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1 peptide, NFGAIL (residues 22-27 of the human islet amyloid polypeptide).
2 creatic islets primarily composed of amylin (islet amyloid polypeptide).
3 d O to N acyl shift regenerates normal human islet amyloid polypeptide.
4 ted during the formation of amyloid by human islet amyloid polypeptide.
5 of this step for a model system derived from islet amyloid polypeptide.
6 med from serum amyloid A, transthyretin, and islet amyloid polypeptide.
7 normally soluble 37 residue peptide hormone, islet amyloid polypeptide.
8 g those formed from tau, alpha-synuclein and islet amyloid polypeptide.
9 a heterogeneous oligomeric solution of human islet amyloid polypeptide.
10 Alzheimer's amyloid beta and, similarly, the islet amyloid polypeptide.
11 lical assemblies of gold nanorods with human islet amyloid polypeptides.
12 of the difficult sequences, for example, the islet amyloid polypeptide (22-27) fragment (with a C-ter
13 od glucose levels, higher insulin, and lower islet amyloid polypeptide accumulation were observed.
15 the two new autoantigens, chromogranin A and islet amyloid polypeptide, all proteins of the secretory
16 aggregation of the amyloid-beta peptide, the islet amyloid polypeptide, alpha-synuclein, and the hung
17 the region S (20)NNFGAILSS (29) of the human islet amyloid polypeptide amylin, reveals that the pepti
20 perhaps the most challenging such system is islet amyloid polypeptide (Amylin), the causative agent
21 arlier studies have shown that deposition of islet amyloid polypeptide amyloid in transplanted islets
22 ments, and amyloid fibrillogenesis assays on islet amyloid polypeptide and amyloid-beta peptide to de
23 at DNA polymorphism physically linked to the islet amyloid polypeptide and liver glycogen synthase ge
24 ells express some beta cell markers, such as islet amyloid polypeptide and Pdx1, but lack other defin
25 mbly of amyloid-beta, alpha synuclein, human islet amyloid polypeptide and prions, the peptides and p
26 e perlecan's interactions with amylin (i.e., islet amyloid polypeptide) and its effects on amylin fib
27 s, including serum amyloid A, transthyretin, islet amyloid polypeptide, and amyloid beta 1-40 peptide
28 well-known amyloids, including Abeta, human islet amyloid polypeptide, and tau have been found to as
29 fibrils which are formed by the regenerated islet amyloid polypeptide are indistinguishable from tho
30 turb amyloid formation relative to wild-type islet amyloid polypeptide as detected using thioflavin T
31 nuclein associated with Parkinson's disease, islet amyloid polypeptide associated with type II diabet
32 We show that NUCB1 inhibits aggregation of islet-amyloid polypeptide associated with type 2 diabete
33 f unrelated sequence, such as transthyretin, islet amyloid polypeptide, beta(2)-microglobulin, and po
34 c peptides (such as amyloid beta-peptide and islet amyloid polypeptide) demonstrate that these polype
35 The 37-residue amylin peptide, also known as islet amyloid polypeptide, forms fibrils that are the ma
36 e compared to a non-amyloidogenic variant of islet amyloid polypeptide from rat and N-acetyl-tyrosina
37 t beta cell-specific expression of the human islet amyloid polypeptide gene is principally regulated
39 VEVLK), derived from splicing of insulin and islet amyloid polypeptides, generates a preferred peptid
40 ll cells Pdx1 binds strongly to the insulin, islet amyloid polypeptide, glucagon, Pdx1, and Pax4 prom
41 yphenols against relevant targets, including islet amyloid polypeptide, glucosidases, and cholinester
42 he misfolding of the beta-cell hormone human islet amyloid polypeptide (h-IAPP) into toxic oligomers
43 rat islets isolated from wild-type or human islet amyloid polypeptide (h-IAPP) transgenic rats, and
46 or the kinetics of fibril formation by human islet amyloid polypeptide (hIAPP or amylin) that is asso
49 cules that are potential inhibitors of human islet amyloid polypeptide (hIAPP) aggregation or amyloid
51 inhibition toward fibril formation of human Islet amyloid polypeptide (hIAPP) and its toxicity, whic
52 olding and amyloid fibril formation by human islet amyloid polypeptide (hIAPP) are thought to be impo
