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Article in Chinese | WPRIM | ID: wpr-912731


Objective:To construct a drug knowledge base based on drug instructions.Methods:Six hundred randomly selected drug instructions were labeled manually and divided into training set and test set. The training was based on bidirectional long short-term memory(Bi-LSTM) and conditional random fields(CRF) model to complete the recognition of medical entities. The extracted entities were standardized by the hybrid model of " similarity calculation and rule mapping table" , and then the drug information was imported into the Access database.Results:In the task of named entity recognition based on Bi-LSTM and CRF model, except for the crowd entities, the other entities had achieved good results with an F-value higher than 85%. Based on the hybrid model of " similarity calculation and rule mapping table" , the accuracy of entity standardization was 88.23%.Conclusions:The effect of the machine learning model in this study is similar to that of other named entity recognition and entity standardization studies, which can complete the task of drug knowledge base construction satisfactorily.

Article in Chinese | WPRIM | ID: wpr-383713


Objective To investigate the effect of silence of human protection of telomeres 1 (hPOT1), which was induced by RNA interference, on expression of telomeric repeat factor 1 (TRF1), telomeric repeat factor 2 (TRF2) and Tankyrase 1 in human gastric cancer cell BGC823. Methods The ex-pression of TRF1 ,TRF2 and Tankyrasel at mRNA level were determined by semi-quantitative RT-PCR. Re-sults Significant increase in expression of TRFI, marked decrease of TRF2 and Tankyrase1 at mRNA level were observed in cells of hPOT1 siRNA. Conclusion The significant increase in expression of TRF1 and the marked decease in TRF2 and Tnakyrasel at mRNA level after the inhibited expression of hPOT1 in human gastric cancer cell BGC823 indicate that hPOTI is highly correlated with the expressions of other three te-lomere-specific binding proteins.

Article in Chinese | WPRIM | ID: wpr-562459


Objective The C-terminal domain of rodent Muc3 is proteolytically cleaved.This study is to explore the relationship between N-linked oligosaccharides in SEA module and the proteolytic cleavage within C-terminal domain of rodent Muc3.Methods Truncated rodent Muc3 C-terminal domains with complete SEA module(p20SEA) were produced by site-directed mutagenesis to insert a stop code in the required place.Proteins were detected by pulse/chase and immunoprecipitation method,or SDS/PAGE and Western blot.Inhibition of glycosylation of the expressed protein was performed by using tunicamycin.Results Muc3 C-terminal domain was posttranslationally cleaved to produce a V5-tagged 30 000 extracellular glycopeptide and a Myc-tagged 49 000 membrane-associated glycopeptide.Treatment with tunicamycin to transfected COS-1 cells led to the abundant production of 60 000 uncleaved and whole-length Muc3 C-terminal domain,the 30 000 N-terminal fragment shifted to 22 000 and 49 000 C-terminal fragment shifted to 41 000 after deglycosylation.The truncated Muc3 C-terminal domain containing complete SEA module but without the following residues led to production of 36 000 uncleaved and whole-length protein,and 30 000 cleaved product shifted to 22 000 after deglycosylation.Conclusion Proteolytic cleavage in both complete rodent C-terminal domain and complete SEA module without the following residues were partially inhibited by tunicamycin.

Article in Chinese | WPRIM | ID: wpr-525278


ObjectiveTo discuss the diagnosis and treatment of rupture of spleen in a base-level hospital with limited conditions. MethodsThe clinical data, diagnosis of bleeding by ultrasound, and results of (nonoperative) and operative treatment of 317 patients with rupture of spleen in Vila Central Hospital of the (Republic) of Vanuatu were retrospectively analyzed. ResultsUltrasound diagnosed 30 patients with (subcapsular) hemorrhage and 287 patients with true rupture of spleen. Based on ultrasound results, (conservative) treatment was used for 29 patients and 288 patients underwent operation. Conclusions(Ultrasonography) had a high positive diagnostic rate for rupture of spleen, and the diagnosis of bleeding volume was consistent with the findings at operation. The findings on ultrasonography can be considered in selection of cases with appropriate indications for splenectomy. Ultrasonography is an effective method for use in the (treatment) of rupture of spleen.

Article in Chinese | WPRIM | ID: wpr-563837


Objective To explore the correlation between membrane targeting of rodent Muc3 C-terminal domain and proteolytic cleavage blockage within its SEA module and N-linked oligosaccharides inhibition.Methods COS-1 cells were transfected with three different expression vectors containing rodent Muc3 C-terminal domain,namely p20,p20t and p20s/a by lipofectAMINE reagent.Inhibition of N-glycosylation of the expressed protein was performed by using tunicamycin.The transfected COS-1 cells(fixed or unfixed) were detected by immunolocalization experiments(anti-V5 and anti-Myc antibody) for the protein expression.Results In fixed COS-1 cells,the expressed product of p20 transfectant detected using both anti-Myc and anti-V5 antibodies was found to localize in perinuclear position and on the plasma membrane.While in the unfixed cells,immunostaining was only confined on cell surface using anti-V5 antibody.The expressed product of p20t transfectant was detected by anti-V5 antibody to localize only in perinuclear region,as observed in a few fixed cells.The distribution of p20s/a fluorescence resembled that of p20 transfectant.Plasma membrane targeting of the non-glycosylated products due to tunicamycin treatment still occurred in transfected COS-1 cells and resembled the glycosylated products.Conclusions The blockage of proteolytic cleavage within C-terminal domain of rodent Muc3 and its inhibition of N-linked oligosaccharides in SEA module cannot affect its membrane targeting.The only apparent requirement for membrane targeting is the transmembrane and/or cytoplasmic tail segments which exist in the C-terminal domains of rMuc3.