Single-molecule atomic force microscopy force spectroscopy study of Aβ-40 interactions. - Wikidata - awgldk - TriplyDB

Single-molecule atomic force microscopy force spectroscopy study of Aβ-40 interactions.

Single-molecule atomic force microscopy force spectroscopy study of Aβ-40 interactions.

http://www.wikidata.org/entity/Q42008466

about

Diverse metastable structures formed by small oligomers of α-synuclein probed by force spectroscopy Bapineuzumab alters aβ composition: implications for the amyloid cascade hypothesis and anti-amyloid immunotherapy Atomic force microscopy with sub-picoNewton force stability for biological applications.Nano-assembly of amyloid β peptide: role of the hairpin fold.The structure of misfolded amyloidogenic dimers: computational analysis of force spectroscopy data.Nanoprobing of misfolding and interactions of amyloid β 42 protein.Effect of spermidine on misfolding and interactions of alpha-synuclein Cu(2+) affects amyloid-β (1-42) aggregation by increasing peptide-peptide binding forces.Nanoimaging for Molecular Pharmaceutics of Alzheimer's and other Neurodegenerative Disorders.Preventing disulfide bond formation weakens non-covalent forces among lysozyme aggregates Direct Detection of α-Synuclein Dimerization Dynamics: Single-Molecule Fluorescence Analysis.Protein misfolding occurs by slow diffusion across multiple barriers in a rough energy landscape.Copper-induced structural conversion templates prion protein oligomerization and neurotoxicity.Interpreting the widespread nonlinear force spectra of intermolecular bonds APOBEC3G Interacts with ssDNA by Two Modes: AFM Studies.Nanoprobing of the effect of Cu(2+) cations on misfolding, interaction and aggregation of amyloid β peptide.Novel polymer linkers for single molecule AFM force spectroscopy Single-Molecule Force Spectroscopy Studies of APOBEC3A-Single-Stranded DNA Complexes.Mechanism of amyloid β-protein dimerization determined using single-molecule AFM force spectroscopy.A Metal-free Click Chemistry Approach for the Assembly and Probing of Biomolecules.α-Synuclein misfolding assessed with single molecule AFM force spectroscopy: effect of pathogenic mutations.Probing interactions between human lung adenocarcinoma A549 cell and its aptamers at single-molecule resolution.Aβ42 and Aβ40: similarities and differences.Amyloid misfolding, aggregation, and the early onset of protein deposition diseases: insights from AFM experiments and computational analyses.Molecular mechanism of misfolding and aggregation of Aβ(13-23).Effect of acidic pH on the stability of α-synuclein dimers.Role of monomer arrangement in the amyloid self-assembly.Effect of electrostatics on aggregation of prion protein Sup35 peptide Comparison of three competing dynamic force spectroscopy models to study binding forces of amyloid-β (1-42).Single-molecule assays for investigating protein misfolding and aggregation.APP/Aβ structural diversity and Alzheimer's disease pathogenesis.Effects of force fields on the conformational and dynamic properties of amyloid β(1-40) dimer explored by replica exchange molecular dynamics simulations.Exploring the energy profile of human IgG/rat anti-human IgG interactions by dynamic force spectroscopy.Structural properties of amyloid β(1-40) dimer explored by replica exchange molecular dynamics simulations.Monomer Dynamics of Alzheimer Peptides and Kinetic Control of Early Aggregation in Alzheimer's Disease.A peptide-display protein scaffold to facilitate single molecule force studies of aggregation-prone peptides.Single-molecule probing of amyloid nano-ensembles using the polymer nanoarray approach.The mechanical response of hIAPP nanowires based on different bending direction simulations.

