Evidence map›Paper›PMID 25130489›Full record

ArticleAngewandte Chemie (International ed. in English)2014

Characterizing methyl-bearing side chain contacts and dynamics mediating amyloid β protofibril interactions using ¹³C(methyl)-DEST and lifetime line broadening.

Nicolas L Fawzi, David S Libich, Jinfa Ying, Vitali Tugarinov, G Marius Clore

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Studies of Dynamic Binding of Amino Acids to TiOLangmuir : the ACS journal of surfaces and colloids · 2020
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Probing transient non-native states in amyloid beta fiber elongation by NMR.Chemical communications (Cambridge, England) · 2019
    Article
  11. Analytical chemistry · 2019
    Article
  12. Review
  13. Chemical Exchange.Methods in enzymology · 2019
    Article
  14. Article
  15. Article
  16. Folding of maltose binding protein outside of and in GroEL.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  17. Review
  18. Flexibility and Solvation of Amyloid-β Hydrophobic Core.The Journal of biological chemistry · 2016
    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.

Nicolas L FawziDepartment of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI 02912 (USA). nicolas_fawzi@brown.edu.
David S Libich
Jinfa Ying
Vitali Tugarinov
G Marius Clore

Funding

Training CoreP20GM103430 · NIGMS · UNIVERSITY OF RHODE ISLAND · PI Bongsup P Cho · 2012 to 2026
$63.6M
Structure and Dynamics Of Macromolecules In Solution By NMRZIADK029023 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI CLORE, GIDEON · 2009 to 2025
$41.5M
COBRE for Skeletal Health and RepairP20GM104937 · NIGMS · RHODE ISLAND HOSPITAL · PI CHEN, QIAN · 2012 to 2016
$10.8M
NMR STUDIES OF THREE-DIMENSIONAL STRUCTURE OF MACROMOLECULES IN SOLUTIONZ01DK029023 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI CLORE, G. MARIUS · 1988 to 2008
$949k
Intramural NIH HHS Z01 DK029023NIGMS NIH HHS P20 GM103430NIGMS NIH HHS P20 GM103430-13NIGMS NIH HHS P20 GM104937NIGMS NIH HHS P20 GM104937-07
6 · The paper itself

Abstract

Many details pertaining to the formation and interactions of protein aggregates associated with neurodegenerative diseases are invisible to conventional biophysical techniques. We recently introduced (15)N dark-state exchange saturation transfer (DEST) and (15)N lifetime line-broadening to study solution backbone dynamics and position-specific binding probabilities for amyloid β (Aβ) monomers in exchange with large (2-80 MDa) protofibrillar Aβ aggregates. Here we use (13)C(methyl)DEST and lifetime line-broadening to probe the interactions and dynamics of methyl-bearing side chains in the Aβ-protofibril-bound state. We show that all methyl groups of Aβ40 populate direct-contact bound states with a very fast effective transverse relaxation rate, indicative of side-chain-mediated direct binding to the protofibril surface. The data are consistent with position-specific enhancements of (13)C(methyl)-R₂(tethered) values in tethered states, providing further insights into the structural ensemble of the protofibril-bound state.

Indexed as

Amino Acid SequenceAmyloid beta-PeptidesCarbon IsotopesKineticsMolecular Sequence DataNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularProtein Interaction Domains and MotifsAmyloid beta-PeptidesCarbon IsotopesNitrogen Isotopesamyloid βhigh-molecular-weight assembliesNMR spectroscopyprotein-protein interactions

Identifiers

PMID25130489
PMCPMC4539159

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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.