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    <title>Cell Stress &amp; Chaperones : PubMed Central (PMC3 - NLM DTD)</title>
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    <description>Mostrando recursos 1 - 20 de 951</description>
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    <title>Universia-Recursos de Aprendizaje</title>
    <url>http://biblioteca.universia.net/img/logotipo.jpg</url>
    <link>http://biblioteca.universia.net/</link>
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  <item rdf:about="http://biblioteca.universia.net/ficha.do?id=9142053">
    <title>Antibodies against heat shock proteins in environmental stresses and diseases: friend or foe?</title>
    <link>http://biblioteca.universia.net/ficha.do?id=9142053</link>
    <description>Heat shock proteins (Hsps) can be found in two forms, intracellular and extracellular. The intracellular Hsps are induced as a result of stress and have been found to be cytoprotective in many instances due to their chaperone functions in protein folding and in protein degradation. The origin and role of extracellular Hsps is less clear. Although they were suspected originally to be released from damaged cells (necrosis), their presence in most normal individuals rather suggests that they hav...</description>
    <dc:creator>Wu, Tangchun; Tanguay, Robert M.</dc:creator>
  </item>
  <item rdf:about="http://biblioteca.universia.net/ficha.do?id=9142054">
    <title>Birth defects and antiheat shock protein 70 antibodies in early pregnancy</title>
    <link>http://biblioteca.universia.net/ficha.do?id=9142054</link>
    <description>It has been suggested that induction of the heat shock response in the mammalian embryo during the critical period of organogenesis can result in anatomical malformation. We measured serum heat shock protein 70 (Hsp70), anti-Hsp70, and anti-Hsp60 in samples taken from expectant mothers at 16 weeks gestation. Samples from women whose babies were born with a birth defect (n = 30) were compared with controls who gave birth to healthy babies (n = 46). Anti-Hsp70 levels were significantly elevated...</description>
    <dc:creator>Child, David F.; Hudson, Peter R.; Hunter-Lavin, Claire; Mukhergee, Sagarika; China, Susnata; Williams, Clive P.; Williams, John H. H.</dc:creator>
  </item>
  <item rdf:about="http://biblioteca.universia.net/ficha.do?id=9142055">
    <title>Toxoplasma gondiiderived heat shock protein 70 stimulates maturation of murine bone marrowderiv...</title>
    <link>http://biblioteca.universia.net/ficha.do?id=9142055</link>
    <description>Toxoplasma gondii?derived heat shock protein 70 (T.g.HSP70) induced maturation of bone marrowderived dendritic cells (DCs) of wild-type (WT) C57BL/6 mice as evidenced by an increase in surface expression of MHC class I and II molecules and costimulatory molecules such as CD40, CD80, and CD86. Functionally, decreased phagocytic ability and increased alloreactive T cell stimulatory ability were observed in T.g.HSP70-stimulated DCs. These phenotypic and functional changes of T.g.HSP70-stimulat...</description>
    <dc:creator>Aosai, Fumie; Rodriguez Pena, Martha S.; Mun, Hye-Seong; Fang, Hao; Mitsunaga, Tetsuya; Norose, Kazumi; Kang, Hyun Kyu; Bae, Yoe-Sik; Yano, Akihiko</dc:creator>
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  <item rdf:about="http://biblioteca.universia.net/ficha.do?id=9142056">
    <title>A genomewide analysis of genes for the heat shock protein 70 chaperone system in the ascidian Cio...</title>
    <link>http://biblioteca.universia.net/ficha.do?id=9142056</link>
    <description>Molecular chaperones play crucial roles in various aspects of the biogenesis and maintenance of proteins in the cell. The heat shock protein 70 (HSP70) chaperone system, in which HSP70 proteins act as chaperones, is one of the major molecular chaperone systems conserved among a variety of organisms. To shed light on the evolutionary history of the constituents of the chordate HSP70 chaperone system and to identify all of the components of the HSP70 chaperone system in ascidians, we carried ou...</description>
    <dc:creator>Wada, Shuichi; Hamada, Mayuko; Satoh, Nori</dc:creator>
  </item>
  <item rdf:about="http://biblioteca.universia.net/ficha.do?id=9142057">
    <title>Heat shock protein 70 binds its own messenger ribonucleic acid as part of a gene expression self-...</title>
