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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 Alzheimer's amyloid beta and, similarly, the islet amyloid polypeptide.
9 of the difficult sequences, for example, the islet amyloid polypeptide (22-27) fragment (with a C-ter
10 od glucose levels, higher insulin, and lower islet amyloid polypeptide accumulation were observed.
11 the two new autoantigens, chromogranin A and islet amyloid polypeptide, all proteins of the secretory
12 the region S (20)NNFGAILSS (29) of the human islet amyloid polypeptide amylin, reveals that the pepti
14 perhaps the most challenging such system is islet amyloid polypeptide (Amylin), the causative agent
15 arlier studies have shown that deposition of islet amyloid polypeptide amyloid in transplanted islets
16 ments, and amyloid fibrillogenesis assays on islet amyloid polypeptide and amyloid-beta peptide to de
17 at DNA polymorphism physically linked to the islet amyloid polypeptide and liver glycogen synthase ge
18 ells express some beta cell markers, such as islet amyloid polypeptide and Pdx1, but lack other defin
19 mbly of amyloid-beta, alpha synuclein, human islet amyloid polypeptide and prions, the peptides and p
20 e perlecan's interactions with amylin (i.e., islet amyloid polypeptide) and its effects on amylin fib
21 s, including serum amyloid A, transthyretin, islet amyloid polypeptide, and amyloid beta 1-40 peptide
22 fibrils which are formed by the regenerated islet amyloid polypeptide are indistinguishable from tho
23 turb amyloid formation relative to wild-type islet amyloid polypeptide as detected using thioflavin T
24 nuclein associated with Parkinson's disease, islet amyloid polypeptide associated with type II diabet
25 We show that NUCB1 inhibits aggregation of islet-amyloid polypeptide associated with type 2 diabete
26 f unrelated sequence, such as transthyretin, islet amyloid polypeptide, beta(2)-microglobulin, and po
27 c peptides (such as amyloid beta-peptide and islet amyloid polypeptide) demonstrate that these polype
28 The 37-residue amylin peptide, also known as islet amyloid polypeptide, forms fibrils that are the ma
29 e compared to a non-amyloidogenic variant of islet amyloid polypeptide from rat and N-acetyl-tyrosina
30 t beta cell-specific expression of the human islet amyloid polypeptide gene is principally regulated
32 ll cells Pdx1 binds strongly to the insulin, islet amyloid polypeptide, glucagon, Pdx1, and Pax4 prom
33 he misfolding of the beta-cell hormone human islet amyloid polypeptide (h-IAPP) into toxic oligomers
34 rat islets isolated from wild-type or human islet amyloid polypeptide (h-IAPP) transgenic rats, and
37 or the kinetics of fibril formation by human islet amyloid polypeptide (hIAPP or amylin) that is asso
40 cules that are potential inhibitors of human islet amyloid polypeptide (hIAPP) aggregation or amyloid
41 inhibition toward fibril formation of human Islet amyloid polypeptide (hIAPP) and its toxicity, whic
42 olding and amyloid fibril formation by human islet amyloid polypeptide (hIAPP) are thought to be impo
43 cluding type 2 diabetes mellitus where human islet amyloid polypeptide (hIAPP) forms fibrils in the p
44 of membrane-embedded aggregates of the human islet amyloid polypeptide (hIAPP) implicated in type II
45 hemizygous transgenic mice expressing human islet amyloid polypeptide (hIAPP) in pancreatic beta-cel
47 enic mice expressing the amyloidogenic human islet amyloid polypeptide (hIAPP) in their islet beta-ce
49 the fibrillating core fragment of the human islet amyloid polypeptide (hIAPP) involved in type-2 dia
57 ow the fiber formation kinetics of the human islet amyloid polypeptide (hIAPP) that is involved in ty
58 n an intrinsically disordered protein, human islet amyloid polypeptide (hIAPP) that is known to misfo
60 death involves membrane disruption by human islet amyloid polypeptide (hIAPP), the major constituent
61 f dimers composed of residues 20-29 of human islet amyloid polypeptide (hIAPP), which form fibrils in
62 natures, we studied the aggregation of human islet amyloid polypeptide (hIAPP), which is implicated i
63 ersity in amyloid fibers of aggregated human islet amyloid polypeptide (hIAPP), which is involved wit
70 egy to characterize the orientation of human islet amyloid polypeptides (hIAPPs) at lipid/aqueous int
71 fatty [ZDF] rats, and rats expressing human islet amyloid polypeptide [HIP]; n = 36/group) on a norm
79 e composed of a 37-residue peptide, known as islet amyloid polypeptide (IAPP) (also known as amylin)
82 characterized by islet amyloid derived from islet amyloid polypeptide (IAPP) and increased beta-cell
84 The combinatorial peptidergic therapy of islet amyloid polypeptide (IAPP) and leptin (LEP) analog
87 abetes, contains the islet beta-cell peptide islet amyloid polypeptide (IAPP) as its unique amyloidog
92 edictions by demonstrating that without AWI, islet amyloid polypeptide (IAPP) fibrilization was aboli
93 s in type 2 diabetes attributes the cause to islet amyloid polypeptide (IAPP) for its deleterious eff
94 the acute secretory dynamics of insulin and islet amyloid polypeptide (IAPP) from islets of Langerha
95 ween nucleotides -2798 and +450 of the human islet amyloid polypeptide (IAPP) gene using transgenic m
