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1.
Zhongguo Xue Xi Chong Bing Fang Zhi Za Zhi ; 29(4): 436-440, 2017 Aug 15.
Artigo em Chinês | MEDLINE | ID: mdl-29508575

RESUMO

Objective To study the application of autoregressive integrated moving average (ARIMA) model to predict the monthly reported malaria cases in China, so as to provide a reference for prevention and control of malaria. Methods SPSS 24.0 software was used to construct the ARIMA models based on the monthly reported malaria cases of the time series of 20062015 and 2011-2015, respectively. The data of malaria cases from January to December, 2016 were used as validation data to compare the accuracy of the two ARIMA models. Results The models of the monthly reported cases of malaria in China were ARIMA (2, 1, 1) (1, 1, 0)12 and ARIMA (1, 0, 0) (1, 1, 0)12 respectively. The comparison between the predictions of the two models and actual situation of malaria cases showed that the ARIMA model based on the data of 2011-2015 had a higher accuracy of forecasting than the model based on the data of 2006-2015 had. Conclusion The establishment and prediction of ARIMA model is a dynamic process, which needs to be adjusted unceasingly according to the accumulated data, and in addition, the major changes of epidemic characteristics of infectious diseases must be considered.


Assuntos
Previsões , Malária/epidemiologia , Modelos Estatísticos , China/epidemiologia , Humanos , Incidência
3.
J Biol Chem ; 272(30): 19046-50, 1997 Jul 25.
Artigo em Inglês | MEDLINE | ID: mdl-9228088

RESUMO

O-Linked fucose is an unusual form of glycosylation recently shown to modify the hydroxyls of serine or threonine residues at a strict consensus site within epidermal growth factor-like domains of several serum proteins. Here we demonstrate that Chinese hamster ovary cells modify numerous proteins with O-linked fucose and that the fucose is elongated on specific proteins. We have identified at least two forms of O-linked fucose elongation in Chinese hamster ovary cells: a disaccharide (Glcbeta1,3Fuc) and a larger oligosaccharide of indeterminate structure. Interestingly, it appears that the level of monosaccharide accumulates in the cells over time whereas the disaccharide does not. Analysis of the O-linked fucose-containing saccharides on individual proteins revealed that some proteins are modified with the monosaccharide only, whereas others are modified with monosaccharide and disaccharide, or monosaccharide and oligosaccharide. These results suggest that elongation of the O-linked fucose monosaccharide is a protein-specific phenomena. The presence of elongated O-linked fucose moieties suggests that a novel glycosylation pathway exists in mammalian cells with O-linked fucose as the core.


Assuntos
Fucose/metabolismo , Amidoidrolases/metabolismo , Animais , Células CHO , Configuração de Carboidratos , Sequência de Carboidratos , Cromatografia em Gel , Cricetinae , Feminino , Glicosilação , Modelos Biológicos , Dados de Sequência Molecular , Ovário/metabolismo , Elongação Traducional da Cadeia Peptídica , Peptídeo-N4-(N-acetil-beta-glucosaminil) Asparagina Amidase
4.
Glycobiology ; 4(6): 895-901, 1994 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-7734851

RESUMO

During studies on the fucosylation of endogenous proteins in parental (Pro5) and N-acetyl-D-glucosamine (GlcNAc) transferase I-deficient (Lec1) Chinese hamster ovary (CHO) cells, we observed that Lec1 cells incorporate approximately 10-fold less [3H]fucose into macromolecules than Pro5 cells. Interestingly, most of the labelled oligosaccharides from both cell types could be released from the macromolecules by digestion with peptide N-glycosidase F (PNGase F). This was unexpected for Lec1 cells because they do not synthesize complex- or hybrid-type N-glycans. Structural analyses of the fucosylated oligosaccharides from Lec1 cells showed the fucose to be in an alpha 1,6 linkage to the core GlcNAc of relatively small oligomannose N-glycans (Man4GlcNAc2 and Man5GlcNAc2, where Man is D-mannose). Comparing the sizes of oligomannose N-glycans from Pro5 and Lec1 cells demonstrated a much higher proportion of the small (Man4GlcNAc2 and Man5GlcNAc2) oligomannose species in Lec1 cells. These results suggest that the core alpha 1,6 fucosyltransferase will fucosylate small (Man4-Man5GlcNAc2), but not large (Man8-Man9GlcNAc2) oligomannose N-glycans.


Assuntos
Fucose/metabolismo , Manose/metabolismo , N-Acetilglucosaminiltransferases/deficiência , Oligossacarídeos/metabolismo , Animais , Células CHO , Sequência de Carboidratos , Cricetinae , Fucose/química , Glicoproteínas/química , Glicoproteínas/metabolismo , Manose/química , Dados de Sequência Molecular , Oligossacarídeos/química , Polissacarídeos/química , Polissacarídeos/metabolismo
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