From Peptide Fragments to Whole Protein: Copper(II) Load and Coordination Features of IAPP.

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From Peptide Fragments to Whole Protein: Copper(II) Load and Coordination Features of IAPP.

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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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From Peptide Fragments to Whole Protein: Copper

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From Peptide Fragments to Whol ...... Coordination Features of IAPP.

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From Peptide Fragments to Whole Protein: Copper

@nl

From Peptide Fragments to Whol ...... Coordination Features of IAPP.

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From Peptide Fragments to Whole Protein: Copper

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From Peptide Fragments to Whol ...... Coordination Features of IAPP.

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P1476

From Peptide Fragments to Whol ...... Coordination Features of IAPP.

@en

P2093

Adriana Pietropaolo

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Diego La Mendola

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Giovanni Tabbì

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P2860

NMR solution structure of rat aβ(1-16): toward understanding the mechanism of rats' resistance to Alzheimer's disease

Structures of rat and human islet amyloid polypeptide IAPP(1-19) in micelles by NMR spectroscopy

A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity

Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation

The aggregation potential of human amylin determines its cytotoxicity towards islet beta-cells.

Environmental factors differently affect human and rat IAPP: conformational preferences and membrane interactions of IAPP17-29 peptide derivatives.

Copper(II)-human amylin complex protects pancreatic cells from amylin toxicity.

Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology.

Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspective

Tissue expression and secretion of amylin.

P304

17898-17902

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P31

scholarly article

P356

10.1002/CHEM.201704910

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P407

English

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P478

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P50

P577

2017-11-07T00:00:00Z

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P698

29111583

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