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Dissertations / Theses on the topic 'GRPEL1'

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Published: 4 June 2021

Last updated: 4 February 2022

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1

Yan, Junxia. "Combined linkage analysis and exome sequencing identifies novel genes for familial goiter." Kyoto University, 2014. http://hdl.handle.net/2433/188654.

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2

Hage, Aziz El. "Protéines chaperons intervenant dans l'assemblage des ribosomes chez Escherichia coli." Paris 7, 2004. http://www.theses.fr/2004PA077059.

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3

Linke, Katrin. "Characterization of the DnaK-DnaJ-GrpE system under oxidative heat stress." [S.l.] : [s.n.], 2005. http://deposit.ddb.de/cgi-bin/dokserv?idn=974431346.

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4

Emond, Audrey. "Étude du rôle du general receptor for phosphoinositides 1 (GRP1) dans l'adipogenèse." Mémoire, Université de Sherbrooke, 2011. http://savoirs.usherbrooke.ca/handle/11143/4075.

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Many studies have shown that peroxisome-proliferator-activated receptor [gamma] (PPAR[gamma]) plays an important role in adipose tissue formation by activating genes implicated in adipogenesis. PPAR[gamma] heterodimerizes with retinoid X receptor [alpha] (RXR[alpha]), in the presence of ligand, on PPAR response elements (PPREs) in the promoter of target genes involved in adipocyte differentiation. General receptor for phosphoinositides 1 (GRP1) is a corepressor of thyroid hormone receptors (TRs), a nuclear receptor like PPAR[gamma]. GRP1 decreases TRs' transcriptional activity by lowering dime

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5

Cronin, Thomas Charles. "Structural Determinants of Phosphoinositide Recognition by Grp1 Family Pleckstrin Homology Domains: a Dissertation." eScholarship@UMMS, 2005. http://escholarship.umassmed.edu/gsbs_diss/165.

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Pleckstrin homology (PH) domains, which play an essential role in membrane trafficking and signal transduction, recognize phosphoinositides with a diverse range of affinities and specificities. The PH domains of the Grp1 family of Arf GTPase exchange factors recognize a select group of phosphoinositides with dramatic differences in specificity, despite 90% sequence identity. The work described in this thesis has focused on the structural basis for these differences. The structure of the Grp1 PH domain revealed structural determinants for phosphoinositide recognition. Through a wide range of cr

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6

Naylor, Dean Jason. "The Mammalian mitochondrial Hsp70 chaperone system, new GrpE-like members and novel organellar substrates." Title page, contents and summary only, 1999. http://web4.library.adelaide.edu.au/theses/09PH/09phn331.pdf.

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Bibliography: leaves 104-136. The DnaK (Hsp70), DnaJ and GrpE heat shock proteins of Escherichia coli work synergistically in a diverse number of vital cellular processes including the folding of nascent polypeptides, assembly and disassembly of multimeric proteins, refolding of malfolded proteins, degredation of unstable and non-native polypeptides, regulation of the stress response and the mediation of protein translocation across membranes. In this study Dna-K-affinity purification was employed to identify a mammalian mitrochondrial GrpE homologue (mt-GrpE#1) for the first time. The results

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7

Barthel, Sandra [Verfasser]. "Physiologische Veränderungen bei der Thylakoidmembranbiogenese und die Funktionsweise des Nukleotidaustauschfaktors GrpE in Cyanobakterien / Sandra Barthel." Mainz : Universitätsbibliothek Mainz, 2011. http://d-nb.info/1031783741/34.

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8

DE, CROUY CHANEL AXELLE. "Interaction entre les machines chaperons dnak/dnaj/grpe et groel/groes et leurs proteines substrats." Paris 7, 1997. http://www.theses.fr/1997PA077103.

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Les molecules chaperons forment une classe de proteine qui fixent selectivement les polypeptides naissants, non replies, mal replies, ou agreges, en reconnaissant des regions hydrophobes exposees par les proteines depliees. Cette propriete est la base de l'implication des machines chaperons (dnak/dnaj/grpe) et (groel/groes) dans des processus cellulaires tels que le repliement, l'adressage, la renaturation des proteines, et le controle des interactions proteine-proteine. Les chaperons fonctionnent en collaboration avec leur cochaperon. Nous avons etudie l'interaction entre les machines chapero

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9

Sand, Olivier. "Rôle des protéines de choc thermique DnaK, DnaJ et GrpE dans la transcription tardive du bactériophage Mu." Doctoral thesis, Universite Libre de Bruxelles, 1995. http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/212581.

