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Dissertations / Theses on the topic 'Molecular chaperone DnaK'

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1

Simpkins, Sean A. "The DnaK molecular chaperone of Rhizobium leguminosarum." Thesis, University of East Anglia, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.302035.

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2

Anglès, Frédéric. "Impact of the molecular chaperone HSP70/DnaK on the Escherichia coli central metabolism." Thesis, Toulouse 3, 2015. http://www.theses.fr/2015TOU30126.

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Le réseau de protéines chaperons est hautement conservé dans l'ensemble du vivant. Il régule l'homéostasie des protéines au sein de la cellule en condition de croissance normale ainsi qu'en réponse à des stress environnementaux. Les chaperons membres de la famille HSP70 (Heat Shock Protein 70 kDa), famille particulièrement conservée, agissent tout au long de la biogénèse des protéines et orchestrent une pléthore de processus cellulaires liés au repliement et/ou au remodelage de protéines. Le cycle ATP-dépendant du chaperon HSP70 repose sur une étroite collaboration avec ses partenaires co-chap
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3

Akhrymuk, Alena [Verfasser]. "Studies on the interaction between the molecular chaperone DnaK and Nucleotide exchange factor GrpE from Thermus thermophilus / Alena Akhrymuk." Dortmund : Universitätsbibliothek Technische Universität Dortmund, 2004. http://d-nb.info/1011532042/34.

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4

Adell, Moruno Maria. "Caracterización bioquímica y estructural de la chaperona DnaK de Mycoplasma genitalium." Doctoral thesis, Universitat de Barcelona, 2015. http://hdl.handle.net/10803/299789.

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Mycoplasma genitalium es un patógeno humano considerado uno de los organismos autorreplicativos más pequeños que existen. Su genoma fue completamente secuenciado en 1995, y actualmente, se ha convertido en un intenso objeto de estudio porque ha sido descrito como modelo ideal de célula mínima. M. genitalium presenta una morfología celular caracterizada por una extensión de la membrana en uno de los polos de la célula, conocido como Organela Terminal (OT). La OT está involucrada en procesos celulares tales como adhesión, división celular y motilidad con implicaciones directas en patogenicidad y
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5

Krenek, Sascha, Martin Schlegel, and Thomas U. Berendonk. "Convergent evolution of heat-inducibility during subfunctionalization of the Hsp70 gene family." Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2013. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-126934.

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Background: Heat-shock proteins of the 70 kDa family (Hsp70s) are essential chaperones required for key cellular functions. In eukaryotes, four subfamilies can be distinguished according to their function and localisation in different cellular compartments: cytosol, endoplasmic reticulum, mitochondria and chloroplasts. Generally, multiple cytosol-type Hsp70s can be found in metazoans that show either constitutive expression and/or stress-inducibility, arguing for the evolution of different tasks and functions. Information about the hsp70 copy number and diversity in microbial eukaryotes is, ho
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6

Bruel, Nicolas. "Hsp33 controls elongation factor-tu stability and allows escherichia coli growth in the absence of the major dnak and triggerfactor chaperones." Toulouse 3, 2013. http://thesesups.ups-tlse.fr/2098/.

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Le repliement intracellulaire des protéines nouvellement synthétisées est assisté par des réseaux cellulaires de protéines chaperons. Chez Escherichia coli, la coopération entre les protéines chaperons Trigger Factor (TF) et DnaK est prédominante dans ce processus. En accord avec ceci, la délétion simultanée des gènes codants pour ces deux protéines chaperons conduit à une croissance bactérienne très réduite et à l'accumulation d'un grand nombre de protéines cytoplasmiques sous forme d'agrégats. Au cours de cette étude, nous avons utilisé ces phénotypes afin de mettre en évidence des interacti
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7

Partensky, Peretz. "Contributions of DNA, histone chaperones and chromatin remodeling enzymes to nucleosome positioning." Diss., Search in ProQuest Dissertations & Theses. UC Only, 2009. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3390069.

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8

Georg, Raphaela de Castro. "Análise da expressão gênica em resposta ao choque térmico e cádmio no fungo aquático Blastocladiella emersonii." Universidade de São Paulo, 2006. http://www.teses.usp.br/teses/disponiveis/46/46131/tde-18042007-125925/.

