut geeignet, um die einzelnen Schritte des Zusammenbaus der RNAi Maschinerie mit hoher Empfi ndlichkeit und Spezi fität in Echtzeit zu untersuchen und die Aktivität der RNAi Maschinerie zu studieren. Es konnte ein Zusammenhang zwischen der Aktivität der RNAi Maschinerie und den Ergebnissen der FCCS Messungen hergestellt werden. Der Einfluss von verschiedenen chemischen Modikationen auf den Zusammenbau und die Aktivität der RNAi Maschinerie wurde mit diesen neuartigen Methoden untersucht
Teichmann, Anke. "Fluoreszenzmikroskopische Untersuchungen zur Interaktion G-Protein gekoppelter Rezeptoren". Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2013. http://dx.doi.org/10.18452/16671.
Pełny tekst źródłaThe heptahelical G protein-coupled receptors (GPCRs) are important drug targets. Following activation by their ligands, they exert their function via the binding of G proteins and activation of specific signal transduction cascades. To date, the functional significance of the oligomerization of GPCRs is not completely understood. For some GPCRs it could be shown that the oligomerization modulates receptor transport and/or the dynamics of receptor activation. Most importantly, it is not clear whether the GPCRs exist exclusively as oligomers or in a certain monomer-dimer ratio (M/D) or whether a given ratio is dynamic. In this work, the homo-oligomerization of the endothelin-B-receptor (ETBR), the vasopressin-V2-receptor (V2R) and the corticotropin-releasing-factor-receptors type 1 (CRF1R) and type 2(a) (CRF2(a)R) was analysed. In addition, the M/D of these GPCRs was determined. For the detection of the protein-protein interactions, the following biophysical methods were established: fluorescence-resonance-energy-transfer (FRET) and fluorescence-crosscorrelation-spectroscopy (FCCS). With the help of FCCS, a specific M/D could be determined for each of the GPCRs. Using FRET, differences in the interaction dynamics between family 1 (V2R) and family 2 GPCRs (CRF1R) could be described. Moreover, it was experimentally verified that the CRF2(a)R is exclusively expressed as a monomer, in contrast to the other GPCRs and even the highly homologous CRF1R. Using signal peptide swap experiments, it could be demonstrated that the N-terminal pseudo signal peptide of the CRF2(a)R, which is so far unique in the superfamily of GPCRs, prevents oligomerization of the receptor. In addition, a relation of receptor oligomerization and G protein coupling selectivity was established for the CRF1R and the CRF2(a)R which is novel for the GPCR protein family.
Montenegro-Galindo, Gladys Rocio. "Synthesis and Protein Adsorption Studies of Pegylated-Polyester Nanoparticles with Different Peg Architectures". University of Akron / OhioLINK, 2013. http://rave.ohiolink.edu/etdc/view?acc_num=akron1384629996.
Pełny tekst źródłaComar, William D. Ph D. "ESTABLISHING AND MANIPULATING THE DIMERIC INTERFACE OF VISUAL/NON-VISUAL OPSINS". University of Akron / OhioLINK, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=akron152882487417841.
Pełny tekst źródłaLee, Chun-Ying, i 李俊穎. "Kinetic Analysis of DNA Binding of Topoisomerase II by FCCS and FRET". Thesis, 2014. http://ndltd.ncl.edu.tw/handle/38279347969736043706.
Pełny tekst źródła國立臺灣大學
化學研究所
102
Type II topoisomerases are essential enzymes that are involved in chromosome segregation and structural modifications, and in regulating intracellular DNA supercoiling. In the past decades, the enzymatic function of topoisomerase II has been widely studied by biochemists. It acts by transiently breaking one DNA double strand (cleavage), allowing the second double strand to pass through the opened DNA gate, followed by rejoining the broken ends (religation) to close the gate. However, part of the mechanisms still remains unclear. Recently, optical techniques have been applied to investigate the kinetics of topoisomerase, especially single molecule methods. In this study, we describe three applications of confocal spectroscopy: fluorescence cross-correlation spectroscopy (FCCS), Forster resonance energy transfer (FRET) in solution, and single molecule FRET analysis in gel-based system. In our system, we use a unique oligonucleotide substrate with a pair of fluorophore straddling the topoisomerase II cleavage site to monitor the kinetic behavior of this enzyme. FCCS is a biophysical technique that measures fluorescence fluctuations in a confined focal volume to determine diffusion coefficient, and thus, the binding kinetics of DNA and topoisomerase II can be addressed. FRET monitors the distance between a pair of fluorophores on the DNA. The energy transfer efficiency depends on the DNA conformational change induced by the enzyme binding. Both solution and gel-based FRET system can be used to investigate the dynamics of DNA gate during the catalytic cycle. To sum up, our method provides an opportunity to study the individual steps in a Top II catalytic cycle: to measure the binding by FCCS and to monitor catalytic reactions by FRET.