Dissertations / Theses on the topic 'Arntz'
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Jaklin, Sandra [Verfasser], and Wolf E. [Akademischer Betreuer] Arntz. "Recruitment dynamics of North Sea macrozoobenthos in intertidal soft bottoms: larval availability, settlement and dispersal / Sandra Jaklin. Gutachter: Wolf E. Arntz. Betreuer: Wolf E. Arntz." Bremen : Staats- und Universitätsbibliothek Bremen, 2003. http://d-nb.info/1072563657/34.
Full textWitt, Jan [Verfasser], Wolf [Akademischer Betreuer] Arntz, and Karsten [Akademischer Betreuer] Reise. "Analysing brackish benthic communities of the Weser estuary: spatial distribution, variability and sensitivity of estuarine invertebrates / Jan Witt. Gutachter: Wolf Arntz ; Karsten Reise. Betreuer: Wolf Arntz." Bremen : Staats- und Universitätsbibliothek Bremen, 2004. http://d-nb.info/1072301792/34.
Full textArntz, Ulrike-Dorothea [Verfasser]. "Ergebnisse der Exzision des Os pisiforme bei Pisotriquetralerkrankungen / Ulrike-Dorothea Arntz." Berlin : Medizinische Fakultät Charité - Universitätsmedizin Berlin, 2013. http://d-nb.info/1064099491/34.
Full textQuéric, Nadia-Valérie [Verfasser], Wolf E. Akademischer Betreuer] Arntz, and Antje [Akademischer Betreuer] [Boetius. "Bacterial community patterns along small- and large-scale environmental radients in Arctic deep-sea sediments / Nadia-Valérie Quéric. Gutachter: Wolf E. Arntz ; Antje Boetius. Betreuer: Wolf E. Arntz." Bremen : Staats- und Universitätsbibliothek Bremen, 2008. http://d-nb.info/1072302683/34.
Full textArntz, Joachim [Verfasser]. "Der Begriff der Friedensbedrohung in Satzung und Praxis der Vereinten Nationen. / Joachim Arntz." Berlin : Duncker & Humblot, 2014. http://d-nb.info/1237961297/34.
Full textOtero, Moreno Concepción [Verfasser], and Reiner [Akademischer Betreuer] Arntz. "Kultur- und Sprachvergleich in der Translationsdidaktik - Schwerpunkt Spanisch / Concepcion Otero Moreno. Betreuer: Reiner Arntz." Hildesheim : Universitätsbibliothek Hildesheim, 2011. http://d-nb.info/1023791854/34.
Full textErdsiek, Daniel [Verfasser], and Melanie [Akademischer Betreuer] Arntz. "Essays on Overqualification, Work Organisation, and Technology: Empirical Evidence for Germany / Daniel Erdsiek ; Betreuer: Melanie Arntz." Heidelberg : Universitätsbibliothek Heidelberg, 2017. http://d-nb.info/1180738519/34.
Full textStecher, Jens-Erik [Verfasser], Wolf [Akademischer Betreuer] Arntz, Michael [Akademischer Betreuer] Türkay, and Thomas [Akademischer Betreuer] Brey. "Die Lebensgemeinschaften des Seegats der Otzumer Balje in Abhängigkeit von morphodynamischen Prozessen / Jens-Erik Stecher. Gutachter: Michael Türkay ; Thomas Brey. Betreuer: Wolf Arntz." Bremen : Staats- und Universitätsbibliothek Bremen, 2012. http://d-nb.info/107204644X/34.
Full textBailey, Fiona Jane, and mikewood@deakin edu au. "The origins of inflated responsibility in obsessive compulsive disorder." Deakin University. School of Psychology, 2002. http://tux.lib.deakin.edu.au./adt-VDU/public/adt-VDU20050902.121410.
Full textDougherty, Edward J. "Analysis of the role of bHLH/PAS proteins in aryl hydrocarbon receptor signaling." [Tampa, Fla] : University of South Florida, 2008. http://purl.fcla.edu/usf/dc/et/SFE0002441.
Full textLi, Yi. "Study of Arnt-interacting proteins on Arnt-dependent signaling pathways." Scholarly Commons, 2006. https://scholarlycommons.pacific.edu/uop_etds/2786.
Full textMeinnel, Thierry. "Interaction de la methionyl-arnt synthetase avec ses arnt specifiques." Palaiseau, École polytechnique, 1990. http://www.theses.fr/1990EPXX0005.
