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Pesquisa : G02.111.570.160 [Categoria DeCS]
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  1 / 20359 MEDLINE  
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[PMID]:28659043
[Au] Autor:Liu X; Zhang J; Guo K; Jia A; Zhang M; Shi Y; Liu C; Xiao L; Sun Z
[Ad] Endereço:a Key Laboratory for Biosensors of Shandong Province , Biology Institute of Shandong Academy of Sciences , Jinan , China.
[Ti] Título:Three new oleanane-type triterpenoid saponins from the seeds of Celosia cristata L.
[So] Source:Nat Prod Res;32(2):167-174, 2018 Jan.
[Is] ISSN:1478-6427
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Phytochemical investigation of the 1-butanol soluble fraction of 60% ethanol extract of the seeds of Celosia cristata L. led to the identification of three new oleanane-type triterpenoid saponins. Using D and D NMR experiment methods, ESI-MS analysis and acid hydrolysis, their structures were identified as 3-O-[ß-D-xylopyranosyl-(1 â†’ 3)-ß-D-glucuronopyranosyl]-2ß-hydroxy-oleanolic acid-28-O-ß-D-glucopyranoside (1), 3-O-[ß-D-xylopyranosyl-(1 â†’ 3)-ß-D-glucuronopyranosyl]-2ß, 23-dihydroxy-oleanolic acid-28-O-ß-D-glucopyranoside (2) and 3-O-[ß-D-glucopyranosyl-(1 â†’ 4)-ß-D-glucopyranosyl]-2-hydroxyl-medicagenic acid-28-O-ß-D-glucopyranosyide (3), respectively.
[Mh] Termos MeSH primário: Celosia/química
Ácido Oleanólico/análogos & derivados
Ácido Oleanólico/isolamento & purificação
Saponinas/isolamento & purificação
[Mh] Termos MeSH secundário: Configuração de Carboidratos
Sequência de Carboidratos
Hidrólise
Espectroscopia de Ressonância Magnética
Estrutura Molecular
Ácido Oleanólico/química
Saponinas/química
Sementes/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Saponins); 0 (oleanane); 6SMK8R7TGJ (Oleanolic Acid)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180228
[Lr] Data última revisão:
180228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170630
[St] Status:MEDLINE
[do] DOI:10.1080/14786419.2017.1343317


  2 / 20359 MEDLINE  
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[PMID]:28745644
[Au] Autor:Leviatan Ben-Arye S; Yu H; Chen X; Padler-Karavani V
[Ad] Endereço:Department of Cell Research and Immunology, Tel Aviv University.
[Ti] Título:Profiling Anti-Neu5Gc IgG in Human Sera with a Sialoglycan Microarray Assay.
[So] Source:J Vis Exp;(125), 2017 Jul 13.
[Is] ISSN:1940-087X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cells are covered with a cloak of carbohydrate chains (glycans) that is commonly altered in cancer and that includes variations in sialic acid (Sia) expression. These are acidic sugars that have a 9-carbon backbone and that cap vertebrate glycans on cell surfaces. Two of the major Sia forms in mammals are N-acetylneuraminic acid (Neu5Ac) and its hydroxylated form, N-glycolylneuraminic acid (Neu5Gc). Humans cannot produce endogenous Neu5Gc due to the inactivation of the gene encoding cytidine 5'monophosphate-Neu5Ac (CMP-Neu5Ac) hydroxylase (CMAH). Foreign Neu5Gc is acquired by human cells through the dietary consumption of red meat and dairy and subsequently appears on diverse glycans on the cell surface, accumulating mostly on carcinomas. Consequently, humans have circulating anti-Neu5Gc antibodies that play diverse roles in cancer and other chronic inflammation-mediated diseases and that are becoming potential diagnostic and therapeutic targets. Here, we describe a high-throughput sialoglycan microarray assay to assess such anti-Neu5Gc antibodies in the human sera. Neu5Gc-containing glycans and their matched pairs of controls (Neu5Ac-containing glycans), each with a core primary amine, are covalently linked to epoxy-coated glass slides. We exemplify the printing of 56 slides in a 16-well format using a specific nano-printer capable of generating up to 896 arrays per print. Each slide can be used to screen 16 different human sera samples for the evaluation of anti-Neu5Gc antibody specificity, intensity, and diversity. The protocol describes the complexity of this robust tool and provides a basic guideline for those aiming to investigate the response to Neu5Gc dietary carbohydrate antigen in diverse clinical samples in an array format.
