ArticleBiophysical journal2011
Structure and dynamics of oligomeric intermediates in β2-microglobulin self-assembly.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed.
- Molecular Mechanisms of Inhibition of Protein Amyloid Fibril Formation: Evidence and Perspectives Based on Kinetic Models.International journal of molecular sciences · 2022Review
- Visualizing and trapping transient oligomers in amyloid assembly pathways.Biophysical chemistry · 2021Review
- Structural Heterogeneity in the Preamyloid Oligomers of β-2-Microglobulin.Journal of molecular biology · 2020Article
- The Early Phase of β2-Microglobulin Aggregation: Perspectives From Molecular Simulations.Frontiers in molecular biosciences · 2020Review
- A specific nanobody prevents amyloidogenesis of D76N βScientific reports · 2017Article
- Uncovering the Early Assembly Mechanism for Amyloidogenic β2-Microglobulin Using Cross-linking and Native Mass Spectrometry.The Journal of biological chemistry · 2016Article
- ESI-IMS-MS: A method for rapid analysis of protein aggregation and its inhibition by small molecules.Methods (San Diego, Calif.) · 2016Article
- The power of ion mobility-mass spectrometry for structural characterization and the study of conformational dynamics.Nature chemistry · 2014Review
- Insights into the role of the beta-2 microglobulin D-strand in amyloid propensity revealed by mass spectrometry.Molecular bioSystems · 2014Article
- Robotically assisted titration coupled to ion mobility-mass spectrometry reveals the interface structures and analysis parameters critical for multiprotein topology mapping.Analytical chemistry · 2013Article
- Mass spectrometry coupled experiments and protein structure modeling methods.International journal of molecular sciences · 2013Review
- The role of initial oligomers in amyloid fibril formation by human stefin B.International journal of molecular sciences · 2013Article
- A tale of a tail: Structural insights into the conformational properties of the polyglutamine protein ataxin-3.International journal of mass spectrometry · 2013Article
- Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly.Biochimica et biophysica acta · 2013Review
- Selective molecular recognition in amyloid growth and transmission and cross-species barriers.Journal of molecular biology · 2012Review
- Integrating mass spectrometry of intact protein complexes into structural proteomics.Proteomics · 2012Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
β(2)-Microglobulin is a 99-residue protein with a propensity to form amyloid-like fibrils in vitro which exhibit distinct morphologies dependent on the solution conditions employed. Here we have used ion mobility spectrometry-mass spectrometry to characterize the oligomeric species detected during the formation of worm-like fibrils of β(2)-microglobulin at pH 3.6. Immediately upon sample dissolution, β(2)-microglobulin monomer and oligomers-the latter ranging in size from dimer to hexamer-are present as a pool of rapidly interconverting species. Increasing the ionic strength of the solution initiates fibril formation without a lag-phase whereupon these oligomers become more stable and higher-order species (7-mer to >14-mer) are observed. The oligomers detected have collision cross-sectional areas consistent with a linearly stacked assembly comprising subunits of native-like volume. The results provide insights into the identity and properties of the transient, oligomeric intermediates formed during assembly of worm-like fibrils and identify species that differ significantly from the oligomers previously characterized during the nucleated assembly of long, straight fibrils. The data presented demonstrate the interrelationship between different fibril-forming pathways and identify their points of divergence.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.