Publications by authors named "E S X Moh"

Chondroitin sulphate (CS) is a sulphated glycosaminoglycan (GAG) polysaccharide found on proteoglycans (CSPGs) in extracellular and pericellular matrices. Chondroitinase ABC (CSase ABC) derived from Proteus vulgaris is an enzyme that has gained attention for the capacity to cleave chondroitin sulphate (CS) glycosaminoglycans (GAG) from various proteoglycans such as Aggrecan, Neurocan, Decorin etc. The substrate specificity of CSase ABC is well-known for targeting various structural motifs of CS chains and has gained popularity in the field of neuro-regeneration by selective degradation of CS GAG chains.

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Bioremediation of extremely high-chloride wastewater poses significant challenges due to the adverse effects of elevated salt concentrations on most microorganisms, where chloride levels can be as high as 7% (w/v). Mangrove wetlands derived fungus, Aspergillus aculeatus, emerged as a promising candidate, capable of removing approximately 40% of chloride ions in environments with concentration of 15% (w/v), representative of industrial wastewater conditions. Transcriptomics and biochemical assays conducted under increasing salt conditions revealed that elevated chloride concentrations induce the expression and activity of S-adenosyl methionine-dependent methyltransferase, which facilitates the conversion of chloride into chloromethane.

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Article Synopsis
  • Metabolic diseases like obesity and type 2 diabetes involve insulin resistance, particularly in neurons of the arcuate nucleus of the hypothalamus that help regulate metabolism.
  • The study highlights how the perineuronal net, an extracellular matrix that surrounds these neurons, becomes altered during metabolic diseases, contributing to insulin resistance.
  • Disrupting this protective net in obese mice improves brain insulin access, reverses insulin resistance in neurons, and boosts metabolic health, revealing extracellular matrix changes as critical to understanding metabolic diseases.
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The analysis of the structures of glycans present on glycoproteins is an essential component for determining glycoprotein function; however, detailed glycan structural assignment on glycopeptides from proteomics mass spectrometric data remains challenging. Glycoproteomic analysis by mass spectrometry currently can provide significant, yet incomplete, information about the glycans present, including the glycan monosaccharide composition and in some circumstances the site(s) of glycosylation. Advancements in mass spectrometric resolution, using high-mass accuracy instrumentation and tailored MS/MS fragmentation parameters, coupled with a dedicated definition of diagnostic fragmentation ions have enabled the determination of some glycan structural features, or glycotopes, expressed on glycopeptides.

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  • Synthetic vascular grafts often fail due to poor blood compatibility and narrowing, presenting a significant challenge in medical procedures.
  • The engineered form of perlecan domain V (rDV) enhances blood vessel healing by supporting the signaling of growth factors and promoting endothelial cell growth.
  • Testing on electrospun silk fibroin vascular grafts shows that coating them with rDV improves graft performance and encourages the formation of blood vessel lining in animal models.
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