S20G mutant amylin exhibits increased in vitro amyloidogenicity and increased intracellular cytotoxicity compared to wild-type amylin.
about
Porcine islet amyloid polypeptide fragments are refractory to amyloid formationNeuroendocrine hormone amylin in diabetesMolecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes MellitusCausative factors for formation of toxic islet amyloid polypeptide oligomer in type 2 diabetes mellitusMechanisms of islet amyloidosis toxicity in type 2 diabetesAtomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the processSecondary Structure of Rat and Human Amylin across Force FieldsProtein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival.Progressive deterioration of insulin secretion in Japanese type 2 diabetic patients in comparison with those who carry the S20G mutation of the islet amyloid polypeptide gene: A long-term follow-up studyExpression of wild-type and mutant S20G hIAPP in physiologic knock-in mouse models fails to induce islet amyloid formation, but induces mild glucose intoleranceProtective role of human insulin against the cytotoxicity associated with human mutant S20G islet amyloid polypeptide.Selection for nonamyloidogenic mutants of islet amyloid polypeptide (IAPP) identifies an extended region for amyloidogenicity.Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20Conformations of islet amyloid polypeptide monomers in a membrane environment: implications for fibril formation.Biphasic effects of insulin on islet amyloid polypeptide membrane disruption.Amyloidogenicity and cytotoxicity of islet amyloid polypeptide.Computational re-engineering of Amylin sequence with reduced amyloidogenic potential.Effect of sequence variation on the mechanical response of amyloid fibrils probed by steered molecular dynamics simulationType 2 diabetes as a protein misfolding disease.Insights into the consequences of co-polymerisation in the early stages of IAPP and Aβ peptide assembly from mass spectrometry.Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.Pancreatic β-Cell Membrane Fluidity and Toxicity Induced by Human Islet Amyloid Polypeptide Species.Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity.Apoptosis induced by islet amyloid polypeptide soluble oligomers is neutralized by diabetes-associated specific antibodies.Human IAPP-induced pancreatic β cell toxicity and its regulation by autophagy.Prion-Like Protein Aggregates and Type 2 Diabetes.The role of the 14-20 domain of the islet amyloid polypeptide in amyloid formationAutophagy protects against human islet amyloid polypeptide-associated apoptosisImplications of peptide assemblies in amyloid diseases.Kinetic profile of amyloid formation in the presence of an aromatic inhibitor by nuclear magnetic resonance.β-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation InhibitorThe S20G substitution in hIAPP is more amyloidogenic and cytotoxic than wild-type hIAPP in mouse isletsUnderstanding co-polymerization in amyloid formation by direct observation of mixed oligomers.Inhibition of IAPP aggregation by insulin depends on the insulin oligomeric state regulated by zinc ion concentration.Amylin gene promoter mutations predispose to Type 2 diabetes in New Zealand Maori.Seeding specificity in amyloid growth induced by heterologous fibrils.Luminescent platforms for monitoring changes in the solubility of amylin and huntingtin in living cells.Lysophosphatidylcholine modulates the aggregation of human islet amyloid polypeptide.Inhibition of hIAPP Amyloid Aggregation and Pancreatic β-Cell Toxicity by OH-Terminated PAMAM Dendrimer.
P2860
Q24311789-2C2C60FE-414F-4B36-A6A0-96FD44FC4937Q26751000-F3F28B9A-A718-43B5-A72E-74DA72B3C03BQ26774381-BFF1F341-91D3-45F7-97A1-5AFC94B78617Q26775893-FB50B1D0-7F3E-4842-89EB-BBDB475E9BF2Q26823708-5FBD6645-4389-47BE-A8FE-5DEA72810845Q27655644-C3C6FC73-48A7-4BB6-805C-6EB9CC1D2204Q28546876-F7A17ABC-C15F-4535-8C66-427427BCD1F8Q33356197-3A1FEAA9-3D57-46C0-A973-6E7656BAD7D4Q33585856-411A1D34-C3FB-422B-8AB1-61BD85D82378Q33609793-F051F3B5-6325-4550-803F-1BE6981248A0Q33628217-2AD58223-4B20-4BB3-B23A-4FA13EB1C2D9Q33653452-7AD9DCA8-2310-48AC-BB42-3B4AF55375E7Q34114138-B5C4CDE1-7E6B-498C-9DEC-B25FDC1A4E5CQ34469511-2394B582-E704-4F8F-8284-5F099B4EEFBFQ34536499-5603F8F4-E317-41E8-A908-3E45C02360B4Q34810595-0E93F83D-0650-4680-AB30-4B3C96FE45EBQ35612061-4442E691-AEC0-49F4-8E11-A1BE4E570763Q35743222-49720F27-0E88-4C96-8DAC-7D735712ECA6Q35822682-932E316D-CC3A-4642-ACC8-E4F822720A02Q36224635-194C1048-259F-4365-BCA7-D4B75127A419Q36327915-5A2874AB-6582-4068-9065-173113B10014Q36583195-CA23AD0A-A481-4EC2-AEE2-56023953957EQ37120813-B356568E-AD82-4F51-98EF-42B27D033A1CQ37552594-9438FF8F-82A5-40B5-B028-902186373861Q37614686-DF183CFE-EFA0-47D7-B7E0-183924D15952Q38974302-664A6DBE-E712-4DE9-B7E4-922EB2FEDC5FQ39118904-7F60AABC-A972-4DE3-A8CC-DB52B8214982Q39125816-8F0662CC-B9F7-4A98-B3D7-795CB382EF31Q39160829-F0FB1E9F-8AE2-44E4-B601-2001C376E125Q39431937-F1D9CA35-A84D-4E7C-80EA-2BCD38918F05Q39731518-09C2363B-C8FF-4C2F-8E2D-82553DBA5C52Q41117781-684F800D-2707-4D83-8485-B505EA79AD02Q41640199-699E8622-86A7-42F0-B5D6-424B93312407Q41774231-6B1C7BD6-89E8-4B5A-8F36-B9A374FA2534Q43130494-E64561EF-E0E4-43D3-B29F-31E42A3448C7Q44393188-33310B2B-B33A-4D2D-8DF9-5E14ED68E13FQ44748898-16488408-DC5E-42F3-85D1-5BA8A476C7B9Q45296620-691BEBFD-4909-48D4-A72B-03CC4AD53691Q47427685-BDD914FB-6185-41B4-9EBA-9D6A43DB6502Q50887393-AB2FA150-3BE2-448E-8CB3-C741F309E1DE
P2860
S20G mutant amylin exhibits increased in vitro amyloidogenicity and increased intracellular cytotoxicity compared to wild-type amylin.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
S20G mutant amylin exhibits in ...... compared to wild-type amylin.
@ast
S20G mutant amylin exhibits in ...... compared to wild-type amylin.
@en
type
label
S20G mutant amylin exhibits in ...... compared to wild-type amylin.
@ast
S20G mutant amylin exhibits in ...... compared to wild-type amylin.
@en
prefLabel
S20G mutant amylin exhibits in ...... compared to wild-type amylin.
@ast
S20G mutant amylin exhibits in ...... compared to wild-type amylin.
@en
P2093
P2860
P1476
S20G mutant amylin exhibits in ...... compared to wild-type amylin.
@en
P2093
H J Hiddinga
K Tateishi
N L Eberhardt
S Sakagashira
T Hanabusa
P2860
P304
P356
10.1016/S0002-9440(10)64848-1
P407
P577
2000-12-01T00:00:00Z