54 cluding type 2 diabetes mellitus where human islet amyloid polypeptide (hIAPP) forms fibrils in the p
56 of membrane-embedded aggregates of the human islet amyloid polypeptide (hIAPP) implicated in type II
57 hemizygous transgenic mice expressing human islet amyloid polypeptide (hIAPP) in pancreatic beta-cel
60 enic mice expressing the amyloidogenic human islet amyloid polypeptide (hIAPP) in their islet beta-ce
62 In type 2 diabetes, aggregation of human islet amyloid polypeptide (hIAPP) into fibrils is a hall
63 the fibrillating core fragment of the human islet amyloid polypeptide (hIAPP) involved in type-2 dia
72 ow the fiber formation kinetics of the human islet amyloid polypeptide (hIAPP) that is involved in ty
73 n an intrinsically disordered protein, human islet amyloid polypeptide (hIAPP) that is known to misfo
76 death involves membrane disruption by human islet amyloid polypeptide (hIAPP), the major constituent
77 f dimers composed of residues 20-29 of human islet amyloid polypeptide (hIAPP), which form fibrils in
79 natures, we studied the aggregation of human islet amyloid polypeptide (hIAPP), which is implicated i
80 ersity in amyloid fibers of aggregated human islet amyloid polypeptide (hIAPP), which is involved wit
81 f prion protein (PrP(106-126)) and the human islet amyloid polypeptide (hIAPP), with giant lipid vesi
88 egy to characterize the orientation of human islet amyloid polypeptides (hIAPPs) at lipid/aqueous int
89 fatty [ZDF] rats, and rats expressing human islet amyloid polypeptide [HIP]; n = 36/group) on a norm
97 e composed of a 37-residue peptide, known as islet amyloid polypeptide (IAPP) (also known as amylin)
100 characterized by islet amyloid derived from islet amyloid polypeptide (IAPP) and increased beta-cell
102 The combinatorial peptidergic therapy of islet amyloid polypeptide (IAPP) and leptin (LEP) analog
105 abetes, contains the islet beta-cell peptide islet amyloid polypeptide (IAPP) as its unique amyloidog
109 We showed previously that C4BP enhances islet amyloid polypeptide (IAPP) fibril formation in vit
110 edictions by demonstrating that without AWI, islet amyloid polypeptide (IAPP) fibrilization was aboli
111 formation outside of neural environments in islet amyloid polypeptide (IAPP) fibrils and plaques, wh
112 s in type 2 diabetes attributes the cause to islet amyloid polypeptide (IAPP) for its deleterious eff
114 the acute secretory dynamics of insulin and islet amyloid polypeptide (IAPP) from islets of Langerha
115 ween nucleotides -2798 and +450 of the human islet amyloid polypeptide (IAPP) gene using transgenic m
118 ctrometric analysis revealed the presence of islet amyloid polypeptide (IAPP) in antigen-containing f
119 lassical hormone markers peptide YY (YY) and islet amyloid polypeptide (IAPP) in combination with the
120 disease characterized by the aggregation of islet amyloid polypeptide (IAPP) in pancreatic beta cell
121 (Abeta) and tau in the brain during AD, and islet amyloid polypeptide (IAPP) in pancreatic islets in
135 by soluble forms of amyloid proteins such as islet amyloid polypeptide (IAPP) is implicated in cell d
145 enic mechanisms and whether links exist with islet amyloid polypeptide (IAPP) misfolding, a process c
146 eatic beta cell by effectively knocking down islet amyloid polypeptide (IAPP) mRNA, a potential proap
150 that the N-terminal loop (N_loop) of amylin (islet amyloid polypeptide (IAPP) residues 1-8) forms ext
151 ersus lean murine transgenic model for human islet amyloid polypeptide (IAPP) that develops islet pat
152 We previously reported a peptide KS20 from islet amyloid polypeptide (IAPP) to be the target Ag for
154 ntain deposits of islet amyloid derived from islet amyloid polypeptide (IAPP), a 37-amino acid protei
155 like peptide 2 (SHLP2), on the misfolding of islet amyloid polypeptide (IAPP), a critical pathogenic
156 he amyloidogenic type II diabetes-associated islet amyloid polypeptide (IAPP), a hydrophobic-hydrophi
158 which inhibits in vitro amyloid formation by islet amyloid polypeptide (IAPP), a peptide hormone whos
159 id not have any effect on the aggregation of islet amyloid polypeptide (IAPP), a peptide which shares
160 aracterized by amyloid deposits derived from islet amyloid polypeptide (IAPP), a protein co-expressed
