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These results suggest that protein segment structures represent polymorphs of their parent protein and that segment 19-29 S20G may serve as a model for the toxic spine of human IAPP.
All-atom explicit-water molecular dynamics (MD) simulations studying adsorption, orientation, and surface interaction of hIAPP aggregates with different sizes (monomer to tetramer) and conformations (monomer with alpha-helix and tetramer with beta-sheet-rich U-turn) upon adsorption. hIAPP monomer with alpha-helical conformation and hIAPP pentamer with beta-sheet conformation can adsorb on both POPC and POPC/POPE (zeige HMBS Proteine) bilayers.
Data (including data from studies using tissues from transgenic mice) suggest that IL1B (zeige IL1B Proteine) plays dual roles by (1) mediating islet amyloid-induced FAS (zeige FAS Proteine) up-regulation and apoptosis in pancreatic beta-cells and (2) down-regulating IAPP precursor processing thereby potentiating islet amyloid formation. (IL1B (zeige IL1B Proteine) = interleukin-1beta; FAS (zeige FAS Proteine) = FAS (zeige FAS Proteine) cell surface death receptor; IAPP = islet amyloid polypeptide)
Data suggest that single aromatic/hydrophobic amino acid residues within IAPP (islet amyloid polypeptide) amyloid core region are able to control its interaction with amyloid-beta(1-40) or amyloid-beta(1-42) but not IAPP self-assembly; four aromatic/hydrophobic residues are able to control both IAPP amyloid self-assembly and its cross-interaction with amyloid-beta(1-40) or amyloid-beta(1-42).
Data show that aluminum (Al3+) could inhibit islet amyloid polypeptide hIAPP(11-28) fibrillogenesis.
The absence of BACE2 (zeige BACE2 Proteine) ameliorates glucose tolerance defects induced by IAPP overexpression in the beta-cell and promotes beta-cell survival.
This study supports the elucidation of the structural basis of IAPP amyloid formation and highlights the extent of amyloid fibril polymorphism.
Data suggest that a single GlcNAc residue at CTR (zeige CALCR Proteine) N130 (asparagine 130) is responsible for enhanced affinity of calcitonin (zeige CALCA Proteine) for CTR (zeige CALCR Proteine) ECD (zeige SHFM1 Proteine); the same appears to apply for enhanced affinity of amylin for RAMP2 (zeige RAMP2 Proteine)-CTR (zeige CALCR Proteine) ECD (zeige SHFM1 Proteine). [GlcNAc = N-acetylglucosamine; CTR (zeige CALCR Proteine) = calcitonin receptor (zeige CALCR Proteine); ECD (zeige SHFM1 Proteine) = extracellular domain; RAMP2 (zeige RAMP2 Proteine) = receptor (calcitonin) activity modifying protein 2 (zeige RAMP2 Proteine)].
The kinetics of human amylin amyloid formation can be monitored by SYPRO-orange fluorescence and match the time course determined with thioflavin-T assays.
effect of cholesterol on the amyloidogenicity of IAPP
These data suggest participation by both soluble and fibrillar aggregates in IAPP-induced islet inflammation. IAPP-induced activation of TLR2 and secretion of IL-1 (zeige IL1A Proteine) may be important therapeutic targets to prevent amyloid-associated beta cell dysfunction.
Hypothalamic amylin is transcriptionally regulated by leptin (zeige LEP Proteine), that it can act directly on ObRb (zeige LEPR Proteine) neurons in concert with leptin (zeige LEP Proteine), and that it regulates feeding.
Matrix Metalloproteinase-9 (zeige MMP9 Proteine) Protects Islets from Amyloid-induced Toxicity.
Data indicate that T-cell receptors that react to chromogranin A (ChgA (zeige CHGA Proteine)) and islet amyloid polypeptide precursor (IAPP) autoantigens were impaired when the thymic stromal cells lacked thymus-specific serine protease (TSSP (zeige PRSS16 Proteine)).
Study the physiologic actions of IAPP on pancreatic beta cells, which secrete this peptide together with insulin (zeige INS Proteine) upon glucose stimulation. Explore the signaling pathways and mitogenic actions of IAPP on beta cells.
deletion of the DeltaN isoforms of p63 (zeige CKAP4 Proteine) or p73 (zeige ARHGAP24 Proteine) leads to metabolic reprogramming and regression of p53 (zeige TP53 Proteine)-deficient tumours through upregulation of IAPP, the gene that encodes amylin, a 37-amino-acid peptide co-secreted with insulin (zeige INS Proteine) by the beta cells of the pancreas
The stability, conformational dynamics and association force of different single-layer models of the full-length wild-type and glycine mutants of amylin, were investigated.
studies have identified a novel TXNIP (zeige TXNIP Proteine)/miR (zeige MLXIP Proteine)-124a/FoxA2 (zeige FOXA2 Proteine)/IAPP signaling cascade linking the critical beta-cell signaling pathways of TXNIP (zeige TXNIP Proteine) and IAPP
MMP-9 (zeige MMP9 Proteine) constitutes an endogenous islet protease that limits islet amyloid deposition and its toxic effects via degradation of hIAPP.
Data suggest that amylin and leptin (zeige LEP Proteine) play additive roles in regulating energy homeostasis via activation of overlapping signalling pathways; mechanisms may be different in hypothalamus, muscle, and liver and in cases of endoplasmic reticulum stress.
Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism.
Islet amyloid polypeptide (diabetes-associated peptide; amylin)
, diabetes-associated peptide
, insulinoma amyloid peptide
, islet amyloid polypeptide
, amyloid protein