Full textBalg, Christian. "Synthèse d'inhibiteurs des aminoacyl-ARNt synthétases et des aminoacyl-ARNt amidotransférases." Thesis, Université Laval, 2011. http://www.theses.ulaval.ca/2011/28241/28241.pdf.
Full textFECHTER, PIERRE. "Contribution a l'etude de la reaction de tyrosylation des arnt et des pseudo-arnt." Université Louis Pasteur (Strasbourg) (1971-2008), 2001. http://www.theses.fr/2001STR13027.
Full textFender, Aurélie. "Etude comparative de couples ARNt / aminoacyl-ARNt synthétases chez la levure et la mitochondrie humaine." Phd thesis, Université Louis Pasteur - Strasbourg I, 2005. http://tel.archives-ouvertes.fr/tel-00139137.
Full textLes aspects fonctionnels et structuraux ont été davantage explorés par des essais de cristallisation et des approches in vivo.
Jusqu'à présent, il était admis que les règles de reconnaissance et d'aminoacylation d'ARNt isoaccepteurs pour un système donné devaient être identiques. L'analyse d'une famille d'ARNt isoaccepteurs de l'arginine de levure et de sa relation particulière avec l'ARNtAsp nous ont permis d'établir que : (i) les isoaccepteurs sont arginylés avec des efficacités différentes (un facteur 20 les sépare) et sont protégés de la misaminoacylation par des antidéterminants idiosyncrasiques, (ii) l'isoaccepteur ARNt4
Arg possède des propriétés d'aspartylation, vestiges de son histoire évolutive, puisque seulement deux mutations sont
suffisantes pour convertir sa spécificité – c'est un exemple de génération de la diversité moléculaire par duplication de gènes. Les systèmes d'aminoacylation mt de mammifères restent peu étudiés, et ce malgré la « bizarrerie » structurale et l'implication dans des
pathologies sévères de leurs ARNt, codés par le génome mt. Nos efforts ont permis l'assignement des 10 gènes nucléaires manquants codant pour les aaRS mt humaines. Ceux-ci
sont portés par un jeu de gènes différents de celui codant pour les sysnthétases cytoplasmiques. L'analyse détaillée du système d'aspartylation, choisi comme système modèle a révélé (i) une identité de l'ARNt mt moins stringente que celle des ARNt classiques, (ii) une adaptation subtile et ciblée de l'aaRS mt, codée par le génome nucléaire et de type bactérien. Ceci illustre un processus de co-évolution entre les génomes mt et nucléaire
humain. De plus, j'ai déterminé les signaux qui protègent l'ARNtAsp mt d'être un substrat des aaRS non mt. De manière surprenante, ce n'est pas la dégénérescence structurale globale de
l'ARNt qui empêche le plus cette aminoacylation croisée mais une simple paire de bases du bras D.
EILER, SYLVIA. "Etude structurale du complexe aspartyl-arnt synthetase d'e. Coli - arnt#a#s#p d'e. Coli." Université Louis Pasteur (Strasbourg) (1971-2008), 1998. http://www.theses.fr/1998STR13189.
Full textMOULINIER, LUC. "Etude structurale d'un complexe heterologue : aspartyl-arnt synthetase d'e. coli-arnt#a#s#p de levure." Université Louis Pasteur (Strasbourg) (1971-2008), 1997. http://www.theses.fr/1997STR13256.
Full textJühling, Tina. "ARNt "manchots" : structure, fonctionnalité et évolution." Thesis, Strasbourg, 2016. http://www.theses.fr/2016STRAJ119/document.
Full textTRNAs are adapter molecules linking the genetic information of messenger RNAs with the primary amino acid sequence of proteins. tRNAs have a typical cloverleaf-like secondary structure. Some mitochondrial tRNAs show a high derivation from this canonical tRNA structure. An extreme case of structural truncations can be observed in mitochondria of the nematode R. culicivorax. This study aims the functional characterization of such “bizarre” tRNAs in defining their structural properties and their functionality with interacting partner proteins such as CCA-adding enzymes and aminoacyl-tRNA synthetases. This work reveals that armless tRNAs form a hairpin-shaped secondary structure. 3D structures exhibit a high intrinsic flexibility. Initial tests could not demonstrate aminoacylation activity. However, armless tRNAs represent functional molecules for CCA-incorporation, indicating adaptations of CCA-adding enzymes to armless tRNAs
Bimai, Louise. "Etude biochimique et structurale de deux enzymes de thiolation des ARNt dépendantes d’un centre [4Fe-4S] : la s2U54-ARNt thiolase TtuA et la s2U34-ARNt thiolase NcsA." Electronic Thesis or Diss., Paris Sciences et Lettres (ComUE), 2018. https://theses.hal.science/tel-03270824.
