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Registro Completo |
Biblioteca(s): |
Ebooks. |
Data corrente: |
01/02/2013 |
Data da última atualização: |
01/02/2013 |
Autoria: |
POCKLEY, A. G.; CALDERWOOD, S. K.; SANTORO, M. G. |
Afiliação: |
A. Graham Pockley; Stuart K. Calderwood; M. Gabriella Santoro. |
Título: |
Prokaryotic and Eukaryotic Heat Shock Proteins in Infectious Disease. |
Ano de publicação: |
2010 |
Fonte/Imprenta: |
Springer eBooks. |
Volume: |
4 |
Páginas: |
XI, 311 p. |
Descrição Física: |
digital. |
Série: |
Heat Shock Proteins, |
ISBN: |
9789048129768 |
DOI: |
10.1007/978-90-481-2976-8 |
Idioma: |
Inglês |
Conteúdo: |
Prokaryotic and Eukaryotic Heat Shock Proteins in Infectious Disease provides the most current review of the literature relating to the role and influence of heat shock (stress) proteins on the establishment, progression and resolution of infectious disease. Written by leaders in the field of heat shock proteins (HSP) and their biological and immunological properties, the contributors provide a fascinating insight into the complex relationship between, and the involvement of prokaryotic and eukaryotic HSP in disease states. It has been known for some considerable time that heat shock proteins from prokaryotic organisms are immunodominant molecules that are intimately involved in the induction of potential protective inflammatory responses, and this aspect of HSP biology is updated herein. In addition to regulating heat shock protein gene expression, the transcription factor HSF1 also appears to play an important role in regulating immune responses to infection. Heat shock proteins are now known to influence infectious disease processes in a number of diverse ways: they are involved in the propagation of prions, the replication and morphogenesis of viruses, and the resistance of parasites to chemotherapy. These proteins also appear to be important mediators of bacteria-host interactions and inflammation, the latter via interactions with cell surface molecules and structures such as Toll-like receptors and lipid rafts. Heat shock proteins can be expressed on the surface of infected cells, and this is likely to provide a target for the innate immune response. Elevated levels of circulating HSP are present in infectious diseases and these proteins might therefore regulate inflammatory responses to pathogenic challenge on a systemic basis. Heat shock proteins are also implicated in the impact of genital tract infections on the reproductive outcome, as well as in the local and systemic consequences of periodontal disease. Fever-range temperatures can induce the expression of heat shock proteins, and the final chapter in the book examines the influence of fever-range hyperthermia on a variety of cells and the organization of plasma membranes. This book is an essential read for graduates and postgraduates in Biology, pro- and eukaryotic Biochemistry, Immunology, Microbiology, Inflammatory and Infectious Disease, and Pathology. Menos Prokaryotic and Eukaryotic Heat Shock Proteins in Infectious Disease provides the most current review of the literature relating to the role and influence of heat shock (stress) proteins on the establishment, progression and resolution of infectious disease. Written by leaders in the field of heat shock proteins (HSP) and their biological and immunological properties, the contributors provide a fascinating insight into the complex relationship between, and the involvement of prokaryotic and eukaryotic HSP in disease states. It has been known for some considerable time that heat shock proteins from prokaryotic organisms are immunodominant molecules that are intimately involved in the induction of potential protective inflammatory responses, and this aspect of HSP biology is updated herein. In addition to regulating heat shock protein gene expression, the transcription factor HSF1 also appears to play an important role in regulating immune responses to infection. Heat shock proteins are now known to influence infectious disease processes in a number of diverse ways: they are involved in the propagation of prions, the replication and morphogenesis of viruses, and the resistance of parasites to chemotherapy. These proteins also appear to be important mediators of bacteria-host interactions and inflammation, the latter via interactions with cell surface molecules and structures such as Toll-like receptors and lipid rafts. Heat shock proteins can be expressed on the sur... Mostrar Tudo |
Palavras-Chave: |
Biomedicine; Biomedicine general. |
Thesaurus Nal: |
medicine. |
Categoria do assunto: |
-- |
URL: |
https://dx.doi.org/10.1007/978-90-481-2976-8
|
Marc: |
LEADER 03035nam a2200217 a 4500 001 1947841 005 2013-02-01 008 2010 bl uuuu u0uu1 u #d 020 $a9789048129768 024 7 $a10.1007/978-90-481-2976-8$2DOI 100 1 $aPOCKLEY, A. G. 245 $aProkaryotic and Eukaryotic Heat Shock Proteins in Infectious Disease.$h[electronic resource] 260 $aSpringer eBooks.$c2010 300 $aXI, 311 p. 4$cdigital. 490 $aHeat Shock Proteins,$v4 520 $a<P></P> <P>Prokaryotic and Eukaryotic Heat Shock Proteins in Infectious Disease provides the most current review of the literature relating to the role and influence of heat shock (stress) proteins on the establishment, progression and resolution of infectious disease. Written by leaders in the field of heat shock proteins (HSP) and their biological and immunological properties, the contributors provide a fascinating insight into the complex relationship between, and the involvement of prokaryotic and eukaryotic HSP in disease states. It has been known for some considerable time that heat shock proteins from prokaryotic organisms are immunodominant molecules that are intimately involved in the induction of potential protective inflammatory responses, and this aspect of HSP biology is updated herein. In addition to regulating heat shock protein gene expression, the transcription factor HSF1 also appears to play an important role in regulating immune responses to infection. Heat shock proteins are now known to influence infectious disease processes in a number of diverse ways: they are involved in the propagation of prions, the replication and morphogenesis of viruses, and the resistance of parasites to chemotherapy. These proteins also appear to be important mediators of bacteria-host interactions and inflammation, the latter via interactions with cell surface molecules and structures such as Toll-like receptors and lipid rafts. Heat shock proteins can be expressed on the surface of infected cells, and this is likely to provide a target for the innate immune response. Elevated levels of circulating HSP are present in infectious diseases and these proteins might therefore regulate inflammatory responses to pathogenic challenge on a systemic basis. Heat shock proteins are also implicated in the impact of genital tract infections on the reproductive outcome, as well as in the local and systemic consequences of periodontal disease. Fever-range temperatures can induce the expression of heat shock proteins, and the final chapter in the book examines the influence of fever-range hyperthermia on a variety of cells and the organization of plasma membranes. This book is an essential read for graduates and postgraduates in Biology, pro- and eukaryotic Biochemistry, Immunology, Microbiology, Inflammatory and Infectious Disease, and Pathology.</P> <P></P> 650 $amedicine 653 $aBiomedicine 653 $aBiomedicine general 700 1 $aCALDERWOOD, S. K. 700 1 $aSANTORO, M. G.
