Evidence map›Paper›PMID 21442608›Full record

ReviewBiopolymers2011

Minireview: structural insights into early folding events using continuous-flow time-resolved small-angle X-ray scattering.

Sagar V Kathuria, Liang Guo, Rita Graceffa, Raul Barrea, R Paul Nobrega, C Robert Matthews, Thomas C Irving, Osman Bilsel

Abstract readReview
In one paragraph

Review in Biopolymers, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Review
  2. Review
  3. Aging can transform single-component protein condensates into multiphase architectures.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. Article
  5. Article
  6. Article
  7. IUCrJ · 2021
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Emerging applications of small angle solution scattering in structural biology.Protein science : a publication of the Protein Society · 2015
    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

8 authors.

Sagar V KathuriaDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Liang Guo
Rita Graceffa
Raul Barrea
R Paul Nobrega
C Robert Matthews
Thomas C Irving
Osman Bilsel

Funding

X-RAY STUDIES OF NEUROFIBRILLARY TANGLES IN ALZHEIMER'S DISEASE BRAIN TISSUEP41RR008630 · NCRR · ILLINOIS INSTITUTE OF TECHNOLOGY · PI VOLZ, KARL W · 2001 to 2011
$14.4M
Time resolved SAXS studies on the RP2/Arl3 complex pp.484-485P41GM103622 · NIGMS · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2012 to 2020
$11.9M
MUTAGENESIS AS A PROBE OF THE FOLDING OF TRP SYNTHASER01GM023303 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI BILSEL, OSMAN, MATTHEWS, C ROBERT · 1985 to 2017
$5.4M
FOLDING MECHANISMS OF MULTISUBUNIT PEPTIDES AND PROTEINSR01GM054836 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI MATTHEWS, C ROBERT · 1996 to 2013
$3.7M
NCRR NIH HHS P41 RR008630NCRR NIH HHS RR-08630NIGMS NIH HHS GM23303NIGMS NIH HHS GM54836NIGMS NIH HHS P41 GM103622NIGMS NIH HHS R01 GM023303NIGMS NIH HHS R01 GM054836
6 · The paper itself

Abstract

Small-angle X-ray scattering (SAXS) is a powerful method for obtaining quantitative structural information on the size and shape of proteins, and it is increasingly used in kinetic studies of folding and association reactions. In this minireview, we discuss recent developments in using SAXS to obtain structural information on the unfolded ensemble and early folding intermediates of proteins using continuous-flow mixing devices. Interfacing of these micromachined devices to SAXS beamlines has allowed access to the microsecond time regime. The experimental constraints in implementation of turbulence and laminar flow-based mixers with SAXS detection and a comparison of the two approaches are presented. Current improvements and future prospects of microsecond time-resolved SAXS and the synergy with ab initio structure prediction and molecular dynamics simulations are discussed.

Indexed as

Protein FoldingScattering, Small AngleAnimalsMagnetic Resonance SpectroscopyProteinsSolutionsX-Ray DiffractionProteinsSolutions

Identifiers

PMID21442608
PMCPMC3278217

What OpenQuestion holds

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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.