Evidence map›Paper›PMID 22244760›Full record

ArticleStructure (London, England : 1993)2012

Computational reconstruction of multidomain proteins using atomic force microscopy data.

Minh-Hieu Trinh, Michael Odorico, Michael E Pique, Jean-Marie Teulon, Victoria A Roberts, Lynn F Ten Eyck, Elizabeth D Getzoff, Pierre Parot, Shu-Wen W Chen, Jean-Luc Pellequer

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Recent advances in RNA structurome.Science China. Life sciences · 2022
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. DOT2: Macromolecular docking with improved biophysical models.Journal of computational chemistry · 2013
    Article
  16. Article
  17. 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

10 authors.

Minh-Hieu TrinhCEA, iBEB, Department of Biochemistry and Nuclear Toxicology, F-30207 Bagnols sur Cèze, France.
Michael Odorico
Michael E Pique
Jean-Marie Teulon
Victoria A Roberts
Lynn F Ten Eyck
Elizabeth D Getzoff
Pierre Parot
Shu-Wen W Chen
Jean-Luc Pellequer

Funding

Computation and Mass Spec: Predicting Protein ComplexesR01GM070996 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TEN EYCK, LYNN F. · 2004 to 2007
$1.3M
NIGMS NIH HHS GM070996NIGMS NIH HHS R01 GM070996
6 · The paper itself

Abstract

Classical structural biology techniques face a great challenge to determine the structure at the atomic level of large and flexible macromolecules. We present a novel methodology that combines high-resolution AFM topographic images with atomic coordinates of proteins to assemble very large macromolecules or particles. Our method uses a two-step protocol: atomic coordinates of individual domains are docked beneath the molecular surface of the large macromolecule, and then each domain is assembled using a combinatorial search. The protocol was validated on three test cases: a simulated system of antibody structures; and two experimentally based test cases: Tobacco mosaic virus, a rod-shaped virus; and Aquaporin Z, a bacterial membrane protein. We have shown that AFM-intermediate resolution topography and partial surface data are useful constraints for building macromolecular assemblies. The protocol is applicable to multicomponent structures connected in the polypeptide chain or as disjoint molecules. The approach effectively increases the resolution of AFM beyond topographical information down to atomic-detail structures.

Indexed as

Models, MolecularProtein Structure, TertiaryAquaporinsComputational BiologyEscherichia coli ProteinsMicroscopy, Atomic ForceProteinsTobacco Mosaic VirusaqpZ protein, E coliAquaporinsEscherichia coli ProteinsProteins

Identifiers

PMID22244760
PMCPMC3264848

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.