[Mh] Termos MeSH primário: Imunoglobulina G/sangue
Ácidos Neuramínicos/imunologia
Análise Serial de Proteínas
[Mh] Termos MeSH secundário: Animais
Especificidade de Anticorpos
Sequência de Carboidratos
Ensaios de Triagem em Larga Escala
Seres Humanos
Imunoensaio
Gravação em Vídeo
[Pt] Tipo de publicação:JOURNAL ARTICLE; VIDEO-AUDIO MEDIA
[Nm] Nome de substância:
0 (Immunoglobulin G); 0 (Neuraminic Acids); 1113-83-3 (N-glycolylneuraminic acid)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180126
[Lr] Data última revisão:
180126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.3791/56094


  3 / 20359 MEDLINE  
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[PMID]:28460348
[Au] Autor:Sizova OV; Kondakova AN; Shashkov AS; Knirel YA; Shaikhutdinova RZ; Ivanov SA; Platonov ME; Hurst MRH; Dentovskaya SV
[Ad] Endereço:N. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, 119991, Moscow, Russian Federation.
[Ti] Título:Structure and gene cluster of a tyvelose-containing O-polysaccharide of an entomopathogenic bacterium Yersinia entomophaga MH96 related to Yersinia pseudotuberculosis.
[So] Source:Carbohydr Res;445:93-97, 2017 Jun 05.
[Is] ISSN:1873-426X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:An O-polysaccharide was isolated from the lipopolysaccharide of an entomopathogenic bacterium Yersinia entomophaga MH96 by mild acid hydrolysis and studied by 2D NMR spectroscopy. The following structure of the branched tetrasaccharide repeating unit of the polysaccharide was established: where Tyv indicates 3,6-dideoxy-d-arabino-hexose (tyvelose). The structure established is consistent with the gene content of the O-antigen gene cluster. The O-polysaccharide structure and gene cluster of Y. entomophaga are related to those of some Y. pseudotuberculosis serotypes.
[Mh] Termos MeSH primário: Hexoses/química
Família Multigênica
Antígenos O/química
Yersinia pseudotuberculosis/química
Yersinia pseudotuberculosis/genética
[Mh] Termos MeSH secundário: Sequência de Carboidratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hexoses); 0 (O Antigens); 5658-12-8 (tyvelose)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180125
[Lr] Data última revisão:
180125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE


  4 / 20359 MEDLINE  
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[PMID]:29236390
[Au] Autor:Pismenetskaya IU; Butters TD
[Ti] Título:Serum glycomarkers of endoplasmic reticulum and lysosomal-endosomal system stress in human healthy aging and diseases.
[So] Source:Ukr Biochem J;89(1):59-70, 2017 Jan-Feb.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:To verify the idea that extracellular free oligosaccharides might be able to reflect the functional status of the endoplasmic reticulum (ER) and lysosomal-endosomal system, HPLC-profiles of serum-derived free oligosaccharides (FOS) in human healthy aging, acute myeloproliferative neoplasms, and cardiovascular pathologies were compared with intracellular glycans. After plasma deproteinization and FOS purification the oligosaccharides were labelled with anthranilic acid, separated into the neutral and charged with QAE Sephadex (Q25-120) chromatography and analysed using high-performance liquid chromatography (HPLC). The charged FOS were digested with a sialidase and compared with free oligosaccharides from transferrin for structural decoding. HPLC-profiles of serum-derived FOS revealed mild delay of the dolichol phosphate cycle in ER, moderate intensification of ER-associated degradation (ERAD) and degradation in endosomal-lysosomal system with aging; an inhibition of the dolichol phosphate cycle, intensification of ERAD and increasing of lysosomal exocytosis in acute myeloproliferative neoplasms; intensification of ERAD and glycocojugate degradation with endosomal-lysosomal system in cardiovascular diseases. As serum free oligosaccharides are able to reflect specifically perturbations in ER and endosomal-lysosomal system under wide range of stressors they can serve as extracellular markers of functionality of these organelles.
