Exploring the influence of EGCG on the β-sheet-rich oligomers of human islet amyloid polypeptide (hIAPP1-37) and identifying its possible binding sites from molecular dynamics simulation (Q35150371)

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English	Exploring the influence of EGCG on the β-sheet-rich oligomers of human islet amyloid polypeptide (hIAPP1-37) and identifying its possible binding sites from molecular dynamics simulation	scientific article

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scholarly article

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Europe PubMed Central

6 August 2017

Exploring the influence of EGCG on the β-sheet-rich oligomers of human islet amyloid polypeptide (hIAPP1-37) and identifying its possible binding sites from molecular dynamics simulation (English)

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Europe PubMed Central

6 August 2017

object named as

Jingjing Guo

2

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author name string

Qianqian Wang

1

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Europe PubMed Central

6 August 2017

Pingzu Jiao

3

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Europe PubMed Central

6 August 2017

Huanxiang Liu

4

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Europe PubMed Central

6 August 2017

Xiaojun Yao

5

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Europe PubMed Central

6 August 2017

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16 April 2014

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Europe PubMed Central

6 August 2017

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Europe PubMed Central

6 August 2017

9

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Europe PubMed Central

6 August 2017

4

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Europe PubMed Central

6 August 2017

e94796

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Europe PubMed Central

6 August 2017

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Creative Commons Attribution 4.0 International

16 April 2014

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April 2022 Public Data File from Crossref

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All-atom empirical potential for molecular modeling and dynamics studies of proteins

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Exploring the influence of carbon nanoparticles on the formation of β-sheet-rich oligomers of IAPP₂₂₋₂₈ peptide by molecular dynamics simulation.

1 reference

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Toward the molecular mechanism(s) by which EGCG treatment remodels mature amyloid fibrils

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Molecular dynamics simulations of amyloid fibrils: an in silico approach.

1 reference

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Probing ion channel activity of human islet amyloid polypeptide (amylin).

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1 reference

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Comparison of three amyloid assembly inhibitors: the sugar scyllo-inositol, the polyphenol epigallocatechin gallate, and the molecular tweezer CLR01

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Lipid interaction and membrane perturbation of human islet amyloid polypeptide monomer and dimer by molecular dynamics simulations.

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The effect of curcumin on the stability of Aβ dimers

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Small-molecule conversion of toxic oligomers to nontoxic β-sheet-rich amyloid fibrils

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

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Dewetting transitions in the self-assembly of two amyloidogenic β-sheets and the importance of matching surfaces

1 reference

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13 July 2018

EGCG disaggregates amyloid-like fibrils formed by Plasmodium falciparum merozoite surface protein 2

1 reference

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13 July 2018

Resveratrol inhibits the formation of multiple-layered β-sheet oligomers of the human islet amyloid polypeptide segment 22-27

1 reference

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13 July 2018

The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity.

1 reference

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13 July 2018

Residue-specific, real-time characterization of lag-phase species and fibril growth during amyloid formation: a combined fluorescence and IR study of p-cyanophenylalanine analogs of islet amyloid polypeptide

1 reference

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Direct observation of nucleation and growth in amyloid self-assembly

1 reference

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13 July 2018

EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3989243

13 July 2018

Exploration of the mechanism for LPFFD inhibiting the formation of beta-sheet conformation of A beta(1-42) in water.

1 reference

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13 July 2018

Molecular dynamics simulations of Ibuprofen binding to Abeta peptides

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3989243

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The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: insights from type II diabetes

1 reference

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13 July 2018

EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers

1 reference

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Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR.

1 reference

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Peptide fibrillization

1 reference

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Atomic structures of amyloid cross-beta spines reveal varied steric zippers

1 reference

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Monomer adds to preformed structured oligomers of Abeta-peptides by a two-stage dock-lock mechanism.

1 reference

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A century-old debate on protein aggregation and neurodegeneration enters the clinic

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Protein misfolding, functional amyloid, and human disease

1 reference

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Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide (IAPP) as nanomolar affinity inhibitor of IAPP cytotoxic fibrillogenesis

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Non-steroidal anti-inflammatory drugs have anti-amyloidogenic effects for Alzheimer's beta-amyloid fibrils in vitro

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Amyloid ion channels: a common structural link for protein-misfolding disease

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Molecular basis for amyloid fibril formation and stability

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Inhibition of islet amyloid polypeptide fibril formation: a potential role for heteroaromatic interactions

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Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases

1 reference

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Formation of partially ordered oligomers of amyloidogenic hexapeptide (NFGAIL) in aqueous solution observed in molecular dynamics simulations

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Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes

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Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in Alzheimer's disease

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Protein folding and misfolding

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A possible role for pi-stacking in the self-assembly of amyloid fibrils

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Aspirin and non-steroidal anti-inflammatory drugs inhibit amyloid-beta aggregation

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Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation

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Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3989243

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Comparative Molecular Dynamics Study of Human Islet Amyloid Polypeptide (IAPP) and Rat IAPP Oligomers

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1 reference

https://pubmed.ncbi.nlm.nih.gov/24739876

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Replica exchange molecular dynamics simulations of amyloid peptide aggregation

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Curcumin binds to Aβ1-40 peptides and fibrils stronger than ibuprofen and naproxen

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Molecular insight into conformational transition of amyloid β-peptide 42 inhibited by (-)-epigallocatechin-3-gallate probed by molecular simulations

1 reference

https://pubmed.ncbi.nlm.nih.gov/24739876

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1 reference

https://pubmed.ncbi.nlm.nih.gov/24739876

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based on heuristic

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https://pubmed.ncbi.nlm.nih.gov/24739876

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based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1371/JOURNAL.PONE.0094796

1 reference

Europe PubMed Central

6 August 2017

2014PLoSO...994796W

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1 reference

Europe PubMed Central

6 August 2017

1 reference

Europe PubMed Central

6 August 2017

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