Arg354 in the catalytic centre of bovine liver catalase is protected from methylglyoxal-mediated glycation.

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Arg354 in the catalytic centre of bovine liver catalase is protected from methylglyoxal-mediated glycation.

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2015 nî lūn-bûn

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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Arg354 in the catalytic centre ...... hylglyoxal-mediated glycation.

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Arg354 in the catalytic centre ...... hylglyoxal-mediated glycation.

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Arg354 in the catalytic centre ...... hylglyoxal-mediated glycation.

@ast

Arg354 in the catalytic centre ...... hylglyoxal-mediated glycation.

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Arg354 in the catalytic centre ...... hylglyoxal-mediated glycation.

@ast

Arg354 in the catalytic centre ...... hylglyoxal-mediated glycation.

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P1476

Arg354 in the catalytic centre ...... thylglyoxal-mediated glycation

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P2093

Christian Q Scheckhuber

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P2860

Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism

Glutathione metabolism and its selective modification

Identification of the binding site of methylglyoxal on glutathione peroxidase: methylglyoxal inhibits glutathione peroxidase activity via binding to glutathione binding sites Arg 184 and 185.

Methylglyoxal modification of protein. Chemical and immunochemical characterization of methylglyoxal-arginine adducts.

Selective vulnerability of spinal motor neurons to reactive dicarbonyl compounds, intermediate products of glycation, in vitro: implication of inefficient glutathione system in spinal motor neurons.

The formation of methylglyoxal from triose phosphates. Investigation using a specific assay for methylglyoxal.

Advanced glycation end products, their receptors and diabetic angiopathy.

Electron crystallography of ultrathin 3D protein crystals: atomic model with charges

Advanced glycation end products: sparking the development of diabetic vascular injury.

Methylglyoxal, the dark side of glycolysis

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s13104-015-1793-5

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scholarly article

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10.1186/S13104-015-1793-5

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Christian Q Scheckhuber

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2015-12-30T00:00:00Z

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