98 ctrometric analysis revealed the presence of islet amyloid polypeptide (IAPP) in antigen-containing f
99 lassical hormone markers peptide YY (YY) and islet amyloid polypeptide (IAPP) in combination with the
100 disease characterized by the aggregation of islet amyloid polypeptide (IAPP) in pancreatic beta cell
101 (Abeta) and tau in the brain during AD, and islet amyloid polypeptide (IAPP) in pancreatic islets in
114 by soluble forms of amyloid proteins such as islet amyloid polypeptide (IAPP) is implicated in cell d
122 enic mechanisms and whether links exist with islet amyloid polypeptide (IAPP) misfolding, a process c
126 that the N-terminal loop (N_loop) of amylin (islet amyloid polypeptide (IAPP) residues 1-8) forms ext
127 ersus lean murine transgenic model for human islet amyloid polypeptide (IAPP) that develops islet pat
128 We previously reported a peptide KS20 from islet amyloid polypeptide (IAPP) to be the target Ag for
130 ntain deposits of islet amyloid derived from islet amyloid polypeptide (IAPP), a 37-amino acid protei
131 like peptide 2 (SHLP2), on the misfolding of islet amyloid polypeptide (IAPP), a critical pathogenic
133 id not have any effect on the aggregation of islet amyloid polypeptide (IAPP), a peptide which shares
134 in beta cells and islet amyloid derived from islet amyloid polypeptide (IAPP), a protein co-expressed
138 y beta-cell loss, islet amyloid derived from islet amyloid polypeptide (IAPP), and increased beta-cel
139 posits, composed primarily of the 37-residue islet amyloid polypeptide (IAPP), are a characteristic f
140 The aggregation of the 37-residue protein, islet amyloid polypeptide (IAPP), as either insoluble am
142 ulin and other peptide hormones, such as the islet amyloid polypeptide (IAPP), is limited to beta-cel
144 umulate misfolded aggregates composed of the islet amyloid polypeptide (IAPP), its role in the diseas
145 ta peptide (A beta), prion protein (PrP) and islet amyloid polypeptide (IAPP), leading us to believe
146 au proteins, the PrP prion protein, insulin, islet amyloid polypeptide (IAPP), lysozyme, myoglobin, a
147 nderstood how the building block of amyloid, islet amyloid polypeptide (IAPP), misfolds and accumulat
148 unique component the islet beta-cell peptide islet amyloid polypeptide (IAPP), or amylin, which is co
149 venous injection with preformed fibrils from islet amyloid polypeptide (IAPP), proIAPP, or amyloid-be
150 e formation of amyloid deposits derived from islet amyloid polypeptide (IAPP), was considered to be a
152 r accumulation of islet amyloid derived from islet amyloid polypeptide (IAPP), which beta cells coexp
153 of the intrinsically disordered polypeptide islet amyloid polypeptide (IAPP), which is associated wi
154 proteins, amyloid-beta (Abeta) peptides and islet amyloid polypeptide (IAPP), whose misfolding prope
179 ically unrelated amyloidogenic peptides, the islet amyloid polypeptide (IAPP, the peptide comprising
184 onin-gene-related peptide (CGRP) and amylin (islet amyloid polypeptide, IAPP), two intrinsically diso
185 eimer disease and islet amyloid derived from islet amyloid polypeptide in the pancreas in type 2 diab
187 structure of a type-2 diabetes related human islet amyloid polypeptide intermediate stabilized in nan
188 ex dynamics of gelation by full-length human islet amyloid polypeptide (involved in type II diabetes)
190 indicate that ordering at the C terminus of islet amyloid polypeptide is coincident with, and thus i
194 an islet amyloid polypeptide (hIAPP), murine islet amyloid polypeptide (mIAPP) does not exhibit amylo
195 idence to the assumption that aggregation of islet amyloid polypeptide might be an important cause of
196 on (insulin I and II, Glut2, glucose kinase, islet amyloid polypeptide, nestin, pancreatic duodenal h
198 iously characterized alpha-helical cytotoxic islet amyloid polypeptide oligomers which interact with
200 wn to bind within a region of the endogenous islet amyloid polypeptide, pax-4, and glucokinase genes
201 s of disease-related amyloids (Abeta, prion, islet amyloid polypeptide, polyglutamine, and lysozyme)
202 ial fibrillary acidic protein (GFAP), prepro-islet amyloid polypeptide (ppIAPP), and islet-specific g
204 altered transfection efficiency, because the islet amyloid polypeptide promoter and viral promoters a
205 ons within these sequences using transfected islet amyloid polypeptide promoter expression constructs
206 A-reactive BDC-2.5 and BDC-10.1 TCRs or the islet amyloid polypeptide-reactive TCR BDC-6.9 and BDC-5
207 ice, and HIP rats (rats transgenic for human islet amyloid polypeptide), representative of types 1 an
210 rafted with a large hydrophobic peptide from islet amyloid polypeptide (residues 8-37) that contains
212 t capped peptides containing the part of the islet amyloid polypeptide that may be responsible for th
213 ted using inhibitors of amyloid formation by islet amyloid polypeptide, the causative agent of amyloi
214 roach allows studies of amyloid formation by islet amyloid polypeptide to be carried out from a well-
215 on modify islet disease progression in human islet amyloid polypeptide transgenic (HIP) rats, a model
217 , alpha-Synuclein (Parkinson's disease), and islet amyloid polypeptide (type 2 diabetes) inhibit fibr
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