Cargando…

Insights into the role of the beta-2 microglobulin D-strand in amyloid propensity revealed by mass spectrometry

In vivo beta-2 microglobulin (β(2)m) forms amyloid fibrils that are associated with the disease dialysis-related amyloidosis. Here, electrospray ionisation-ion mobility spectrometry-mass spectrometry has been used to compare the oligomers formed from wild-type β(2)m with those formed from a variant...

Descripción completa

Detalles Bibliográficos
Autores principales:	Leney, Aneika C., Pashley, Clare L., Scarff, Charlotte A., Radford, Sheena E., Ashcroft, Alison E.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Royal Society of Chemistry 2014
Materias:	Chemistry
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4006425/ https://www.ncbi.nlm.nih.gov/pubmed/24336936 http://dx.doi.org/10.1039/c3mb70420c

Ejemplares similares

Comparison of the aggregation of homologous β(2)-microglobulin variants reveals protein solubility as a key determinant of amyloid formation
por: Pashley, Clare L., et al.
Publicado: (2016)

Investigation of D76N β(2)-Microglobulin Using Protein Footprinting and Structural Mass Spectrometry
por: Cornwell, Owen, et al.
Publicado: (2021)

The role of conformational flexibility in β(2)-microglobulin amyloid fibril formation at neutral pH
por: Hodkinson, John P, et al.
Publicado: (2012)

Second Order Rate Constants of Donor-Strand Exchange Reveal Individual Amino Acid Residues Important in Determining the Subunit Specificity of Pilus Biogenesis
por: Leney, Aneika C., et al.
Publicado: (2011)

Ion Mobility Spectrometry–Mass Spectrometry Defines the Oligomeric Intermediates in Amylin Amyloid Formation and the Mode of Action of Inhibitors
por: Young, Lydia M., et al.
Publicado: (2013)

Understanding the complex mechanisms of β(2)-microglobulin amyloid assembly
por: Eichner, Timo, et al.
Publicado: (2011)

Examination of Ataxin-3 (atx-3) Aggregation by Structural Mass Spectrometry Techniques: A Rationale for Expedited Aggregation upon Polyglutamine (polyQ) Expansion
por: Scarff, Charlotte A., et al.
Publicado: (2015)

Amphipathic Polymers Enable the Study of Functional Membrane Proteins in the Gas Phase
por: Leney, Aneika C., et al.
Publicado: (2012)

Screening and classifying small molecule inhibitors of amyloid formation using ion mobility spectrometry-mass spectrometry
por: Young, Lydia M., et al.
Publicado: (2014)

Intermolecular Alignment in β(2)-Microglobulin Amyloid Fibrils
por: Debelouchina, Galia T., et al.
Publicado: (2010)

Advances in ion mobility spectrometry–mass spectrometry reveal key insights into amyloid assembly()
por: Woods, L.A., et al.
Publicado: (2013)

Stacked Sets of Parallel, In-register β-Strands of β(2)-Microglobulin in Amyloid Fibrils Revealed by Site-directed Spin Labeling and Chemical Labeling
por: Ladner, Carol L., et al.
Publicado: (2010)

Native Mass Spectrometry: What is in the Name?
por: Leney, Aneika C., et al.
Publicado: (2016)

HDX-ESI-MS Reveals Enhanced Conformational Dynamics of the Amyloidogenic Protein β(2)-Microglobulin upon Release from the MHC-1
por: Hodkinson, John P., et al.
Publicado: (2009)

Comparing Hydrogen Deuterium Exchange and Fast Photochemical Oxidation of Proteins: a Structural Characterisation of Wild-Type and ΔN6 β(2)-Microglobulin
por: Cornwell, Owen, et al.
Publicado: (2018)

A Common β-Sheet Architecture Underlies in Vitro and in Vivo β(2)-Microglobulin Amyloid Fibrils
por: Jahn, Thomas R., et al.
Publicado: (2008)

Extracellular matrix components modulate different stages in β(2)-microglobulin amyloid formation
por: Benseny-Cases, Núria, et al.
Publicado: (2019)

Globular Tetramers of β(2)-Microglobulin Assemble into Elaborate Amyloid Fibrils
por: White, Helen E., et al.
Publicado: (2009)

