Zn(++) binding disrupts the Asp(23)-Lys(28) salt bridge without altering the hairpin-shaped cross-β Structure of Aβ(42) amyloid aggregates.
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(13)C-(13)c homonuclear recoupling in solid-state nuclear magnetic resonance at a moderately high magic-angle-spinning frequencyCurcumin alters the salt bridge-containing turn region in amyloid β(1-42) aggregates.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Steric Crowding of the Turn Region Alters the Tertiary Fold of Amyloid-β18-35 and Makes It Soluble.Zn(II) ions substantially perturb Cu(II) ion coordination in amyloid-β at physiological pH.On the mechanism of photoinduced dimer dissociation in the plant UVR8 photoreceptor.Zinc and Copper Differentially Modulate Amyloid Precursor Protein Processing by γ-Secretase and Amyloid-β Peptide Production.Thermodynamically stable amyloid-β monomers have much lower membrane affinity than the small oligomers.Divalent copper ion bound amyloid-β(40) and amyloid-β(42) alloforms are less preferred than divalent zinc ion bound amyloid-β(40) and amyloid-β(42) alloforms.Effects of Zn2+ binding on the structural and dynamic properties of amyloid β peptide associated with Alzheimer's disease: Asp1 or Glu11?A folding transition underlies the emergence of membrane affinity in amyloid-β.Major Reaction Coordinates Linking Transient Amyloid-β Oligomers to Fibrils Measured at Atomic Level.Carnosine inhibits Aβ(42) aggregation by perturbing the H-bond network in and around the central hydrophobic cluster.Sine-squared shifted pulses for recoupling interactions in solid-state NMR.Curcumin Dictates Divergent Fates for the Central Salt Bridges in Amyloid-β40 and Amyloid-β42.Solid-state NMR sequential assignment of an Amyloid-β(1-42) fibril polymorph.Nucleoside-2',3'/3',5'-bis(thio)phosphate antioxidants are also capable of disassembly of amyloid beta42-Zn(ii)/Cu(ii) aggregates via Zn(ii)/Cu(ii)-chelation.Significant structural differences between transient amyloid-β oligomers and less-toxic fibrils in regions known to harbor familial Alzheimer's mutations.Fe(2+) binding on amyloid β-peptide promotes aggregation.pH changes the aggregation propensity of amyloid-β without altering the monomer conformation.Zinc ion rapidly induces toxic, off-pathway amyloid-β oligomers distinct from amyloid-β derived diffusible ligands in Alzheimer's disease.Zinc-Mediated Binding of Nucleic Acids to Amyloid-β Aggregates: Role of Histidine Residues
P2860
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P2860
Zn(++) binding disrupts the Asp(23)-Lys(28) salt bridge without altering the hairpin-shaped cross-β Structure of Aβ(42) amyloid aggregates.
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2011年の論文
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2011年論文
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2011年論文
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2011年論文
@zh-hk
2011年論文
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2011年論文
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2011年论文
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name
Zn(++) binding disrupts the As ...... of Aβ(42) amyloid aggregates.
@ast
Zn(++) binding disrupts the As ...... of Aβ(42) amyloid aggregates.
@en
type
label
Zn(++) binding disrupts the As ...... of Aβ(42) amyloid aggregates.
@ast
Zn(++) binding disrupts the As ...... of Aβ(42) amyloid aggregates.
@en
prefLabel
Zn(++) binding disrupts the As ...... of Aβ(42) amyloid aggregates.
@ast
Zn(++) binding disrupts the As ...... of Aβ(42) amyloid aggregates.
@en
P2093
P2860
P1433
P1476
Zn(++) binding disrupts the As ...... e of Aβ(42) amyloid aggregates
@en
P2093
Debanjan Bhowmik
Muralidharan Chandrakesan
Perunthiruthy K Madhu
Venus Singh Mithu
P2860
P304
P356
10.1016/J.BPJ.2011.10.023
P407
P577
2011-12-01T00:00:00Z