Evidence map›Paper›PMID 19277710›Full record

ArticleJournal of cancer research and clinical oncology2009

A novel role for DYX1C1, a chaperone protein for both Hsp70 and Hsp90, in breast cancer.

Yuxin Chen, Muzi Zhao, Saiqun Wang, Jie Chen, Yun Wang, Qinhong Cao, Wenbin Zhou, Jin Liu, Zhiyang Xu, Guoqing Tong and 1 more

Open access · greenAbstract read
In one paragraph

Article in Journal of cancer research and clinical oncology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
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  5. Role of the Novel Hsp90 Co-Chaperones in Dynein Arms' Preassembly.International journal of molecular sciences · 2019
    Review
  6. Primary Ciliary Dyskinesia (PCD): A genetic disorder of motile cilia.Translational science of rare diseases · 2019
    Article
  7. Establishment of the early cilia preassembly protein complex during motile ciliogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  8. Article
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  11. Article
  12. Article
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  14. Review
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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

11 authors at 2 institutions in 1 country.

Yuxin ChenLab of Reproductive Medicine, Department of Cell Biology and Medical Genetics, Nanjing Medical University, 210029 Nanjing, Jiangsu, People's Republic of China.
Muzi Zhao
Saiqun Wang
Jie Chen
Yun Wang
Qinhong Cao
Wenbin Zhou
Jin Liu
Zhiyang Xu
Guoqing Tong
Jianmin Li
Nanjing Medical University · CNNanjing Maternity and Child Health Care Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

aimsWith three consecutive tetratricopeptide repeat (TPR) motifs at its C-terminus essential for neuronal migration, and a p23 domain at its N-terminus, DYX1C1 was the first gene proposed to have a role in developmental dyslexia. In this study, we attempted to identify the potential interaction of DYX1C1 and heat shock protein, and the role of DYX1C1 in breast cancer. MAIN

methodsGST pull-down, a yeast two-hybrid system, RT-PCR, site-directed mutagenesis approach. KEY

findingsOur study initially confirmed DYX1C1, a dyslexia related protein, could interact with Hsp70 and Hsp90 via GST pull-down and a yeast two-hybrid system. And we verified that EEVD, the C-terminal residues of DYX1C1, is responsible for the identified association. Further, DYX1C1 mRNA was significantly overexpressed in malignant breast tumor, linking with the up-regulated expression of Hsp70 and Hsp90. SIGNIFICANCE: These results suggest that DYX1C1 is a novel Hsp70 and Hsp90-interacting co-chaperone protein and its expression is associated with malignancy.

Indexed as

Amino Acid SequenceBreast NeoplasmsCytoskeletal ProteinsFemaleHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansMolecular Sequence DataMutagenesis, Site-DirectedNerve Tissue ProteinsNuclear ProteinsReverse Transcriptase Polymerase Chain ReactionRNA, MessengerTwo-Hybrid System TechniquesUp-RegulationCytoskeletal ProteinsDNAAF4 protein, humanHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsNerve Tissue ProteinsNuclear ProteinsRNA, Messenger

Identifiers

PMID19277710
PMCPMC12160223
OpenAlexW1982567857

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.