Vanillin Affects Amyloid Aggregation and Non-Enzymatic Glycation in Human Insulin.

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Vanillin Affects Amyloid Aggregation and Non-Enzymatic Glycation in Human Insulin.

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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2017年學術文章

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Vanillin Affects Amyloid Aggregation and Non-Enzymatic Glycation in Human Insulin.

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Vanillin Affects Amyloid Aggregation and Non-Enzymatic Glycation in Human Insulin.

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Vanillin Affects Amyloid Aggregation and Non-Enzymatic Glycation in Human Insulin.

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Vanillin Affects Amyloid Aggregation and Non-Enzymatic Glycation in Human Insulin.

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Vanillin Affects Amyloid Aggregation and Non-Enzymatic Glycation in Human Insulin.

@en

Vanillin Affects Amyloid Aggregation and Non-Enzymatic Glycation in Human Insulin.

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P1476

Vanillin Affects Amyloid Aggregation and Non-Enzymatic Glycation in Human Insulin

@en

P2093

Clara Iannuzzi

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Gaetano Irace

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Marcella Cammarota

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Margherita Borriello

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P2860

The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds

Curcumin and its derivatives: their application in neuropharmacology and neuroscience in the 21st century

Molecular basis for insulin fibril assembly

A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils

Advanced glycation end products and diabetic complications

Protein misfolding, functional amyloid, and human disease

Bioavailability of curcumin: problems and promises

Molecular mechanism of Thioflavin-T binding to amyloid fibrils

The role of assembly in insulin's biosynthesis

Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo

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15086

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scholarly article

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10.1038/S41598-017-15503-5

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P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Antimo Di Maro

Ivana Sirangelo

P577

2017-11-08T00:00:00Z

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P698

29118444

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P932

5678370

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