ReviewFEBS letters2009
Glimpses of the molecular mechanisms of beta2-microglobulin fibril formation in vitro: aggregation on a complex energy landscape.
Review in FEBS letters, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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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
31 citing papers in PubMed, 63 citations in OpenAlex.
- Plant Hormone Cytokinin as Aggregation Modulator of Gelsolin Amyloidosis.Journal of peptide science : an official publication of the European Peptide Society · 2025Article
- The residues 4 to 6 at the N-terminus in particular modulate fibril propagation of β-microglobulin.Acta biochimica et biophysica Sinica · 2022Article
- Collagen I Weakly Interacts with the β-Sheets of βJournal of the American Chemical Society · 2020Article
- 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
- Article
- Extracellular matrix components modulate different stages in βThe Journal of biological chemistry · 2019Article
- Understanding co-polymerization in amyloid formation by direct observation of mixed oligomers.Chemical science · 2017Article
- Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation.International journal of molecular sciences · 2017Article
- Stepwise unfolding of human βEuropean biophysics journal : EBJ · 2017Article
- A Population Shift between Sparsely Populated Folding Intermediates Determines Amyloidogenicity.Journal of the American Chemical Society · 2016Article
- A covalent homodimer probing early oligomers along amyloid aggregation.Scientific reports · 2015Article
- Structural and Thermodynamic Characteristics of Amyloidogenic Intermediates of β-2-Microglobulin.Scientific reports · 2015Article
- Distinguishing closely related amyloid precursors using an RNA aptamer.The Journal of biological chemistry · 2014Article
- A simulated intermediate state for folding and aggregation provides insights into ΔN6 β2-microglobulin amyloidogenic behavior.PLoS computational biology · 2014Article
- Conformer-specific characterization of nonnative protein states using hydrogen exchange and top-down mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Assessing the effect of loop mutations in the folding space of β2-microglobulin with molecular dynamics simulations.International journal of molecular sciences · 2013Article
- The role of amyloidogenic protein oligomerization in neurodegenerative disease.Journal of molecular medicine (Berlin, Germany) · 2013Review
- Understanding protein aggregation from the view of monomer dynamics.Molecular bioSystems · 2013Review
- The role of conformational flexibility in β2-microglobulin amyloid fibril formation at neutral pH.Rapid communications in mass spectrometry : RCM · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Beta(2)-microglobulin (beta(2)m) is a 99-residue protein that aggregates to form amyloid fibrils in dialysis-related amyloidosis. The protein provides a powerful model for exploration of the structural molecular mechanisms of fibril formation from a full-length protein in vitro. Fibrils have been assembled from beta(2)m under both low pH conditions, where the precursor is disordered, and at neutral pH where the protein is initially natively folded. Here we discuss the roles of sequence and structure in amyloid formation, the current understanding of the structural mechanisms of the early stages of aggregation of beta(2)m at both low and neutral pH, and the common and distinct features of these assembly pathways.
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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.