[Mh] Termos MeSH primário: Doenças Cardiovasculares/sangue
Fosfatos de Dolicol/sangue
Degradação Associada com o Retículo Endoplasmático
Glicoconjugados/sangue
Envelhecimento Saudável/sangue
Transtornos Mieloproliferativos/sangue
Oligossacarídeos/sangue
[Mh] Termos MeSH secundário: Biomarcadores/sangue
Biomarcadores/química
Sequência de Carboidratos
Doenças Cardiovasculares/diagnóstico
Estudos de Casos e Controles
Retículo Endoplasmático/metabolismo
Endossomos/metabolismo
Glicosilação
Seres Humanos
Lisossomos/metabolismo
Transtornos Mieloproliferativos/diagnóstico
Oligossacarídeos/química
Coloração e Rotulagem/métodos
ortoaminobenzoatos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Dolichol Phosphates); 0 (Glycoconjugates); 0 (Oligosaccharides); 0 (ortho-Aminobenzoates); 0YS975XI6W (anthranilic acid)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE
[do] DOI:10.15407/ubj89.01.059


  5 / 20359 MEDLINE  
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[PMID]:28465241
[Au] Autor:Kizuka Y; Kitazume S; Taniguchi N
[Ad] Endereço:Disease Glycomics Team, Systems Glycobiology Research Group, Global Research Cluster, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. Electronic address: y.kizuka@riken.jp.
[Ti] Título:N-glycan and Alzheimer's disease.
[So] Source:Biochim Biophys Acta;1861(10):2447-2454, 2017 10.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Alzheimer's disease (AD) is a major form of dementia. Many evidence-based clinical trials have been performed, but no effective treatment has yet been developed. This suggests that our understanding of AD patho-mechanisms is still insufficient. In particular, the pathological roles of posttranslational modifications including glycosylation have remained poorly understood, but recent advances in glycobiology technology have gradually revealed that sugar modifications of AD-related molecules are profoundly involved in the onset and progression of this disease. SCOPE OF REVIEW: We summarize the roles of N-glycans in AD pathogenesis and progression, particularly focusing on key AD-related molecules, including amyloid precursor protein (APP), α-, ß-, and γ-secretases, and tau. MAJOR CONCLUSIONS: Biochemical, genetic and pharmacological studies have gradually revealed how N-glycans regulate AD development and progression through functional modulation of the key glycoproteins. These findings suggest that further glycobiology approaches in AD research will reveal novel glycan-based drug targets and early biomarkers of AD. However, N-glycan structures of these molecules in physiological and disease conditions and their precise functions are still largely unclear. Deeper glycobiology studies will be needed to reveal how AD pathology is regulated by glycosylation. GENERAL SIGNIFICANCE: It is now known that N-glycans play significant roles in AD development. However, specific pathological functions of particular glycan epitopes on each AD-related glycoprotein are still poorly understood. Future glycobiology studies with more sensitive glycoproteomic techniques and a wider variety of chemical glycosylation inhibitors could contribute to the development of novel glycan-based AD therapeutics. This article is part of a Special Issue entitled Neuro-glycoscience, edited by Kenji Kadomatsu and Hiroshi Kitagawa.
