Cross-beta order and diversity in nanocrystals of an amyloid-forming peptide.
about
Structure of the cross-beta spine of amyloid-like fibrilsFactors That Drive Peptide Assembly from Native to Amyloid Structures: Experimental and Theoretical Analysis of [Leu-5]-Enkephalin MutantsSolid-state NMR as a probe of amyloid structureA multiscale approach to characterize the early aggregation steps of the amyloid-forming peptide GNNQQNY from the yeast prion sup-35Defining the conformational features of anchorless, poorly neuroinvasive prionsConformational switching within individual amyloid fibrils.Linear data mining the Wichita clinical matrix suggests sleep and allostatic load involvement in chronic fatigue syndrome.Parallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p.Molecular basis for amyloid fibril formation and stability.Strain-specific morphologies of yeast prion amyloid fibrils.Separating instability from aggregation propensity in γS-crystallin variants.Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMRMolecular dynamics analyses of cross-beta-spine steric zipper models: beta-sheet twisting and aggregation.Indexing amyloid peptide diffraction from serial femtosecond crystallography: new algorithms for sparse patternsStructural complexity of a composite amyloid fibril.A peptide study of the relationship between the collagen triple-helix and amyloidFrom conversion to aggregation: protofibril formation of the prion protein.Structural basis of infectious and non-infectious amyloidsAn amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibrilAmyloid-a state in many guises: survival of the fittest fibril fold.Ab initio structure determination from prion nanocrystals at atomic resolution by MicroED.Switching in amyloid structure within individual fibrils: implication for strain adaptation, species barrier and strain classificationBiological roles of prion domains.Nanomechanics of functional and pathological amyloid materials.Taking the measure of MicroED.High-Resolution Macromolecular Structure Determination by MicroED, a cryo-EM Method.The architecture of amyloid-like peptide fibrils revealed by X-ray scattering, diffraction and electron microscopy.Oligomerization of amyloid Abeta16-22 peptides using hydrogen bonds and hydrophobicity forces.Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines.The Rho Termination Factor of Clostridium botulinum Contains a Prion-Like Domain with a Highly Amyloidogenic Core.Phosphorylation as a tool to modulate aggregation propensity and to predict fibril architecture.Characterizing the assembly of the Sup35 yeast prion fragment, GNNQQNY: structural changes accompany a fiber-to-crystal switch.Dichotomous versus palm-type mechanisms of lateral assembly of amyloid fibrils.Characterization of large amyloid fibers and tapes with Fourier transform infrared (FT-IR) and Raman spectroscopy.Unraveling the aggregation propensity of human insulin C-peptide.Crystallographic insights into the self-assembly of KLVFF amyloid-beta peptides.The diversity and utility of amyloid fibrils formed by short amyloidogenic peptides.Macromolecular microcrystallography
P2860
Q24548308-B889768A-7614-4E76-BE78-C7748B95F258Q27684284-5A19C546-B195-4A28-A4AE-7AC31005C71BQ28388671-8A68209E-B929-445F-B161-6BCE7A666F77Q28478191-1940E656-7653-47BB-A7B7-7F2D3404243EQ28486278-312AF60E-2500-41B5-9C93-E8A571510524Q30481423-D99D4D18-DCB2-423D-A215-985393A3A26FQ31036503-A8427740-7BA2-45A9-AF85-1D04BA5E4F9EQ33220809-7ADEC33A-5170-4C3F-A6FD-205E6DFAD5EAQ33722932-E31F31A5-A03C-49AB-9579-A9C14A8CD046Q33900709-690D17A1-102A-42EA-A90F-B372BF03DE21Q34494376-F8BD710A-9F45-48BF-B18D-2FF381E8492CQ34520914-4A311FA9-0B26-4A3E-8FB7-356FCC28DFDBQ34984401-24D98273-BD3D-4CA5-8D17-B2AF1879E12AQ35063247-8EDC6A62-0DBD-4D9B-8438-7F719876DCC1Q35302543-3F8323D7-EE6B-4FAD-9DEC-746725716F5AQ36103947-439F81CD-46D8-40B8-884E-E1115812A152Q36601530-F49F40FA-7667-4496-90F9-F1431C229B88Q36944974-8B5FA252-B1C4-49AC-BECB-7E4714F729DBQ36986109-11ABE11B-BD6D-4BCB-AD04-7B3F6AC31276Q37016493-1D07A271-9DF0-4D51-871C-C466110E66C9Q37323015-ADB5F3D5-FE8B-4908-8C02-39A7BE896FBFQ37364765-C0215E29-2E42-4170-8EC5-12D63CC02BC5Q37378382-6DC2165E-A418-44A5-A4E2-8C8B5BDD0F2BQ37908990-B37D3BC6-8B84-43D0-B33F-539B15117021Q38709854-4F277E29-E3EB-4A5C-8E32-01B3F1AB62F7Q38940053-75C54BF3-8F7B-4926-B0CF-EB2B684132BDQ39338479-049D8616-C078-45F1-B10E-59A468E0A29BQ40307349-3EA59753-593D-4BA7-8B87-763195D386A4Q41540882-2E4E82D9-094E-4010-94F4-9EC14473B1E1Q41773166-63887E9B-3238-4F0B-B70D-DF7DC7F86FB2Q42123605-75A832BF-3285-47D8-9E2C-95E310710BA6Q42934740-1443CD19-79BE-496C-9642-09977604DF78Q43072334-A5EA52C7-6956-42EF-B539-17F62BC08135Q44991893-DDA571B7-6CCC-4404-B94E-0039271AFE32Q46600113-FB476CFC-63A1-40C0-B5BA-0F878A206CA3Q47311832-467E74D3-80F2-4229-85C1-008BFB5B5EE5Q48286492-371F3440-4B7F-4F34-8903-93D45846E52EQ58321503-5C832BC1-5277-4990-B954-7FDC3EDBC436
P2860
Cross-beta order and diversity in nanocrystals of an amyloid-forming peptide.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh
2003年學術文章
@zh-hant
name
Cross-beta order and diversity in nanocrystals of an amyloid-forming peptide.
@en
Cross-beta order and diversity in nanocrystals of an amyloid-forming peptide.
@nl
type
label
Cross-beta order and diversity in nanocrystals of an amyloid-forming peptide.
@en
Cross-beta order and diversity in nanocrystals of an amyloid-forming peptide.
@nl
prefLabel
Cross-beta order and diversity in nanocrystals of an amyloid-forming peptide.
@en
Cross-beta order and diversity in nanocrystals of an amyloid-forming peptide.
@nl
P2093
P1476
Cross-beta order and diversity in nanocrystals of an amyloid-forming peptide.
@en
P2093
Chris Long
David Eisenberg
Donald L D Caspar
Eric Fontano
Melinda Balbirnie
Robert Grothe
Ruben Diaz-Avalos
P304
P356
10.1016/S0022-2836(03)00659-4
P407
P577
2003-07-01T00:00:00Z