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maackia amurensis/противгабичен лек
Врската е зачувана во таблата со исечоци
Страница 1 од 16 резултати
Application of partial-filling capillary electrophoresis using lectins and glycosidases for the characterization of oligosaccharides in a therapeutic antibody.
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Oligosaccharides in therapeutic recombinant antibodies play important roles in regulation of various biological functions. To monitor the glycosylation profiles of antibody pharmaceuticals in the manufacturing process, a highly sensitive and specific method is required. We extended partial-filling
New Therapeutic Strategies for Osteoarthritis by Targeting Sialic Acid Receptors.
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Osteoarthritis (OA) is the most common degenerative joint disease characterized by articular cartilage degradation and joint degeneration. The articular cartilage is mainly formed by chondrocytes and a collagen-proteoglycan extracellular matrix that contains high levels of glycosylated proteins. It
Apoptosis induction by Maackia amurensis agglutinin in childhood acute lymphoblastic leukemic cells.
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Malignant transformation is known to be associated with changes in cell surface carbohydrate-architecture, which can be detected by lectins. In the present study, Maackia amurensis agglutinin (MAA), specific for NeuNAcalpha(2-->3)Gal/GalNAc showed strong binding with lymphoblasts of children having
Maackia amurensis agglutinin enhances paclitaxel induced cytotoxicity in cultured non-small cell lung cancer cells.
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Maackia amurensis agglutinin (MAA) is gaining recognition as the potential diagnostic agent for cancer. Previous studies from our laboratory have demonstrated that this lectin could interact specifically with the cells and biopsy samples of non-small cell lung cancer (NSCLC) origin but not with
Heat shock protein 60 is a disease-associated sialoglycoprotein in human non-small cell lung cancer.
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The diagnostic and therapeutic potential of Maackia amurensis agglutinin (MAA) have been reported in various malignancies. Earlier, we have found that MAA specifically interacted with human non-small cell lung-cancer (NSCLC) cells and induced apoptosis in these cells. The present study was designed
Elimination of abnormal sialylglycoproteins in fibroblasts with sialidosis and galactosialidosis by normal gene transfer and enzyme replacement.
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Sialidosis and galactosialidosis are lysosomal storage diseases caused by the genetic defects of lysosomal sialidase (neuraminidase-1; NEU1) and lysosomal protective protein/cathepsin A (PPCA), respectively, associated with a NEU1 deficiency, excessive accumulation of sialylglycoconjugates, and
A quantitative, high-throughput method identifies protein-glycan interactions via mass spectrometry.
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Glycan binding by glycan-binding proteins and processing by carbohydrate-active enzymes is implicated in physiological and pathophysiological processes. Comprehensive mapping of glycan interactions is essential to understanding of glycan-mediated biology and can guide the development of new
Differences in carbohydrate composition of FSH preparations detected with lectin-ELISA systems.
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FSH is a glycoprotein containing N-linked carbohydrates which exhibit a variety of forms ranging from mono- to multibranched structures. Variation in glycosylation, particularly the degree of terminal sialylation, determines the half-life of the hormone and hence its in vivo bioactivity. The
A quantitative, high-throughput method identifies protein-glycan interactions via mass spectrometry.
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Glycan binding by glycan-binding proteins and processing by carbohydrate-active enzymes is implicated in physiological and pathophysiological processes. Comprehensive mapping of glycan interactions is essential to understanding of glycan-mediated biology and can guide the development of new
[Hepatoprotector properties of polyphenolic complexes from wood and cell culture of Maackia amurensis].
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Polyphenolic complexes (PPCs) extracted from core wood and cell culture of Maackia amurensis decrease the acute toxicity of tetrachloromethane, suppress the necrosis of hepatocytes and the cellular infiltration in liver parenchyma, prevent the development of fatty and protein dystrophy in the liver,
The effect of plant lectins on the survival and malignant behaviors of thyroid cancer cells.
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Altered or aberrant glycosylation is a common phenomenon in cancer cells and it originates from changes in the expression of the enzymes, glycosyltransferase, and glycosidase which up-regulate in response to some oncogenes in the glycan synthesis pathway. In this present study, it has been aimed to
Enhanced expression of α2,3-linked sialic acids promotes gastric cancer cell metastasis and correlates with poor prognosis.
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Gastric cancer (GC) is a highly metastatic disease and one of the leading causes of cancer death in the world. Aberrant glycosylation is one of many molecular changes that accompany malignant transformation. This study was aimed at identification of glycan profiling changes in GC progression and its
Differential expression of the α2,3-sialic acid residues in breast cancer is associated with metastatic potential.
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Aberrant sialylation is closely associated with the malignant phenotype of cancer cells and metastatic potential. However, the precise nature of the molecules in breast cancers has not been unveiled. In this study, we investigated the expression levels of α2,3-sialic acid residues of 50 primary
Topical administration of interleukin-1 receptor antagonist as a therapy for aqueous-deficient dry eye in autoimmune disease.
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OBJECTIVE
Dry eye is commonly associated with autoimmune diseases such as Sjögren's syndrome (SS), in which exocrinopathy of the lacrimal gland leads to aqueous tear deficiency and keratoconjunctivitis sicca (KCS). KCS is among the most common and debilitating clinical manifestations of SS that is
The blood-brain barrier transmigrating single domain antibody: mechanisms of transport and antigenic epitopes in human brain endothelial cells.
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Antibodies against receptors that undergo transcytosis across the blood-brain barrier (BBB) have been used as vectors to target drugs or therapeutic peptides into the brain. We have recently discovered a novel single domain antibody, FC5, which transmigrates across human cerebral endothelial cells
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