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1.
J Neural Eng ; 20(4)2023 08 21.
Artigo em Inglês | MEDLINE | ID: mdl-37552978

RESUMO

Objective.The combination of the motor imagery (MI) electroencephalography (EEG) signals and deep learning-based methods is an effective way to improve MI classification accuracy. However, deep learning-based methods often need too many trainable parameters. As a result, the trade-off between the network decoding performance and computational cost has always been an important challenge in the MI classification research.Approach.In the present study, we proposed a new end-to-end convolutional neural network (CNN) model called the EEG-circular dilated convolution (CDIL) network, which takes into account both the lightweight model and the classification accuracy. Specifically, the depth-separable convolution was used to reduce the number of network parameters and extract the temporal and spatial features from the EEG signals. CDIL was used to extract the time-varying deep features that were generated in the previous stage. Finally, we combined the features extracted from the two stages and used the global average pooling to further reduce the number of parameters, in order to achieve an accurate MI classification. The performance of the proposed model was verified using three publicly available datasets.Main results.The proposed model achieved an average classification accuracy of 79.63% and 94.53% for the BCIIV2a and HGD four-classification task, respectively, and 87.82% for the BCIIV2b two-classification task. In particular, by comparing the number of parameters, computation and classification accuracy with other lightweight models, it was confirmed that the proposed model achieved a better balance between the decoding performance and computational cost. Furthermore, the structural feasibility of the proposed model was confirmed by ablation experiments and feature visualization.Significance.The results indicated that the proposed CNN model presented high classification accuracy with less computing resources, and can be applied in the MI classification research.


Assuntos
Algoritmos , Interfaces Cérebro-Computador , Movimento , Redes Neurais de Computação , Eletroencefalografia/métodos , Imaginação
2.
Org Biomol Chem ; 21(17): 3552-3556, 2023 05 03.
Artigo em Inglês | MEDLINE | ID: mdl-36807630

RESUMO

The hydroxyl groups in the amino acid residues of echinocandin B were related to the biological activity, the instability, and the drug resistance. The modification of hydroxyl groups was expected to obtain the new lead compounds for next generation of echinocandin drug development. In this work one method for heterologous production of the tetradeoxy echinocandin was achieved. A reconstructed biosynthetic gene cluster for tetradeoxy echinocandins composed of ecdA/I/K and htyE was designed and successfully hetero-expressed in Aspergillus nidulans. The target product of echinocandin E (1) together with one unexpected derivative echinocandin F (2), were isolated from the fermentation culture of engineered strain. Both of compounds were unreported echinocandin derivatives and the structures were identified on the basis of mass and NMR spectral data analysis. Compared with echinocandin B, echinocandin E demonstrated superior stability and comparable antifungal activity.


Assuntos
Aspergillus nidulans , Equinocandinas , Equinocandinas/farmacologia , Equinocandinas/química , Equinocandinas/genética , Antifúngicos/farmacologia , Antifúngicos/metabolismo , Proteínas Fúngicas/metabolismo , Aspergillus nidulans/genética , Aspergillus nidulans/metabolismo , Família Multigênica , Aminoácidos/metabolismo , Testes de Sensibilidade Microbiana
3.
Mar Drugs ; 20(6)2022 May 24.
Artigo em Inglês | MEDLINE | ID: mdl-35736144

RESUMO

Marine natural products (MNPs) are an important source of biologically active metabolites, particularly for therapeutic agent development after terrestrial plants and nonmarine microorganisms. Sequencing technologies have revealed that the number of biosynthetic gene clusters (BGCs) in marine microorganisms and the marine environment is much higher than expected. Unfortunately, the majority of them are silent or only weakly expressed under traditional laboratory culture conditions. Furthermore, the large proportion of marine microorganisms are either uncultivable or cannot be genetically manipulated. Efficient heterologous expression systems can activate cryptic BGCs and increase target compound yield, allowing researchers to explore more unknown MNPs. When developing heterologous expression of MNPs, it is critical to consider heterologous host selection as well as genetic manipulations for BGCs. In this review, we summarize current progress on the heterologous expression of MNPs as a reference for future research.


Assuntos
Produtos Biológicos , Produtos Biológicos/metabolismo , Vias Biossintéticas/genética , Família Multigênica/genética
4.
Biochem Biophys Res Commun ; 516(3): 907-913, 2019 08 27.
Artigo em Inglês | MEDLINE | ID: mdl-31272719

RESUMO

Despite the conservative DNA sequences among LuxI (Acyl Homoserine Lactones synthase gene) homologs, structure-product relationship of AHL synthase remains to be elucidated. In this study, through degenerate primers and in vitro expression methods, we collected the information of the gene sequences and AHL profiles from nine LuxIs among Ensifer adhaerens strains. The chromosome-encoded LuxI (C-LuxI) distinguished themselves from the plasmid-encoded ones (P-LuxI) not only in the DNA sequences, but also in AHL profiles. The C-LuxIs produced only C14-HSL, while the P-LuxIs produced predominantly C8-HSL and 3-oxo-C8-HSL. Sequence-product relationship analysis updated our recognition of the role of T140 (EsaI) in the 3-oxo-HSL production. Computational calculation based on 3D structures of these LuxIs revealed the linear relationship between the chain length and the affinity of amides to AHL synthase in C-LuxI, which was not found in the P-LuxI. We hereby proposed the linear docking affinity as a criterion for the prediction of long-chain AHL production by an AHL synthase. This study extends our understanding on the structure-product relationship of AHL synthases and revealed the distinct chromosome and plasmid origin of this enzyme among E. adhaerens.


Assuntos
Acil-Butirolactonas/química , Cromossomos Bacterianos/química , Regulação Bacteriana da Expressão Gênica , Ligases/química , Plasmídeos/química , Rhizobiaceae/genética , Acil-Butirolactonas/metabolismo , Agrobacterium tumefaciens/genética , Agrobacterium tumefaciens/metabolismo , Sequência de Aminoácidos , Sítios de Ligação , Clonagem Molecular , Escherichia coli/genética , Escherichia coli/metabolismo , Expressão Gênica , Vetores Genéticos/química , Vetores Genéticos/metabolismo , Ligases/genética , Ligases/metabolismo , Simulação de Acoplamento Molecular , Filogenia , Plasmídeos/metabolismo , Ligação Proteica , Conformação Proteica em alfa-Hélice , Conformação Proteica em Folha beta , Domínios e Motivos de Interação entre Proteínas , Percepção de Quorum/genética , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Proteínas Recombinantes/metabolismo , Rhizobiaceae/enzimologia , Alinhamento de Sequência , Homologia de Sequência de Aminoácidos , Especificidade por Substrato
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