Abedini A - Search Results

1

Characterization of the heparin binding site in the N-terminus of human pro-islet amyloid polypeptide: implications for amyloid formation.

Abedini A, Tracz SM, Cho JH, Raleigh DP. Abedini A, et al. Biochemistry. 2006 Aug 1;45(30):9228-37. doi: 10.1021/bi0510936. Biochemistry. 2006. PMID: 16866369

2

Role of aromatic interactions in amyloid formation by peptides derived from human Amylin.

Tracz SM, Abedini A, Driscoll M, Raleigh DP. Tracz SM, et al. Among authors: abedini a. Biochemistry. 2004 Dec 21;43(50):15901-8. doi: 10.1021/bi048812l. Biochemistry. 2004. PMID: 15595845

3

Destabilization of human IAPP amyloid fibrils by proline mutations outside of the putative amyloidogenic domain: is there a critical amyloidogenic domain in human IAPP?

Abedini A, Raleigh DP. Abedini A, et al. J Mol Biol. 2006 Jan 13;355(2):274-81. doi: 10.1016/j.jmb.2005.10.052. Epub 2005 Nov 8. J Mol Biol. 2006. PMID: 16303136

4

The role of His-18 in amyloid formation by human islet amyloid polypeptide.

Abedini A, Raleigh DP. Abedini A, et al. Biochemistry. 2005 Dec 13;44(49):16284-91. doi: 10.1021/bi051432v. Biochemistry. 2005. PMID: 16331989

5

Recovery and purification of highly aggregation-prone disulfide-containing peptides: application to islet amyloid polypeptide.

Abedini A, Singh G, Raleigh DP. Abedini A, et al. Anal Biochem. 2006 Apr 15;351(2):181-6. doi: 10.1016/j.ab.2005.11.029. Epub 2005 Dec 15. Anal Biochem. 2006. PMID: 16406209

6

Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology.

Marek P, Abedini A, Song B, Kanungo M, Johnson ME, Gupta R, Zaman W, Wong SS, Raleigh DP. Marek P, et al. Among authors: abedini a. Biochemistry. 2007 Mar 20;46(11):3255-61. doi: 10.1021/bi0621967. Epub 2007 Feb 21. Biochemistry. 2007. PMID: 17311418

7

A single-point mutation converts the highly amyloidogenic human islet amyloid polypeptide into a potent fibrillization inhibitor.

Abedini A, Meng F, Raleigh DP. Abedini A, et al. J Am Chem Soc. 2007 Sep 19;129(37):11300-1. doi: 10.1021/ja072157y. Epub 2007 Aug 28. J Am Chem Soc. 2007. PMID: 17722920 No abstract available.

8

Amyloid formation by pro-islet amyloid polypeptide processing intermediates: examination of the role of protein heparan sulfate interactions and implications for islet amyloid formation in type 2 diabetes.

Meng F, Abedini A, Song B, Raleigh DP. Meng F, et al. Among authors: abedini a. Biochemistry. 2007 Oct 30;46(43):12091-9. doi: 10.1021/bi7004834. Epub 2007 Oct 9. Biochemistry. 2007. PMID: 17924651

9

The ability of rodent islet amyloid polypeptide to inhibit amyloid formation by human islet amyloid polypeptide has important implications for the mechanism of amyloid formation and the design of inhibitors.

Cao P, Meng F, Abedini A, Raleigh DP. Cao P, et al. Among authors: abedini a. Biochemistry. 2010 Feb 9;49(5):872-81. doi: 10.1021/bi901751b. Biochemistry. 2010. PMID: 20028124 Free PMC article.

10

The sulfated triphenyl methane derivative acid fuchsin is a potent inhibitor of amyloid formation by human islet amyloid polypeptide and protects against the toxic effects of amyloid formation.

Meng F, Abedini A, Plesner A, Middleton CT, Potter KJ, Zanni MT, Verchere CB, Raleigh DP. Meng F, et al. Among authors: abedini a. J Mol Biol. 2010 Jul 16;400(3):555-66. doi: 10.1016/j.jmb.2010.05.001. Epub 2010 May 7. J Mol Biol. 2010. PMID: 20452363 Free PMC article.

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