Full textTransfer RNAs are essential components of cellular translation machinery. To achieve their function they possess several post-transcriptional chemical modifications. These modifications improve recognition between tRNA and its partners during translation and thus ensure translation fidelity and efficiency. Sulfur is present in several of these modified nucleosides: as thiouridine and its derivatives (s4U8, s2U34, m5s2U54), 2-thioadenosine derivatives (ms2i6A37, ms2t6A37) and 2-thiocytidine (s2C32).My project consisted in the structural and functional study of enzymes of the TtcA/TtuA family a [4Fe-4S]-dependent superfamily, involved in the thiolation of transfer RNAs (tRNAs).My aim was to show that enzymes that catalyze the simple non-redox substitution of the C2-uridine carbonyl oxygen by sulfur at position 54 (TtuA) and 34 (Ncs6/Ctu1/NcsA) in tRNAs use an iron-sulfur cluster cofactor and elucidate the biochemical and structural mechanisms of the TtuA and NcsA reactions.The thiolation of the universally conserved methyl-uridine at position 54, catalyzed by TtuA, stabilizes tRNAs from thermophilic bacteria and hyperthermophilic archaea and is required for growth at high temperature of these organisms. On the other hand, the thiolation of uridine 34 in the anticodon loop of tRNAs, which is required for normal growth and stress resistance in yeast, is carried out by two completely different systems: the well-studied MnmA protein (present in bacteria and in the eukaryotic mitochondrion) and the Nsc6/NcsA/Ctu1 proteins in all other organisms, including the eukaryotic cytoplasm.Spectroscopic and crystallographic analysis, together with activity tests enzymatic of TtuA and NcsA showed that: (i) the [4Fe-4S] cluster is ligated by three cysteines only that are fully conserved, allowing the fourth unique iron to bind an exogenous sulfide, which likely acts as the sulfurating agent; (ii) the ATP-binding site is adjacent to the cluster. A new mechanism for tRNA sulfuration was proposed, in which the unique iron of the catalytic [4Fe-4S] cluster functions as a sulfur carrier, opening new perspectives regarding functions of iron-sulfur cluster in biology
Kobbi, Lydia. "Rôle de la lysyl-ARNt synthétase mitochondriale humaine dans la réplication du VIH-1." Phd thesis, Université Paris Sud - Paris XI, 2011. http://tel.archives-ouvertes.fr/tel-00684390.
Full textDesgagnés, Julie. "Synthèse d'inhibiteurs de la glutamyl-ARNt synthétase." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp04/mq25555.pdf.
Full textFrancin-Allami, Mathilde. "L'extension polypeptidique N-terminale de la lysyl-ARNt synthétase de mammifère : un domaine fonctionnel de fixation générale des ARNt." Châtenay-Malabry, Ecole centrale de Paris, 2002. http://www.theses.fr/2002ECAP0866.
Full textChampagne, Nathalie. "Étude de l'expression du gène gltX codant pour la glutamyl-ARNt synthétase et d'un opéron d'ARNt codant pour trois ARNt[exposant Val] et un ARNt[exposant Lys] (valU) chez Escherichia coli." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/nq25392.pdf.
Full textRyckelynck, Michael. "Aspects fonctionnels et structuraux de la régulation de l'expression d'une aminoacyl-ARNt synthétase eucaryote : l'aspartyl-ARNt synthétase de Saccharomyces cerevisiae." Phd thesis, Université Louis Pasteur - Strasbourg I, 2006. http://tel.archives-ouvertes.fr/tel-00139129.
Full textWe have established the folding of the 300-nucleotides long 5' end of mRNAApRS and identified the structural signals involved in the regulation process. We propose that the mRNAAspRS fragment folds in two independent and symmetrically structured domains spaced by two single-stranded connectors. Domain I displays a tRNAAsp anticodon-like stem-loop structure that is restricted in domain II to a short double-stranded helix. The overall mRNA structure, based on enzymatic and chemical probing, support a model where each monomer of yeast AspRS binds one individual domain and recognizes the mRNA structure like it recognizes its cognate tRNAAsp.
