The controlling roles of Trp60 and Trp95 in beta2-microglobulin function, folding and amyloid aggregation properties
about
D-strand perturbation and amyloid propensity in beta-2 microglobulinThe two tryptophans of β2-microglobulin have distinct roles in function and folding and might represent two independent responses to evolutionary pressureSystemic amyloidosis: lessons from β2-microglobulin.Equilibrium unfolding thermodynamics of beta2-microglobulin analyzed through native-state H/D exchangeInsights into the role of the beta-2 microglobulin D-strand in amyloid propensity revealed by mass spectrometryEffect of tetracyclines on the dynamics of formation and destructuration of beta2-microglobulin amyloid fibrils.Energy landscapes of functional proteins are inherently risky.Wild type beta-2 microglobulin and DE loop mutants display a common fibrillar architectureDecoding the Structural Bases of D76N ß2-Microglobulin High Amyloidogenicity through Crystallography and Asn-Scan Mutagenesis.Structure, stability, and aggregation of β-2 microglobulin mutants: insights from a Fourier transform infrared study in solution and in the crystalline stateEnergetics and mechanism of the normal-to-amyloidogenic isomerization of β2-microglobulin: on-the-fly string method calculationsThe Implication and Significance of Beta 2 Microglobulin: A Conservative Multifunctional Regulator.Glimpses of the molecular mechanisms of beta2-microglobulin fibril formation in vitro: aggregation on a complex energy landscapebeta(2)-microglobulin: from physiology to amyloidosis.Understanding the complex mechanisms of β2-microglobulin amyloid assembly.Fast real-time NMR methods for characterizing short-lived molecular states.Comparative Analyses of the Relative Effects of Various Mutations in Major Histocompatibility Complex I-a Way to Predict Protein-Protein Interactions.Insights from molecular dynamics simulations for computational protein design.Increased β-Sheet Dynamics and D-E Loop Repositioning Are Necessary for Cu(II)-Induced Amyloid Formation by β-2-Microglobulin.A covalent homodimer probing early oligomers along amyloid aggregation.Capillary electrophoresis analysis of different variants of the amyloidogenic protein β2 -microglobulin as a simple tool for misfolding and stability studies.Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability.β2-microglobulin gene duplication in cetartiodactyla remains intact only in pigs and possibly confers selective advantage to the species.Delineating the conformational elements responsible for Cu(2+)-induced oligomerization of beta-2 microglobulin.Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein beta2-microglobulin revealed by real-time two-dimensional NMR.DE-loop mutations affect beta2 microglobulin stability, oligomerization, and the low-pH unfolded formStudying interactions by molecular dynamics simulations at high concentration.Assessing the effect of loop mutations in the folding space of β2-microglobulin with molecular dynamics simulations.The role of conformational flexibility in β2-microglobulin amyloid fibril formation at neutral pH.Optimized fast mixing device for real-time NMR applications.An Asp to Asn mutation is a toxic trigger in beta-2 microglobulin: structure and biophysics.NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules.Dynamics of free versus complexed β2-microglobulin and the evolution of interfaces in MHC class I molecules.Reduction of conformational mobility and aggregation in W60G β2-microglobulin: assessment by 15N NMR relaxation.Conformational dynamics in crystals reveal the molecular bases for D76N beta-2 microglobulin aggregation propensity.Characterization of β2-microglobulin conformational intermediates associated to different fibrillation conditionsDetermination of protein folding kinetic types using sequence and predicted secondary structure and solvent accessibility
P2860
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P2860
The controlling roles of Trp60 and Trp95 in beta2-microglobulin function, folding and amyloid aggregation properties
description
2008 nî lūn-bûn
@nan
2008 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
The controlling roles of Trp60 ...... amyloid aggregation properties
@ast
The controlling roles of Trp60 ...... amyloid aggregation properties
@en
The controlling roles of Trp60 ...... amyloid aggregation properties
@nl
type
label
The controlling roles of Trp60 ...... amyloid aggregation properties
@ast
The controlling roles of Trp60 ...... amyloid aggregation properties
@en
The controlling roles of Trp60 ...... amyloid aggregation properties
@nl
prefLabel
The controlling roles of Trp60 ...... amyloid aggregation properties
@ast
The controlling roles of Trp60 ...... amyloid aggregation properties
@en
The controlling roles of Trp60 ...... amyloid aggregation properties
@nl
P2093
P50
P1476
The controlling roles of Trp60 ...... amyloid aggregation properties
@en
P2093
Carlo E M Pucillo
Devrim Gümral
Elena Betto
Enrico Rennella
Gennaro Esposito
Monica Stoppini
Paolo Viglino
Sara Raimondi
Sofia Giorgetti
Vittorio Bellotti
P304
P356
10.1016/J.JMB.2008.03.002
P407
P50
P577
2008-05-09T00:00:00Z