Co Chaperones
Mostrando 13-24 de 47 artigos, teses e dissertações.
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13. Estudos estruturais do sistema chaperone molecular HSP70 humano
A função de uma proteína depende da estrutura nativa obtida a partir de sua estrutura primária de aminoácidos por um processo denominado de enovelamento protéico. Falhas neste processo podem levar à formação de agregados protéicos que têm relação com doenças humanas; como as doenças amilóides. Durante a evolução, as células têm desenvolvi
Publicado em: 2004
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14. Molecular chaperone genes in the sugarcane expressed sequence database (SUCEST)
Algumas proteínas ao serem sintetizadas necessitam do auxílio de chaperones moleculares para seu correto enovelamento. Chaperones também estão envolvidas na dissolução de agregados protéicos, fazendo com que seu estudo seja de relevância biotecnológica e médica. Portanto, a identificação de seqüências de chaperones moleculares é uma tarefa imp
Genetics and Molecular Biology. Publicado em: 2001-12
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15. Comparison of the carboxy-terminal DP-repeat region in the co-chaperones Hop and Hip
Functional steroid receptor complexes are assembled and maintained by an ordered pathway of interactions involving multiple components of the cellular chaperone machinery. Two of these components, Hop and Hip, serve as co-chaperones to the major heat shock proteins (Hsps), Hsp70 and Hsp90, and participate in intermediate stages of receptor assembly. In an ef
Cell Stress Society International.
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16. A novel type of co-chaperone mediates transmembrane recruitment of DnaK-like chaperones to ribosomes
Recently, the homolog of yeast protein Sec63p was identified in dog pancreas microsomes. This pancreatic DnaJ-like protein was shown to be an abundant protein, interacting with both the Sec61p complex and lumenal DnaK-like proteins, such as BiP. The pancreatic endoplasmic reticulum contains a second DnaJ-like membrane protein, which had been termed Mtj1p in
Oxford University Press.
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17. The Unique Chaperone Operon of Thermotoga maritima: Cloning and Initial Characterization of a Functional Hsp70 and Small Heat Shock Protein
The hyperthermophilic eubacterium Thermotoga maritima possesses an operon encoding an Hsp70 molecular chaperone protein and a protein with meaningful homology to the small heat shock protein family of chaperones. This represents the first demonstrated co-operon organization for these two important classes of molecular chaperones. We have cloned and initially
American Society for Microbiology.
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18. Tic40, a membrane-anchored co-chaperone homolog in the chloroplast protein translocon
The function of Tic40 during chloroplast protein import was investigated. Tic40 is an inner envelope membrane protein with a large hydrophilic domain located in the stroma. Arabidopsis null mutants of the atTic40 gene were very pale green and grew slowly but were not seedling lethal. Isolated mutant chloroplasts imported precursor proteins at a lower rate th
Oxford University Press.
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19. TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes
The role in protein folding of the eukaryotic chaperonin TRiC/CCT is only partially understood. Here, we show that a group of WD40 β-propeller proteins in the yeast cytosol interact transiently with TRiC upon synthesis and require the chaperonin to reach their native state. TRiC cooperates in the folding of these proteins with the ribosome-associated heat s
Oxford University Press.
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20. SecB is a bona fide generalized chaperone in Escherichia coli
It is known that the DnaK and Trigger Factor (TF) chaperones cooperate in the folding of newly synthesized cytosolic proteins in Escherichia coli. We recently showed that despite a very narrow temperature range of growth and high levels of aggregated cytosolic proteins, E. coli can tolerate deletion of both chaperones, suggesting that other chaperones might
National Academy of Sciences.
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21. Chaperone action in the posttranslational topological reorientation of the hepatitis B virus large envelope protein: Implications for translocational regulation
The large L envelope protein of the hepatitis B virus utilizes a new folding pathway to acquire a dual transmembrane topology in the endoplasmic reticulum (ER). The process involves cotranslational membrane integration and subsequent posttranslational translocation of its preS subdomain into the ER. Here, we demonstrate that the conformational and functional
The National Academy of Sciences.
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22. CHIP activates HSF1 and confers protection against apoptosis and cellular stress
Induction of molecular chaperones is the characteristic protective response to environmental stress, and is regulated by a transcriptional program that depends on heat shock factor 1 (HSF1), which is normally under negative regulatory control by molecular chaperones Hsp70 and Hsp90. In metazoan species, the chaperone system also provides protection against
Oxford University Press.
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23. Purification and characterization of recombinant human p50csk protein-tyrosine kinase from an Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL.
An Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL was engineered and has been successfully used to produce large quantities of the recombinant human protein-tyrosine kinase p50csk. The co-overproduction of the two chaperones with p50csk results in increased solubility of the kinase and allows purification of milligr
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24. The Hsp90-binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo
Hsp90 is required for the normal activity of steroid receptors, and in steroid receptor complexes it is typically bound to one of the immunophilin-related co-chaperones: the peptidylprolyl isomerases FKBP51, FKBP52 or CyP40, or the protein phosphatase PP5. The physiological roles of the immunophilins in regulating steroid receptor function have not been well
Oxford University Press.