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Neste trabalho realizamos um programa de seqüenciamento em larga escala de cDNAs obtidos de bibliotecas construídas a partir de mRNA de células de B. emersonii submetidas ao choque térmico e ao estresse por cádmio. Obtivemos 6350 seqüências expressas (ESTs) de alta qualidade, que representam 2326 seqüências únicas putativas (unigenes) do fungo. Destes unigenes putativos, 1282 genes foram classificados em pelo menos uma das categorias do Consórcio Gene Ontology (GO). A análise do transcriptoma parcial de B. emersonii determinado até o momento permitiu a identificação de 78 unigenes codificando
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9

Ludewig, Michael Hans. "The characterisation of trypanosomal type 1 DnaJ-like proteins." Thesis, Rhodes University, 2010. http://hdl.handle.net/10962/d1015205.

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Trypanosomes are protozoans, of which many are parasitic, and possess complex lifecycles which alternate between mammalian and arthropod hosts. As is the case with most organisms, molecular chaperones and heat shock proteins are encoded within the genomes of these protozoans. These proteins are an integral part of maintaining the structural integrity of proteins during normal and stress conditions. Heat shock protein 40 (Hsp40) is a co-chaperone of heat shock protein 70 (Hsp70) and in some cases can act as a chaperone. These proteins work together to bind non-native polypeptide structures to p
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10

Ramey, Christopher Joshua. "The role of histone H3/H4 chaperone anti-silencing function1 in maintaining genomic integrity /." Connect to full text via ProQuest. IP filtered, 2006.

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Thesis (Ph.D. in Molecular Biology) -- University of Colorado at Denver and Health Sciences Center, 2006.<br>Typescript. Includes bibliographical references (leaves 119-130). Free to UCDHSC affiliates. Online version available via ProQuest Digital Dissertations;
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11

Girard, Martine. "Proteomic analysis of clathrin-coated vesicles and functional characterization of the mammalian DnaJ domain-containing protein receptor-mediated endocytosis 8." Thesis, McGill University, 2008. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=115684.

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Clathrin-mediated endocytosis (CME) plays a central role in the regulation of multiple cellular processes such as uptake of nutrients, recycling of housekeeping receptors and transporters, as well as for cell surface removal and downregulation of signaling receptors. Once endocytosed, cargo passes through early endosomes where sorting mechanisms traffic the cargo to the recycling pathway or to degradation in the lysosome. The general objectives of this doctoral research were to identify and characterize new players of the clathrin-mediated trafficking pathway to reveal differences between the
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12

Linger, Jeffrey G. "The role of histone chaperones in double-strand DNA repair and replication-independent histone exchange /." Connect to full text via ProQuest. IP filtered, 2006.

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Thesis (Ph.D. in Biochemistry) -- University of Colorado, 2006.<br>Typescript. Includes bibliographical references (leaves 153-171). Free to UCDHSC affiliates. Online version available via ProQuest Digital Dissertations;
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13

Kang, Hyun-Jin, Yunxi Cui, Holly Yin, et al. "A Pharmacological Chaperone Molecule Induces Cancer Cell Death by Restoring Tertiary DNA Structures in Mutant hTERT Promoters." AMER CHEMICAL SOC, 2016. http://hdl.handle.net/10150/621444.

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Activation of human telomerase reverse transcriptase (hTERT) is necessary for limitless replication in tumorigenesis. Whereas hTERT is transcriptionally silenced in normal cells, most tumor cells reactivate hTERT expression by alleviating transcriptional repression through diverse genetic and epigenetic mechanisms. Transcription-activating hTERT promoter mutations have been found to occur at high frequencies in multiple cancer types. These mutations have been shown to form new transcription factor binding-sites that drive hTERT expression, but this model cannot fully account for differences in
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14

Hennessy, Fritha. "Characterisation of the J domain aminoacid residues important for the interaction of DNAJ-like proteins with HSP70 chaperones." Thesis, Rhodes University, 2004. http://hdl.handle.net/10962/d1003996.

