Conformationally restricted short peptides inhibit human islet amyloid polypeptide (hIAPP) fibrillization. - Wikidata - wikimedia - TriplyDB

Conformationally restricted short peptides inhibit human islet amyloid polypeptide (hIAPP) fibrillization.

Conformationally restricted short peptides inhibit human islet amyloid polypeptide (hIAPP) fibrillization.

http://www.wikidata.org/entity/Q36935342

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Influence of Aluminium and EGCG on Fibrillation and Aggregation of Human Islet Amyloid Polypeptide Mechanism of Inhibition of Human Islet Amyloid Polypeptide-Induced Membrane Damage by a Small Organic Fluorogen.Inhibition of amyloid oligomerization into different supramolecular architectures by small molecules: mechanistic insights and design rules.Inhibitory Mechanism of Epigallocatechin Gallate on Fibrillation and Aggregation of Amidated Human Islet Amyloid Polypeptide.Rational design of an orthosteric regulator of hIAPP aggregation.Disaggregation of Amylin Aggregate by Novel Conformationally Restricted Aminobenzoic Acid containing α/β and α/γ Hybrid Peptidomimetics.Self-assembly of a nine-residue amyloid-forming peptide fragment of SARS corona virus E-protein: mechanism of self aggregation and amyloid-inhibition of hIAPP.Inhibition of Alzheimer's amyloid-β peptide aggregation and its disruption by a conformationally restricted α/β hybrid peptide.Role and Cytotoxicity of Amylin and Protection of Pancreatic Islet β-Cells from Amylin Cytotoxicity

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P2860

Conformationally restricted short peptides inhibit human islet amyloid polypeptide (hIAPP) fibrillization.

http://www.wikidata.org/entity/Q36935342

description

2013 nî lūn-bûn

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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2013年论文

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name

Conformationally restricted sh ...... eptide (hIAPP) fibrillization.

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type

label

Conformationally restricted sh ...... eptide (hIAPP) fibrillization.

@en

prefLabel

Conformationally restricted sh ...... eptide (hIAPP) fibrillization.

@en

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Chemical Communications

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Conformationally restricted sh ...... eptide (hIAPP) fibrillization.

@en

P2093

Anurag Misra

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

Aseem Mishra

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

Chaitanya Thota

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

Madhvi Gupta

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

Suryanarayanarao Ramakumar

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

T Sri Vaishnavi

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

Virander Singh Chauhan

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

P2860

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

Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients

Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis

Atomic structure of the cross-β spine of islet amyloid polypeptide (amylin)

Dynamic -Helix Structure of Micelle-bound Human Amylin

Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process

Atomic View of a Toxic Amyloid Small Oligomer

Shape complementarity at protein/protein interfaces

AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility

Beta-cell deficit and increased beta-cell apoptosis in humans with type 2 diabetes

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2688-2690

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scholarly article

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10.1039/C3CC38982K

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26

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49

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2013-04-01T00:00:00Z

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235716886

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23435449

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3684849

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