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4. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | RIBEIRO, C.; FALCAO, P. R. K.; NESHICH, G.; SANTORO, M. Serine proteases analysis based on phylogenetic trees constructed from the sequence and structure alignments. In: ANNUAL INTERNATIONAL CONFERENCE ON INTELLIGENT SYSTEMS FOR MOLECULAR BIOLOGY, 14.; ANNUAL AB3C CONFERENCE, 2., 2006, Fortaleza. Conference Program... Fortaleza: ISCB, 2006. Não paginado. ISMB, X-MEETING 2006. Poster I-48. Na publicação: Paula Kuser.Tipo: Resumo em Anais de Congresso |
Biblioteca(s): Embrapa Agricultura Digital. |
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5. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | MELO, R. C.; MAZONI, I.; NESHICH, G.; SANTORO, M. M.; MEIRA JÚNIOR, W. Contacts as the key elements for comparing two protein structures. In: ANNUAL INTERNATIONAL CONFERENCE ON INTELLIGENT SYSTEMS FOR MOLECULAR BIOLOGY, 14.; ANNUAL AB3C CONFERENCE, 2., 2006, Fortaleza. Conference Program... Fortaleza: ISCB, 2006. Não paginado. ISMB, X-MEETING 2006. Poster I-6.Tipo: Resumo em Anais de Congresso |
Biblioteca(s): Embrapa Agricultura Digital. |
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Biblioteca(s): Embrapa Agricultura Digital. |
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Biblioteca(s): Embrapa Agricultura Digital. |
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Biblioteca(s): Embrapa Agricultura Digital. |
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11. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | VIANA, P. A.; REZENDE, S. T. de; ALVES, A. de A.; MANFRINI, R. M.; ALVES, R. J.; BEMQUERER, M. P.; SANTORO, M. M.; GUIMARÃES, V. M. Activity of Debaryomyces hansenii UFV-1 alfa-galactosidades against alfa-D-galactophyranoside derivatives. Carbohydrate Research, v. 346, p. 602-605, 2011.Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 1 |
Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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12. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | LIMA, F. L.; CARVALHO, M. A. R. de; APOLÔNIO, A. C. M.; BEMQUERER, M. P.; SANTORO, M. M.; OLIVEIRA, J. S.; ALVIANO, C. S.; FARIAS, L. de M. Actinomycetemcomitin: a new bacteriocin produced by Aggregatibacter (Actinobacillus) actinomycetemcomitans. Journal of Industrial Microbiology and Biotechnology, v. 35, p. 103-110, 2008.Tipo: Artigo em Periódico Indexado | Circulação/Nível: Internacional - A |
Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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13. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | LIMA, F. L.; CARVALHO, M. A. R.; SANTORO, M. M.; BEMQUERER, M. P.; OLIVEIRA, J. S.; APOLÔNIO, A. C. M.; ALVIANO, C. S.; FARIAS, L. M. Actinomycetemcomitin: a new bacteriocin produced by Aggregatibacter (Actinobacillus) Actinomycetemcomitans. In: ANNUAL MEETING OF THE SBBq, 36.; IUBMB CONFERENCE, 10., 2007, Salvador, BA. Infectious diseases: biochemistry of parasites, vectors and hosts: program and abstracts. São Paulo, SP: Brazilian Society for Biochemistry and Molecular Biology, 2007.Tipo: Resumo em Anais de Congresso |
Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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14. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | MELO, R. C.; RIBEIRO, C.; MURRAY, C. S.; VELOSO, C. J. M.; SILVEIRA, C. H. da; NESHICH, G.; MEIRA JUNIOR, W.; CARCERONI, R. L.; SANTORO, M. M. Finding protein-protein interaction patterns by contact map matching. Genetics and Molecular Research, v. 6, n. 4, p. 946-963, 2007.Tipo: Artigo em Periódico Indexado | Circulação/Nível: Internacional - A |
Biblioteca(s): Embrapa Agricultura Digital. |
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Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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