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The 70 kDa heat shock proteins (Hsp70s) are vital for normal protein folding, as they stabilise the unfolded state of nascent polypeptides, allowing these sufficient time to attain a correct tertiary structure. Hsp70s are aided by the DnaJ-like family of proteins, which interact with Hsp70s in order to enhance the chaperone activity of these proteins. DnaJ-like proteins contain a J domain, a seventy amino acid domain consisting of four α-helices, which is defined by the presence of an invariant tripeptide of histidine, proline and aspartic acid (HPD motif). This motif is key to the interaction
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15

Rodrigues, Leonardo Augusto Zebral. "Análise da atividade do promotor de BiP (Binding Protein) de soja em plantas transgênicas de tabaco." Universidade Federal de Viçosa, 2005. http://www.locus.ufv.br/handle/123456789/10075.

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Submitted by Marco Antônio de Ramos Chagas (mchagas@ufv.br) on 2017-04-17T18:21:20Z No. of bitstreams: 1 texto completo.pdf: 2822554 bytes, checksum: 7bef13d6e29446a21866e18f47787668 (MD5)<br>Made available in DSpace on 2017-04-17T18:21:20Z (GMT). No. of bitstreams: 1 texto completo.pdf: 2822554 bytes, checksum: 7bef13d6e29446a21866e18f47787668 (MD5) Previous issue date: 2005-02-23<br>A proteína BiP ("binding protein") de plantas tem sido descrita como um importante mediador de translocação, dobramento e montagem de proteínas recém-sintetizadas no lúmem do retículo endoplasmático, exibin
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16

Tilitsky, Joseph. "How the E. Coli Hsp70 Molecular Chaperone, DnaK, Binds a Client Protein." 2017. https://scholarworks.umass.edu/masters_theses_2/588.

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Protein folding is essential for all cellular life. While some proteins are able to reach their folded state reliably using nothing but their amino acid sequence, a great number of essential proteins are unable to do so without the aid of molecular chaperones. One family of molecular chaperone, the Hsp70 family, is found in virtually all cell types and across all domains of life. Certain to the function of Hsp70s are how they bind their client proteins. Substantial effort has been expended to study how Hsp70s work on model peptides as a substrate mimic, but relatively little work has been perf
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17

Sivendran, Renuka. "Understanding the allosteric mechanism of the Escherichia coli Hsp70 molecular chaperone, DnaK." 2004. https://scholarworks.umass.edu/dissertations/AAI3152743.

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The Hsp70 family molecular chaperones prevent protein aggregation under heat shock conditions. They are highly conserved, and have a N-terminal ATPase domain, which binds and hydrolyzes ATP, and a C-terminal substrate-binding domain, which binds unfolded stretches of polypeptides. The communication between the two domains is vital for chaperone function. The nucleotide state regulates the substrate affinity, and substrate binding stimulates the ATP hydrolysis rate. Our study to understand this allosteric mechanism showed that the interdomain linker region is crucial for the stimulation of the
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18

"The requirement of J-domain structural rigidity for cochaperone-mediated allostery in the DnaJ-DnaK molecular chaperone machine." Tulane University, 2008.

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Functions of the Hsp40/DnaJ -- Hsp70/DnaK chaperone machine involve cyclic conformational changes in DnaK that are coupled to ATP hydrolysis in the ATPase domain of DnaK and stimulated by the J-domain of DnaJ. Experiments with recombinant forms of the DnaJ J-domain (Jd) and the DnaK ATPase domain (Kase) revealed that the Jd-Kase interaction involves more than mere binding. JdD35N, a variant with a D-to-N substitution in the conserved HPD tripeptide of Jd, had increased affinity for Kase but was unable to stimulate ATP hydrolysis in DnaK. NMR studies on Jd and JdD35N revealed increased bending
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19

Lin, Min Guan, and 林旻冠. "Critical residues of the molecular chaperone DnaK and the nucleotide exchange factor GrpE from Bacillus licheniformis ATCC 14580." Thesis, 2011. http://ndltd.ncl.edu.tw/handle/45568928937646451482.

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碩士<br>國立嘉義大學<br>生化科技學系研究所<br>99<br>Many molecular chaperones are heat-shock proteins (Hsp) and play an important role in the protection of the host cell against various stresses. DnaK system is a known for assisting protein folding and avoiding intracellular protein aggregation, it has two co-chaperones DnaJ and GrpE, they could accelerate the DnaK activity. In this study two researches are conducted to invesigate the effect of specific residues of DnaK and GrpE for structural and chaperone activity in Bacillus licheniformis ATCC 14580 heat shock protein 70 (BlDnaK) system. A DNA fragment enco
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20

Chen, Wei-Ling, and 陳韋伶. "The effect of post translational phosphorylation on molecular chaperone DnaK/ DnaJ/ GrpE ATPase activity and substrate protein refolding ability from Methanohalophilus portucalensis FDF1T." Thesis, 2018. http://ndltd.ncl.edu.tw/handle/ug9d57.