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10

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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11

Kuschel, Margret. "Funktionelle Analyse von Proteinen der Gpr1/Fun34/yaaH-Proteinfamilie in den Hefen Yarrowia lipolytica und Saccharomyces cerevisiae." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2006. http://nbn-resolving.de/urn:nbn:de:swb:14-1141977427706-70045.

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Trans-dominante Mutationen im GPR1-Gen der Hefe Yarrowia lipolytica führen zur Sensitivität der Hefezellen gegenüber Essigsäure. Die Deletion dieses Genes hat dem gegenüber keinen Effekt auf den Phänotyp. In dieser Arbeit wurde das Gpr1-Protein aus Y. lipolytica und dessen Orthologe Ycr010cp, Ydr384cp und Ynr002cp von S. cerevisiae weiter charakterisiert. S. cerevisiae-Transformanden, welche die Mutantenallele GPR1-1 bzw. GPR1-2 exprimierten, zeigten bei gleichzeitiger Anwesenheit von Glucose eine erhöhte Sensitivität gegenüber Essigsäure. Mittels Ort-spezifischer und zufälliger Mutagenese kon

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12

Kuschel, Margret. "Funktionelle Analyse von Proteinen der Gpr1/Fun34/yaaH-Proteinfamilie in den Hefen Yarrowia lipolytica und Saccharomyces cerevisiae." Doctoral thesis, Technische Universität Dresden, 2005. https://tud.qucosa.de/id/qucosa%3A24677.

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Trans-dominante Mutationen im GPR1-Gen der Hefe Yarrowia lipolytica führen zur Sensitivität der Hefezellen gegenüber Essigsäure. Die Deletion dieses Genes hat dem gegenüber keinen Effekt auf den Phänotyp. In dieser Arbeit wurde das Gpr1-Protein aus Y. lipolytica und dessen Orthologe Ycr010cp, Ydr384cp und Ynr002cp von S. cerevisiae weiter charakterisiert. S. cerevisiae-Transformanden, welche die Mutantenallele GPR1-1 bzw. GPR1-2 exprimierten, zeigten bei gleichzeitiger Anwesenheit von Glucose eine erhöhte Sensitivität gegenüber Essigsäure. Mittels Ort-spezifischer und zufälliger Mutagenese kon

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13

Linke, Katrin [Verfasser]. "Characterization of the DnaK-DnaJ-GrpE system under oxidative heat stress / Katrin Linke." 2005. http://d-nb.info/974431346/34.

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14

Wu, Chih-Chuang, and 吳至忠. "Crystallographic Studies of the Hsp70 Chaperone System: Insight into the DnaK and GrpE Intermolecular Interaction." Thesis, 2012. http://ndltd.ncl.edu.tw/handle/34843853763337046286.

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博士<br>國立陽明大學<br>生化暨分子生物研究所<br>100<br>Crystallographic Studies of the Hsp70 Chaperone System: Insight into the DnaK and GrpE Intermolecular Interaction Abstract The 70-kDa heat shock proteins (Hsp70s) are highly conserved molecular chaperones composed of an N-terminal nucleotide binding domain (NBD) and a C-terminal substrate binding domain (SBD) in a bilobate mode. In prokaryotic cell,The conserved, ATP-dependent bacterial DnaK chaperones (Hsp70 homologous)process client substrates with the aid of the co-chaperones DnaJ and GrpE, this DnaK chaperone machine is usually termed DnaK chaperone cy

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15

Laloraya, Shikha. "A eukaryotic GrpE related protein, Mgelp, modulates the function of mitochondrial Hsp70 in translocation of mitochondrial preproteins." 1996. http://catalog.hathitrust.org/api/volumes/oclc/34990513.html.

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16

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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17

Chen, Shih-Shan, and 陳仕珊. "Cloning, Gene Expression, and Functional Characterization of Heat Shock Protein DnaK, DnaJ, and GrpE in Methanohalophilis portucalensis FDF1T." Thesis, 2012. http://ndltd.ncl.edu.tw/handle/91744110930687703344.

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碩士<br>國立中興大學<br>生命科學系所<br>100<br>Cellular protein loses their function and structure when encountering the abiotic stress. Heat shock protein DnaK belongs to molecular chaperone and cooperates with its co-chaperone DnaJ and nucleotide exchanger GrpE. DnaK system also co-operate with these two molecular chaperone, chaperonin GroEL/GroES and ClpB belongs to the members of AAA+ protein superfamily. These three systems constitute the ATP-dependent folding function of both nascent polypeptides as well as the salvage of stress-denatured proteins. DnaK system is highly conserved and ubiquitous in euk

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18

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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19

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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