Link Aggregation

Trade and world economic integration are seen as the impetus for accelerating the well-beings of the domestic Vietnamese communities and international community in the region. However, an understanding of the link between trade and economic integration from the perspective of Vietnam is missing. Empirical studies on Vietnamese trade are in lack to address these determinants (see, Le, 1996; Nguyen, 2010). This thesis identifies the key factors that have driven the impressive growth of Vietnamese exports during the world economic integration process (1986-2010).

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After studying this chapter you will be able to: Explain the operation of link aggregation in a switched LAN environment, describe EtherChannel technology, configure link aggregation to improve performance on high-traffic switch links, configure link aggregation with EtherChannel, verify and troubleshoot link aggregation with EtherChannel.

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Chapter 5 explain the operation of link aggregation in a switched LAN environment, describe EtherChannel technology, configure link aggregation to improve performance on high-traffic switch links, configure link aggregation with EtherChannel, verify and troubleshoot link aggregation with EtherChannel.

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Bài giảng "Một số hướng nghiên cứu và ứng dụng" do Lê Thanh Hương cung cấp cho người đọc các nội dung: Web ngữ nghĩa, những gì có thể làm được, các loại ứng dụng, what needs to be done, aggregation Inference example, application patterns,... Mời các bạn cùng tham khảo.

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Misfolded proteins, aggregates, and inclusion bodies are hall-marks of the cytopathology of neurodegenerative disorders including Huntington’s disease, Amyotropic lateral sclerosis, Parkinson’s disease, Prion diseases, and Alzheimer’s disease. The appearance of proteins with altered folded states is regula-ted by the protein folding quality control machinery and age-dependent. We have identified an unexpected molecular link between metabolic state, accumulation of damaged proteins, the heat-shock response and chaperones, and longevity....

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The unfolding process of the Blue Copper Protein (BCP) rusticyanin (Rc) has been studied using a wide variety of biochemical techniques. Fluorescence and CD spectroscop-ies reveal that the copper ion plays an essential role in sta-bilizing the protein and that the oxidized form is more efficient than the reducedspecies in this respect. Theaddition of guanidinium chloride to Rc samples produces aggrega-tion of the protein. Gel filtration chromatography and glutaraldehyde cross-linking experiments confirm the for-mation of such aggregates. ...

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Protein misfolding and deposition underlie an increasing number of debili-tating human disorders. Alzheimer’s disease is pathologically characterized by the presence of numerous insoluble amyloid plaques in the brain, com-posed primarily of the 42 amino acid humanb-amyloid peptide (Ab42). Disease-linked mutations in Ab42 occur in or near a central hydrophobic cluster comprising residues 17–21.

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a-synuclein is one of a family of proteins whose function remains unknown. This protein has become linked to a number of neurodegenera-tive disease although its potential causative role in these diseases remains mysterious. In diseases such as Parkinson’s disease and Lewy body demen-tias, a-synuclein becomes deposited in aggregates termed Lewy bodies.

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Accumulation ofa-synuclein resulting in the formation of oligomers and protofibrils has been linked to Parkinson’s disease and Lewy body demen-tia. In contrast, b-synuclein (b-syn), a close homologue, does not aggregate and reducesa-synuclein (a-syn)-related pathology.

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As limited structural information is available on prion protein (PrP) mis-folding and aggregation, a causative link between the specific (supra)mole-cular structure of PrP and transmissible spongiform encephalopathies remains to be elucidated.

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Protein aggregation can proceed via disordered or ordered mechanisms, with the latter being associated with amyloid fibril formation, which has been linked to a number of debilitating conditions including Alzheimer’s, Parkinson’s and Creutzfeldt-Jakob diseases. Small heat-shock proteins (sHsps), such as aB-crystallin, act as chaperones to prevent protein aggre-gation and are thought to play a key role in the prevention of protein-mis-folding diseases.

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Fragile X mental retardation protein (FMRP) is an RNA binding protein necessary for correct spatiotemporal control of neuronal gene expression in humans. Lack of functional FMRP causes fragile X mental retardation, which is the most common inherited neurodevelopmental disorder in humans.

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