Monitoring Copopulated Conformational States During Protein Folding Events Using Electrospray Ionization-Ion Mobility Spectrometry-Mass Spectrometry
por: Smith, David P., et al.
Publicado: (2007)

A comparison of the folding characteristics of free and ribosome-tethered polypeptide chains using limited proteolysis and mass spectrometry
por: Rajabi, Khadijeh, et al.
Publicado: (2015)

Disease-relevant β(2)-microglobulin variants share a common amyloid fold
por: Wilkinson, Martin, et al.
Publicado: (2023)

Systematic analysis of the use of amphipathic polymers for studies of outer membrane proteins using mass spectrometry
por: Watkinson, Thomas G., et al.
Publicado: (2015)

Collagen I Weakly Interacts with the β-Sheets of β(2)-Microglobulin and Enhances Conformational Exchange To Induce Amyloid Formation
por: Hoop, Cody L., et al.
Publicado: (2019)

The Role of Chaperone-subunit Usher Domain Interactions in the Mechanism of Bacterial Pilus Biogenesis Revealed by ESI-MS
por: Morrissey, Bethny, et al.
Publicado: (2012)

The role of the I(T)-state in D76N β(2)-microglobulin amyloid assembly: A crucial intermediate or an innocuous bystander?
por: Smith, Hugh I., et al.
Publicado: (2020)

A tale of a tail: Structural insights into the conformational properties of the polyglutamine protein ataxin-3
por: Scarff, Charlotte A., et al.
Publicado: (2013)

The structure of a β(2)-microglobulin fibril suggests a molecular basis for its amyloid polymorphism
por: Iadanza, Matthew G., et al.
Publicado: (2018)

Molecular dynamics simulations of mechanical failure in polymorphic arrangements of amyloid fibrils containing structural defects
por: Ndlovu, Hlengisizwe, et al.
Publicado: (2013)

β(2)-Microglobulin Amyloid Fibril-Induced Membrane Disruption Is Enhanced by Endosomal Lipids and Acidic pH
por: Goodchild, Sophia C., et al.
Publicado: (2014)

Ionization methods in organic mass spectrometry
por: Ashcroft, Alison E.
Publicado: (1997)

β(2)-Microglobulin Amyloid Fibrils Are Nanoparticles That Disrupt Lysosomal Membrane Protein Trafficking and Inhibit Protein Degradation by Lysosomes
por: Jakhria, Toral, et al.
Publicado: (2014)

Discovering protein–protein interaction stabilisers by native mass spectrometry
por: Bellamy-Carter, Jeddidiah, et al.
Publicado: (2021)

Direct Monitoring of Protein O-GlcNAcylation by High-Resolution Native Mass Spectrometry
por: Leney, Aneika C., et al.
Publicado: (2017)

Glimpses of the molecular mechanisms of β(2)-microglobulin fibril formation in vitro: Aggregation on a complex energy landscape
por: Platt, Geoffrey W., et al.
Publicado: (2009)

Analysis of Amyloid Nanostructures Using Photo-cross-linking: In Situ Comparison of Three Widely Used Photo-cross-linkers
por: Preston, George W., et al.
Publicado: (2013)

Identification of a novel site of interaction between ataxin-3 and the amyloid aggregation inhibitor polyglutamine binding peptide 1
por: Knight, Patrick D, et al.
Publicado: (2017)

Understanding co-polymerization in amyloid formation by direct observation of mixed oligomers
por: Young, Lydia M., et al.
Publicado: (2017)

The Double-Edged Sword of Beta2-Microglobulin in Antibacterial Properties and Amyloid Fibril-Mediated Cytotoxicity
por: Chiou, Shean-Jaw, et al.
Publicado: (2021)

Mutational Analysis of the Ability of Resveratrol To Inhibit Amyloid Formation by Islet Amyloid Polypeptide: Critical Evaluation of the Importance of Aromatic–Inhibitor and Histidine–Inhibitor Interactions
por: Tu, Ling-Hsien, et al.
Publicado: (2014)

Fibril Growth Kinetics Reveal a Region of β(2)-microglobulin Important for Nucleation and Elongation of Aggregation
por: Platt, Geoffrey W., et al.
Publicado: (2008)

Cannot write session to /tmp/vufind_sessions/sess_su17kr7mi3htbajhp55ipb3nr1