Evidence map›Paper›PMID 18774715›Full record

ArticleBioorganic & medicinal chemistry letters2008

Two-color labeling of temporally defined protein populations in mammalian cells.

Kimberly E Beatty, David A Tirrell

Open access · bronzeAbstract read
In one paragraph

Article in Bioorganic & medicinal chemistry letters, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

35 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Article
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  4. Review
  5. Article
  6. Article
  7. An Optimized Synthesis of Fmoc-l-Homopropargylglycine-OH.The Journal of organic chemistry · 2022
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Visualizing in situ translational activity for identifying and sorting slow-growing archaeal-bacterial consortia.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  13. Super-Resolution Imaging of Plasma Membrane Proteins with Click Chemistry.Frontiers in cell and developmental biology · 2016
    Article
  14. Article
  15. Article
  16. Article
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  18. Article
  19. Article
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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 at 1 institution in 1 country.

Kimberly E BeattyDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
David A Tirrell
California Institute of Technology · US

Funding

NEW AMINO ACIDS FOR PROTEIN ENGINEERINGR01GM062523 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI TIRRELL, DAVID A · 2001 to 2013
$3.6M
NIGMS NIH HHS GM62523NIGMS NIH HHS R01 GM062523
6 · The paper itself

Abstract

The proteome undergoes complex changes in response to disease, drug treatment, and normal cellular signaling processes. Characterization of such changes requires methods for time-resolved protein identification and imaging. Here, we describe the application of two reactive methionine (Met) analogues, azidohomoalanine (Aha) and homopropargylglycine (Hpg), to label two protein populations in fixed cells. Reactive lissamine rhodamine (LR), 7-dimethylaminocoumarin (DMAC), and bodipy-630 (BDPY) dyes were prepared and examined for use in selective dye-labeling of newly synthesized proteins in Rat-1 fibroblasts. The LR and DMAC, but not BDPY, fluorophores were found to enable selective, efficient labeling of subsets of the proteome; cells labeled with Aha and Hpg exhibited fluorescence emission three- to sevenfold more intense than that of control cells treated with Met. We also examined simultaneous and sequential pulse-labeling of cells with Aha and Hpg. After pulse-labeling, cells were treated with reactive LR and DMAC dyes, and labeled cells were imaged by fluorescence microscopy and analyzed by flow cytometry. The results of these studies demonstrate that amino acid labeling can be used to achieve selective two-color imaging of temporally defined protein populations in mammalian cells.

Indexed as

AnimalsAzidesCatalysisCoumarinsCyclizationFibroblastsFluorescent DyesIndicators and ReagentsMethionineMicroscopy, FluorescenceMolecular StructureProteinsRatsAzidesCoumarinsFluorescent DyesIndicators and ReagentsMethionineProteins

Identifiers

PMID18774715
PMCPMC3182832
OpenAlexW1997695395

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.