Evidence map›Paper›PMID 23798434›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Vibrational imaging of newly synthesized proteins in live cells by stimulated Raman scattering microscopy.

Lu Wei, Yong Yu, Yihui Shen, Meng C Wang, Wei Min

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
106citing papers in PubMed, 1 pooled it
30.8field-weighted citation impact, top 1% 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

106 citing papers in PubMed, 1 synthesis or guideline pooled it, 239 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Raman imaging of molecular groups in the wavenumber silent region.Analytical and bioanalytical chemistry · 2026
    Review
  11. Review
  12. Review
  13. Review
  14. Imaging Cellular Metabolic Rewiring with SuMMIT-SRS.bioRxiv : the preprint server for biology · 2025
    Article
  15. Review
  16. Article
  17. Article
  18. Condenzymes: Biomolecular condensates with inherent catalytic activities.bioRxiv : the preprint server for biology · 2025
    Article
  19. Review
  20. Article

46 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

5 authors at 2 institutions in 1 country.

Lu WeiDepartment of Chemistry, Columbia University, New York, NY 10027, USA.
Yong Yu
Yihui Shen
Meng C Wang
Wei Min
Baylor College of Medicine · USColumbia University · US

Funding

Label-Free Chemical Imaging for Biological ApplicationsDP2EB016573 · NIBIB · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI MIN, WEI · 2012 to 2012
$2.4M
LIPID SIGNALING IN REGULATION OF LONGEVITYR01AG045183 · NIA · BAYLOR COLLEGE OF MEDICINE · PI WANG, MENG CARLA · 2013 to 2017
$1.8M
NIA NIH HHS R01 AG045183NIBIB NIH HHS DP2 EB016573
6 · The paper itself

Abstract

Synthesis of new proteins, a key step in the central dogma of molecular biology, has been a major biological process by which cells respond rapidly to environmental cues in both physiological and pathological conditions. However, the selective visualization of a newly synthesized proteome in living systems with subcellular resolution has proven to be rather challenging, despite the extensive efforts along the lines of fluorescence staining, autoradiography, and mass spectrometry. Herein, we report an imaging technique to visualize nascent proteins by harnessing the emerging stimulated Raman scattering (SRS) microscopy coupled with metabolic incorporation of deuterium-labeled amino acids. As a first demonstration, we imaged newly synthesized proteins in live mammalian cells with high spatial-temporal resolution without fixation or staining. Subcellular compartments with fast protein turnover in HeLa and HEK293T cells, and newly grown neurites in differentiating neuron-like N2A cells, are clearly identified via this imaging technique. Technically, incorporation of deuterium-labeled amino acids is minimally perturbative to live cells, whereas SRS imaging of exogenous carbon-deuterium bonds (C-D) in the cell-silent Raman region is highly sensitive, specific, and compatible with living systems. Moreover, coupled with label-free SRS imaging of the total proteome, our method can readily generate spatial maps of the quantitative ratio between new and total proteomes. Thus, this technique of nonlinear vibrational imaging of stable isotope incorporation will be a valuable tool to advance our understanding of the complex spatial and temporal dynamics of newly synthesized proteome in vivo.

Indexed as

HEK293 CellsHumansMicroscopyProtein BiosynthesisProteinsSpectrum Analysis, RamanProteinsprotein synthesisstable isotope labelingstimulated Raman microscopy

Identifiers

PMID23798434
PMCPMC3710790
OpenAlexW2011641087

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.