Probing neuroserpin polymerization and interaction with amyloid-beta peptides using single molecule fluorescence.
about
Assessing the causes and consequences of co-polymerization in amyloid formationThe extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptideTwo-Step Amyloid Aggregation: Sequential Lag Phase IntermediatesEarly amyloidogenic oligomerization studied through fluorescence lifetime correlation spectroscopy.Single-molecule fluorescence coincidence spectroscopy and its application to resonance energy transfer.A novel monoclonal antibody to characterize pathogenic polymers in liver disease associated with alpha1-antitrypsin deficiency.Defining the mechanism of polymerization in the serpinopathies.The tempered polymerization of human neuroserpin.Direct observation of the interconversion of normal and toxic forms of α-synucleinThree new alpha1-antitrypsin deficiency variants help to define a C-terminal region regulating conformational change and polymerization.Functional and dysfunctional conformers of human neuroserpin characterized by optical spectroscopies and Molecular DynamicsAntithrombin III deficiency in Indian patients with deep vein thrombosis: identification of first India based AT variants including a novel point mutation (T280A) that leads to aggregation.Local conformational flexibility provides a basis for facile polymer formation in human neuroserpinDetermining serpin conformational distributions with single molecule fluorescenceUnravelling the twists and turns of the serpinopathies.Imaging the cell surface and its organization down to the level of single molecules.Protein accumulation in the endoplasmic reticulum as a non-equilibrium phase transition.The pathological Trento variant of alpha-1-antitrypsin (E75V) shows nonclassical behaviour during polymerization.Glaucoma is associated with plasmin proteolytic activation mediated through oxidative inactivation of neuroserpin.Two latent and two hyperstable polymeric forms of human neuroserpin.Probing the folding pathway of a consensus serpin using single tryptophan mutants.On the molecular structure of human neuroserpin polymers.Molecular bases of neuroserpin function and pathology.SOLVING SINGLE BIOMOLECULES BY ADVANCED FRET-BASED SINGLE-MOLECULE FLUORESCENCE TECHNIQUES
P2860
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P2860
Probing neuroserpin polymerization and interaction with amyloid-beta peptides using single molecule fluorescence.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
@zh
2009年學術文章
@zh-hant
name
Probing neuroserpin polymeriza ...... single molecule fluorescence.
@en
Probing neuroserpin polymeriza ...... single molecule fluorescence.
@nl
type
label
Probing neuroserpin polymeriza ...... single molecule fluorescence.
@en
Probing neuroserpin polymeriza ...... single molecule fluorescence.
@nl
prefLabel
Probing neuroserpin polymeriza ...... single molecule fluorescence.
@en
Probing neuroserpin polymeriza ...... single molecule fluorescence.
@nl
P2093
P2860
P50
P1433
P1476
Probing neuroserpin polymeriza ...... g single molecule fluorescence
@en
P2093
David A Lomas
Didier Belorgey
Paul D Dunne
Peter Hägglöf
Susanna Karlsson-Li
P2860
P304
P356
10.1016/J.BPJ.2009.07.057
P407
P577
2009-10-01T00:00:00Z