ArticleThe Journal of biological chemistry2010
Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein beta2-microglobulin revealed by real-time two-dimensional NMR.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 60 citations in OpenAlex.
- Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics.Magnetic resonance (Gottingen, Germany) · 2021Review
- Collagen I Weakly Interacts with the β-Sheets of βJournal of the American Chemical Society · 2020Article
- The Early Phase of β2-Microglobulin Aggregation: Perspectives From Molecular Simulations.Frontiers in molecular biosciences · 2020Review
- Optimized fast mixing device for real-time NMR applications.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2017Article
- A strategy for co-translational folding studies of ribosome-bound nascent chain complexes using NMR spectroscopy.Nature protocols · 2016Article
- A Population Shift between Sparsely Populated Folding Intermediates Determines Amyloidogenicity.Journal of the American Chemical Society · 2016Article
- Structural and Thermodynamic Characteristics of Amyloidogenic Intermediates of β-2-Microglobulin.Scientific reports · 2015Article
- Mechanisms of amyloid formation revealed by solution NMR.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- Two dimensional NMR spectroscopic approaches for exploring plant metabolome: A review.Journal of advanced research · 2015Review
- Spatially selective heteronuclear multiple-quantum coherence spectroscopy for biomolecular NMR studies.Chemphyschem : a European journal of chemical physics and physical chemistry · 2014Article
- A simulated intermediate state for folding and aggregation provides insights into ΔN6 β2-microglobulin amyloidogenic behavior.PLoS computational biology · 2014Article
- Ultrafast 2D NMR: an emerging tool in analytical spectroscopy.Annual review of analytical chemistry (Palo Alto, Calif.) · 2014Review
- Protein folding on the ribosome studied using NMR spectroscopy.Progress in nuclear magnetic resonance spectroscopy · 2013Review
- The role of conformational flexibility in β2-microglobulin amyloid fibril formation at neutral pH.Rapid communications in mass spectrometry : RCM · 2012Article
- Selective molecular recognition in amyloid growth and transmission and cross-species barriers.Journal of molecular biology · 2012Review
- Understanding the complex mechanisms of β2-microglobulin amyloid assembly.The FEBS journal · 2011Review
- An introduction to NMR-based approaches for measuring protein dynamics.Biochimica et biophysica acta · 2011Review
- Inhibition of beta2-microglobulin amyloid fibril formation by alpha2-macroglobulin.The Journal of biological chemistry · 2011Article
- Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy.Journal of biomolecular NMR · 2011Article
- Conformational conversion during amyloid formation at atomic resolution.Molecular cell · 2011Article
Corrections and comments
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Authors and funding
14 authors at 6 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Beta2-microglobulin (beta2m), the light chain of class I major histocompatibility complex, is responsible for the dialysis-related amyloidosis and, in patients undergoing long term dialysis, the full-length and chemically unmodified beta2m converts into amyloid fibrils. The protein, belonging to the immunoglobulin superfamily, in common to other members of this family, experiences during its folding a long-lived intermediate associated to the trans-to-cis isomerization of Pro-32 that has been addressed as the precursor of the amyloid fibril formation. In this respect, previous studies on the W60G beta2m mutant, showing that the lack of Trp-60 prevents fibril formation in mild aggregating condition, prompted us to reinvestigate the refolding kinetics of wild type and W60G beta2m at atomic resolution by real-time NMR. The analysis, conducted at ambient temperature by the band selective flip angle short transient real-time two-dimensional NMR techniques and probing the beta2m states every 15 s, revealed a more complex folding energy landscape than previously reported for wild type beta2m, involving more than a single intermediate species, and shedding new light into the fibrillogenic pathway. Moreover, a significant difference in the kinetic scheme previously characterized by optical spectroscopic methods was discovered for the W60G beta2m mutant.
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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.