Evidence map›Paper›PMID 11854485›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

An NMR approach to structural proteomics.

Adelinda Yee, Xiaoqing Chang, Antonio Pineda-Lucena, Bin Wu, Anthony Semesi, Brian Le, Theresa Ramelot, Gregory M Lee, Sudeepa Bhattacharyya, Pablo Gutierrez and 14 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing 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

85 citing papers in PubMed.

  1. Article
  2. Article
  3. Enzymology of the metazoan tRNA ligase complex: a lifetime in cycles.Cellular and molecular life sciences : CMLS · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Antifungal symbiotic peptide NCR044 exhibits unique structure and multifaceted mechanisms of action that confer plant protection.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Article
  18. Structural diversity in the Mycobacteria DUF3349 superfamily.Protein science : a publication of the Protein Society · 2020
    Article
  19. Article
  20. Article

25 more citing papers are in PubMed but not listed here.

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

24 authors.

Adelinda YeeOntario Cancer Institute and Department of Medical Biophysics, University of Toronto, 101 College Street, Toronto, ON, Canada M5G 1L7.
Xiaoqing Chang
Antonio Pineda-Lucena
Bin Wu
Anthony Semesi
Brian Le
Theresa Ramelot
Gregory M Lee
Sudeepa Bhattacharyya
Pablo Gutierrez
Aleksej Denisov
Chang-Hun Lee
John R Cort
Guennadi Kozlov
Jack Liao
Grzegorz Finak
Limin Chen
David Wishart
Weontae Lee
Lawrence P McIntosh
Kalle Gehring
Michael A Kennedy
Aled M Edwards
Cheryl H Arrowsmith

Funding

STRUCTURAL GENOMICS OF EUKARYOTIC MODEL ORGANISMSP50GM062413 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI MONTELIONE, GAETANO T · 2000 to 2004
$33.5M
NIGMS NIH HHS P50 GM062413NIGMS NIH HHS P50 GM62413-02
6 · The paper itself

Abstract

The influx of genomic sequence information has led to the concept of structural proteomics, the determination of protein structures on a genome-wide scale. Here we describe an approach to structural proteomics of small proteins using NMR spectroscopy. Over 500 small proteins from several organisms were cloned, expressed, purified, and evaluated by NMR. Although there was variability among proteomes, overall 20% of these proteins were found to be readily amenable to NMR structure determination. NMR sample preparation was centralized in one facility, and a distributive approach was used for NMR data collection and analysis. Twelve structures are reported here as part of this approach, which allowed us to infer putative functions for several conserved hypothetical proteins.

Indexed as

Bacterial ProteinsDatabases as TopicEscherichia coliMagnetic Resonance SpectroscopyModels, MolecularOpen Reading FramesProteinsSoftwareSpecies SpecificityBacterial ProteinsProteins

Identifiers

PMID11854485
PMCPMC122278

What OpenQuestion holds

Textmetadata
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.