Evidence map›Paper›PMID 20648672›Full record

ArticleJournal of mass spectrometry : JMS2010

Elucidating the higher-order structure of biopolymers by structural probing and mass spectrometry: MS3D.

Daniele Fabris, Eizadora T Yu

Abstract read
In one paragraph

Article in Journal of mass spectrometry : JMS, 2010. 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. Journal of the American Chemical Society · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Development of Large-scale Cross-linking Mass Spectrometry.Molecular & cellular proteomics : MCP · 2018
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Automated assignment of MS/MS cleavable cross-links in protein 3D-structure analysis.Journal of the American Society for Mass Spectrometry · 2015
    Article
  11. Review
  12. Article
  13. Structure-specific ribonucleases for MS-based elucidation of higher-order RNA structure.Journal of the American Society for Mass Spectrometry · 2014
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review
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.

Daniele FabrisDepartment of Chemistry and Biochemistry, University of Maryland Baltimore County, Baltimore, MD, USA. fabris@albany.edu
Eizadora T Yu

Funding

Structural determinants of HIV-1 5'-UTR riboswitch and NC actuation by MS3DR01GM064328 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI FABRIS, DANIELE · 2001 to 2013
$3.8M
Data Portal Enabling New Protein Structure CollaborationR01RR019864 · NCRR · SANDIA CORP-SANDIA NATIONAL LABORATORIES · PI PANCERELLA, CARMEN M · 2004 to 2008
$2.6M
NCRR NIH HHS R01 RR019864NCRR NIH HHS RR019864NIGMS NIH HHS GM643208NIGMS NIH HHS R01 GM064328
6 · The paper itself

Abstract

Chemical probing represents a very versatile alternative for studying the structure and dynamics of substrates that are intractable by established high-resolution techniques. The implementation of MS-based strategies for the characterization of probing products has not only extended the range of applicability to virtually all types of biopolymers but has also paved the way for the introduction of new reagents that would not have been viable with traditional analytical platforms. As the availability of probing data is steadily increasing on the wings of the development of dedicated interpretation aids, powerful computational approaches have been explored to enable the effective utilization of such information to generate valid molecular models. This combination of factors has contributed to making the possibility of obtaining actual 3D structures by MS-based technologies (MS3D) a reality. Although approaches for achieving structure determination of unknown targets or assessing the dynamics of known structures may share similar reagents and development trajectories, they clearly involve distinctive experimental strategies, analytical concerns and interpretation paradigms. This Perspective offers a commentary on methods aimed at obtaining distance constraints for the modeling of full-fledged structures while highlighting common elements, salient distinctions and complementary capabilities exhibited by methods used in dynamics studies. We discuss critical factors to be addressed for completing effective structural determinations and expose possible pitfalls of chemical methods. We survey programs developed for facilitating the interpretation of experimental data and discuss possible computational strategies for translating sparse spatial constraints into all-atom models. Examples are provided to illustrate how the concerted application of very diverse probing techniques can lead to the solution of actual biological systems.

Indexed as

AnimalsBiopolymersComputational BiologyHumansMass SpectrometryMiceModels, MolecularMolecular ConformationMolecular Probe TechniquesBiopolymers

Identifiers

PMID20648672
PMCPMC3432860

What OpenQuestion holds

Textmetadata
LicenceTDM
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.