Evidence map›Paper›PMID 19632474›Full record

ArticleMethods in enzymology2009

Segmental isotopic labeling of proteins for nuclear magnetic resonance.

Dongsheng Liu, Rong Xu, David Cowburn

Abstract read
In one paragraph

Article in Methods in enzymology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Review
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  8. Review
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  14. Protein Structure Determination in Living Cells.International journal of molecular sciences · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. A promiscuous split intein with expanded protein engineering applications.Proceedings of the National Academy of Sciences of the United States of America · 2017
    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

3 authors.

Dongsheng LiuNew York Structural Biology Center, New York, USA.
Rong Xu
David Cowburn

Funding

Structural Biology of Protein KinasesR01GM047021 · NIGMS · ROCKEFELLER UNIVERSITY · PI COWBURN, DAVID · 1992 to 2008
$2.4M
Segmental Labeling for Protein Structure by NMRR01EB001991 · NIBIB · ROCKEFELLER UNIVERSITY · PI MUIR, TOM · 2003 to 2007
$2.2M
NIBIB NIH HHS EB001991NIBIB NIH HHS R01 EB001991NIGMS NIH HHS GM47021NIGMS NIH HHS R01 GM047021
6 · The paper itself

Abstract

Nuclear magnetic resonance (NMR) spectroscopy has emerged as one of the principle techniques of structural biology. It is not only a powerful method for elucidating the three-dimensional structures under near physiological conditions but also a convenient method for studying protein-ligand interactions and protein dynamics. A major drawback of macromolecular NMR is its size limitation, caused by slower tumbling rates and greater complexity of the spectra as size increases. Segmental isotopic labeling allows for specific segment(s) within a protein to be selectively examined by NMR, thus significantly reducing the spectral complexity for large proteins and allowing for the application of a variety of solution-based NMR strategies. Two related approaches are generally used in the segmental isotopic labeling of proteins: expressed protein ligation and protein trans-splicing. Here, we describe the methodology and recent application of expressed protein ligation and protein trans-splicing for NMR structural studies of proteins and protein complexes. We also describe the protocol used in our lab for the segmental isotopic labeling of a 50-kDa protein Csk (C-terminal Src kinase) using expressed protein ligation methods.

Indexed as

Amino Acid SequenceAnalytic Sample Preparation MethodsAnimalsCloning, MolecularCSK Tyrosine-Protein KinaseGene ExpressionHumansInteinsIsotope LabelingMesnaModels, MolecularMolecular Sequence DataNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularPeptidesProtein SplicingCSK protein, humanCSK Tyrosine-Protein KinaseMesnaNitrogen IsotopesPeptidesProtein-Tyrosine KinasesProto-Oncogene ProteinsRecombinant Fusion Proteinssrc-Family KinasesSulfhydryl Reagents

Identifiers

PMID19632474
PMCPMC2861560

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.