Evidence map›Paper›PMID 22036904›Full record

ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2012

AssignFit: a program for simultaneous assignment and structure refinement from solid-state NMR spectra.

Ye Tian, Charles D Schwieters, Stanley J Opella, Francesca M Marassi

Abstract read
In one paragraph

Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Applications of NMR to membrane proteins.Archives of biochemistry and biophysics · 2017
    Review
  4. Article
  5. Article
  6. Review
  7. Sparse labeling of proteins: structural characterization from long range constraints.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014
    Review
  8. Article
  9. Article
  10. Membrane protein structure determination in membrana.Accounts of chemical research · 2013
    Article
  11. Article
  12. Membrane protein structure determination: back to the membrane.Methods in molecular biology (Clifton, N.J.) · 2013
    Article
  13. 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

4 authors.

Ye TianSanford Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.
Charles D Schwieters
Stanley J Opella
Francesca M Marassi

Funding

Tumor Microenvironment and Cancer ImmunologyP30CA030199 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI Michael Jackson · 1985 to 2026
$107.2M
RESOURCE FOR SOLID STATE NMR OF PROTEINSP41EB002031 · NIBIB · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI OPELLA, STANLEY J · 2003 to 2018
$16.3M
Target IdentificationP01AI074805 · NIAID · FLORIDA STATE UNIVERSITY · PI CROSS, TIMOTHY A · 2009 to 2013
$8.7M
Biomedical ImagingZIACT000090 · CIT · CENTER FOR INFORMATION TECHNOLOGY · PI TRUS, BENES L · 2009 to 2018
$7.8M
Structure Determination of Membrane Proteins in Phospholipid BilyaersR01GM099986 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI OPELLA, STANLEY J · 2012 to 2015
$1.1M
Computational methods for NMR structure determination of proteins in membranesR21GM094727 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI MARASSI, FRANCESCA M · 2010 to 2011
$509k
Intramural NIH HHSNCI NIH HHS P30 CA030199NCI NIH HHS P30CA030199NIAID NIH HHS P01 AI074805NIBIB NIH HHS P41 EB002031NIBIB NIH HHS P41EB002031NIGMS NIH HHS R01 GM099986NIGMS NIH HHS R21 GM094727NIGMS NIH HHS R21GM094727
6 · The paper itself

Abstract

AssignFit is a computer program developed within the XPLOR-NIH package for the assignment of dipolar coupling (DC) and chemical shift anisotropy (CSA) restraints derived from the solid-state NMR spectra of protein samples with uniaxial order. The method is based on minimizing the difference between experimentally observed solid-state NMR spectra and the frequencies back calculated from a structural model. Starting with a structural model and a set of DC and CSA restraints grouped only by amino acid type, as would be obtained by selective isotopic labeling, AssignFit generates all of the possible assignment permutations and calculates the corresponding atomic coordinates oriented in the alignment frame, together with the associated set of NMR frequencies, which are then compared with the experimental data for best fit. Incorporation of AssignFit in a simulated annealing refinement cycle provides an approach for simultaneous assignment and structure refinement (SASR) of proteins from solid-state NMR orientation restraints. The methods are demonstrated with data from two integral membrane proteins, one α-helical and one β-barrel, embedded in phospholipid bilayer membranes.

Indexed as

AlgorithmsModels, ChemicalModels, MolecularSoftwareAmino Acid SequenceComputer SimulationMagnetic Resonance SpectroscopyMolecular Sequence DataProtein ConformationProteinsProteins

Identifiers

PMID22036904
PMCPMC3257385

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.