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18 results for “thermal proteins”
FIGURE 2 in The thermal dependence of the protein-sparing effect in rainbow trout (Oncorhynchus mykiss, Walbaum 1792)
FIGURE 2 Ammonia quotient (AQ) of rainbow trout (Oncorhynchus mykiss) fed three isonitrogenous diets with different energy contents [high energy (HE) = 20.50 MJ kg 1, medium energy (ME) = 18.76 MJ kg 1, low energy (LE) = 17.35 MJ kg 1) at five temperatures (12 C, 14 C, 16 C, 18 C, 20 C). A quadratic dependency model was used to analyse the data. Parabolas describe the quadratic dependency of AQ values on temperature. Calculated lowest AQ values for each parabola are marked with a cross (). Each data point represents the measurement of one tank with rainbow trout at each respective diet and temperature. (n = 3)
FIGURE 1 in The thermal dependence of the protein-sparing effect in rainbow trout (Oncorhynchus mykiss, Walbaum 1792)
FIGURE 1 Percentage of retainable energy (RE) relative to gross energy intake (GEI) of rainbow trout (Oncorhynchus mykiss) fed three isonitrogenous diets with different energy contents [high energy (HE) = 20.50 MJ kg 1, medium energy (ME) = 18.76 MJ kg 1, low energy (LE) = 17.35 MJ kg 1) at five temperatures (12 C, 14 C, 16 C, 18 C, 20 C). Each data point represents measurement of one tank with rainbow trout at each respective diet and temperature (n = 3)
Fig. 5 in Expression profile of two HSP70 chaperone proteins in response to extreme thermal acclimation in Xestia c-nigrum (Lepidoptera: Noctuidae)
Fig. 5. Xc-HSC70 mRNA expression profiles induced by cold (−7 to 5 °C) and heat (37 to 47 °C) in 2nd, 3rd, 4th, 5th, and 6th instars and pupae of Xestia cnigrum. The relative quantities indicate the levels of the HSC70 gene transcript normalized against transcript levels of β-actin as an internal standard and compared with the transcript levels of the untreated control at 25 °C. An asterisk indicates a significant difference between the control and heat shock conditions (significant, * P <0.05). The data are denoted as the mean ± SEM (error bar).
Fig. 7 in Expression profile of two HSP70 chaperone proteins in response to extreme thermal acclimation in Xestia c-nigrum (Lepidoptera: Noctuidae)
Fig. 7. Expression levels of 2 HSP70s at different developmental stages relative to expression levels in 2nd instars at 25 °C. The data are denoted as the mean ± SEM (error bar), and the different lowercase or uppercase letters indicate a significant differenwce in the means as assessed using multi-comparison tests (P <0.05).
Fig. 4 in Expression profile of two HSP70 chaperone proteins in response to extreme thermal acclimation in Xestia c-nigrum (Lepidoptera: Noctuidae)
Fig. 4. Phylogenetic tree of Xc-HSC70 and Xc-HSP70 amino acid sequences from different species. A 3-letter code has been included to indicate the order name of the corresponding insect and vertebrate orders (COL = Coleoptera, LEP = Lepidoptera, DIP = Diptera, HYM = Hymenoptera, and VER =Vertebrata). The values indicated on the branches correspond to bootstrap percentages (BP).
Fig. 3 in Expression profile of two HSP70 chaperone proteins in response to extreme thermal acclimation in Xestia c-nigrum (Lepidoptera: Noctuidae)
Fig. 3. Schematic structure of the Xc-HSC70 gene. Exons are shown as boxes in which white boxes represent untranslated regions, whereas the black boxes are the protein-coding exons; introns are indicated as lines between the boxes. The numbers above and below the drawing represent the sizes (base pairs) of each exon and intron, respectively. The start codon (ATG) and stop codon (TAA) are also indicated. The genomic DNA sequence of Xc-HSC70 has been deposited in GenBank under accession no. KF731994.
Fig. 2 in Expression profile of two HSP70 chaperone proteins in response to extreme thermal acclimation in Xestia c-nigrum (Lepidoptera: Noctuidae)
Fig. 2. Nucleotide and deduced amino acid sequences of the Xc-HSP70 gene. The signature sequences of the HSP70 family are shown in boxes, the nuclear localization signal sequence is underlined, the consensus sequence EEVD at the C-terminus is indicated in italics, and the start and stop codons are in bold. The nucleotides and amino acids are numbered along the lef and right margins. The sequence encoding Xc-HSP70 has been deposited in GenBank under accession no. HQ698836.
