Similar articles for PMID: 32027132

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1

Copper(II) and Amylin Analogues: A Complicated Relationship.

Alghrably M, Dudek D, Emwas AH, Jaremko Ł, Jaremko M, Rowińska-Żyrek M. Alghrably M, et al. Inorg Chem. 2020 Feb 17;59(4):2527-2535. doi: 10.1021/acs.inorgchem.9b03498. Epub 2020 Feb 6. Inorg Chem. 2020. PMID: 32027132 Free article.

2

New Insight in Copper-Ion Binding to Human Islet Amyloid: The Contribution of Metal-Complex Speciation To Reveal the Polypeptide Toxicity.

Magrì A, La Mendola D, Nicoletti VG, Pappalardo G, Rizzarelli E. Magrì A, et al. Chemistry. 2016 Sep 5;22(37):13287-300. doi: 10.1002/chem.201602816. Epub 2016 Aug 5. Chemistry. 2016. PMID: 27493030

3

Rapid assessment of human amylin aggregation and its inhibition by copper(II) ions by laser ablation electrospray ionization mass spectrometry with ion mobility separation.

Li H, Ha E, Donaldson RP, Jeremic AM, Vertes A. Li H, et al. Anal Chem. 2015 Oct 6;87(19):9829-9837. doi: 10.1021/acs.analchem.5b02217. Anal Chem. 2015. PMID: 26352401 Free PMC article.

4

Zn(II) - pramlintide: Stability, binding sites and unexpected aggregation.

Łoboda D, Rowińska-Żyrek M. Łoboda D, et al. J Inorg Biochem. 2017 Sep;174:150-155. doi: 10.1016/j.jinorgbio.2017.06.008. Epub 2017 Jun 23. J Inorg Biochem. 2017. PMID: 28672144

5

Active-Site Environment of Copper-Bound Human Amylin Relevant to Type 2 Diabetes.

Seal M, Dey SG. Seal M, et al. Inorg Chem. 2018 Jan 2;57(1):129-138. doi: 10.1021/acs.inorgchem.7b02266. Epub 2017 Dec 18. Inorg Chem. 2018. PMID: 29251925

6

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

Lee EC, Ha E, Singh S, Legesse L, Ahmad S, Karnaukhova E, Donaldson RP, Jeremic AM. Lee EC, et al. Phys Chem Chem Phys. 2013 Aug 14;15(30):12558-71. doi: 10.1039/c3cp44542a. Phys Chem Chem Phys. 2013. PMID: 23793354 Free PMC article.

7

The role of copper(II) in the aggregation of human amylin.

Sinopoli A, Magrì A, Milardi D, Pappalardo M, Pucci P, Flagiello A, Titman JJ, Nicoletti VG, Caruso G, Pappalardo G, Grasso G. Sinopoli A, et al. Metallomics. 2014 Oct;6(10):1841-52. doi: 10.1039/c4mt00130c. Epub 2014 Aug 1. Metallomics. 2014. PMID: 25080969

8

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

Magrì A, Pietropaolo A, Tabbì G, La Mendola D, Rizzarelli E. Magrì A, et al. Chemistry. 2017 Dec 19;23(71):17898-17902. doi: 10.1002/chem.201704910. Epub 2017 Nov 30. Chemistry. 2017. PMID: 29111583

9

Potentiometric and spectroscopic studies on the copper(II) complexes of rat amylin fragments. The anchoring ability of specific non-coordinating side chains.

Dávid Á, Kállay C, Sanna D, Lihi N, Sóvágó I, Várnagy K. Dávid Á, et al. Dalton Trans. 2015 Oct 21;44(39):17091-9. doi: 10.1039/c5dt02445e. Epub 2015 Sep 15. Dalton Trans. 2015. PMID: 26369733

10

Structural basis for the inhibition of truncated islet amyloid polypeptide aggregation by Cu(II): insights into the bioinorganic chemistry of type II diabetes.

Rivillas-Acevedo L, Sánchez-López C, Amero C, Quintanar L. Rivillas-Acevedo L, et al. Inorg Chem. 2015 Apr 20;54(8):3788-96. doi: 10.1021/ic502945k. Epub 2015 Mar 31. Inorg Chem. 2015. PMID: 25826050

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