Finally, the consequences of an increased concentration of AspRS in the cell have been tested. In vitro, high AspRS concentrations lead to mis-aspartylation of tRNAAsn and tRNAGlu. In vivo, the design of a reporter gene conferring an antibiotic resistance, dependent on mischarged tRNAs, did not allow to detect any cross aminoacylation. However, the proteomic analysis of yeasts overexpressing AspRS pointed out the conditions of AspRS accumulation in the cell by detecting the presence of an additional control mechanism at the post-translational level.
Ryckelynck, Michaël. "Aspects fonctionnels et structuraux de la régulation de l'expression d'une aminoacyl-ARNt synthétase eucaryote : l'aspartyl-ARNt synthétase de Saccharomyces cerevisiae." Strasbourg 1, 2005. https://publication-theses.unistra.fr/public/theses_doctorat/2005/RYCKELYNCK_Michael_2005.pdf.
Full textAccurate translation of genetic information necessitates the tuned expression of a large group of genes. Amongst them, controlled expression of the enzymes catalyzing the aminoacylation of tRNAs, the aminoacyl-tRNA synthetases (aaRS), is essential to insure translational fidelity. Here, it is shown that expression of AspRS is regulated in Saccharomyces cerevisiae by a feedback mechanism, that necessitates the binding of AspRS to its messenger RNA. The correlation between AspRS expression and mRNAAspRS and tRNAAsp concentrations, as well as the presence of AspRS in the nucleus, suggest an original regulation mechanism. It is proposed that the surplus of AspRS, not sequestered by tRNAAsp, is imported in the nucleus where it binds to mRNAAspRS and thus inhibits its accumulation. We have established the folding of the 300-nucleotides long 5' end of mRNAApRS and identified the structural signals involved in the regulation process. We propose that the mRNAAspRS fragment folds in two independent and symmetrically structured domains spaced by two single-stranded connectors. Domain I displays a tRNAAsp anticodon-like stem-loop structure that is restricted in domain II to a short double-stranded helix. The overall mRNA structure, based on enzymatic and chemical probing, support a model where each monomer of yeast AspRS binds one individual domain and recognizes the mRNA structure like it recognizes its cognate tRNAAsp. Finally, the consequences of an increased concentration of AspRS in the cell have been tested. In vitro, high AspRS concentrations lead to mis-aspartylation of tRNAAsn and tRNAGlu. In vivo, the design of a reporter gene conferring an antibiotic resistance, dependent on mischarged tRNAs, did not allow to detect any cross aminoacylation. However, the proteomic analysis of yeasts overexpressing AspRS pointed out the conditions of AspRS accumulation in the cell by detecting the presence of an additional control mechanism at the post-translational level
Crépin, Thibaut. "Etudes structurales et fonctionnelles de méthionyl-ARNt synthétases." Palaiseau, Ecole polytechnique, 2002. http://www.theses.fr/2002EPXX0032.
Full textCela, Madinaveitia Marta. "Import des ARNt dans Plasmodium : sélection à l'entrée ?" Thesis, Strasbourg, 2018. http://www.theses.fr/2018STRAJ067/document.
Full textMy study focused on the specificity of the interaction between two proteins of the malaria parasite (Plasmodium), tRip (tRNA import protein) and the apicoplastic tyrosyl-tRNA synthetase (api-TyrRS), with the transfer RNA (tRNA). Plasmodium is an intracellular parasite with a vestigial organelle, the apicoplast, which has its own translation system. The messenger RNA sequence was adapted to produce api-TyrRS in vitro, and I studied the specificity of apicoplastic tRNATyr recognition, which avoids erroneous interactions rather than favoring the correct ones. The tRip protein is located on the surface of the parasite, and is responsible for importing tRNAs from the host. My results suggest that this import takes place during the blood phase of the parasite. In addition, not all tRNAs are recognized uniformly. The post-transcriptional modifications of the tRNAs define the affinity of tRip, and potentialy, the import rate of this tRNA. Finally, I identified a short nucleotide sequence that binds specifically to tRip. It is a good starting point for designing a molecule that specifically targets the malaria parasite
Derbali, Habib. "La caractérisation de l'amidotransférase ARNt-dépendante (AdT) de Pseudomonas aeruginosa PAO1." Master's thesis, Université Laval, 2008. http://hdl.handle.net/20.500.11794/19806.
