Groes
Mostrando 1-12 de 131 artigos, teses e dissertações.
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1. Exploração ou gratidão? Patronagem íntima e a gramática moral das trocas sexuais econômicas entre jovens curtidoras e europeus mais velhos, expatriados, em Maputo – Moçambique
Resumo Neste artigo exploro uma categoria particular de mulheres inserida em sistemas de intercâmbio locais assim como na paisagem urbana transnacional de trocas íntimas. As curtidoras em Maputo mostram o poder do erotismo feminino e como ele se conecta com o parentesco, as dinâmicas de gênero e as moralidades de intercâmbio. Baseando-me na produção f
Cad. Pagu. Publicado em: 22/08/2016
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2. Increased expression and purification of soluble iron-regulatory protein 1 from Escherichia coli co-expressing chaperonins GroES and GroEL
Iron is an essential metal for all living organisms. However, iron homeostasis needs to be tightly controlled since iron can mediate the production of reactive oxygen species, which can damage cell components and compromise the integrity and/or cause DNA mutations, ultimately leading to cancer. In eukaryotes, iron-regulatory protein 1 (IRP1) plays a central
Brazilian Journal of Medical and Biological Research. Publicado em: 14/02/2008
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3. Zoneamento bioclimático da ovinocultura no Estado do Paraná
Utilizaram-se 45 fêmeas ovinas adultas (15 Hampshire Down [HD], 15 Texel [TE] e 15 Ile de France [IF]), para propor um zoneamento bioclimático da ovinocultura no Estado do Paraná. Mediram-se a temperatura retal (Tr), da epiderme (Te), do interior do velo (Tiv) e da superfície do velo (Tsv); a frequência respiratória (Fr); a temperatura do ar (Ta), pres
Revista Brasileira de Zootecnia. Publicado em: 2001-04
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4. Cell cycle expression of the heat shock groESL operon in Caulobacter crescentus / Expressão do operon de choque térmico groESL durante o ciclo celular de Caulobacter crescentus
Caulobacter crescentus is an aquatic free-living Gram-negative bacterium whose cell cycle depends on cell differentiation. The asymmetrical predivisional cell gives rise to two morphologically and functionally different daughter cells: the swarmer cell an the stalked cell. The expression of the groESL operon is induced by heat shock and is cell cycle control
Publicado em: 1999
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5. Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity.
The mechanism of GroEL (chaperonin)-mediated protein folding is only partially understood. We have analysed structural and functional properties of the interaction between GroEL and the co-chaperonin GroES. The stoichiometry of the GroEL 14mer and the GroES 7mer in the functional holo-chaperonin is 1:1. GroES protects half of the GroEL subunits from proteoly
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6. GroES in the asymmetric GroEL14–GroES7 complex exchanges via an associative mechanism
The interaction of the chaperonin GroEL14 with its cochaperonin GroES7 is dynamic, involving stable, asymmetric 1:1 complexes (GroES7⋅GroEL7–GroEL7) and transient, metastable symmetric 2:1 complexes [GroES7⋅GroEL7–GroEL7⋅GroES7]. The transient formation of a 2:1 complex permits exchange of free GroES7 for GroES7 bound in the stable 1:1 complex. Ele
The National Academy of Sciences.
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7. Characterization of the groEL and groES Loci in Bifidobacterium breve UCC 2003: Genetic, Transcriptional, and Phylogenetic Analyses
The bacterial heat shock response is characterized by the elevated expression of a number of chaperone complexes, including the GroEL and GroES proteins. The groES and groEL genes are highly conserved among eubacteria and are typically arranged as an operon. Genome analysis of Bifidobacterium breve UCC 2003 revealed that the groES and groEL genes are located
American Society for Microbiology.
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8. Identification of Clinically Relevant Enterococcus Species by Direct Sequencing of groES and Spacer Region
We determined the groESL sequences (groES, groEL, and the intergenic spacer) of 10 clinically relevant Enterococcus species and evaluated the feasibility of identifying Enterococcus species on the basis of these sequences. Seven common clinical Enterococcus species, E. faecalis, E. faecium, E. casseliflavus, E. gallinarum, E. avium, E. raffinosus, and E. hir
American Society for Microbiology.
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9. Two classes of extragenic suppressor mutations identify functionally distinct regions of the GroEL chaperone of Escherichia coli.
The GroES and GroEL proteins of Escherichia coli function together as the GroE molecular chaperone machine to (i) prevent denaturation and aggregation and (ii) assist the folding and oligomerization of other proteins without being part of the final structure. Previous genetic and biochemical analyses have determined that this activity requires interactions o
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10. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.
As a basic principle, assisted protein folding by GroEL has been proposed to involve the disruption of misfolded protein structures through ATP hydrolysis and interaction with the cofactor GroES. Here, we describe chaperonin subreactions that prompt a re-examination of this view. We find that GroEL-bound substrate polypeptide can induce GroES cycling on and
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11. Differential T-Cell Recognition of Native and Recombinant Mycobacterium tuberculosis GroES
Mycobacterium tuberculosis GroES was purified from culture filtrate, and its identity was confirmed by immunoblot analysis and N-terminal sequencing. Comparing the immunological recognition of native and recombinant GroES, we found that whereas native GroES elicited a strong proliferative response and release of gamma interferon-γ by peripheral blood mononu
American Society for Microbiology.
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12. Bacteriophage-encoded cochaperonins can substitute for Escherichia coli’s essential GroES protein
The Escherichia coli chaperonin machine is composed of two members, GroEL and GroES. The GroEL chaperonin can bind 10–15% of E. coli’s unfolded proteins in one of its central cavities and help them fold in cooperation with the GroES cochaperonin. Both proteins are absolutely essential for bacterial growth. Several large, lytic bacteriophages, such as T4
Oxford University Press.