Trehalose (α-D-glucopyranosyl-α-D-glucopyranoside) is a non-reducing disaccharide present in fungi, algae and several invertebrate phyla such as nematodes, annelids and arthropods (see Elbein, 1974). In many insects, trehalose constitutes the major haemolymph (blood) sugar, whereas glucose is often present at much lower concentrations (for a review, see Wyatt, 1967; Becker et al., 1996). Trehalose is synthesized and released into the haemolymph by the fat body, the central organ of intermediary metabolism in insects (Candy and Kilby, 1959, 1961).. Trehalose is split into two glucose units by the enzyme trehalase (EC 3.2.1.28), which is present in many insect tissues (for a review, see Becker et al., 1996). In locusts, the enzyme has been found in thoracic ganglia (Strang and Clement, 1980), brain and skeletal muscle. Trehalase activity is very low in locust haemolymph, and it is doubtful whether this activity is due to a `true trehalase (Vaandrager et al., 1989). High activity has been found ...
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Trehalase deficiency: Find the most comprehensive real-world symptom and treatment data on trehalase deficiency at PatientsLikeMe. 1 patients with trehalase deficiency experience fatigue, insomnia, depressed mood, pain, and anxious mood.
G6P -, UDP TRE6P tsl1 subunit of trehalose-6-phosphate synthase\/phosphatase complex\; homologous to TPS3 gene product YMR261C 2.4.1.15 TPS3 trehalose-6-P synthetase, 115 kD regulatory UDPG + G6P -, UDP + TRE6P tps3 subunit of trehalose-6-phosphate synthase\/phosphatase complex YDR074W 3.1.3.12 TPS2 Trehalose-6-phosphate phosphatase TRE6P -, TRE + PI tps2 YPR026W 3.2.1.28 ATH1 Acid trehalase TRE -, 2 GLC ath1 YBR001C 3.2.1.28 NTH2 Neutral trehalase, highly homologous to NthIp TRE -, 2 GLC nth2 YDR001C 3.2.1.28 NTH1 neutral trehalase TRE -, 2 GLC nth1 Glycogen Metabolism (sucorose and sugar metabolism) YEL011W 2.4.1.18 glc3 Branching enzyme, 1,4-glucan-6-(1,4-glucano)- GLYCOGEN + PI -, G1P glc3 transferase YPR160W 2.4.1.1 GPH1 Glycogen phosphorylase GLYCOGEN + PI -, G1P gph1 YFR015C 2.4.1.11 GSY1 Glycogen synthase (UDP-gluocse--starch UDPG -, UDP + GLYCOGEN gsy1 glucosyltransferase) YLR258W 2.4.1.11 GSY2 Glycogen synthase (UDP-gluocse--starch UDPG -, UDP + GLYCOGEN gsy2 glucosyltransferase) ...
Nature Biotechnology journal featuring biotechnology articles and science research papers of commercial interest in pharmaceutical, medical, and environmental sciences.Production of a periplasmic trehalase in Gluconobacter oxydans and growth on trehalose. K. Kosciow a,.Kidney International aims to inform the renal researcher and practicing nephrologists on all aspects of renal research ...
While E. coli only synthesizes trehalose under conditions of high osmolarity, it can degrade the sugar under conditions of both low and high osmolarity. In fact, E. coli can grow with trehalose as the sole carbon source. Different pathways are employed under different osmolarity conditions. Under high osmotic conditions the bacterium synthesizes large amounts of trehalose, which is used as an osmoprotectant [ Giaever88 ]. Trehalose molecules that leak from the cytoplasm into the periplasm can be recycled by the action of the TreA, a periplasmic trehalase. TreA breaks trehalose into two glucose molecules, which are then recycled by transport back into the cytoplasm through the glucose PTS [ Styrvold91 ]. Another function of TreA is the utilization of external trehalose under conditions of high osmolarity [ Boos87 ]. A second trehalase, which is cytoplasmic (encoded by the treF gene), is active during the transition period between high and low osmolarity. As the cells are shifting their metabolism ...
