scholarly article | Q13442814 |
P819 | ADS bibcode | 2011PLoSO...620289R |
P356 | DOI | 10.1371/JOURNAL.PONE.0020289 |
P932 | PMC publication ID | 3102090 |
P698 | PubMed publication ID | 21633500 |
P5875 | ResearchGate publication ID | 51184774 |
P50 | author | Aphrodite Kapurniotu | Q89122692 |
Erika Andreetto | Q127595596 | ||
Nasrollah Rezaei-Ghaleh | Q43376210 | ||
Markus Zweckstetter | Q28320715 | ||
P2093 | author name string | Li-Mei Yan | |
P2860 | cites work | A Single-Point Mutation Converts the Highly Amyloidogenic Human Islet Amyloid Polypeptide into a Potent Fibrillization Inhibitor | Q59600449 |
Nuclear magnetic resonance investigation of 15N-labeled histidine in aqueous solution | Q67715398 | ||
Aggregation of an amyloidogenic fragment of human islet amyloid polypeptide | Q73435436 | ||
Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro | Q77223240 | ||
IAPP mimic blocks Abeta cytotoxic self-assembly: cross-suppression of amyloid toxicity of Abeta and IAPP suggests a molecular link between Alzheimer's disease and type II diabetes | Q79489683 | ||
Exploiting cross-amyloid interactions to inhibit protein aggregation but not function: nanomolar affinity inhibition of insulin aggregation by an IAPP mimic | Q39952634 | ||
Production of the Alzheimer amyloid beta protein by normal proteolytic processing | Q41599298 | ||
Binding of amyloid beta-peptide to ganglioside micelles is dependent on histidine-13. | Q41816548 | ||
On the nucleation of amyloid beta-protein monomer folding | Q42215600 | ||
Identification of hot regions of the Abeta-IAPP interaction interface as high-affinity binding sites in both cross- and self-association | Q44259570 | ||
In vitro aging of beta-amyloid protein causes peptide aggregation and neurotoxicity | Q44418518 | ||
Solution NMR studies of the A beta(1-40) and A beta(1-42) peptides establish that the Met35 oxidation state affects the mechanism of amyloid formation | Q44769438 | ||
Association of highly compact type II diabetes related islet amyloid polypeptide intermediate species at physiological temperature revealed by diffusion NMR spectroscopy | Q46613594 | ||
Structure-based design and study of non-amyloidogenic, double N-methylated IAPP amyloid core sequences as inhibitors of IAPP amyloid formation and cytotoxicity | Q46792358 | ||
Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. | Q48093908 | ||
Deposition of monomeric, not oligomeric, Abeta mediates growth of Alzheimer's disease amyloid plaques in human brain preparations. | Q48140756 | ||
Characterization of chemical exchange between soluble and aggregated states of beta-amyloid by solution-state NMR upon variation of salt conditions | Q49092413 | ||
Positioning of the Alzheimer Abeta(1-40) peptide in SDS micelles using NMR and paramagnetic probes. | Q53387908 | ||
Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers | Q22251089 | ||
Abeta and tau form soluble complexes that may promote self aggregation of both into the insoluble forms observed in Alzheimer's disease | Q24302457 | ||
Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus | Q24310340 | ||
The Alzheimer's peptide a beta adopts a collapsed coil structure in water | Q27626446 | ||
Stabilization of a -hairpin in monomeric Alzheimer's amyloid- peptide inhibits amyloid formation | Q27650192 | ||
The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics | Q27860914 | ||
Protein misfolding, functional amyloid, and human disease | Q28131732 | ||
A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR | Q28387681 | ||
Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins | Q29547593 | ||
A beta oligomers - a decade of discovery | Q29615152 | ||
3D structure of Alzheimer's amyloid-beta(1-42) fibrils | Q29617475 | ||
NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, A beta(1-40)(ox) and A beta(1-42)(ox). | Q30666112 | ||
