Evidence map›Paper›PMID 24656078›Full record

ReviewJournal of magnetic resonance (San Diego, Calif. : 1997)2014

Sparse labeling of proteins: structural characterization from long range constraints.

James H Prestegard, David A Agard, Kelley W Moremen, Laura A Lavery, Laura C Morris, Kari Pederson

Abstract readReview
In one paragraph

Review in Journal of magnetic resonance (San Diego, Calif. : 1997), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. 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

6 authors.

James H PrestegardComplex Carbohydrate Research Center, University of Georgia, Athens, GA 30602, United States. Electronic address: jpresteg@ccrc.uga.edu.
David A AgardThe Howard Hughes Medical Institute, Dept. Biochem. & Biophys., Univ. Calif. San Francisco, San Francisco, CA 94158, United States.
Kelley W MoremenComplex Carbohydrate Research Center, University of Georgia, Athens, GA 30602, United States.
Laura A LaveryThe Howard Hughes Medical Institute, Dept. Biochem. & Biophys., Univ. Calif. San Francisco, San Francisco, CA 94158, United States.
Laura C MorrisComplex Carbohydrate Research Center, University of Georgia, Athens, GA 30602, United States.
Kari PedersonComplex Carbohydrate Research Center, University of Georgia, Athens, GA 30602, United States.

Funding

University of Georgia ProjectU54GM094597 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI MONTELIONE, GAETANO T · 2010 to 2014
$36.9M
TR&D3. Approaches to Proteoglycan Function at Biochemical and Cellular LevelsP41GM103390 · NIGMS · UNIVERSITY OF GEORGIA · PI MOREMEN, KELLEY W. · 2012 to 2019
$14.5M
Structural Basis of Protein HomeostasisU01GM098254 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI AGARD, DAVID A., FRYDMAN, JUDITH · 2012 to 2014
$3.2M
Howard Hughes Medical InstituteNIGMS NIH HHS P41 GM103390NIGMS NIH HHS U01 GM098254NIGMS NIH HHS U54 GM094597
6 · The paper itself

Abstract

Structural characterization of biologically important proteins faces many challenges associated with degradation of resolution as molecular size increases and loss of resolution improving tools such as perdeuteration when non-bacterial hosts must be used for expression. In these cases, sparse isotopic labeling (single or small subsets of amino acids) combined with long range paramagnetic constraints and improved computational modeling offer an alternative. This perspective provides a brief overview of this approach and two discussions of potential applications; one involving a very large system (an Hsp90 homolog) in which perdeuteration is possible and methyl-TROSY sequences can potentially be used to improve resolution, and one involving ligand placement in a glycosylated protein where resolution is achieved by single amino acid labeling (the sialyltransferase, ST6Gal1). This is not intended as a comprehensive review, but as a discussion of future prospects that promise impact on important questions in the structural biology area.

Indexed as

Models, MolecularMolecular ConformationNuclear Magnetic Resonance, BiomolecularProteinsProtein Structure, TertiarySpin LabelsProteinsSpin LabelsGlycoproteinLigand dockingNMR assignmentsParamagnetic constraintsProtein NMRResidual dipolar couplingSparse labeling

Identifiers

PMID24656078
PMCPMC3964372

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.