Guan-Chiun Lee, Chih-Hsin Lin, Yu-Chen Tao, Jinn-Moon Yang, Kai-Cheng Hsu, Yin-Jung Huang, Shih-Han Huang, Pin-Jui Kung, Wan-Ling Chen, Chien-Ming Wang, Yih-Ru Wu, Chiung-Mei Chen, Jung-Yaw Lin, Hsiu Mei Hsieh-Li, Guey-Jen Lee-Chen, The potential of lactulose and melibiose, two novel trehalase-indigestible and autophagy-inducing disaccharides, for polyQ-mediated neurodegenerative disease treatment, NeuroToxicology, 2015, 48, ...
Both training and nutrient intake are potent activators of protein synthesis, although nutrient-induced increases are short-lived.
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The levels of trehalose and the activity of trehalase during the development of Ascaris suum eggs were investigated. The level of trehalose in the zygote was high (2.96 ± 0.07 mg/g). During cleavage of eggs, it decreased (0.91 ± 0.35 mg/g). A higher concentration of the sugar was recorded at the blastula and during gastrulation, but it did not reach the uncleaved eggs level. In the early motile larvae, the concentration of trehalose was high (4.58 ± 2.01 mg/g). It decreased with development of L1 larvae (3.10 ± 1.47 mg/g). A rapid increase in trehalose reserves was observed between the L1 and L2 stages. The highest content of trehalose was found in invasive L2 larvae (5.78 ± 1.39 mg/g).. The activity of trehalase at the zygote stage was high (560.22 ± 322.31 U/mg). It decreased at the beginning of cleavage. It was the lowest at the 4-6-cell stage (189.76 ± 114.97 U/mg). An increase in the enzyme activity occurred after reaching the blastula stage (348.44 ± 343.34 U/mg). The highest ...
Organisms ranging from bacteria, yeast, fungi, insects, invertebrates, and lower and higher plants have enzymes that can make trehalose.[5] In nature, trehalose can be found in plants, and microorganisms. In animals, trehalose is prevalent in shrimp, and also in insects, including grasshoppers, locusts, butterflies, and bees, in which trehalose serves as blood-sugar. Trehalose is then broken down into glucose by the catabolic enzyme trehalase for use. Trehalose is also present in the nutrition exchange liquid of hornets and their larvae.[citation needed]. Trehalose is the major carbohydrate energy storage molecule used by insects for flight. One possible reason for this is that the glycosidic linkage of trehalose, when acted upon by an insect trehalase, releases two molecules of glucose, which is required for the rapid energy requirements of flight. This is double the efficiency of glucose release from the storage polymer starch, for which cleavage of one glycosidic linkage releases only one ...
Recently, high concentrations of intracellular trehalose (>200mM) were employed to enhance the cryoprotection and desiccation protection of human erythrocytes. However, significant challenges must be overcome if this advancement is to be translated into clinical practice. It is here demonstrated that 247 ± 5 mM intracellular trehalose caused the lysis of 60 ± 2% of erythrocytes upon resuspension in PBS of physiological osmolality (300 mOsm) and caused surviving cells to swell up to 140 ± 2% of isotonic cell volume. Trehalose loaded cells also exhibited 24 ± 1% incidence of phosphatidylserine translocation upon resuspension in 300 mOsm PBS, likely due to loading induced cell swelling. Un-loading of trehalose from erythrocytes using the membrane-permeabilizing biopolymer PP-50 was investigated as a technique to mitigate these damaging effects. After erythrocyte un-loading from 247 ± 5 mM to 39 ± 2 mM intracellular trehalose, cell lysis at 300 mOsm PBS was reduced from 60 ± 2% to 17 ± 3%. ...
