Evidence map›Paper›PMID 17074807›Full record

ArticleMolecular and cellular biology2007

BiP internal ribosomal entry site activity is controlled by heat-induced interaction of NSAP1.

Sungchan Cho, Sung Mi Park, Tae Don Kim, Jong Heon Kim, Kyong-Tai Kim, Sung Key Jang

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

39 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. PTBP1 Positively Regulates the Translation of Circadian Clock Gene,International journal of molecular sciences · 2020
    Article
  6. Article
  7. RNA Regulators in Leukemia and Lymphoma.Cold Spring Harbor perspectives in medicine · 2020
    Review
  8. IRES Trans-Acting Factors, Key Actors of the Stress Response.International journal of molecular sciences · 2019
    Review
  9. Cap-Independent mRNA Translation in Germ Cells.International journal of molecular sciences · 2019
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. 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

6 authors at 1 institution in 1 country.

Sungchan ChoDepartment of Life Science, Pohang University of Science and Technology, San 31, Hyoja Dong, Pohang, Kyungbuk 790-784, Republic of Korea.
Sung Mi Park
Tae Don Kim
Jong Heon Kim
Kyong-Tai Kim
Sung Key Jang
Pohang University of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TheBiP protein, a stress response protein, plays an important role in the proper folding and assembly of nascent protein and in the scavenging of misfolded proteins in the endoplasmic reticulum lumen. Translation of BiP is directed by an internal ribosomal entry site (IRES) in the 5' nontranslated region of the BiP mRNA. BiP IRES activity increases when cells are heat stressed. Here we report that NSAP1 specifically enhances the IRES activity of BiP mRNA by interacting with the IRES element. Overexpression of NSAP1 in 293T cells increased the IRES activity of BiP mRNA, whereas knockdown of NSAP1 by small interfering RNA (siRNA) reduced the IRES activity of BiP mRNA. The amount of NSAP1 bound to the BiP IRES increased under heat stress conditions, and the IRES activity of BiP mRNA was increased. Moreover, the increase in BiP IRES activity with heat treatment was not observed in cells lacking NSAP1 after siRNA treatment. BiP mRNAs were redistributed from the heavy polysome to the light polysome in NSAP1 knockdown cells. Together, these data indicate that NSAP1 modulates IRES-dependent translation of BiP mRNA through an RNA-protein interaction under heat stress conditions.

Indexed as

AdenoviridaeBase SequenceCell LineCell Line, TumorEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHeLa CellsHeterogeneous-Nuclear RibonucleoproteinsHumansModels, GeneticMolecular ChaperonesMolecular Sequence DataPlasmidsProtein BindingRNA, MessengerSubcellular FractionsEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHeterogeneous-Nuclear RibonucleoproteinsMolecular ChaperonesRNA, MessengerSYNCRIP protein, human

Identifiers

PMID17074807
PMCPMC1800651
OpenAlexW2126967087

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.