Evidence map›Paper›PMID 21077676›Full record

ArticleJournal of the American Chemical Society2010

Intermolecular alignment in β2-microglobulin amyloid fibrils.

Galia T Debelouchina, Geoffrey W Platt, Marvin J Bayro, Sheena E Radford, Robert G Griffin

Open access · bronzeAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
5.9field-weighted citation impact, top 3% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

38 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Disease-relevant βNature communications · 2023
    Article
  3. Article
  4. Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. The structure of a βNature communications · 2018
    Article
  7. Article
  8. Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  9. Article
  10. Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils.Journal of the American Chemical Society · 2016
    Article
  11. Article
  12. Review
  13. Structure and assembly of the mouse ASC inflammasome by combined NMR spectroscopy and cryo-electron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  14. Mechanisms of amyloid formation revealed by solution NMR.Progress in nuclear magnetic resonance spectroscopy · 2015
    Review
  15. Article
  16. Physical and structural basis for polymorphism in amyloid fibrils.Protein science : a publication of the Protein Society · 2014
    Review
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Galia T DebelouchinaDepartment of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Geoffrey W Platt
Marvin J Bayro
Sheena E Radford
Robert G Griffin
University of Leeds · GB

Funding

OverallP41EB002026 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$17.9M
XRAY CRYSTALLOGRAPHIC STRUCTURE ANALYSIS: PROTEIN SORTINGP41RR001081 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BABBITT, PATRICIA CLEMENT · 1985 to 2011
$17.6M
Solid State NMR Studies of Peptides and ProteinsR01EB003151 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2004 to 2015
$6.5M
NCRR NIH HHS P41 RR001081NCRR NIH HHS P41 RR-01081NIBIB NIH HHS EB002026NIBIB NIH HHS EB003151NIBIB NIH HHS P41 EB002026NIBIB NIH HHS R01 EB003151Wellcome TrustWellcome Trust 062164Wellcome Trust 075675
6 · The paper itself

Abstract

The deposition of amyloid-like fibrils, composed primarily of the 99-residue protein β2-microglobulin (β2m), is one of the characteristic symptoms of dialysis-related amyloidosis. Fibrils formed in vitro at low pH and low salt concentration share many properties with the disease related fibrils and have been extensively studied by a number of biochemical and biophysical methods. These fibrils contain a significant β-sheet core and have a complex cryoEM electron density profile. Here, we investigate the intrasheet arrangement of the fibrils by means of (15)N-(13)C MAS NMR correlation spectroscopy. We utilize a fibril sample grown from a 50:50 mixture of (15)N,(12)C- and (14)N,(13)C-labeled β2m monomers, the latter prepared using 2-(13)C glycerol as the carbon source. Together with the use of ZF-TEDOR mixing, this sample allowed us to observe intermolecular (15)N-(13)C backbone-to-backbone contacts with excellent resolution and good sensitivity. The results are consistent with a parallel, in-register arrangement of the protein subunits in the fibrils and suggest that a significant structural reorganization occurs from the native to the fibril state.

Indexed as

Protein MultimerizationAmyloidbeta 2-MicroglobulinModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein Structure, SecondaryProtein Structure, TertiaryAmyloidbeta 2-Microglobulin

Identifiers

PMID21077676
PMCPMC2996106
OpenAlexW58721248

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.