161 in beta cells and islet amyloid derived from islet amyloid polypeptide (IAPP), a protein co-expressed
166 y beta-cell loss, islet amyloid derived from islet amyloid polypeptide (IAPP), and increased beta-cel
167 posits, composed primarily of the 37-residue islet amyloid polypeptide (IAPP), are a characteristic f
168 The aggregation of the 37-residue protein, islet amyloid polypeptide (IAPP), as either insoluble am
170 ulin and other peptide hormones, such as the islet amyloid polypeptide (IAPP), is limited to beta-cel
172 umulate misfolded aggregates composed of the islet amyloid polypeptide (IAPP), its role in the diseas
173 ta peptide (A beta), prion protein (PrP) and islet amyloid polypeptide (IAPP), leading us to believe
174 au proteins, the PrP prion protein, insulin, islet amyloid polypeptide (IAPP), lysozyme, myoglobin, a
175 nderstood how the building block of amyloid, islet amyloid polypeptide (IAPP), misfolds and accumulat
176 unique component the islet beta-cell peptide islet amyloid polypeptide (IAPP), or amylin, which is co
177 venous injection with preformed fibrils from islet amyloid polypeptide (IAPP), proIAPP, or amyloid-be
178 e formation of amyloid deposits derived from islet amyloid polypeptide (IAPP), was considered to be a
180 r accumulation of islet amyloid derived from islet amyloid polypeptide (IAPP), which beta cells coexp
181 of the intrinsically disordered polypeptide islet amyloid polypeptide (IAPP), which is associated wi
182 proteins, amyloid-beta (Abeta) peptides and islet amyloid polypeptide (IAPP), whose misfolding prope
202 elucidate the impact of protein glycation on islet amyloid polypeptide (IAPP, also known as amylin) a
208 ically unrelated amyloidogenic peptides, the islet amyloid polypeptide (IAPP, the peptide comprising
214 onin-gene-related peptide (CGRP) and amylin (islet amyloid polypeptide, IAPP), two intrinsically diso
215 eimer disease and islet amyloid derived from islet amyloid polypeptide in the pancreas in type 2 diab
217 structure of a type-2 diabetes related human islet amyloid polypeptide intermediate stabilized in nan
218 ex dynamics of gelation by full-length human islet amyloid polypeptide (involved in type II diabetes)
220 indicate that ordering at the C terminus of islet amyloid polypeptide is coincident with, and thus i
224 an islet amyloid polypeptide (hIAPP), murine islet amyloid polypeptide (mIAPP) does not exhibit amylo
225 idence to the assumption that aggregation of islet amyloid polypeptide might be an important cause of
226 on (insulin I and II, Glut2, glucose kinase, islet amyloid polypeptide, nestin, pancreatic duodenal h
228 iously characterized alpha-helical cytotoxic islet amyloid polypeptide oligomers which interact with
230 wn to bind within a region of the endogenous islet amyloid polypeptide, pax-4, and glucokinase genes
231 s of disease-related amyloids (Abeta, prion, islet amyloid polypeptide, polyglutamine, and lysozyme)
232 ial fibrillary acidic protein (GFAP), prepro-islet amyloid polypeptide (ppIAPP), and islet-specific g
234 altered transfection efficiency, because the islet amyloid polypeptide promoter and viral promoters a
235 ons within these sequences using transfected islet amyloid polypeptide promoter expression constructs
236 A-reactive BDC-2.5 and BDC-10.1 TCRs or the islet amyloid polypeptide-reactive TCR BDC-6.9 and BDC-5
237 ice, and HIP rats (rats transgenic for human islet amyloid polypeptide), representative of types 1 an
240 rafted with a large hydrophobic peptide from islet amyloid polypeptide (residues 8-37) that contains
242 rity of insulin B chain and hybrid-insulin C-islet amyloid polypeptide-specific CD4(+) T cells exhibi
243 t capped peptides containing the part of the islet amyloid polypeptide that may be responsible for th
244 ted using inhibitors of amyloid formation by islet amyloid polypeptide, the causative agent of amyloi
245 roach allows studies of amyloid formation by islet amyloid polypeptide to be carried out from a well-
246 on modify islet disease progression in human islet amyloid polypeptide transgenic (HIP) rats, a model
248 , alpha-Synuclein (Parkinson's disease), and islet amyloid polypeptide (type 2 diabetes) inhibit fibr