Evidence map›Paper›PMID 19815514›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

2D IR provides evidence for mobile water molecules in beta-amyloid fibrils.

Yung Sam Kim, Liu Liu, Paul H Axelsen, Robin M Hochstrasser

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
12.5field-weighted citation impact, top 1% 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

73 citing papers in PubMed, 153 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. An N-terminal acidic β-sheet domain is responsible for the metal-accumulation properties of amyloid-β protofibrils: a molecular dynamics study.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Amyloid-Like Protein Aggregation Toward Pesticide Reduction.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Glutamine Side ChainJournal of the American Chemical Society · 2019
    Article
  18. Article
  19. Review
  20. Article

13 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

Yung Sam KimDepartment of Chemistry, University of Pennsylvania, 231 South 34 Street, Philadelphia, PA 19104-6323, USA.
Liu Liu
Paul H Axelsen
Robin M Hochstrasser
University of Pennsylvania · US

Funding

ZN-INDUCED PEPTIDE FOLDINGP41RR001348 · NCRR · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1985 to 2011
$8.7M
Ultrafast Processing in Proteins and Other AssembliesR01GM012592 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GAI, FENG · 1985 to 2013
$3.5M
Structure determination by vibrational spectroscopyR01GM076201 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI AXELSEN, PAUL H · 2007 to 2018
$3.2M
ULTRAFAST PROCESSES IN PROTEINS AND OTHER ASSEMBLIESR37GM012592 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI HOCHSTRASSER, ROBIN MAIN · 1992 to 2001
$493k
NCRR NIH HHS P01 RR01348NCRR NIH HHS P41 RR001348NIGMS NIH HHS GM12592NIGMS NIH HHS GM76201NIGMS NIH HHS R01 GM012592NIGMS NIH HHS R01 GM076201NIGMS NIH HHS R37 GM012592
6 · The paper itself

Abstract

The motion of water molecules close to amide groups causes their vibrational frequencies to vary rapidly in time. These variations are uniquely sensed by 2-dimensional infrared spectroscopy (2D IR). Here, it is proposed from 2-dimensional experiments on fibrils of amyloid beta (Abeta)40 that there are water molecules in the fibrils. The spatial locations of the water (D(2)O) were inferred from the responses of 18 amide modes of Abeta40 labeled with (13)C = (18)O. Fast frequency variations were found for residues L17 and V18 and for the apposed residues L34 and V36, suggesting cavities or channels containing mobile water molecules can form between the 2 sheets. Spectroscopic analysis showed that there are 1.2 water molecules per strand in the fibrils. The (13)C = (18)O substitution of 1 residue per strand creates a linear array of isotopologs along the fibril axis that manifests clearly identifiable vibrational transitions. Here, it is shown from the distributions of amide-I' vibrational frequencies that the regularity of these chains is strongly residue dependent and in most cases the distorted regions are also those associated with the putative mobile water molecules. It is proposed that Abeta40 fibrils contain structurally significant mobile water molecules within the intersheet region.

Indexed as

Amyloid beta-PeptidesBinding SitesBiophysical PhenomenaIn Vitro TechniquesKineticsModels, MolecularPeptide FragmentsProtein Structure, QuaternarySpectrophotometry, InfraredSpectroscopy, Fourier Transform InfraredThermodynamicsWaterAmyloid beta-Peptidesamyloid beta-protein (1-40)Peptide FragmentsWater

Identifiers

PMID19815514
PMCPMC2764887
OpenAlexW2035385837

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.