Small heat shock proteins

Ebook "Heat shock proteins and plants" provides the most up-to-date and concise reviews and progress on the role of heat shock proteins in plant biology, structure and function and is subdivided into chapters focused on Small Plant HSPs (Part I), Larger Plant HSPs (Part II) and HSPs for Therapeutic Gain (Part III).

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Ebook "Heat shock proteins in neural cells" address the role of heat shock proteins and cellular stress responses in the brain, with a major focus on nerve cells and glia, namely oligodendrocytes and astrocytes. Chapter 1 summarizes the classification and functional roles of heat shock proteins which are particularly abundant in brain cells.

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Ebook "Molecular chaperones (Topics in Current chemistry, 328)" describes all three families of known peptidyl prolyl isomerases (PPIases) including the FKBPs, cyclophilins and parvulins. These chaperones catalyse conformational interconversions of peptide bonds which can be critical to the correct folding of many proteins. The structural and chemical features of PPIases and the catalytic cycle are described, and a discussion of chaperoning versus catalysis is also included.

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In living organisms, small heat shock proteins (sHSPs) are triggered in response to stress situations. This family of proteins is large in plants and, in the case of tomato (Solanum lycopersicum), 33 genes have been identified, most of them related to heat stress response and to the ripening process.

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As air temperatures increase globally, more and more plants are exposed to heat-stress conditions. Although many studies have explored regulation networks in plants with the aim of improving their heat-stress tolerance, only few have revealed them in trees.

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Small heat shock proteins (sHSPs) belong to the class of molecular chaperones that respond to biotic and abiotic stresses in plants. A previous study has showed strong induction of the gene GmHsp22.4 in response to the nematode Meloidogyne javanica in a resistant soybean genotype, while repression in a susceptible one.

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Small heat shock proteins (sHSPs) are critical for plant response to biotic and abiotic stresses, especially heat stress. They have also been implicated in various aspects of plant development.

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The presence of hypoxia in head and neck squamous cell carcinoma (HNSCC) is associated with therapeutic resistance and increased risk of metastasis formation. αB-crystallin (HspB5) is a small heat shock protein, which is also associated with metastasis formation in HNSCC.

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Because anaplastic lymphoma kinase (ALK) is dependent on Hsp90 for protein stability, Hsp90 inhibitors are effective in controlling growth of lung cancer cells with ALK rearrangement. We investigated the mechanism of acquired resistance to 17-(Dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), a geldanamycin analogue Hsp90 inhibitor, in H3122 and H2228 non-small cell lung cancer cell lines with ALK rearrangement.

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Studies have shown that HSP20 (heat-shock protein 20) genes play important roles in regulating plant growth, development, and stress response. However, the grape HSP20 gene family has not been well studied.

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To examine functions of two small heat shock proteins of Escherichia coli, IbpA and IbpB, we constructed His–IbpA and His–IbpB, in which a polyhistidine tag was fused to the N-terminals. Both purified His–IbpA and His–IbpB formed multimers, which have molecular masses of about 2.0– 3.0 MDa and consist of about 100–150 subunits.

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Oviparously developing embryos of the brine shrimp, Artemia franciscana, synthesize abundant quantities of a small heat shock/a-crystallin protein, termed p26. Wild-type p26 functions as a molecular chaperone in vitro and is thought to help encysted Artemia embryos survive severe physiological stress encountered during diapause and anoxia. Full-length and truncated p26 cDNA derivatives were generated by PCR amplification of p26-3-6-3, then cloned in either pET21(+) or pRSETC and expressed in Escherichia coli BL21(DE3)....

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Mycobacterium tuberculosisheat shock protein 16.3 (MTB HSP 16.3) accumulates as the dominant protein in the latent stationary phase of tuberculosis infection. MTB HSP 16.3 displays several characteristics of small heat shock proteins (sHsps): its expression is increased in response to stress, it protects against protein aggregationin vitro, and it contains thecoreÔa-crystallinÕdomainfound inall sHsps.

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The interaction of heat shock protein with molecular mass 25 kDa (HSP25) and its point mutants S77D + S81D (2D mutant) and S15D + S77D + S81D (3D mutant) with intact and thermally denatured actinwas analyzedbymeans of fluorescence spectroscopy and ultracentrifugation. Wild typeHSP25 did not affect the polymerization of intact actin. The HSP25 3D mutant decreased the initial rate without affecting the maximal extent of intact actin polymerization. G-actin heated at 40–45
C was partially denatured, but retained its ability to polymerize....

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Embryos of the brine shrimp,Artemia franciscana, exhibit remarkable resistance to physiological stress, which is tem-porally correlated with the presence of two proteins, one a small heat shock/a-crystallin protein termed p26 and the other called artemin, of unknown function.Artemin was sequenced previously by Edman degradation, and its rela-tionship to ferritin, an iron storage protein, established.The isolation from anArtemiaexpressed sequence tag library of artemin and ferritin cDNAs extends this work. ...

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The small heat shock proteins function as molecular chaperones, an activ-ity often requiring reversible oligomerization and which protects against irreversible protein denaturation. An abundantly produced small heat shock protein termed p26 is thought to contribute to the remarkable stress resistance exhibited by encysted embryos of the crustacean,Artemia francis-cana. Three novel sequence motifs termed G, R and TS were individually deleted from p26 by site-directed mutagenesis.

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Small heat shock proteins (sHSPs) function as molecular chaperones, pre-venting stress induced aggregation of partially denatured proteins and pro-moting their return to native conformations when favorable conditions pertain. Sequence similarity between sHSPs resides predominately in an internal stretch of residues termed the a-crystallin domain, a region usually flanked by two extensions.

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The mammalian small heat shock proteinaB-crystallin can be phosphorylated at three different sites, Ser19, Ser45 and Ser59. We compared the intracellular distribution of wild-type, nonphosphorylatable and all possible pseudophos-phorylation mutants ofaB-crystallin by immunoblot and immunocytochemical analyses of stable and transiently transfected cells. We observed that pseudophosphorylation at two (especially S19D/S45D) or all three (S19D/S45D/ S59D) sites induced the partial translocationofaB-crystallin from the detergent-soluble to the detergent-insoluble frac-tion....

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A hallmark ofa-crystallin-type small heat shock proteins (sHsps) is their highly dynamic oligomeric structure which promotes intermolecular interactions involved in subunit exchange and substrate binding (chaperone-like activity). We studied the oligomeric features of two classes of bacterial sHsps by size exclusion chromatography and nanoelectro-spray mass spectrometry.Proteins of both classes formed large complexes that rapidly dissociated upon dilution and at physiologically relevant heat shock temperatures....

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Small Hsps (sHsps) and the structurally related eye lens a-crystallins are ubiquitous stress proteins that exhibit ATP-independent molecular chaperone activity. We studied the chaperone activity of dodecameric wheatTaHsp16.9C-I, a class I cytosolic sHsp from plants and the only eukaryotic sHsp for which a high resolution structure is available, along with the related wheat proteinTaHsp17.8C-II, which represents the evolutionarily distinct class II plant cytosolic sHsps. Despite the available structural information on TaHsp16.

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