The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
An Ankyrin-like Protein with Transmembrane Domains Is Specifically Lost after Oncogenic Transformation of Human Fibroblasts
Open accessAbstract
We have identified a novel transformation-sensitive mRNA, which is present in cultured fibroblasts but is lacking in SV40 transformed cells as well as in many mesenchymal tumor cell lines. The corresponding gene is located on human chromosome 8 in band 8q13. The open reading frame of the mRNA encodes a protein of 1119 amino acids forming two distinct domains. The N-terminal domain consists of 18 repeats that are related to the cytoskeletal protein ankyrin. The C-terminal domain contains six putative transmembrane segments that resemble many ion channels. This overall structure is reminiscent of TRP-like proteins that function as store-operated calcium channels. The novel protein with an Mr of 130 kDa is expressed at a very low level in human fibroblasts and at a moderate level in liposarcoma cells. Overexpression in eukaryotic cells appears to interfere with normal growth, suggesting that it might play a direct or indirect role in signal transduction and growth control.
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The TRP Superfamily of Cation Channels
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Metadata
- Authors
- Jaquemar, D., Schenker, T., & Trueb, B.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-03
- Volume
- 274
- Issue
- 11
- Pages
- 7325-7333
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2011350367
- Cited by
- 332
- References
- 26
- FWCI
- 0.60
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: An Ankyrin-like Protein with Transmembrane Domains Is Specifically Lost after Oncogenic Transformation of Human Fibroblasts. https://app.cochat.ai/papers/10.1074/jbc.274.11.7325
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- Jaquemar, D., Schenker, T., & Trueb, B. (1999). An Ankyrin-like Protein with Transmembrane Domains Is Specifically Lost after Oncogenic Transformation of Human Fibroblasts. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.274.11.7325
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.