P2860

Q21132346-B5A5B200-5A4D-4AE5-9190-2974D8703DD6 Q28488690-620E96EF-2E6C-4559-935E-1763DE69A4B4 Q30540229-70C8412F-697E-4CF2-ADB4-3EA089B8D969 Q30853267-7645E6B4-B6CB-408D-8B3C-6C83FA8556FB Q30879019-BEF22A9E-B541-4DD2-892B-0BB8BCF4F428 Q33605232-CE7BA7A8-AC98-4542-818E-E97A9829CE53 Q34291522-6215F165-F4E3-40BA-B45E-691A1F32FFAF Q34639502-E04173D8-863B-4501-A2E1-3111701E41DD Q34887269-7983B741-8DC4-4687-B2A1-67D7C010D3B1 Q35097236-288DBC6A-F905-4BD9-AB93-53276EAEB65F Q35529960-E4A78D65-4509-4206-A210-306F48576484 Q35845795-0D5C4558-F0DB-4C75-9C37-0425CDD33A3D Q36078399-0E7CB19D-147F-48E1-9B5E-3552E1C4AD81 Q36187458-E718E1D8-0968-44FA-AD06-E70F34F3BC02 Q36209528-B78B9C8E-3769-483F-9CA6-F283940B8AA4 Q36652253-70432CC4-2418-4745-AF1F-26F16A981998 Q36974525-84483BDC-F62E-4E7E-90AE-8C38169AA12F Q37064877-4F1B6082-B7FF-4707-9614-0E1A6C49EECB Q37217625-29C96557-9443-491D-9FE1-A6DB2AF7C800 Q37317672-6A6A5368-1DB7-4404-BCC9-EF3D2C3B7F92 Q37351690-ABEE89A5-8B52-48CF-A3FC-9C508A0E251A Q38303776-412AA799-B27D-48FD-AFF8-DCEB3C6BFB12 Q38505163-B25802F5-12E5-4719-A258-B5B9E0CD7B28 Q39004129-56E0682E-D772-42E9-B9B4-24ACDF72A506 Q41509201-6CAB61BE-DC06-45B2-8109-E1BAE51775D5 Q41634522-F5A2D8B6-40C6-497B-A4D8-2BED29D5B106 Q41647318-4D413F80-A4F8-421A-8CB0-FDA4C9C7051D Q42399435-4F2E9237-7334-4F4F-98F7-2BC058FBBAB5 Q43693544-C8659735-07ED-4F19-824A-09661222E769 Q46164744-D0585573-85CA-4077-A5B6-2B1DEE1B6619 Q46320596-39BE54ED-9209-4EB5-A22E-3E44BC36117F Q47299318-AC1BADE5-3181-4DBB-B2AA-FC577A0D42CB Q47759826-3F94FC99-2BCB-4C87-A55F-BB5875E1D3F3 Q48046294-C4200CA9-4876-4EBB-97EF-6B850B0462F5 Q49425578-916BE776-38D6-45A5-817E-2C591F1537B3 Q50125039-5A0A017F-138F-4B9E-8ABE-28C41E7FDF6F Q50941257-DF4677CE-981B-4DB6-9D72-5958FA88C333 Q53488011-68F3C711-29EE-4B14-A8C6-8933BABFDE62

P2860

Single-molecule atomic force microscopy force spectroscopy study of Aβ-40 interactions.

http://www.wikidata.org/entity/Q42008466

description

2011 nî lūn-bûn

@nan

2011年の論文

@ja

2011年学术文章

@wuu

2011年学术文章

@zh-cn

2011年学术文章

@zh-hans

2011年学术文章

@zh-my

2011年学术文章

@zh-sg

2011年學術文章

@yue

2011年學術文章

@zh

2011年學術文章

@zh-hant

name

Single-molecule atomic force microscopy force spectroscopy study of Aβ-40 interactions.

@en

Single-molecule atomic force microscopy force spectroscopy study of Aβ-40 interactions.

@nl

type

label

Single-molecule atomic force microscopy force spectroscopy study of Aβ-40 interactions.

@en

Single-molecule atomic force microscopy force spectroscopy study of Aβ-40 interactions.

@nl

prefLabel

Single-molecule atomic force microscopy force spectroscopy study of Aβ-40 interactions.

@en

Single-molecule atomic force microscopy force spectroscopy study of Aβ-40 interactions.

