Evidence map›Paper›PMID 25422450›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Actin stress in cell reprogramming.

Jun Guo, Yuexiu Wang, Frederick Sachs, Fanjie Meng

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

46 citing papers in PubMed, 96 citations in OpenAlex.

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  11. Review
  12. Gut feelings: mechanosensing in the gastrointestinal tract.Nature reviews. Gastroenterology & hepatology · 2022
    Review
  13. Article
  14. Article
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  16. Review
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  18. Article
  19. Article
  20. Extracellular Matrix and Cellular Plasticity in Musculoskeletal Development.Frontiers in cell and developmental biology · 2020
    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

4 authors at 3 institutions in 2 countries.

Jun GuoDepartment of Biochemistry, Nanjing Medical University, Nanjing, Jiangsu 210029, China;
Yuexiu WangDepartment of Physiology, Capital Medical University, Beijing 100069, China; and.
Frederick SachsPhysiology and Biophysics Department, Center for Single Molecule Studies, University at Buffalo, The State University of New York at Buffalo, Buffalo, NY 14214.
Fanjie MengPhysiology and Biophysics Department, Center for Single Molecule Studies, University at Buffalo, The State University of New York at Buffalo, Buffalo, NY 14214 fmeng2@buffalo.edu.
University at Buffalo, State University of New York · USCapital Medical University · CNNanjing Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell mechanics plays a role in stem cell reprogramming and differentiation. To understand this process better, we created a genetically encoded optical probe, named actin-cpstFRET-actin (AcpA), to report forces in actin in living cells in real time. We showed that stemness was associated with increased force in actin. We reprogrammed HEK-293 cells into stem-like cells using no transcription factors but simply by softening the substrate. However, Madin-Darby canine kidney (MDCK) cell reprogramming required, in addition to a soft substrate, Harvey rat sarcoma viral oncogene homolog expression. Replating the stem-like cells on glass led to redifferentiation and reduced force in actin. The actin force probe was a FRET sensor, called cpstFRET (circularly permuted stretch sensitive FRET), flanked by g-actin subunits. The labeled actin expressed efficiently in HEK, MDCK, 3T3, and bovine aortic endothelial cells and in multiple stable cell lines created from those cells. The viability of the cell lines demonstrated that labeled actin did not significantly affect cell physiology. The labeled actin distribution was similar to that observed with GFP-tagged actin. We also examined the stress in the actin cross-linker actinin. Actinin force was not always correlated with actin force, emphasizing the need for addressing protein specificity when discussing forces. Because actin is a primary structural protein in animal cells, understanding its force distribution is central to understanding animal cell physiology and the many linked reactions such as stress-induced gene expression. This new probe permits measuring actin forces in a wide range of experiments on preparations ranging from isolated proteins to transgenic animals.

Indexed as

Cellular Reprogramming3T3 CellsActinsAnimalsAnisotropyAortaBacterial ProteinsCattleCell DifferentiationCytoskeletonDogsEndothelial CellsFluorescence Resonance Energy TransferHEK293 CellsHumansLuminescent ProteinsActinsBacterial ProteinsLuminescent ProteinsRecombinant Proteinsyellow fluorescent protein, Bacteriaactincell mechanicsforce probereprogrammingstem cell

Identifiers

PMID25422450
PMCPMC4267376
OpenAlexW1974524647

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.