Evidence map›Paper›PMID 21121676›Full record

ArticleJournal of proteome research2011

Mass spectrometry detection of histidine phosphorylation on NM23-H1.

John D Lapek, Gregory Tombline, Alan E Friedman

Abstract read
In one paragraph

Article in Journal of proteome research, 2011. 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
0.9field-weighted citation impact, top 27% of its field
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, 24 citations in OpenAlex.

  1. NucleariScience · 2024
    Article
  2. Article
  3. Article
  4. Article
  5. NME/NM23/NDPK and Histidine Phosphorylation.International journal of molecular sciences · 2020
    Review
  6. Article
  7. Histidine kinases and the missing phosphoproteome from prokaryotes to eukaryotes.Laboratory investigation; a journal of technical methods and pathology · 2018
    Review
  8. Review
  9. Article
  10. Laparoscopic surgery inhibits the proliferation and metastasis of cervical cancer cells.International journal of clinical and experimental medicine · 2015
    Article
  11. Cardiac mitochondrial matrix and respiratory complex protein phosphorylation.American journal of physiology. Heart and circulatory physiology · 2012
    Review
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 at 1 institution in 1 country.

John D LapekDepartment of Environmental Medicine, University of Rochester Medical Center, Rochester, New York 14642, USA.
Gregory Tombline
Alan E Friedman
University of Rochester Medical Center · US

Funding

VISUAL INDICES OF NEUROTOXICITYP30ES001247 · NIEHS · UNIVERSITY OF ROCHESTER · PI B Paige Lawrence · 1985 to 2026
$42.8M
UNIVERSITY OF ROCHESTER'S RESEARCH ASSOCIATE ORGANIZATIONUL1RR024160 · NCRR · UNIVERSITY OF ROCHESTER · PI PEARSON, THOMAS ARTHUR · 2006 to 2011
$38.7M
Training in Environment ToxicologyT32ES007026 · NIEHS · UNIVERSITY OF ROCHESTER · PI Alison Elder, Marissa Sobolewski Terry · 1985 to 2026
$20.2M
The University of Rochester's Clinical and Translational Science InstituteKL2RR024136 · NCRR · UNIVERSITY OF ROCHESTER · PI PEARSON, THOMAS ARTHUR · 2006 to 2011
$4.3M
The University of Rochester's Clinical and Translational Science InstituteTL1RR024135 · NCRR · UNIVERSITY OF ROCHESTER · PI PEARSON, THOMAS ARTHUR · 2006 to 2011
$3.7M
BCL-2, ROS, AND CELL DEATH IN DEVELOPMENTAL TOXICITYR01ES007026 · NIEHS · UNIVERSITY OF WASHINGTON · PI MIRKES, PHILIP E · 1996 to 2002
$1.2M
NCRR NIH HHS 1 UL1 RR024160-1NCRR NIH HHS KL2 RR024136NCRR NIH HHS TL1 RR024135NCRR NIH HHS UL1 RR024160NIEHS NIH HHS ES01247NIEHS NIH HHS ES07026NIEHS NIH HHS P30 ES001247NIEHS NIH HHS R01 ES007026NIEHS NIH HHS T32 ES007026
6 · The paper itself

Abstract

Phosphorylation is a ubiquitous protein post-translational modification that is intimately involved in most aspects of cellular regulation. Currently, most proteomic analyses are performed with phosphorylation searches for serine, threonine, and tyrosine modifications, as the phosphorylated residues of histidine and aspartic acid are acid labile and thus undetectable with most proteomic methodologies. Here, we present a novel buffer system to show histidine phosphorylation of NM23-H1, the product of the first identified putative human metastasis suppressor gene (NME1), which catalyzes the transfer of the γ-phosphate from nucleoside triphosphates to nucleoside diphosphates. On the basis of a pH titration of LC elution buffers and MS/MS identification, recombinant NM23-H1 subjected to autophosphorylation was shown to contain phosphorylated histidine at residue 118 at pH 5 and 6, with each level giving over 75% peptide coverage for identification. The solvent system presented permits the detection of all five possible phosphorylation moieties. Application of histidine and aspartic acid phosphorylation modifications to proteomic analyses will significantly advance the understanding of phosphorylation relay signaling in cellular regulation, including elucidation of the role of NM23-H1 in metastasis.

Indexed as

Amino Acid SequenceAspartic AcidChromatography, LiquidHistidineHumansHydrogen-Ion ConcentrationMolecular Sequence DataNM23 Nucleoside Diphosphate KinasesPhosphorylationProteomicsRecombinant ProteinsTandem Mass SpectrometryAspartic AcidHistidineNM23 Nucleoside Diphosphate KinasesNME1 protein, humanRecombinant Proteins

Identifiers

PMID21121676
PMCPMC3033978
OpenAlexW1981198317

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.