Addition of glucose or fructose to cells of the yeast Saccharomyces cerevisiae grown on a nonfermentable carbon source triggers within a few minutes post-translational activation of trehalase, repression of the CTT1 (catalase) and SSA3 (Hsp70) genes, and induction of the ribosomal protein genes RPL1, RPL25 and RPS33. By using appropriate sugar kinase mutants, it was shown that rapid glucose- or fructose-induced activation of trehalase requires phosphorylation of the sugar. On the other hand, partial induction of RPL1, RPL25 and RPS33 as well as partial repression of CTT1 and SSA3 were observed in the absence of sugar phosphorylation. In glucose-grown nitrogen-starved yeast cells re-addition of a nitrogen source triggers activation of trehalase in a glucose- or fructose-dependent way, but with no apparent requirement for phosphorylation of the sugar. Repression of CTT1 and SSA3 under the same conditions was also largely dependent on the presence of the sugar and also in these cases there was a strong
Trehalose is a non-reducing disaccharide formed by two glucose molecules. It is widely distributed in Nature and has been isolated from certain species of bacteria, fungi, invertebrates and plants, which are capable of surviving in a dehydrated state for months or years and subsequently being revived after a few hours of being in contact with water. This disaccharide has many biotechnological applications, as its physicochemical properties allow it to be used to preserve foods, enzymes, vaccines, cells etc., in a dehydrated state at room temperature. One of the most striking findings a decade ago was the discovery of the genes involved in trehalose biosynthesis, present in a great number of organisms that do not accumulate trehalose to significant levels. In plants, this disaccharide has diverse functions and plays an essential role in various stages of development, for example in the formation of the embryo and in flowering. Trehalose also appears to be involved in the regulation of carbon metabolism
According to the previous results of the molecular identifications of transgenic tobaccos, the representative individuals, CK (non-transgenic), 121 (with p
This natural sugar is used in the food industry as a preservative and flavor enhancer (its in Taco Bells meat filling). And curiously, medical researchers keep running into trehalose when theyre looking for ways to fight neurodegenerative diseases.. A recent example from Emorys Department of Pharmacology: Chris Holler, Thomas Kukar and colleagues were looking for drugs that might boost human cells production of progranulin (PGRN), a growth factor that keeps neurons healthy. Mutations in the progranulin gene are a common cause of frontotemporal dementia.. The Emory scientists discovered two leads: a class of compounds called mTOR inhibitors - the transplant drug rapamycin is one - and trehalose. The team decided to concentrate on trehalose because it increased PGRN levels in neuronal and non-neuronal cell types, unlike the mTOR inhibitors. Their results were published at the end of June in Molecular Neurodegeneration.. The team confirmed their findings by examining the effects of trehalose ...
Complete information for TREHP1 gene (Pseudogene), Trehalase Pseudogene 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
In the present study, TreZ from Zunongwangia sp. was isolated and expressed in E. coli BL21 (DE3). The optimum temperature for TreZ is 50 °C, which is higher than that of many previously reported trehalases, such as those in Apis mellifera L 7 °C [22], Rhodotorula rubra 30 °C [23], Saccharomyces cerevisiae 40 °C [24], and Rhizopus microsporus var. rhizopodiformis 45 °C [25]. However, a trehalase from a thermophilic bacterium Rhodothermus marinus has a higher optimal temperature of 88 °C than TreZ [26].. Another remarkable characteristic of TreZ is its extreme salt-tolerance (Fig. 3). The enzyme was found to be active over a wide NaCl concentration range (0-5 M exhibiting the maximum activity at 1 M NaCl (136 %) and retaining more than 100 % of its original activity at 0.5-3.5 M NaCl. This behavior is similar to that of a xylanase and two amylases from Zunongwangia sp., which showed the optimum activity at 3, 1.5 and 2 M NaCl, respectively [27-29]. TreZ retains activity with or without NaCl ...
