[HTML][HTML] Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide
R Azriel, E Gazit - Journal of Biological Chemistry, 2001 - ASBMB
The development of type II diabetes was shown to be associated with the formation of
amyloid fibrils consisted of the islet amyloid polypeptide (IAPP or amylin). Recently, a short …
amyloid fibrils consisted of the islet amyloid polypeptide (IAPP or amylin). Recently, a short …
Structure of cat islet amyloid polypeptide and identification of amino acid residues of potential significance for islet amyloid formation
C Betsholtz, L Christmanson, U Engström… - Diabetes, 1990 - Am Diabetes Assoc
Cats and humans, unlike most rodent species, develop amyloid in the islets of Langerhans
in conjunction with non-insulin-dependent diabetes mellitus. The amyloid consists of a 37 …
in conjunction with non-insulin-dependent diabetes mellitus. The amyloid consists of a 37 …
The ability of rodent islet amyloid polypeptide to inhibit amyloid formation by human islet amyloid polypeptide has important implications for the mechanism of amyloid …
P Cao, F Meng, A Abedini, DP Raleigh - Biochemistry, 2010 - ACS Publications
Islet amyloid polypeptide (IAPP) is a 37-residue polypeptide hormone that is responsible for
islet amyloid formation in type II diabetes. Human IAPP is extremely amyloidogenic, while rat …
islet amyloid formation in type II diabetes. Human IAPP is extremely amyloidogenic, while rat …
Amyloidogenicity of naturally occurring full‐length animal IAPP variants
LM Palato, S Pilcher, A Oakes, A Lamba… - Journal of Peptide …, 2019 - Wiley Online Library
The aggregation of the 37‐amino acid polypeptide human islet amyloid polypeptide (hIAPP),
as either insoluble amyloid or as small oligomers, appears to play a direct role in the death …
as either insoluble amyloid or as small oligomers, appears to play a direct role in the death …
Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation.
P Westermark, U Engström… - Proceedings of the …, 1990 - National Acad Sciences
Islet amyloid polypeptide (IAPP), a putative polypeptide hormone, is a product of pancreatic
beta-cells and the major constituent of the amyloid deposits seen mainly in islets of type 2 …
beta-cells and the major constituent of the amyloid deposits seen mainly in islets of type 2 …
Aggregation of an amyloidogenic fragment of human islet amyloid polypeptide
Native human islet amyloid polypeptide (hIAPP) has been identified as the major component
of amyloid plaques found in the pancreatic islets of Langerhans of persons affected by type …
of amyloid plaques found in the pancreatic islets of Langerhans of persons affected by type …
The role of His-18 in amyloid formation by human islet amyloid polypeptide
A Abedini, DP Raleigh - Biochemistry, 2005 - ACS Publications
The 37-residue islet amyloid polypeptide (IAPP) is the major protein component of the
amyloid deposits found in type-II diabetes. IAPP is stored in a relatively low pH environment …
amyloid deposits found in type-II diabetes. IAPP is stored in a relatively low pH environment …
Destabilization of human IAPP amyloid fibrils by proline mutations outside of the putative amyloidogenic domain: is there a critical amyloidogenic domain in human …
A Abedini, DP Raleigh - Journal of molecular biology, 2006 - Elsevier
Islet amyloid polypeptide (IAPP; amylin) is responsible for amyloid formation in type-2
diabetes. Not all organisms form islet amyloid, and amyloid formation correlates strongly …
diabetes. Not all organisms form islet amyloid, and amyloid formation correlates strongly …
Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology
Amyloid formation has been implicated in a wide range of human diseases, and a diverse
set of proteins is involved. There is considerable interest in elucidating the interactions …
set of proteins is involved. There is considerable interest in elucidating the interactions …
Role of aromatic interactions in amyloid formation by islet amyloid polypeptide
LH Tu, DP Raleigh - Biochemistry, 2013 - ACS Publications
Aromatic–aromatic and aromatic–hydrophobic interactions have been proposed to play a
role in amyloid formation by a range of polypeptides, including islet amyloid polypeptide …
role in amyloid formation by a range of polypeptides, including islet amyloid polypeptide …