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1.
BMC Psychol ; 12(1): 95, 2024 Feb 24.
Artigo em Inglês | MEDLINE | ID: mdl-38402398

RESUMO

BACKGROUND: There is a mutual influence between emotions and diseases. Thus, the subject of emotions has gained increasing attention. OBJECTIVE: The primary objective of this study was to conduct a comprehensive review of the developments in emotion recognition technology over the past decade. This review aimed to gain insights into the trends and real-world effects of emotion recognition technology by examining its practical applications in different settings, including hospitals and home environments. METHODS: This study followed the Preferred Reporting Items for Systematic Reviews (PRISMA) guidelines and included a search of 4 electronic databases, namely, PubMed, Web of Science, Google Scholar and IEEE Xplore, to identify eligible studies published between 2013 and 2023. The quality of the studies was assessed using the Critical Appraisal Skills Programme (CASP) criteria. The key information from the studies, including the study populations, application scenarios, and technological methods employed, was summarized and analyzed. RESULTS: In a systematic literature review of the 44 studies that we analyzed the development and impact of emotion recognition technology in the field of medicine from three distinct perspectives: "application scenarios," "techniques of multiple modalities," and "clinical applications." The following three impacts were identified: (i) The advancement of emotion recognition technology has facilitated remote emotion recognition and treatment in hospital and home environments by healthcare professionals. (ii) There has been a shift from traditional subjective emotion assessment methods to multimodal emotion recognition methods that are grounded in objective physiological signals. This technological progress is expected to enhance the accuracy of medical diagnosis. (iii) The evolving relationship between emotions and disease throughout diagnosis, intervention, and treatment processes holds clinical significance for real-time emotion monitoring. CONCLUSION: These findings indicate that the integration of emotion recognition technology with intelligent devices has led to the development of application systems and models, which provide technological support for the recognition of and interventions for emotions. However, the continuous recognition of emotional changes in dynamic or complex environments will be a focal point of future research.

2.
PLoS One ; 17(7): e0271633, 2022.
Artigo em Inglês | MEDLINE | ID: mdl-35853031

RESUMO

DNA barcoding is a supplementary tool in plant systematics that is extensively used to resolve species-level controversies. This study assesses the significance of using two DNA barcoding loci (e.g., psbA-trnH and trnC-petN) in distinguishing 33 plant samples of the genus Syringa. Results showed that the average genetic distance K2P of psbA-trnH DNA marker was 0.0521, which is much higher than that of trnC-petN, which is 0.0171. A neighbor-joining phylogenetic tree based on psbA-trnH and trnC-petN indicated that the identification rate of psbA-trnH and trnC-petN alone were 75% and 62.5%, respectively. The barcode combination of psbA-trnH+trnC-petN could identify 33 samples of the genus Syringa accurately and effectively with an identification rate of 87.5%. The 33 Syringa samples were divided into four groups: Group I is series Syringa represented by Syringa oblata; Group II is series Villosae represented by Syringa villosa; Group III is series Pubescentes represented by Syringa meyeri; and Group IV is section Ligustrina represented by Syringa reticulata subsp. pekinensis. These research results provided strong evidence that the combinatorial barcode of psbA-trnH+trnC-petN had high-efficiency identification ability and application prospects in species of the genus Syringa.


Assuntos
DNA de Cloroplastos , Syringa , Cloroplastos/genética , Código de Barras de DNA Taxonômico/métodos , DNA de Cloroplastos/genética , DNA de Plantas/genética , Genômica , Filogenia , Análise de Sequência de DNA , Syringa/genética
3.
J Microbiol Biotechnol ; 25(11): 1856-62, 2015 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-26198121

RESUMO

In order to improve the stability of endoglucanase under thermal and acidic conditions, the endoglucanase gene was fused to the N-terminus of the Saccharomyces cerevisiae pir gene, encoding the cell wall protein PIR. The fusion gene was transformed into Pichia pastoris GS115 for expression. A resulting strain with high expression and high activity was identified by examining resistance to Geneticin 418, Congo red staining, and quantitative analysis of enzyme activity. SDS-PAGE analysis revealed that the endoglucanase was successfully displayed on the yeast cell surface. The displayed endoglucanase (DEG) showed maximum activity towards sodium carboxyl methyl cellulose at approximately 275 IU/g cell dry weight. DEG exhibited greater than 60% residual activity in the pH range 2.5-8.5, higher than free endoglucanase (FEG), which had 40% residual activity at the same pH range. The highest tolerated temperature for DEG was 70°C, much higher than that of FEG, which was approximately 50°C. Moreover, DEG showed 91.1% activity at 65°C for 120 min, while FEG only kept 77.8% residual activity over the same period. The half-life of DEG was 270 min at 65°C, compared with only 150 min for FEG. DEG could be used repeatedly at least three times. These results suggest that the DEG has broad applications as a yeast whole-cell biocatalyst, due to its novel properties of high catalytic efficiency, acid-thermal stabilities, and reusability.


Assuntos
Técnicas de Visualização da Superfície Celular , Celulase/metabolismo , Pichia/metabolismo , Proteínas Recombinantes de Fusão/metabolismo , Celulase/genética , Vermelho Congo/metabolismo , Estabilidade Enzimática , Expressão Gênica , Gentamicinas/metabolismo , Concentração de Íons de Hidrogênio , Pichia/genética , Proteínas Recombinantes de Fusão/genética , Saccharomyces cerevisiae/genética , Temperatura , Transformação Genética
4.
Wei Sheng Wu Xue Bao ; 46(1): 99-103, 2006 Feb.
Artigo em Chinês | MEDLINE | ID: mdl-16579474

RESUMO

A chitinase-encoding gene from Thermomyces lanuginosus was cloned by Rapid Amplification of cDNA Ends (RACE) using degenerated oligonucleotide primers designed from N-terminal amino acid sequence and the conserved amino acid sequence. The cloned full-length cDNA named chit, 1500bp in size, contained an OFR with 442 amino acids. The gene chit has been registered in GenBank with accession number DQ092332. The alignment results of putative amino acids sequence showed the catalytic domain of chit was high homology with the catalytic domains of the other chitinases in family-18, contained 2 conserved motifs related with catalytic activity of chitinase. The recombinant plasmid was generated by inserting the ORF of mature protein Chit into expression vector pPIC9K, and transformed into Pichia pastoris GS115. The recombinant chitinase was secreted successfully with the expression level of 0.36mg/mL and its activity could reach to 2.261U/mL after methanol induction 6d. The recombinant chitinase exhibited optimum catalytic activity at pH 5.5 and 60 degrees C. The enzyme was stable at 50 degrees C and the half life time at 65 degrees C was 40min.


Assuntos
Ascomicetos/genética , Quitinases/metabolismo , Proteínas Fúngicas/metabolismo , Sequência de Aminoácidos , Ascomicetos/enzimologia , Quitinases/genética , Clonagem Molecular , DNA Complementar/genética , Proteínas Fúngicas/genética , Regulação Fúngica da Expressão Gênica , Alinhamento de Sequência , Homologia de Sequência de Aminoácidos
5.
Wei Sheng Wu Xue Bao ; 45(2): 270-4, 2005 Apr.
Artigo em Chinês | MEDLINE | ID: mdl-15989274

RESUMO

A thermostable extracellular chitinase from culture supernatant of a thermophilic fungus Thermomyces lanuginosus was purified to SDS-PAGE homogeneity, by using ammonium sulfate fraction, DEAE-Sepharose Fast flow chromatography, Phenyl-Sepharose Fast Flow chromatography. A molecular mass of the purified enzyme was between 48-49.8 kD determined by SDS-PAGE and gel filtration chromatography. The chitinase exhibited optimum catalytic activity at pH 4.5 and 55 degrees C respectively. It was thermostable at 50 degrees C and retained 24% activity after 20 min at 70 degrees C. The half life time of the enzyme at 65 degrees C was 25 min. Different metal ions showed different effects on the chitinase activity. Ca2+, Ba2+, Na+, K+ enhanced the enzyme activity, whereas Fe2+, Ag+, Hg2+, Cu2+ caused obvious inhibition. The Km and Vmax values of chitinase on colloidal chitin were 9.56 mg/mL and 22.12 micromol/min respectively. The chitinase showed antifungal activity aginst tested fungi to different degree.


Assuntos
Ascomicetos/enzimologia , Quitinases/isolamento & purificação , Quitinases/metabolismo , Sequência de Aminoácidos , Quitinases/química , Ativação Enzimática , Estabilidade Enzimática , Concentração de Íons de Hidrogênio , Peso Molecular , Temperatura
6.
Artigo em Chinês | MEDLINE | ID: mdl-15627688

RESUMO

Treatment with mercuric chloride (0.01%), salicylic acid (10.0 mg/mL) or riboflavin (1 mmol/L) induced the beta-1, 3-glucanase activity in all the three wheat varieties i.e. 331, Kangdao 680 and Lumai 23 tested, with the strongest inductive effect on variety 331 by treatment with mercuric chloride (0.01%) for 24 h. From leaves of variety 331 treated with mercuric chloride (0.01%) for 24 h, a kind of beta-1, 3-glucanase was purified by fractional precipitation with ammonium sulphate, Phenyl-Sepharose chromatography (Phenyl-Sepharose Fast Flow), ion-exchange chromatography (DEAE-Sepharose Fast Flow) and gel-filtration chromatography (Sephacryl S-100). Through SDS-PAGE and gel filtration, the molecular weight of the purified beta-1, 3-glucanase was determined to be about 52.0-53.6 kD. The purified beta-1, 3-glucanase showed antifungal activity against both Alternaria longipes and Rhizoctonia cerealis on tested plates, and inhibited the germ tube elongation and spore germination of Verticillium dahliae and Fusarium omysporum f.sp cucumerinum.


Assuntos
Antifúngicos/farmacologia , Glucana 1,3-beta-Glucosidase/biossíntese , Folhas de Planta/enzimologia , Triticum/enzimologia , Indução Enzimática/efeitos dos fármacos , Glucana 1,3-beta-Glucosidase/isolamento & purificação , Glucana 1,3-beta-Glucosidase/farmacologia , Cloreto de Mercúrio/farmacologia , Riboflavina/farmacologia , Ácido Salicílico/farmacologia
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