[Mh] Termos MeSH primário: Doença de Alzheimer/metabolismo
Secretases da Proteína Precursora do Amiloide/metabolismo
Precursor de Proteína beta-Amiloide/metabolismo
Polissacarídeos/metabolismo
Processamento de Proteína Pós-Traducional
Proteínas tau/metabolismo
[Mh] Termos MeSH secundário: Doença de Alzheimer/genética
Doença de Alzheimer/patologia
Secretases da Proteína Precursora do Amiloide/genética
Precursor de Proteína beta-Amiloide/genética
Sequência de Carboidratos
Glicosilação
Seres Humanos
Glicoproteínas de Membrana/genética
Glicoproteínas de Membrana/metabolismo
Neprilisina/genética
Neprilisina/metabolismo
Polissacarídeos/química
Proteólise
Receptores Imunológicos/genética
Receptores Imunológicos/metabolismo
Transdução de Sinais
Proteínas tau/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (APP protein, human); 0 (Amyloid beta-Protein Precursor); 0 (MAPT protein, human); 0 (Membrane Glycoproteins); 0 (Polysaccharides); 0 (Receptors, Immunologic); 0 (TREM2 protein, human); 0 (tau Proteins); EC 3.4.- (Amyloid Precursor Protein Secretases); EC 3.4.24.11 (Neprilysin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171130
[Lr] Data última revisão:
171130
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE


  6 / 20359 MEDLINE  
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[PMID]:28741461
[Au] Autor:Griffin LS; Gloster TM
[Ad] Endereço:Biomedical Sciences Research Complex, North Haugh, University of St. Andrews, St. Andrews, KY16 9ST. United Kingdom.
[Ti] Título:The Enzymatic Degradation of Heparan Sulfate.
[So] Source:Protein Pept Lett;24(8):710-722, 2017.
[Is] ISSN:1875-5305
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Glycosaminoglycans (GAGs) such as heparan sulfate (HS) interact with a number of factors in the extracellular matrix (ECM) and as a consequence play a key role in the metabolic processes occurring within the cell. The dynamic synthesis and degradation of HS (and all GAGs) are necessary for ensuring that optimal chains are present for these functions. The degradation of HS begins at the cell surface and finishes in the lysosome, after which components can be recycled. Deficiencies or mutations in the lysosomal enzymes that process GAGs result in rare Mucopolysaccharidoses disorders (MPSs). There are few treatments available for these genetically inherited diseases and those that are available often do not treat the neurological symptoms of the disease. In this review, we discuss the enzymes involved in the degradation of HS and their related diseases, with emphasis on those located in the lysosome.
[Mh] Termos MeSH primário: Matriz Extracelular/enzimologia
Heparitina Sulfato/metabolismo
Lisossomos/enzimologia
Mucopolissacaridoses/enzimologia
[Mh] Termos MeSH secundário: Sequência de Carboidratos
Expressão Gênica
Glicosídeo Hidrolases/deficiência
Glicosídeo Hidrolases/genética
Seres Humanos
Lisossomos/patologia
Mucopolissacaridoses/genética
Mucopolissacaridoses/patologia
Sulfatases/deficiência
Sulfatases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
9050-30-0 (Heparitin Sulfate); EC 3.1.6.- (Sulfatases); EC 3.2.1.- (Glycoside Hydrolases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.2174/0929866524666170724113452


  7 / 20359 MEDLINE  
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[PMID]:28958711
[Au] Autor:Xu L; Zhang Z; Sun X; Wang J; Xu W; Shi L; Lu J; Tang J; Liu J; Su X
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Soochow University Medical College, Suzhou 215123, China. Electronic address: xulan@suda.edu.cn.
[Ti] Título:Glycosylation status of bone sialoprotein and its role in mineralization.
[So] Source:Exp Cell Res;360(2):413-420, 2017 Nov 15.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The highly glycosylated bone sialoprotein (BSP) is an abundant non-collagenous phosphoprotein in bone which enhances osteoblast differentiation and new bone deposition in vitro and in vivo. However, the structural details of its different glycosylation linkages have not been well studied and their functions in bone homeostasis are not clear. Previous studies suggested that the O-glycans, but not the N-glycans on BSP, are highly sialylated. Herein, we employed tandem mass spectrometry (MS/MS) to demonstrate that the N-glycanson the recombinant human integrin binding sialoprotein (rhiBSP) are also enriched in sialic acids (SAs) at their termini. We also identified multiple novel sites of N-glycan modification. Treatment of rhiBSP enhances osteoblast differentiation and mineralization of MC3T3-E1 cells and this effect could be partially reversed by efficient enzymatic removal of its N-glycans. Removal of all terminal SAs has a greater effect in reversing the effect of rhiBSP on osteogenesis, especially on mineralization, suggesting that sialylation at the termini of both N-glycans and O-glycans plays an important role in this regulation. Moreover, BSP-conjugated SAs may affect mineralization via ERK activation of VDR expression. Collectively, our results identified novel N-glycans enriched in SAs on the rhiBSP and demonstrated that SAs at both N- and O-glycans are important for BSP regulation of osteoblast differentiation and mineralization in vitro.