Full textAretz, Ina [Verfasser]. "Proteome and metabolome changes associated with mitochondrial diseases / Ina Aretz." Berlin : Freie Universität Berlin, 2016. http://d-nb.info/1108307728/34.
Full textde, los Reyes Vanessa. "I Love Ricky: How Desi Arnaz Challenged American Popular Culture." Oxford, Ohio : Miami University, 2008. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=miami1209136075.
Full textVillet, Régis. "ARN de transfert assurant la spécificité des transférases de la famille Fem dans la synthèse des précurseurs du peptidoglycane des bactéries à Gram positif." Paris 6, 2007. http://www.theses.fr/2007PA066272.
Full textBRULE, HERVE. "Arnt mitochondriaux humains et pathologies. Contribution a la comprehension des mecanismes moleculaires responsables de dysfonctionnement des arnt par une approche in vitro." Université Louis Pasteur (Strasbourg) (1971-2008), 1998. http://www.theses.fr/1998STR13048.
Full textBey, Gilbert. "Etude structurale de deux aminoacyl-ARNt synthétases de classe 1 : L'arginyl-ANRt synthétase d'escherichia coli et la leucyl-ARNt synthétase d'aquifex aeolicus." Université Louis Pasteur (Strasbourg) (1971-2008), 2003. http://www.theses.fr/2003STR13207.
Full textAminoacyl-tRNA synthetases are a family of enzymes essential for translation. AARSs catalyse the attachment of aminoacids to their cognate tRNAs. For the aminoacylation reaction, they use aminoacids, tRNA and ATP. Furthermore, AARSs are ubiquitous in all kingdoms and are a good witness of the complexity of evolution. In this work, we report two structural studies of two class I AARSs: ArgRS from E. Coli and LeuRS from A. Aeolicus. ArgRS is an AARS which can discriminate 4 cognate isoacceptor tRNAs in E. Coli. Unless ArgRS form yeast, this enzyme need to bind properly the strong identity element A20 of tRNA. After a global view of evolution of ArgRSs in 140 organisms, we present here first crystals for free form and enzyme bound to the major tRNA of E. Coli. LeuRS from A. Aeolicus is a particular LeuRS. In all others organism, this enzyme is a monomer. In this thermopile bacteria, LeuRS is split in two parts, a and ß, and the heterodimer aß is functionally similar to a canonical monomer. Also, we have shown two oligomeric active forms for this enzyme aß et (aß)2. Now, we have obtain well diffracting crystals of the free form and we hope to get phases in a soon future
Yavrom, Sheena. "Evidence that ARNT plays a role in the regulation of the immunoglobulin heavy chain enhancer and identification of a putative ARNT ligand." Scholarly Commons, 1998. https://scholarlycommons.pacific.edu/uop_etds/516.
Full textTouzé, Elodie. "Cristallogenèse et études structurales appliquées aux aminoacyl-ARNt synthétases." Phd thesis, Université Louis Pasteur - Strasbourg I, 2007. http://tel.archives-ouvertes.fr/tel-00206952.
Full textBernier, Stéphane. "Synthèse d'inhibiteurs des glutaminyl, glutamyl et aspartyl-ARNt synthétases." Thesis, Université Laval, 2007. http://www.theses.ulaval.ca/2007/24334/24334.pdf.
Full textTouzé, Elodie Giegé Richard. "Cristallogenèse et études structurales appliquées aux aminoacyl-ARNt synthétases." Strasbourg : Université Louis Pasteur, 2008. http://eprints-scd-ulp.u-strasbg.fr:8080/911/01/TOUZE_Elodie_2007.pdf.
Full textPARK, YOUNG CHUL. "Stabilite d'une proteine dimerique complexe : la tyrosyl-arnt synthetase." Paris 7, 1998. http://www.theses.fr/1998PA077266.
Full textOlieric, Natacha. "Etude structurale de la Leucyl-ARNt synthétase d'Aquifex aeolicus." Strasbourg 1, 2005. http://www.theses.fr/2005STR13220.
Full textYu, Adam Christopher. "Neuroinflammatory conditions modulate ARNT2 and RME-8 expression within the CNS." Thesis, University of British Columbia, 2016. http://hdl.handle.net/2429/58643.
