Chaperonin 60
Mostrando 1-12 de 80 artigos, teses e dissertações.
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1. Hsp60 e imunorregulação: estratégias para identificação de peptídeos imunorreguladores / Hsp60 and immunorregulation: strategies for the identification of immunoregulatory peptides
As proteínas de choque térmico (Hsp) apresentam importantes funções homeostáticas e podem induzir respostas imunológicas tanto inflamatórias como reguladoras. Por essas propriedades, as Hsp e seus peptídeos têm grande potencial como agentes imunomoduladores. Neste estudo, o nosso objetivo foi identificar peptídeos da Hsp60 com potencial imunorregul
Publicado em: 2010
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2. Autorreatividade humoral a peptídeos da miosina cardíaca e proteína de choque térmico 60: estudo sequencial em pacientes transplantados cardíacos e indivíduos sadios / Humoral autoreactivity to peptides from cardiac myosin and heat shock protein 60: sequential study in heart transplanted patients and healthy subjects
The immune response directed to self antigens can contribute to the pathogenesis of autoimmune diseases. However, autoimmunity may also have an immunoregulatory role in allograft rejection and in other inflammatory processes. We analyzed IgG and IgM autoantibodies reactive to peptides from the human cardiac myosin (CM) and the heat shock protein 60 (Hsp60) i
Publicado em: 2009
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3. Brassica napus plastid and mitochondrial chaperonin-60 proteins contain multiple distinct polypeptides.
Plastid chaperonin-60 protein was purified to apparent homogeneity from Brassica napus using a novel protocol. The purified protein, which migrated as a single species by nondenaturing polyacrylamide gel electrophoresis, contained four polypeptides: three variants of p60cpn60 alpha and p60cpn60 beta. Partial amino acid sequence determination demonstrated tha
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4. Crystal Structure of the 65-Kilodalton Heat Shock Protein, Chaperonin 60.2, of Mycobacterium tuberculosis
Chaperonin 60s are a ubiquitous class of proteins that promote folding and assembly of other cellular polypeptides in an ATP-dependent manner. The oligomeric state of chaperonin 60s has been shown to be crucial to their role as molecular chaperones. Chaperonin 60s are also known to be important stimulators of the immune system. Mycobacterium tuberculosis pos
American Society for Microbiology.
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5. Hereditary Spastic Paraplegia SPG13 Is Associated with a Mutation in the Gene Encoding the Mitochondrial Chaperonin Hsp60
SPG13, an autosomal dominant form of pure hereditary spastic paraplegia, was recently mapped to chromosome 2q24-34 in a French family. Here we present genetic data indicating that SPG13 is associated with a mutation, in the gene encoding the human mitochondrial chaperonin Hsp60, that results in the V72I substitution. A complementation assay showed that wild-
The American Society of Human Genetics.
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6. Comparison of Ileum Microflora of Pigs Fed Corn-, Wheat-, or Barley-Based Diets by Chaperonin-60 Sequencing and Quantitative PCR
We have combined the culture-independent methods of high-throughput sequencing of chaperonin-60 PCR product libraries and quantitative PCR to profile and quantify the small-intestinal microflora of pigs fed diets based on corn, wheat, or barley. A total of 2,751 chaperonin-60 PCR product clones produced from samples of ileum digesta were examined. The majori
American Society for Microbiology.
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7. Mycobacterium tuberculosis Chaperonin 60.1 Is a More Potent Cytokine Stimulator than Chaperonin 60.2 (Hsp 65) and Contains a CD14-Binding Domain
Much attention has focused on the Mycobacterium tuberculosis molecular chaperone chaperonin (Cpn) 60.2 (Hsp 65) in the pathology of tuberculosis because of its immunogenicity and ability to directly activate human monocytes and vascular endothelial cells. However, M. tuberculosis is one of a small group of bacteria that contain multiple genes encoding Cpn 60
American Society for Microbiology.
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8. Streptococcus suis Serotypes Characterized by Analysis of Chaperonin 60 Gene Sequences
Streptococcus suis is an important pathogen of swine which occasionally infects humans as well. There are 35 serotypes known for this organism, and it would be desirable to develop rapid methods methods to identify and differentiate the strains of this species. To that effect, partial chaperonin 60 gene sequences were determined for the 35 serotype reference
American Society for Microbiology.
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9. Identification and functional analysis of chaperonin 10, the groES homolog from yeast mitochondria.
Chaperonin 60 (cpn60) and chaperonin 10 (cpn10) constitute the chaperonin system in prokaryotes, mitochondria, and chloroplasts. In Escherichia coli, these two chaperonins are also termed groEL and groES. We have used a functional assay to identify the groES homolog cpn10 in yeast mitochondria. When dimeric ribulose-1,5-bisphosphate carboxylase (Rubisco) is
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10. Identification of a groES-like chaperonin in mitochondria that facilitates protein folding.
Mitochondria contain a polypeptide that is functionally equivalent to Escherichia coli chaperonin 10 (cpn10; also known as groES). This mitochondrial cpn10 has been identified in beef and rat liver and is able to replace bacterial cpn10 in the chaperonin-dependent reconstitution of chemically denatured ribulose-1,5-bisphosphate carboxylase. Thus, like the ba
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11. Purification and characterization of chaperonins 60 and 10 from Methylobacillus glycogenes
Two proteins belonging to the group I chaperonin family were isolated from an obligate methanotroph, Methylobacillus glycogenes. The two proteins, one a GroEL homologue (cpn60: M. glycogenes 60 kDa chaperonin) and the other a GroES homologue (cpn10: M. glycogenes 10 kDa chaperonin), composed a heteropolymeric complex in the presence of ATP. Both proteins wer
Cell Stress Society International.
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12. cpnDB: A Chaperonin Sequence Database
Type I chaperonins are molecular chaperones present in virtually all bacteria, some archaea and the plastids and mitochondria of eukaryotes. Sequences of cpn60 genes, encoding 60-kDa chaperonin protein subunits (CPN60, also known as GroEL or HSP60), are useful for phylogenetic studies and as targets for detection and identification of organisms. Conveniently
Cold Spring Harbor Laboratory Press.