[Mh] Termos MeSH primário: Osso e Ossos/metabolismo
Calcificação Fisiológica
Osteoblastos/metabolismo
Sialoglicoproteínas/metabolismo
[Mh] Termos MeSH secundário: Animais
Metabolismo dos Carboidratos
Sequência de Carboidratos
Linhagem Celular
Glicosilação
Camundongos
Polissacarídeos/metabolismo
Processamento de Proteína Pós-Traducional
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polysaccharides); 0 (Sialoglycoproteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170930
[St] Status:MEDLINE


  8 / 20359 MEDLINE  
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[PMID]:28816453
[Au] Autor:Turupcu A; Oostenbrink C
[Ad] Endereço:Institute of Molecular Modeling and Simulation, University of Natural Resources and Life Sciences , Muthgasse 18, 1190 Vienna, Austria.
[Ti] Título:Modeling of Oligosaccharides within Glycoproteins from Free-Energy Landscapes.
[So] Source:J Chem Inf Model;57(9):2222-2236, 2017 Sep 25.
[Is] ISSN:1549-960X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In spite of the abundance of glycoproteins in biological processes, relatively little three-dimensional structural data is available for glycan structures. Here, we study the structure and flexibility of the vast majority of mammalian oligosaccharides appearing in N- and O-glycosylated proteins using a bottom up approach. We report the conformational free-energy landscapes of all relevant glycosidic linkages as obtained from local elevation simulations and subsequent umbrella sampling. To the best of our knowledge, this represents the first complete conformational library for the construction of N- and O-glycan structures. Next, we systematically study the effect of neighboring residues, by extensively simulating all relevant trisaccharides and one tetrasaccharide. This allows for an unprecedented comparison of disaccharide linkages in large oligosaccharides. With a small number of exceptions, the conformational preferences in the larger structures are very similar as in the disaccharides. This, finally, allows us to suggest several efficient approaches to construct complete N- and O-glycans on glycoproteins, as exemplified on two relevant examples.
[Mh] Termos MeSH primário: Glicoproteínas/química
Simulação de Dinâmica Molecular
Oligossacarídeos/química
[Mh] Termos MeSH secundário: Configuração de Carboidratos
Sequência de Carboidratos
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycoproteins); 0 (Oligosaccharides)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170818
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jcim.7b00351


  9 / 20359 MEDLINE  
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[PMID]:28800704
[Au] Autor:Wang T; Hu XC; Cai ZP; Voglmeir J; Liu L
[Ad] Endereço:Glycomics and Glycan Bioengineering Research Center, College of Food Science and Technology, Nanjing Agricultural University , Nanjing, Jiangsu 210014, China.
[Ti] Título:Qualitative and Quantitative Analysis of Carbohydrate Modification on Glycoproteins from Seeds of Ginkgo biloba.
[So] Source:J Agric Food Chem;65(35):7669-7679, 2017 Sep 06.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recent progress in the relationship between carbohydrate cross-reactive determinants (CCDs) and allergic response highlights the importance of carbohydrate moieties in the innate immune system. Previous research pointed out that the protein allergen in Ginkgo biloba seeds is glycosylated, and the oligosaccharides conjugated to these proteins might also contribute to the allergy. The aim of this study was to analyze carbohydrate moieties, especially N-linked glycans, of glycoproteins from Ginkgo seeds originating from different places for detailed structures, to enable further research on the role played by N-glycans in Ginkgo-caused allergy. Results of monosaccharide composition and immunoblotting assays indicated the existence of N-glycans. Detailed structural elucidation of the N-glycans was further carried out by means of hydrophilic interaction ultraperformance liquid chromatography (HILIC-UPLC) and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). In total, 14 out of 16 structures detected by UPLC were confirmed by MALDI-TOF-MS and tandem mass spectrometry, among which complex-type N-glycans bearing Lewis A determinants and high-mannose-type N-glycans were identified from Ginkgo seeds for the first time. Precise quantification of N-glycans was performed by use of an external standard, and both the absolute amount of each N-glycan and the percentage of different types of N-glycan showed significant diversity among the samples without any pattern of geographic variation.