Author: Duan, G. Y. et al.; Genre: Journal Article; Published online: 2013-12-24; Open Access; Keywords: Arabidopsis thaliana|br/| ; Title: Reconstruction and analysis of nutrient-induced phosphorylation networks in Arabidopsis thaliana
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REGULATION OF THE TREHALOSE SYNTHESIS COMPLEX IN SACCHAROMYCES CEREVISIAE E.T.V. TREVISOL1*, A.D. PANEK1, J.F. DE MESQUITA2, E.C.A. ELEUTHERIO1 1 Programa de Pós-graduação em Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro, 2 Programa de Pós-graduação em Genética e Biologia Molecular, Instituto Biomédico, Universidade Federal do Estado do Rio de Janeiro, E-mail: [email protected] Trehalose…
Encysted embryos of Artemia franciscana undergo a dramatic respiratory depression upon release from the adult female as they enter a state of hypometabolism termed diapause. The mechanisms by which such a respiratory depression is achieved remain unexplained. Evidence presented here shows that strategic enzymes involved in trehalose catabolism are inhibited during diapause, namely trehalase, hexokinase, pyruvate kinase and pyruvate dehydrogenase. Trehalose is the sole source of fuel in the embryos of A. franciscana, and hence downregulation of trehalose catabolism results in severe limitation of metabolic fuel available to the embryo during diapause. Western blot data demonstrates that pyruvate dehydrogenase becomes phosphorylated during entrance into diapause, and as a consequence, one would predict PDH to be strongly inhibited in this state. Restriction of glycolytic flux will lead to metabolic starvation of the mitochondrion, and in turn will reduce mitochondrial oxidative phosphorylation during
The PO reduction in the larvae with autotomized lamellae is the first demonstration of a reduced investment in immune function after autotomy. These results may, to some extent, be compared with the few studies on the effects of wounding on investment in immune function. An important difference is, however, that during autotomy no typical wound is created, instead, a body part is removed at a specific breaking joint, and in the case of lamellae autotomy by damselfly larvae a specialized sphincter directly closes to minimize loss of haemolymph and invasion by pathogens (MacNeill 1960). In line with this, there was no upregulation of PO 0.5 and 1 hour after autotomy, and already a downregulation after 2 hours (see appendix in the electronic supplementary material). Furthermore, the drop in PO (and SOD) levels could not simply be attributed to haemolymph loss as there was no drop in trehalase, another haemolymph enzyme not related to immune function (see appendix in the electronic supplementary ...
Figure 1. Trehalose metabolism by Saccharomyces cerevisiae. Structure of trehalose a-D-glucosyl-1 1-a-D-glucose is shown in the upper panel. Transport is
Accepted name: trehalose 6-phosphate phosphorylase. Reaction: α,α-trehalose 6-phosphate + phosphate = glucose 6-phosphate + β-D-glucose 1-phosphate. Systematic name: α,α-trehalose 6-phosphate:phosphate β-D-glucosyltransferase. Comments: The enzyme from Lactococcus lactis is specific for trehalose 6-phosphate. Differs from EC 2.4.1.64, α,α-trehalose phosphorylase, in that trehalose is not a substrate.. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 403512-51-6. References:. 1. Andersson, U., Levander, F. and Radstrom, P. Trehalose 6-phosphate phosphorylase is part of a novel metabolic pathway for trehalose utilization in Lactococcus lactis. J. Biol. Chem. 276 (2001) 42707-42713. [PMID: 11553642]. ...
Trehalose (mycose, tremalose) sugar molecule. Atoms are represented as spheres and are colour coded: hydrogen (white), carbon (black), oxygen (red). Illustration. - Stock Image F012/9385
Creative-Proteomics offer cas 585-91-1 α, β-[1, 1-2H2]trehalose (α-D-[1-2H]Glcp-(1↔1)-β-D-[1-2H]Glcp). We are specialized in manufacturing Stabel Isotope Labeled Analytical Standard products.
White, odorless, sweet-tasting powder. Trehalose is a disaccharide, two simple sugars in one molecule. In trehalose (as in maltose), the two sugars are both glucose. Trehalose, like maltose, is 45% as sweet as sugar. It does not brown like sugar, and has a very low hygroscopicity (moisture attraction), so it stays free-flowing and dry. In trehalose, one glucose molecule is upside-down relative to the other. In maltose, the two glucose molecules are in the same orientation. This small difference reflects in the properties of trehalose. It does not brown when heated, it does not promote bacterial growth or tooth decay as much as maltose or sugar, and it is less attractive to moisture. Trehalose is found in honey, breads, beer, and seafood. ...
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Intestinal biopsy specimens were obtained from normal volunteers before, during, and after administration of the Norwalk agent of acute infectious nonbacterial gastroenteritis. The small intestine of acutely ill volunteers had an intact mucosa but showed histologic changes that included blunting of villi, shortening of microvilli, dilation of endoplasmic reticulum, and an increase in intracellular multivesiculate bodies. Convalescence biopsy specimens, obtained 2 weeks after illness, showed normal histologic patterns. Specimens obtained from volunteers who remained clinically well did not show histologic changes at any time. At the time of illness, brush-border enzyme activities (alkaline phosphatase, sucrase, and trehalase) were decreased as compared with base-line and convalescent values. Thus definite but reversible pathophysiologic lesions of the small intestine in man were seen during acute gastroenteritis induced by a viral agent. ...
