نتایج جستجو برای: islet amyloid polypeptide

تعداد نتایج: 80109  

2014
Karen Pillay Patrick Govender

Amylin is a peptide that aggregates into species that are toxic to pancreatic beta cells, leading to type II diabetes. This study has for the first time quantified amylin association and dissociation kinetics (association constant (ka ) = 28.7 ± 5.1 L mol-1 s-1 and dissociation constant (kd ) = 2.8 ± 0.6 ×10-4 s-1) using surface plasmon resonance (SPR). Thus far, techniques used for the sizing ...

Journal: :Protein science : a publication of the Protein Society 2008
Jed J W Wiltzius Stuart A Sievers Michael R Sawaya Duilio Cascio Dmitriy Popov Christian Riekel David Eisenberg

Human islet amyloid polypeptide (IAPP or amylin) is a 37-residue hormone found as fibrillar deposits in pancreatic extracts of nearly all type II diabetics. Although the cellular toxicity of IAPP has been established, the structure of the fibrillar form found in these deposits is unknown. Here we have crystallized two segments from IAPP, which themselves form amyloid-like fibrils. The atomic st...

Journal: :FEBS letters 2005
Kia Balali-Mood Richard H Ashley Thomas Hauss Jeremy P Bradshaw

Human islet amyloid polypeptide (hIAPP) forms amyloid deposits in non-insulin-dependent diabetes mellitus (NIDDM). Pre-fibrillar hIAPP oligomers (in contrast to monomeric IAPP or mature fibrils) increase membrane permeability, suggesting an important role in the disease. In the first structural study of membrane-associated hIAPP, lamellar neutron diffraction shows that oligomeric hIAPP inserts ...

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید