Evidence map›Paper›PMID 24896127›Full record

ArticleBiophysical journal2014

Probing the average local structure of biomolecules using small-angle scattering and scaling laws.

Max C Watson, Joseph E Curtis

Abstract read
In one paragraph

Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Commonly used FRET fluorophores promote collapse of an otherwise disordered protein.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  6. Article
  7. Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  8. Quarterly intrinsic disorder digest (April-May-June, 2014).Intrinsically disordered proteins · 2017
    Article
  9. Article
  10. The PTEN Tumor Suppressor Forms Homodimers in Solution.Structure (London, England : 1993) · 2015
    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

2 authors.

Max C WatsonNIST Center for Neutron Research, National Institute of Standards and Technology, Gaithersburg, Maryland. Electronic address: max.watson@nist.gov.
Joseph E CurtisNIST Center for Neutron Research, National Institute of Standards and Technology, Gaithersburg, Maryland. Electronic address: joseph.curtis@nist.gov.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small-angle neutron and x-ray scattering have become invaluable tools for probing the nanostructure of molecules in solution. It was recently shown that the definite integral of the scattering profile exhibits a scaling (power-law) behavior with respect to molecular mass. We derive the origin of this relationship, and discuss how the integrated scattering profile can be used to identify differing levels of disorder over local ≲30 Å length scales. We apply our analysis to globular and intrinsically disordered proteins.

Indexed as

Scattering, Small AngleBacterial ProteinsIntrinsically Disordered ProteinsProtein ConformationProtein FoldingX-Ray DiffractionBacterial ProteinsIntrinsically Disordered Proteins

Identifiers

PMID24896127
PMCPMC4052260

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.