Insight into the Metal Binding Sites in Amylin Aggregates

Vered Wineman-Fisher; Yifat Miller

Insight into the Metal Binding Sites in Amylin Aggregates

Vered Wineman-Fisher, Yifat Miller

Department of Chemistry

Ben-Gurion University of the Negev

Research output: Contribution to journal › Meeting Abstract

Abstract

Amylin peptide consists of 37 residues. The aggregation of Amylin is one of the
symptoms of type 2 diabetes (T2D). Amylin’s oligomers that are toxic lead to
b-cells death and thus to decreasing of insulin’s release to the blood and to progressing of T2D.

Original language	American English
Pages (from-to)	524A-524A
Number of pages	1
Journal	Biophysical Journal
Volume	108
Issue number	2
State	Published - Jan 2015

Cite this

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title = "Insight into the Metal Binding Sites in Amylin Aggregates",

abstract = "Amylin peptide consists of 37 residues. The aggregation of Amylin is one of thesymptoms of type 2 diabetes (T2D). Amylin{\textquoteright}s oligomers that are toxic lead tob-cells death and thus to decreasing of insulin{\textquoteright}s release to the blood and to progressing of T2D.",

author = "Vered Wineman-Fisher and Yifat Miller",

year = "2015",

month = jan,

language = "American English",

volume = "108",

pages = "524A--524A",

journal = "Biophysical Journal",

issn = "0006-3495",

publisher = "Elsevier B.V.",

number = "2",

}

TY - JOUR

T1 - Insight into the Metal Binding Sites in Amylin Aggregates

AU - Wineman-Fisher, Vered

AU - Miller, Yifat

PY - 2015/1

Y1 - 2015/1

N2 - Amylin peptide consists of 37 residues. The aggregation of Amylin is one of thesymptoms of type 2 diabetes (T2D). Amylin’s oligomers that are toxic lead tob-cells death and thus to decreasing of insulin’s release to the blood and to progressing of T2D.

AB - Amylin peptide consists of 37 residues. The aggregation of Amylin is one of thesymptoms of type 2 diabetes (T2D). Amylin’s oligomers that are toxic lead tob-cells death and thus to decreasing of insulin’s release to the blood and to progressing of T2D.

M3 - Meeting Abstract

SN - 0006-3495

VL - 108

SP - 524A-524A

JO - Biophysical Journal

JF - Biophysical Journal

IS - 2

ER -