Preparation and characterisation of dry thin native protein trehalose films on titanium-coated cyclo-olefin polymer (COP) foil generated by spin-coating/drying process and applied for protein transfer by Laser-Induced-Forward-Transfer (LIFT) ...
ATC 코드 S01은 ATC 코드의 안과 약물로 사용하는 약물을 정리한 코드이다. [1] ATC 코드 S 감각기관의 하위그룹을 이룬다.. 동물용 의약품을 위한 코드(ATCvet 코드)의 경우 인체의약품 코드 앞에 Q가 들어가게 된다. 예 : QS01.[2]. ...
ATC 코드 V09는 ATC 코드의 진단용 방사성의약품으로 사용하는 물질을 정리한 코드이다. [1] ATC 코드 V 기타의 하위그룹을 이룬다.. 동물용 의약품을 위한 코드(ATCvet 코드)의 경우 인체의약품 코드 앞에 Q가 들어가게 된다. 예 : QV09.[2]. ...
ATC 코드 G03은 ATC 코드의 성호르몬 및 생식계의 조절인자로 작용하는 감염방지제 및 부패방지제로 작용하는 약물을 정리한 코드이다. [1]ATC 코드 G 비뇨생식기계 및 성호르몬의 하위그룹을 이룬다. ...
Central carbon metabolism.Our data show that a large proportion of differentially expressed transcripts are related to core metabolic activities of the fermenting yeasts (Tables 1 and 2 and Fig. 4). Several enzymes involved in hexose metabolism, glycolysis, trehalose metabolism, and redox balance are differentially expressed between strains at various stages of fermentation. The analysis of the gene expression levels within the framework of enzyme-enzyme and enzyme-metabolite interaction graphs (using the reporter metabolite approach) helped to pinpoint areas of metabolism that could speculatively be related to strain-strain or time point variation.. Trehalose, glucose-6-phosphate, glucose, UDP-glucose, and fructose-6-phosphate scored high on the multiple analyses across time points during fermentation (Table 5). Indeed, these metabolites did show marked differences in concentration between time points (Fig. 5). Trehalose was also a prominent interstrain reporter for days 2 and 5 (Table 4), and ...
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Global Trehalose Consumption Industry 2016 Market Research Report is an in depth study providing complete analysis of the industry for the period 2016 â€
Trehalose is an odorless, white crystalline powder with a sweet taste and is virtually odorless. It prevents starch deterioration and protein denaturati...
The food enzyme with 4‐α‐d‐{(1‐,4)‐α‐d‐glucano}trehalose trehalohydrolase ((4‐α‐d‐[(1,4‐α‐d‐glucano]trehalose glucanohydrolase (trehalose‐producing)), EC 3.2.1.141) and (1‐,4)‐α‐d‐glucan 1‐α‐d‐glucosylmutase ((1,4)‐α‐d‐glucan 1‐α‐d‐glucosylmutase, E .... ...
The food enzyme with 4‐α‐d‐{(1‐,4)‐α‐d‐glucano}trehalose trehalohydrolase ((4‐α‐d‐[(1,4‐α‐d‐glucano]trehalose glucanohydrolase (trehalose‐producing)), EC 3.2.1.141) and (1‐,4)‐α‐d‐glucan 1‐α‐d‐glucosylmutase ((1,4)‐α‐d‐glucan 1‐α‐d‐glucosylmutase, E .... ...
