Evidence map›Paper›PMID 18696217›Full record

ArticleMolecular and cellular biochemistry2009

LIM domain protein TES changes its conformational states in different cellular compartments.

Yingli Zhong, Jiaolian Zhu, Yan Wang, Jianlin Zhou, Kaiqun Ren, Xiaofeng Ding, Jian Zhang

Abstract read
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In one paragraph

Article in Molecular and cellular biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.3field-weighted citation impact, top 44% of its field
1 · What the graph read from it

What it found

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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

10 citing papers in PubMed, 16 citations in OpenAlex.

  1. Study on the expression of testin in the testes of dogs.Journal of veterinary research · 2023
    Article
  2. Article
  3. The Role of Testin in Human Cancers.Pathology oncology research : POR · 2019
    Review
  4. Article
  5. Article
  6. Article
  7. Prickle1 stunts limb growth through alteration of cell polarity and gene expression.Developmental dynamics : an official publication of the American Association of Anatomists · 2013
    Article
  8. Article
  9. Article
  10. Article
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

7 authors at 1 institution in 1 country.

Yingli ZhongKey Laboratory of Protein Chemistry and Developmental Biology of Education Ministry of China, College of Life Science, Hunan Normal University, Changsha, Hunan 410081, People's Republic of China.
Jiaolian Zhu
Yan Wang
Jianlin Zhou
Kaiqun Ren
Xiaofeng Ding
Jian Zhang
Hunan Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human TESTIN (TES) is a putative tumor suppressor and localizes to the cytoplasm as a component of focal adhesions and cell contacts. TES contains a PET domain in the NH(2)-terminus and three tandem LIM domains in the COOH-terminus. It has been hypothesized that interactions between two termini of TES might lead to a "closed" conformational state of the protein. Here, we provide evidence for different conformational states of TES. We confirmed that the NH(2)-terminus of TES can interact with its third LIM domain in the COOH-terminus by GST pull-down assays. In addition, antisera against the full-length or two truncations of TES were prepared to examine the relationship between the conformation and cellular distribution of the protein. We found that these antisera recognize different regions of TES and showed that TES is co-localised with the marker protein B23 in nucleolus, in addition to its localization in endoplasmic reticulum (ER). Furthermore, our co-immunoprecipitation (co-IP) analysis of TES and B23 demonstrated their co-existence in the same complex. Taken together, our results suggest that TES has different conformational states in different cellular compartments, and a "closed" conformational state of TES may be involved in nucleolar localization.

Indexed as

HeLa CellsProtein ConformationAmino Acid SequenceAnimalsBase SequenceCytoskeletal ProteinsHomeodomain ProteinsHumansLIM Domain ProteinsMolecular Sequence DataOrganellesRecombinant Fusion ProteinsRNA-Binding ProteinsTumor Suppressor ProteinsCytoskeletal ProteinsHomeodomain ProteinsLIM Domain ProteinsRecombinant Fusion ProteinsRNA-Binding ProteinsTES protein, humanTumor Suppressor Proteins

Identifiers

PMID18696217
OpenAlexW2021253299

What OpenQuestion holds

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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.