ArticleThe Biochemical journal1994
Subcellular localization of a protein-tyrosine phosphatase: evidence for association with chromatin.
Article in The Biochemical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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.
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.
Who cites it
8 citing papers in PubMed, 29 citations in OpenAlex.
- The liposomal delivery of hydrophobic oxidovanadium complexes imparts highly effective cytotoxicity and differentiating capacity in neuroblastoma tumour cells.Scientific reports · 2020Article
- C3G dynamically associates with nuclear speckles and regulates mRNA splicing.Molecular biology of the cell · 2018Article
- C3G shows regulated nucleocytoplasmic exchange and represses histone modifications associated with euchromatin.Molecular biology of the cell · 2017Article
- Reciprocal Negative Regulation between the Guanine Nucleotide Exchange Factor C3G and β-Catenin.Genes & cancer · 2012Article
- Article
- PTP-S2, a nuclear tyrosine phosphatase, is phosphorylated and excluded from condensed chromosomes during mitosis.Journal of biosciences · 2000Article
- Loss of the exon encoding the juxtamembrane domain is essential for the oncogenic activation of TPR-MET.Oncogene · 1999Article
- Protein tyrosine phosphatase PTP-S binds to the juxtamembrane region of the hepatocyte growth factor receptor Met.The Biochemical journal · 1998Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A non-transmembrane protein-tyrosine phosphatase, PTP-S, has been shown to bind to DNA in vitro through its C-terminal noncatalytic domain. The cellular PTP-S gene product was identified as 42-44 kDa polypeptides in the rat fibroblast cell lines Rat2 and F111, by immunoblotting using polyclonal and monoclonal antibodies. Indirect immunofluorescence-staining experiments showed that PTP-S was predominantly associated with the nuclear compartment in interphase cells, although some fluorescence was present in cytoplasm. This protein appeared to be uniformly distributed throughout the cell during mitosis. Subcellular fractionation followed by immunoblotting supports the immunofluorescence data showing that PTP-S was present in the nucleus as well as cytoplasm. PTP-S could be released from the isolated nuclei by moderate salt concentration (400 mM NaCl) or mild treatment with DNAase I, suggesting that at least part of this protein present in the nucleus was associated with chromatin. PTP-S extracted from nuclei of Rat2 cells binds to DNA, as determined by DNA affinity chromatography. The nuclear location of this phosphatase, and its association with chromatin, provide support to our previous suggestion that the DNA-binding property of this phosphatase may be physiologically relevant.
Indexed as
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What OpenQuestion holds
Registered trials
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.