[Mh] Termos MeSH primário: Ginkgo biloba/metabolismo
Glicoproteínas/metabolismo
Proteínas de Plantas/metabolismo
Sementes/química
[Mh] Termos MeSH secundário: Sequência de Carboidratos
Cromatografia Líquida de Alta Pressão
Ginkgo biloba/química
Glicoproteínas/química
Dados de Sequência Molecular
Proteínas de Plantas/química
Polissacarídeos/química
Polissacarídeos/metabolismo
Sementes/metabolismo
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycoproteins); 0 (Plant Proteins); 0 (Polysaccharides)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170813
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b01690


  10 / 20359 MEDLINE  
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[PMID]:28521605
[Au] Autor:Ogata M; Koizumi A; Otsubo T; Ikeda K; Sakamoto M; Aita R; Kato T; Park EY; Yamanaka T; Hidari KIPJ
[Ad] Endereço:a Department of Chemistry and Biochemistry, National Institute of Technology , Fukushima College , Iwaki , Japan.
[Ti] Título:Chemoenzymatic synthesis and characterization of N-glycolylneuraminic acid-carrying sialoglycopolypeptides as effective inhibitors against equine influenza virus hemagglutination.
[So] Source:Biosci Biotechnol Biochem;81(8):1520-1528, 2017 Aug.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A series of novel sialoglycopolypeptides carrying N-glycolylneuraminic acid (Neu5Gc)-containing trisaccharides having α(2 â†’ 3)- and α(2 â†’ 6)-linkages in the side chains of γ-polyglutamic acid (γ-PGA) were designed as competitive inhibitors against equine influenza viruses (EIV), which critically recognize the Neu5Gc residue for receptor binding. Using horse red blood cells (HRBC) we successfully evaluated the binding activity of the multivalent Neu5Gc ligands to both equine and canine influenza viruses in the hemagglutination inhibition (HI) assay. Our findings show the multivalent α2,3-linked Neu5Gc-ligands (3a-c and 7) selectively inhibit hemagglutination mediated by both influenza viruses and display a strong inhibitory activity. Our results indicate that the multivalent Neu5Gc-ligands can be used as novel probes to elucidate the mechanism of infection/adhesion of Neu5Gc-binding influenza viruses.
[Mh] Termos MeSH primário: Antivirais/farmacologia
Hemaglutinação/efeitos dos fármacos
Orthomyxoviridae/efeitos dos fármacos
Sialoglicoproteínas/farmacologia
Sialiltransferases/química
[Mh] Termos MeSH secundário: Animais
Antivirais/química
Antivirais/metabolismo
Ligação Competitiva
Bombyx
Sequência de Carboidratos
Clonagem Molecular
Cães
Eritrócitos/efeitos dos fármacos
Eritrócitos/virologia
Expressão Gênica
Testes de Inibição da Hemaglutinação
Hemolinfa/química
Cavalos
Seres Humanos
Ácidos Neuramínicos/química
Nucleopolyhedrovirus/genética
Nucleopolyhedrovirus/metabolismo
Ácido Poliglutâmico/análogos & derivados
Ácido Poliglutâmico/química
Ácido Poliglutâmico/metabolismo
Ratos
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Sialoglicoproteínas/biossíntese
Sialoglicoproteínas/química
Sialiltransferases/genética
Sialiltransferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (Neuraminic Acids); 0 (Recombinant Proteins); 0 (Sialoglycoproteins); 0 (poly(gamma-glutamic acid)); 1113-83-3 (N-glycolylneuraminic acid); 25513-46-6 (Polyglutamic Acid); EC 2.4.99.- (Sialyltransferases); EC 2.4.99.4 (beta-galactoside alpha-2,3-sialyltransferase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170520
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2017.1325315



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