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碩士<br>國立中興大學<br>生命科學系所<br>106<br>Molecular chaperone plays an important role to assist folding and assembling of nascent polypeptides, preventing protein misfolding and aggregation which were dam-aged by temperature, pH and osmotic stresses. DnaK belong to heat shock protein 70 of molecular chaperone and cooperates with co-chaperone DnaJ and nucleotide exchange factor GrpE. ATP is required for DnaK to active and remodel their substrate client protein. The molecular chaperone DnaK system is highly conserved in Archaea, Bacteria and Eukarya. Genes related with molecular chaperone in halophilic m
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21

Smock, Robert G. "Components of a Protein Machine: Allosteric Domain Assembly and a Disordered C-terminus Enable the Chaperone Functions of Hsp70." 2011. https://scholarworks.umass.edu/open_access_dissertations/447.

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Hsp70 molecular chaperones protect proteins from aggregation, assist in their native structure formation, and regulate stress responses in the cell. A mechanistic understanding of Hsp70 function will be necessary to explain its physiological roles and guide the therapeutic modulation of various disease states. To this end, several fundamental features of the Hsp70 structure-function relationship are investigated. The central component of Hsp70 chaperone function is its capacity for allosteric signaling between structural domains and tunable binding of misfolded protein substrates. In order to
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22

Fang, Shih-Wen, and 方詩文. "Functional analyses of ATPase activity and substrate protein renaturation of molecular chaperones DnaK/DnaJ/GrpE from Methanohalophilus portucalensis FDF1T." Thesis, 2015. http://ndltd.ncl.edu.tw/handle/97636246211401844626.

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碩士<br>國立中興大學<br>生命科學系所<br>103<br>Molecular chaperone plays an important role to assist newly synthesized polypeptides folding, and protects cells from stress induced proteins misfolding and aggregation. Heat shock protein DnaK belongs to molecular chaperone and cooperates with co-chaperone DnaJ and nucleotide exchange factor GrpE. And ATP is required for DnaK to activate and remodel their substrate client proteins. The molecular chaperone system DnaK (Hsp70) system is highly conserved in sequence and distribution in Bacteria and Eukarya, however, DnaK is also found in mesophilic archaeon. The
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23

Hennessy, Fritha. "Characterisation of the J domain amino acid residues imporatant for the interactionof DNAJ-like proteins with HSP70 chaperones /." 2004. http://eprints.ru.ac.za/64/.

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24

Ma, Xiaojing 1982. "Studies on HIV-1 nucleocapsid chaperone role in protein/nucleic acid interactions by single molecule spectroscopy approaches." Thesis, 2009. http://hdl.handle.net/2152/ETD-UT-2009-12-557.

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HIV-NC is a multifunctional protein which plays an important role in almost every step of the retroviral life cycle. NC is essential in catalyzing stand transfers of HIV-1 reverse transcription, including the annealing of the transactivation response element (TAR) of the viral genome to the complementary TAR DNA in minus-strong-stop DNA. In this dissertation, the research starts with focus on elucidating the reaction mechanism of NC-facilitated TAR DNA/RNA annealing using single molecule spectroscopy (SMS) approaches. The results indicate that nucleation of TAR DNA/RNA annealing occurs in an
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25

Yong, ST, and XF Wang. "A novel, non-apoptotic role for Scythe/BAT3: a functional switch between the pro- and anti-proliferative roles of p21 during the cell cycle." Thesis, 2012. http://hdl.handle.net/10161/4958.

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BACKGROUND: Scythe/BAT3 is a member of the BAG protein family whose role in apoptosis has been extensively studied. However, since the developmental defects observed in Bat3-null mouse embryos cannot be explained solely by defects in apoptosis, we investigated whether BAT3 is also involved in cell-cycle progression. METHODS/PRINCIPAL FINDINGS: Using a stable-inducible Bat3-knockdown cellular system, we demonstrated that reduced BAT3 protein level causes a delay in both G1/S transition and G2/M progression. Concurrent with these changes in cell-cycle progression, we observed a reduction in the
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