Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes.
about
MCP-1 upregulates amylin expression in murine pancreatic β cells through ERK/JNK-AP1 and NF-κB related signaling pathways independent of CCR2Blockade of islet amyloid polypeptide fibrillation and cytotoxicity by the secretory chaperones 7B2 and proSAASA hIAPP-derived all-D-amino-acid inhibits hIAPP fibrillation efficiently at membrane surface by targeting α-helical oligomeric intermediatesApoptosis in pancreatic β-islet cells in Type 2 diabetesCommon mechanisms involved in Alzheimer's disease and type 2 diabetes: a key role of chronic bacterial infection and inflammationPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)The Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPPType 2 diabetes: etiology and reversibilityHsp72 (HSPA1A) Prevents Human Islet Amyloid Polypeptide Aggregation and Toxicity: A New Approach for Type 2 Diabetes TreatmentSex and Immunogen-Specific Benefits of Immunotherapy Targeting Islet Amyloid Polypeptide in Transgenic and Wild-Type Miceβ-cell dysfunction: Its critical role in prevention and management of type 2 diabetes.Urinary collagen fragments are significantly altered in diabetes: a link to pathophysiologySecondary Structure of Rat and Human Amylin across Force FieldsDirect detection of transient alpha-helical states in islet amyloid polypeptideRegular physical exercise training assists in preventing type 2 diabetes development: focus on its antioxidant and anti-inflammatory properties.Novel insights into protein misfolding diseases revealed by ion mobility-mass spectrometry.Human islet amyloid polypeptide monomers form ordered beta-hairpins: a possible direct amyloidogenic precursor.Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions.Islet amyloid formation is an important determinant for inducing islet inflammation in high-fat-fed human IAPP transgenic mice.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 studyDefining and characterizing the progression of type 2 diabetes.Selection for nonamyloidogenic mutants of islet amyloid polypeptide (IAPP) identifies an extended region for amyloidogenicity.Telocytes in human isolated atrial amyloidosis: ultrastructural remodelling.Current status of islet cell replacement and regeneration therapy.The therapeutic potential of metabolic hormones in the treatment of age-related cognitive decline and Alzheimer's disease.Synthetic alpha-helix mimetics as agonists and antagonists of islet amyloid polypeptide aggregation.A susceptibility gene for type 2 diabetes confers substantial risk for diabetes complicating cystic fibrosisNeprilysin impedes islet amyloid formation by inhibition of fibril formation rather than peptide degradation.Beta amyloid and hyperphosphorylated tau deposits in the pancreas in type 2 diabetes.Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanolsMorin hydrate inhibits amyloid formation by islet amyloid polypeptide and disaggregates amyloid fibers.Defining the molecular basis of amyloid inhibitors: human islet amyloid polypeptide-insulin interactions.Nonhuman primates and other animal models in diabetes research.Islet amyloid with macrophage migration correlates with augmented β-cell deficits in type 2 diabetic patientsConformations of islet amyloid polypeptide monomers in a membrane environment: implications for fibril formation.Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide (IAPP) as nanomolar affinity inhibitor of IAPP cytotoxic fibrillogenesisBiphasic effects of insulin on islet amyloid polypeptide membrane disruption.Noncerebral Amyloidoses: Aspects on Seeding, Cross-Seeding, and Transmission.The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity.
P2860
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P2860
Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes.
@ast
Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes.
@en
type
label
Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes.
@ast
Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes.
@en
prefLabel
Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes.
@ast
Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes.
@en
P2093
P356
P1476
Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes.
@en
P2093
Gunilla T Westermark
Per Westermark
Rebecca L Hull
P304
P356
10.1210/JC.2004-0405
P407
P577
2004-08-01T00:00:00Z