    <link>http://biblioteca.universia.net/ficha.do?id=9142057</link>
    <description>Expression of heat shock proteins is a cellular response to a variety of stressors. HSP70, the major stress-induced heat shock protein, is involved in repair and protection after the insult. However, the prolonged presence of this protein is detrimental. Consequently, Hsp70 expression must be tightly regulated. We have previously shown an increase in the degradation of Hsp70 messenger ribonucleic acid (mRNA) paralleling the accumulation of HSP70. Incubation of cells with transcriptional and t...</description>
    <dc:creator>Balakrishnan, Karthik; De Maio, Antonio</dc:creator>
  </item>
  <item rdf:about="http://biblioteca.universia.net/ficha.do?id=9142058">
    <title>Differences in the chaperone-like activities of the four main small heat shock proteins of Drosop...</title>
    <link>http://biblioteca.universia.net/ficha.do?id=9142058</link>
    <description>The Drosophila melanogaster family of small heat shock proteins (sHsps) is composed of 4 main members (Hsp22, Hsp23, Hsp26, and Hsp27) that display distinct intracellular localization and specific developmental patterns of expression in the absence of stress. In an attempt to determine their function, we have examined whether these 4 proteins have chaperone-like activity using various chaperone assays. Heat-induced aggregation of citrate synthase was decreased from 100 to 17 arbitrary units i...</description>
    <dc:creator>Morrow, Geneviève; Heikkila, John J.; Tanguay, Robert M.</dc:creator>
  </item>
  <item rdf:about="http://biblioteca.universia.net/ficha.do?id=9142059">
    <title>Inhibition of apoptosis by p26: implications for small heat shock protein function during Artemia...</title>
    <link>http://biblioteca.universia.net/ficha.do?id=9142059</link>
    <description>p26, an abundantly expressed small heat shock protein, is thought to establish stress resistance in oviparously developing embryos of the crustacean Artemia franciscana by preventing irreversible protein denaturation, but it might also promote survival by inhibiting apoptosis. To test this possibility, stably transfected mammalian cells producing p26 were generated and their ability to resist apoptosis induction determined. Examination of immunofluorescently stained transfected 293H cells by ...</description>
    <dc:creator>Villeneuve, Tania S.; Ma, Xiaocui; Sun, Yu; Oulton, Mindy M.; Oliver, Ann E.; MacRae, Thomas H.</dc:creator>
  </item>
  <item rdf:about="http://biblioteca.universia.net/ficha.do?id=9142060">
    <title>Induction of the 72-kilodalton heat shock protein and protection from ultraviolet Binduced cell ...</title>
    <link>http://biblioteca.universia.net/ficha.do?id=9142060</link>
    <description>It has been demonstrated that hyperthermia protects keratinocytes from ultraviolet B (UVB)-induced cell death in culture and in vivo. This effect is mediated by the antiapoptotic effect of heat shock proteins that are transiently induced after exposure to heat at sublethal temperatures. Consequently, induction of Hsp has been proposed as a novel means of photoprotection. However, in the face of daily UVB exposure of human skin in vivo, this approach would not be useful if keratinocytes become...</description>
    <dc:creator>Merwald, Helga; Kokesch, Claudia; Klosner, Gabriele; Matsui, Mary; Trautinger, Franz</dc:creator>
  </item>
  <item rdf:about="http://biblioteca.universia.net/ficha.do?id=9142061">
    <title>Heat stress enhances recovery of hepatocyte bile acid and organic anion transporters in endotoxem...</title>
    <link>http://biblioteca.universia.net/ficha.do?id=9142061</link>
    <description>Heat stress (HS) reduces the many sequelae of lipopolysaccharide (LPS)-induced endotoxemia. Without HS, endotoxins have been shown to induce a transcriptional down-regulation of hepatocyte transport proteins for bile acids and organic anions. We performed experiments in isolated perfused rat livers at various times after LPS administration with and without HS pretreatment to determine whether HS would correct deficient transport of bromosulfophthalein (BSP). Possible mechanisms involved were ...</description>
    <dc:creator>Bolder, Ulrich; Jeschke, Marc Gerhard; Landmann, Lukas; Wolf, Francine; de Sousa, Corina; Schlitt, Hans-Jürgen; Przkora, René</dc:creator>
  </item>
