ArticleOncogene2005
Mutually antagonistic actions of S100A4 and S100A1 on normal and metastatic phenotypes.
Article in Oncogene, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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.
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
24 citing papers in PubMed.
- Non-Muscle Myosin II A: Friend or Foe in Cancer?International journal of molecular sciences · 2024Review
- Elevated extracellular matrix protein 1 in circulating extracellular vesicles supports breast cancer progression under obesity conditions.Nature communications · 2024Article
- Targeted Destruction of S100A4 Inhibits Metastasis of Triple Negative Breast Cancer Cells.Biomolecules · 2023Article
- Functional interaction between S100A1 and MDM2 may modulate p53 signaling in normal and malignant endometrial cells.BMC cancer · 2022Article
- Interferon Beta Activity Is Modulated via Binding of Specific S100 Proteins.International journal of molecular sciences · 2020Article
- Friend or Foe: S100 Proteins in Cancer.Cancers · 2020Review
- Article
- S100B as an Antagonist To Interfere with the Interface Area Flanked by S100A11 and RAGE V Domain.ACS omega · 2018Article
- Interaction of S100A1 with LATS1 promotes cell growth through regulation of the Hippo pathway in hepatocellular carcinoma.International journal of oncology · 2018Article
- S100B as an antagonist to block the interaction between S100A1 and the RAGE V domain.PloS one · 2018Article
- X-ray crystal structure of human calcium-bound S100A1.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Distinct prognostic values of S100 mRNA expression in breast cancer.Scientific reports · 2017Article
- S100 proteins in cancer.Nature reviews. Cancer · 2015Review
- Joining S100 proteins and migration: for better or for worse, in sickness and in health.Cellular and molecular life sciences : CMLS · 2014Review
- Article
- S100P dissociates myosin IIA filaments and focal adhesion sites to reduce cell adhesion and enhance cell migration.The Journal of biological chemistry · 2012Article
- Article
- Self-association of calcium-binding protein S100A4 and metastasis.The Journal of biological chemistry · 2010Article
- Design of high-affinity S100-target hybrid proteins.Protein science : a publication of the Protein Society · 2009Article
- RAGE (Receptor for Advanced Glycation Endproducts), RAGE ligands, and their role in cancer and inflammation.Journal of translational medicine · 2009Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Increased levels of the homodimeric calcium-binding protein, S100A4, have been shown to cause a metastatic phenotype in at least three independent model systems of breast cancer and its presence in carcinoma cells has been shown to be associated with a reduction in the survival of patients suffering from a range of different cancers. S100A4 has been shown to interact in vitro with another member of the S100 family of proteins, S100A1. The purpose of the present study was to find out whether S100A1 could affect S100A4 function. Fluorescence resonance energy transfer was used to show the interaction of S100A4 and S100A1 in living cells and the binding affinities between S100A4 and S100A1 were determined using a biosensor. S100A1 reduced the S100A4 inhibition of nonmuscle myosin A self-association and phosphorylation in vitro. S100A1 reduced S100A4 induced motility and growth in soft agar and metastasis in vivo. The results show for the first time that interactions between different S100 proteins can affect cancer-related activity, and that the presence of S100A1 protein in carcinoma cells might modulate the effect of S100A4 on their metastatic abilities.
Indexed as
Identifiers
15608682What 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.