ArticleBiomolecules2017
Altered Protein Interactions of the Endogenous Interactome of PTPIP51 towards MAPK Signaling.
Article in Biomolecules, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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.
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Who cites it
5 citing papers in PubMed, 6 citations in OpenAlex.
- Disruption of Mitochondrial-associated ER membranes by HIV-1 tat protein contributes to premature brain aging.CNS neuroscience & therapeutics · 2023Article
- The Potential of Small Molecules to Modulate the Mitochondria-Endoplasmic Reticulum Interplay in Alzheimer's Disease.Frontiers in cell and developmental biology · 2022Review
- PTPIP51 crosslinks the NFκB signaling and the MAPK pathway in SKBR3 cells.Future science OA · 2020Article
- Crosstalks of the PTPIP51 interactome revealed in Her2 amplified breast cancer cells by the novel small molecule LDC3/Dynarrestin.PloS one · 2019Article
- The Importance of the Right Framework: Mitogen-Activated Protein Kinase Pathway and the Scaffolding Protein PTPIP51.International journal of molecular sciences · 2018Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein-protein interactions play a pivotal role in normal cellular functions as well as in carcinogenesis. The protein-protein interactions form functional clusters during signal transduction. To elucidate the fine calibration of the protein-protein interactions of protein tyrosine phosphatase interacting protein 51 (PTPIP51) a small molecule drug, namely LDC-3, directly targeting PTPIP51 is now available. Therefore, LDC-3 allows for the studying of the regulation of the endogenous interactome by modulating PTPIP51 binding capacity. Small interfering ribonucleic acid
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Registered trials
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