Accurate quantitation of water-amide proton exchange rates using the phase-modulated CLEAN chemical EXchange (CLEANEX-PM) approach with a Fast-HSQC (FHSQC) detection scheme | Q32049995 | ||
The metal binding site of the hepatitis C virus NS3 protease. A spectroscopic investigation. | Q32052862 | ||
EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity. | Q33842865 | ||
Synthetic peptide homologous to beta protein from Alzheimer disease forms amyloid-like fibrils in vitro | Q34350864 | ||
Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide (IAPP) as nanomolar affinity inhibitor of IAPP cytotoxic fibrillogenesis | Q34478940 | ||
Structural characterization of a soluble amyloid beta-peptide oligomer. | Q34944603 | ||
Amylin agonists: a novel approach in the treatment of diabetes | Q35961978 | ||
The clinical and biological relationship between Type II diabetes mellitus and Alzheimer's disease | Q36173253 | ||
Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques | Q36277950 | ||
Sedimentation studies on human amylin fail to detect low-molecular-weight oligomers | Q36494750 | ||
Alzheimer's disease: strategies for disease modification | Q37739810 | ||
P275 | copyright license | Creative Commons Attribution 4.0 International | Q20007257 |
P6216 | copyright status | copyrighted | Q50423863 |
P433 | issue | 5 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | e20289 | |
P577 | publication date | 2011-01-01 | |
P1433 | published in | PLOS One | Q564954 |
P1476 | title | Interaction between amyloid beta peptide and an aggregation blocker peptide mimicking islet amyloid polypeptide | |
P478 | volume | 6 |
Q48909920 | A computational study of self-assembled hexapeptide inhibitors against amyloid-β (Aβ) aggregation |
Q36840033 | APP Receptor? To Be or Not To Be. |
Q30175699 | Amyloid β (Aβ) peptide directly activates amylin-3 receptor subtype by triggering multiple intracellular signaling pathways |
Q33893017 | Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies |
Q37191689 | Aβ monomers transiently sample oligomer and fibril-like configurations: ensemble characterization using a combined MD/NMR approach |
Q35072161 | Biochemical insight into the prion protein family |
Q47676441 | Common molecular pathogenesis of disease-related intrinsically disordered proteins revealed by NMR analysis |
Q91822502 | Concomitant disorder and high-affinity zinc binding in the human zinc- and iron-regulated transport protein 4 intracellular loop |
Q92797168 | Epitope Mapping by NMR of a Novel Anti-Aβ Antibody (STAB-MAb) |
Q38002804 | Intrinsically disordered proteins: from sequence and conformational properties toward drug discovery |
Q91710089 | Islet Amyloid Polypeptide: A Partner in Crime With Aβ in the Pathology of Alzheimer's Disease |
Q37080680 | Lessons from two prevalent amyloidoses-what amylin and Aβ have in common |
Q36118412 | NMR characterization of monomeric and oligomeric conformations of human calcitonin and its interaction with EGCG. |
Q27022467 | On the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP Peptides |
Q40387790 | Peptide fibrils as monomer storage of the covalent HIV-1 integrase inhibitor |
Q64781347 | Pre-structured hydrophobic peptide β-strands: A universal amyloid trap? |
Q28550062 | Purification and Characterization of Recombinant N-Terminally Pyroglutamate-Modified Amyloid-β Variants and Structural Analysis by Solution NMR Spectroscopy |
Q39257498 | S100A6 amyloid fibril formation is calcium-modulated and enhances superoxide dismutase-1 (SOD1) aggregation |
Q30379691 | Structural Mechanism of the Interaction of Alzheimer Disease Aβ Fibrils with the Non-steroidal Anti-inflammatory Drug (NSAID) Sulindac Sulfide |
Q47110086 | The Aβ40 and Aβ42 peptides self-assemble into separate homomolecular fibrils in binary mixtures but cross-react during primary nucleation. |
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