  <item rdf:about="http://biblioteca.universia.net/ficha.do?id=9142496">
    <title>Inducible heat shock protein 70 expression as a potential predictive marker of metastasis in brea...</title>
    <link>http://biblioteca.universia.net/ficha.do?id=9142496</link>
    <description>Heat shock protein (Hsp)peptide complexes purified from tumors can prime the immune system against tumor antigens, but how they contribute to the generation of immune responses against naturally occurring tumors is unknown. Murine tumors expressing high amounts of Hsp70 are preferentially rejected by the immune system, suggesting that low Hsp70 expression is advantageous for tumor growth in the host. To determine whether Hsp70 was differentially expressed in human tumors, inducible Hsp70 exp...</description>
    <dc:creator>Torronteguy, Carolina; Frasson, Antonio; Zerwes, Felipe; Winnikov, Erik; da Silva, Vinicius Duval; Ménoret, Antoine; Bonorino, Cristina</dc:creator>
  </item>
  <item rdf:about="http://biblioteca.universia.net/ficha.do?id=9142497">
    <title>Conformational changes resulting from pseudophosphorylation of mammalian small heat shock protein...</title>
    <link>http://biblioteca.universia.net/ficha.do?id=9142497</link>
    <description>The human genome codes for 10 so-called mammalian small heat shock or stress proteins (sHsp) with the various tissues expressing characteristic sets of sHsps. Most sHsps interact with each other and form homo- and hetero-oligomeric complexes. Some of the sHsps are phosphoproteins in vivo, and phosphorylation has been implicated in the regulation of complex size and composition. In this study, we analyze, by the 2-hybrid method, the reporter gene activation pattern of several sHsp pairs that p...</description>
    <dc:creator>Sun, Xiankui; Welsh, Michael J.; Benndorf, Rainer</dc:creator>
  </item>
  <item rdf:about="http://biblioteca.universia.net/ficha.do?id=16279555">
    <title>Our Concepción of the cellular stress response</title>
    <link>http://biblioteca.universia.net/ficha.do?id=16279555</link>
    <dc:creator>Hightower, Lawrence E.</dc:creator>
  </item>
  <item rdf:about="http://biblioteca.universia.net/ficha.do?id=16279556">
    <title>Stress down south: meeting report of the fifth International Workshop on the Molecular Biology of...</title>
    <link>http://biblioteca.universia.net/ficha.do?id=16279556</link>
    <dc:creator>Multhoff, Gabriele; De Maio, Antonio</dc:creator>
  </item>
  <item rdf:about="http://biblioteca.universia.net/ficha.do?id=16279557">
    <title>On the brotherhood of the mitochondrial chaperones mortalin and heat shock protein 60</title>
    <link>http://biblioteca.universia.net/ficha.do?id=16279557</link>
    <description>The heat shock chaperones mortalin/mitochondrial heat shock protein 70 (mtHsp70) and Hsp60 are found in multiple subcellular sites and function in the folding and intracellular trafficking of many proteins. The chaperoning activity of these 2 proteins involves different structural and functional mechanisms. In spite of providing an excellent model for an evolutionarily conserved molecular brotherhood, their individual functions, although overlapping, are nonredundant. As they travel to vari...</description>
    <dc:creator>Deocaris, Custer C.; Kaul, Sunil C.; Wadhwa, Renu</dc:creator>
  </item>
  <item rdf:about="http://biblioteca.universia.net/ficha.do?id=16279558">
    <title>Stress-induced phosphorylation of caveolin-1 and p38, and down-regulation of EGFr and ERK by the ...</title>
    <link>http://biblioteca.universia.net/ficha.do?id=16279558</link>
    <description>We have examined the A431 (human epidermoid carcinoma) and HT29 (human colorectal carcinoma) cellular responses evoked by lectins of dietary origin, Jacalin of Artocarpus integrifolia (native jacalin; nJacalin), peanut agglutinin (PNA) of Arachis hypogea, and recombinant single-chain jacalin (rJacalin), which has the same protein backbone but ?100-fold less affinity for carbohydrates than nJacalin. All three lectins (nJacalin, rJacalin, and PNA) are cycotoxic inhibitors of proliferation of A4...</description>
    <dc:creator>Sahasrabuddhe, Anagh A.; Ahmed, Neesar; Krishnasastry, M.V.</dc:creator>
  </item>
  <item rdf:about="http://biblioteca.universia.net/ficha.do?id=16279559">
    <title>Histidine 89 is an essential residue for Hsp70 in the phosphate transfer reaction</title>
