Evidence map›Paper›PMID 25175010›Full record

ReviewAnalytical biochemistry2014

Review of methods to assign the nuclear magnetic resonance peaks of reductively methylated proteins.

Kevin J Roberson, Megan A Macnaughtan

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Analytical biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

2 authors.

Kevin J RobersonDepartment of Chemistry, Louisiana State University, Baton Rouge, LA 70803, USA.
Megan A MacnaughtanDepartment of Chemistry, Louisiana State University, Baton Rouge, LA 70803, USA. Electronic address: macnau@lsu.edu.

Funding

Post-Expression Isotope Labeling: NMR Insights into Glycoprotein StructureR00RR024105 · NCRR · LOUISIANA STATE UNIV A&M COL BATON ROUGE · PI MACNAUGHTAN, MEGAN ALANE · 2008 to 2010
$740k
NCRR NIH HHS R00 RR024105NCRR NIH HHS R00RR024105
6 · The paper itself

Abstract

Reductive methylation of lysyl side-chain amines has been a successful tool in the advancement of high-resolution structural biology. The utility of this method has continuously gained ground as a protein chemical modification, first as a tool to aid protein crystallization and later as a probe in protein nuclear magnetic resonance (NMR) spectroscopy. As an isotope-labeling strategy for NMR studies, reductive methylation has contributed to the study of protein-protein interactions and global conformational changes. Although more detailed structural studies using this labeling strategy are possible, the hurdle of assigning the NMR peaks to the corresponding reductively methylated amine hinders its use. In this review, we discuss and compare strategies used to assign the NMR peaks of reductively methylated protein amines.

Indexed as

Magnetic Resonance SpectroscopyChemistry Techniques, AnalyticalMethylationModels, MolecularOxidation-ReductionProteinsProteinsChemical modificationDimethyllysineIsotopic labelingLysozymeReductive methylation

Identifiers

PMID25175010
PMCPMC4252242

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.