@nl

P1433

Q42008466-129EA25E-EE38-4EFD-8F7E-25BC1101FBC1

P1476

Q42008466-81B5EAC7-F153-476A-90FB-DE8A9ACF60F2

P2093

Q42008466-65A82EFC-3F50-48CD-B4B6-2A4F9512F678

Q42008466-70055088-E9EA-43DD-8A95-38EFA85107FF

Q42008466-753E1749-DBCF-4A86-83BE-A2B0B17948C2

Q42008466-9E463371-A880-48D1-BD4D-6AB85B1A726C

Q42008466-A3C42859-B156-4DD2-94FF-2A09C629F6DD

Q42008466-B1E11B24-6987-442D-8F25-E06EB1397A99

P2860

Q42008466-02F3BAEC-4360-4D07-A051-BA06D4786CDE

Q42008466-0A6E2FE2-4E59-4599-8C6D-5FA0FC556FB3

Q42008466-0D61E7C1-1FA7-4847-BC7A-2DF2C11D6E24

Q42008466-1A1B2953-78E0-4C6F-9F28-E0327690823F

Q42008466-2847F2C0-E7E8-443B-AD64-AC62D974A7BA

Q42008466-2B2240E7-52A7-47BE-8238-28788D6DF30B

Q42008466-2C9205BD-E7C4-41F5-B7D4-1A1C022EB873

Q42008466-2D866F3A-A0A0-4A2B-A6DF-B83466724D05

Q42008466-2EA9A78C-C394-4BCB-AF52-BE06F0C07F68

Q42008466-35BD3586-7384-47C7-B92A-FA91BD33E1F3

P304

Q42008466-528A19D5-F65F-4F7D-96E4-FC24EDA3B44E

P31

Q42008466-7F78F1BA-6552-4FA6-AA8C-2A53A7FF9981

P356

Q42008466-21BAFF00-5E10-4173-B3F1-F2B9CC668A40

P407

Q42008466-50253419-ECAF-4756-9201-559209272A83

P433

Q42008466-6CB90E64-B074-4624-85D0-C5686ECD924D

P478

Q42008466-04A308B3-F16A-465B-A58D-755A0ED1A9DE

P577

Q42008466-D5BF175D-68DD-40FC-A3E7-C8CDC3593814

P5875

Q42008466-FEE9EDD5-4902-4323-A949-2837E663BFD5

P698

Q42008466-0156C8E1-2F51-4C38-870E-615AB5F4BF22

P932

Q42008466-FDF29E57-2D6B-4BF2-9A1E-004CFC6CA5DE

P356

P1433

P1476

Single-molecule atomic force microscopy force spectroscopy study of Aβ-40 interactions.

@en

P2093

Bo-Hyun Kim

http://www.w3.org/2001/XMLSchema#string

John F W Keana

http://www.w3.org/2001/XMLSchema#string

Nicholas Y Palermo

http://www.w3.org/2001/XMLSchema#string

Sandor Lovas

http://www.w3.org/2001/XMLSchema#string

Tatiana Zaikova

http://www.w3.org/2001/XMLSchema#string

Yuri L Lyubchenko

http://www.w3.org/2001/XMLSchema#string

P2860

Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory

Solid-state synthesis and mechanical unfolding of polymers of T4 lysozyme

Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils

Solution structure of amyloid beta-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?

Protein folding and misfolding

Entropic elasticity of lambda-phage DNA

A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR

Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils

Models for the specific adhesion of cells to cells

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

P304

5154-5162

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1021/BI200147A

http://www.w3.org/2001/XMLSchema#string

P407

P433

23

http://www.w3.org/2001/XMLSchema#string

P478

50

http://www.w3.org/2001/XMLSchema#string

P577

2011-05-17T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

51109169

http://www.w3.org/2001/XMLSchema#string

P698

21553928

http://www.w3.org/2001/XMLSchema#string

P932

3113552

http://www.w3.org/2001/XMLSchema#string