    <link>http://biblioteca.universia.net/ficha.do?id=16279559</link>
    <description>Autophosphorylation of Hsp70 is detected in the process of substrate refolding in the presence of adenosine triphosphate (ATP) in the reaction mixture. But to date, the role and mechanism of Hsp70 autophosphorylation have not been elucidated. In this study we determined the site of histidine phosphorylation of Hsp70 as an intermediate in the process of phosphate transfer reaction by site-directed mutagenesis. We selected two possible sites (ie, His89 and His227) of intermediate histidine phos...</description>
    <dc:creator>Lu, Yuanming; Hu, Qian; Yang, Cuixia; Gao, Feng</dc:creator>
  </item>
  <item rdf:about="http://biblioteca.universia.net/ficha.do?id=16279560">
    <title>Arctigenin from Fructus Arctii is a novel suppressor of heat shock response in mammalian cells</title>
    <link>http://biblioteca.universia.net/ficha.do?id=16279560</link>
    <description>Because heat shock proteins (Hsps) are involved in protecting cells and in the pathophysiology of diseases such as inflammation, cancer, and neurodegenerative disorders, the use of regulators of the expression of Hsps in mammalian cells seems to be useful as a potential therapeutic modality. To identify compounds that modulate the response to heat shock, we analyzed several natural products using a mammalian cell line containing an hsp promoter-regulated reporter gene. In this study, we found...</description>
    <dc:creator>Ishihara, Keiichi; Yamagishi, Nobuyuki; Saito, Youhei; Takasaki, Midori; Konoshima, Takao; Hatayama, Takumi</dc:creator>
  </item>
  <item rdf:about="http://biblioteca.universia.net/ficha.do?id=16279561">
    <title>Overexpressed heat shock protein 70 protects cells against DNA damage caused by ultraviolet C in ...</title>
    <link>http://biblioteca.universia.net/ficha.do?id=16279561</link>
    <description>Heat shock protein 70 (Hsp70) comprises proteins that have been reported to protect cells, tissues, and organisms against damage from a wide variety of stressful stimuli; however, little is known about whether Hsp70 protects against DNA damage. In this study, we investigated the relationship between Hsp70 expression and the levels of ultraviolet C (UVC)induced DNA damage in A549 cells with normal, inhibited, and overexpressed Hsp70 levels. Hsp70 expression was inhibited by treatment with que...</description>
    <dc:creator>Niu, Piye; Liu, Lin; Gong, Zhiyong; Tan, Hao; Wang, Feng; Yuan, Jing; Feng, Youmei; Wei, Qingyi; Tanguay, Robert M; Wu, Tangchun</dc:creator>
  </item>
  <item rdf:about="http://biblioteca.universia.net/ficha.do?id=16279562">
    <title>Overexpression of inducible heat shock protein 70 and its mutants in astrocytes is associated wit...</title>
    <link>http://biblioteca.universia.net/ficha.do?id=16279562</link>
    <description>Wild-type inducible Hsp70 (WT) and 2 folding deficient mutants protect the brain against focal cerebral ischemia in vivo and brain cells from oxygenglucose deprivation (OGD) in vitro, but the protective mechanisms remain unclear. Mitochondria are central to both normal physiological function and the regulation of cell death. We tested the effect of overexpressing Hsp70 and 2 mutants, Hsp70-K71E, an adenosine triphosphatase (ATPase)-deficient point mutant, and Hsp70-381640, a deletion mutant...</description>
    <dc:creator>Ouyang, Yi-Bing; Xu, Li-Jun; Sun, Yun-Juan; Giffard, Rona G.</dc:creator>
  </item>
  <item rdf:about="http://biblioteca.universia.net/ficha.do?id=16279563">
    <title>The function of the ?3 interactive domain in the small heat shock protein and molecular chaperone...</title>
    <link>http://biblioteca.universia.net/ficha.do?id=16279563</link>
    <description>Knowledge of the interactive domains on the surface of small heat shock proteins (sHSPs) is necessary for understanding the assembly of complexes and the activity as molecular chaperones. The primary sequences of 26 sHSP molecular chaperones were aligned and compared. In the interactive ?3 sequence, 73DRFSVNLDVKHFS85 of human ?B crystallin, Ser-76, Asn-78, Lys-82, and His-83 were identified as nonconserved residues on the exposed surface of the ? crystallin core domain. Site-directed mutagene...</description>
    <dc:creator>Ghosh, Joy G.; Estrada, Marcus R.; Houck, Scott A.; Clark, John I.</dc:creator>
  </item>
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