pfc:PflA506_2935 K05343 maltose alpha-D-glucosyltransferase / alpha-amylase [EC:5.4.99.16 3.2.1.1] , (GenBank) trehalose synthase/maltokinase, putative (A) MAKKPKAATFIKDPLWYKDAVIYQVHVKSYFDSNNDGIGDFAGLIAKLDYIADLGVNTIW LLPFYPSPRRDDGYDIAEYRGVHSDYGTMADAKRFIAQAHQRGLRVITELVINHTSDQHP WFQRARKAKPGSAARDFYVWSDDDQKYDGTRIIFLDTEKSNWTWDPVAGQYFWHRFYSHQ PDLNFDNPQVMKAVLSVMRYWLDLGIDGLRLDAIPYLIERDGTNNENLAETHNVLKQIRA EIDAHYPDRMLLAEANQWPEDTQLYFGDRKGDDGDECHMAFHFPLMPRMYMALAQEDRFP ITDILRQTPEIPANCQWAIFLRNHDELTLEMVTDKERDYLWNYYAADRRARINLGIRRRL APLVERDRRRVELLNSLLLSMPGTPTLYYGDEIGMGDNIYLGDRDGVRTPMQWSIDRNGG FSRADPASLVLPPIMDPQYGYQSVNVETQAQDPHSLLNWTRRMLAVRKQSKAFGRGSLKM LSPTNRRILAYTREYTGEDGHTEIILCVANVSRSAQAAELDLSAFAGMVPVEMLGGNAFP PIGQLNFLLTLAPYGFYWFVLAAENQMPSWHVEPAQSMPDFTTLVLKKRMEELLEEPCRT SLEHTSLPAWLPKRRWFAGKDTAIDTVHIAYGVRFGDPQHPVLLSEIEVTSAGQVSRYQL PLGFLGEDQFTSALPQQLALARVRRTRQVGLVTDAFSLEHFILEVIQAMQAGTVLNTPDG DLRFEATHHLAALQLTRESPVRYLSAEQSNSSVVVGESLVLKLIRKVSAGVHPELEMSAY LTAAGYPNISPLLGFMSRQDGQGQDNLLMIAQGYLSNQGDAWSWTQNNLERAIRDELADA ...
car:cauri_0565 K05343 maltose alpha-D-glucosyltransferase / alpha-amylase [EC:5.4.99.16 3.2.1.1] , (GenBank) treS; trehalose synthase (A) MTWHDNAIFYQALVGSYKDAHGEGVGTLRGVIEKLDYLKWLGVDCLWLSPFYASPLRDDG YDIADYYAIHPDYGTMEDFDELVAELHTRGMRLMTDLAFNHTSTDHPWFQASRTDPEGPY GDYYVWGDDPLRYPEIRIIFTDTETSNWAWDPERKQYYFHRFYSHQPDLNYDNPKVHEEV FKILSFWLDKGVDGFRLDAIAYLYERDGVGGESLPETVDFVEKVRAFIDENYPEAIMIAE ANQPPEETMEFYGTGNRFHMVFNFPVMPRLYQALALGDATPVYDIMAELPELPQGCQWGT FLRNHDELTLEMVDEDQRAIMYQHYLPDEQMRAHVGIARRLAPLLGNDYRKIELFYSLLM TLPGAPFLYYGDEIGMNDAPELPDRDAVRTPMQWEPGEGAGFSTSAQTRRPIVGGVGVSV EEQLADDSSLLHRLRGLIQQRKAHPKLGTAPFEAVETGQTGVLGFQRGELLCLHNFTDQT VDLGPVELGPYGYAWLPVEV ...
SUMMARY: The enzymes of N-acetyl-D-glucosamine (GlcNAc) metabolism, GlcNAc-6-phosphate deacetylase and GlcN-6-phosphate deaminase were found to be inducible in Candida albicans. The pattern of induction for these enzymes was the same under conditions of germ-tube formation (37 °C) and where yeast cells metabolized GlcNAc with no change in morphology (28 °C); this indicates that these enzymes are not control points in the dimorphic development of C. albicans. During induction there was a 40- and 25-fold increase in specific activity for the deacetylase and the deaminase, respectively, and the maximum specific activity corresponded to the time when all the GlcNAc had been metabolized. The presence of lomofungin (an inhibitor of transcription) or trichodermin (an inhibitor of translation) in cell suspensions of C. albicans containing GlcNAc prevented the increase in specific activity of these enzymes. 2-Deoxyglucose inhibited germ-tube formation, partially inhibited the induction of the deacetylase (43%)
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DE ARAUJO, Pedro Soares. Role of trehalose in cell stress. Brazilian Journal of Medical and Biological Research, Ribeirao Preto, v. 29, p. 873-5, 1996 ...
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