Fig. 1 in Expression profile of two HSP70 chaperone proteins in response to extreme thermal acclimation in Xestia c-nigrum (Lepidoptera: Noctuidae)
Fig. 1. Nucleotide and deduced amino acid sequences of Xc-HSC70. The signature sequences of the HSP70 family are shown in boxes, the nuclear localization signal sequence is underlined, the consensus sequence EEVD at the C-terminus is indicated in italics, and the start and stop codons are in bold. The nucleotides and amino acids are numbered along the lef and right margins. The sequence encoding Xc-HSC70 has been deposited in GenBank under accession no. KC844151.
Data from: Protein expression parallels thermal tolerance and ecologic changes in the diversification of a diving beetle species complex
Physiological changes associated with evolutionary and ecological processes such as diversification, range expansion or speciation are still incompletely understood, especially for non-model species. Here we study differences in protein expression in response to temperature in a western Mediterranean diving beetle species complex, using two-dimensional differential gel electrophoresis with one Moroccan and one Iberian population each of Agabus ramblae and Agabus brunneus. We identified proteins with significant expression differences after thermal treatments comparing them with a reference EST library generated from one of the species of the complex (A. ramblae). The colonisation during the Middle Pleistocene of the Iberian peninsula by A. ramblae, where maximum temperatures and seasonality are lower than in the ancestral north African range, was associated with changes in the response to 27 °C in proteins related to energy metabolism. The subsequent speciation of A. brunneus from within populations of Iberian A. ramblae was associated with changes in the expression of several stress-related proteins (mostly chaperons) when exposed to 4 °C. These changes are in agreement with the known tolerance to lower temperatures of A. brunneus, which occupies a larger geographical area with a wider range of climatic conditions. In both cases, protein expression changes paralleled the evolution of thermal tolerance and the climatic conditions experienced by the species. However, although the colonisation of the Iberian peninsula did not result in morphological change, the speciation process of A. brunneus within Iberia involved genetic isolation and substantial differences in male genitalia and body size and shape.
Data for: Torii et al., Influence of amino acid substitutions in capsid proteins of coxsackievirus B5 on free chlorine and thermal inactivation
<p>This folder contains the experimental data for the figures shown in the main manuscript.</p>
Data from: Protein expression parallels thermal tolerance and ecologic changes in the diversification of a diving beetle species complex
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Data from: Maternal loading of a small heat shock protein increases embryo thermal tolerance in Drosophila melanogaster
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Data from: Spider silk colour co-varies with thermal properties but not protein structure
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Fig. 6 in Expression profile of two HSP70 chaperone proteins in response to extreme thermal acclimation in Xestia c-nigrum (Lepidoptera: Noctuidae)
Fig. 6. Xc-HSP70 mRNA expression profiles induced by cold (−7 to 5 °C) and heat (37 to 47 °C) in 2nd, 3rd, 4th, 5th, and 6th instars and pupae of Xestia cnigrum. The relative quantities indicate the levels of the HSP70 gene transcript normalized against transcript levels of β-actin as an internal standard and compared with the transcript levels of the untreated control at 25 °C. An asterisk indicates a significant difference between the control and heat shock conditions (significant, * P <0.05). The data are denoted as the mean ± SEM (error bar).
Data from: Hsp70 protein levels and thermotolerance in Drosophila subobscura: a reassessment of the thermal co-adaptation hypothesis
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Data from: Robustness of predictions of extremely thermally stable proteins in ancient organisms
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Protein Thermal Stability Changes Induced by the Global Methylation Inhibitor 3-deazaneplanocin A (DZNep)
GEO Series GSE268629. Homo sapiens. 8 samples. Type: Expression profiling by high throughput sequencing.
The WOPR family protein Ryp1 is a key regulator of gene expression, development, and virulence in the thermally dimorphic fungal pathogen Coccidioides posadasii
GEO Series GSE178277. Coccidioides posadasii str. Silveira. 8 samples. Type: Expression profiling by high throughput sequencing.
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