Full textMedicine, Faculty of
Pathology and Laboratory Medicine, Department of
Graduate
Prévost, Gilles. "Essais de clonage du gène de l'arginyl-ARNt synthétase de Saccharomyces cerevisiae détermination des domaines fonctionnels de l'aspartyl-ARNt synthétase de Saccharomyces cerevisiae /." Grenoble 2 : ANRT, 1988. http://catalogue.bnf.fr/ark:/12148/cb376177246.
Full textQUEVILLON-CHERUEL, SOPHIE. "Le complexe des aminoacyl-arnt synthetases : caracterisation moleculaire de la composante glutaminyl-arnt synthetase et des trois proteines associees p43, p38 et p18." Paris 11, 1995. http://www.theses.fr/1995PA112058.
Full textPrévost, Gilles. "Essais de clonage du gene de l'arginyl-arnt synthetase de saccharomyces cerevisiae : determination des domaines fonctionnels de l'aspartyl-arnt synthetase de saccharomyces cerevisiae." Université Louis Pasteur (Strasbourg) (1971-2008), 1988. http://www.theses.fr/1988STR13015.
Full textGuigou, Ludovic. "L'arginyl-ARNt synthétase de mammifère : rôle des interactions protéine-protéine et protéine-ARN sur son activité." Paris 11, 2005. http://www.theses.fr/2005PA112141.
Full textEach aminoacyl-tRNA synthetase catalyze the esterification of its cognate amino acid to the 3'-end of its cognate tRNA(s). Some aminoacyl-tRNA synthetases (aaRSs) catalyze the amino acid activation step only in the presence of a cognate tRNA. This behaviour has been studied in Arginyl-tRNA synthetase (ArgRS) from hamster. Our results show that three contact points with the tRNA molecule are important in the activation step : bases A76, A20 and C35. These three bases must be presented by a tRNA possessing both rigidity (intact " L " shape) and flexibility (provided by G-U base-pairs). We conclude that the triggering of the activation step in ArgRS implies an induced-fit mechanism. Enzymes from the multi-aaRSs complex found in higher eukaryotes display additional basic domains, some of them interacting with tRNAs. We show that these domains increase the affinity of the enzymes of the complex for their specific tRNAs only. Thus, the catalytic body of each enzyme determines its specificity, while the additionnal basic domains increase the affinity of the enzymes for their specific tRNA(s). The p43 protein, a component of the complex able to interact with tRNAs and ArgRS, does not affect the catalytic parameters of this enzyme. Crystals of a short form of the p43 protein have been obtained and the structure has been solved by molecular replacement, but the N-terminal residues, that are responsible for the interaction with tRNAs, are not visible. Conditions for the isolation of the multi-aaRSs complex have been refined in order to carry out a structural study using cryo-electron microscopy and crystallography
COMMANS, STEPHANE. "Relations structure-fonction de la lysyl-arnt synthetase d'escherichia coli." Paris 11, 1997. http://www.theses.fr/1997PA112110.
Full textCURA, VINCENT. "Etude structurale de la threonyl-arnt synthetase de t. Thermophilus." Université Louis Pasteur (Strasbourg) (1971-2008), 1995. http://www.theses.fr/1995STR13142.
Full textSamsa, William E. "The Role of Brain and Muscle ARNTL 1 (BMAL1) in Bone Homeostasis." Cleveland State University / OhioLINK, 2015. http://rave.ohiolink.edu/etdc/view?acc_num=csu1449481876.
Full textGrenier, Luc. "Conception et caractérisation de nouveaux inhibiteurs antibiotiques de la glutamyl-ARNt synthétase à partir d'approches informatiques." Thesis, Université Laval, 2013. http://www.theses.ulaval.ca/2013/29832/29832.pdf.
Full textAretz, Bodo [Verfasser], and Wolfgang [Akademischer Betreuer] Franz. "Empirical Essays on Wage Dynamics and Donation Options / Bodo Aretz. Betreuer: Wolfgang Franz." Mannheim : Universitätsbibliothek Mannheim, 2012. http://d-nb.info/1034490753/34.
Full textRahim, Titissa. "Investigating the regulation of ARNT2, a neuroprotective protein, in models of multiple sclerosis." Thesis, University of British Columbia, 2016. http://hdl.handle.net/2429/58253.
Full textMedicine, Faculty of
Pathology and Laboratory Medicine, Department of
Graduate