ArticleOncogene2005
The C-terminal region of S100A4 is important for its metastasis-inducing properties.
Article in Oncogene, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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.
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Who cites it
14 citing papers in PubMed, 42 citations in OpenAlex.
- Targeted Destruction of S100A4 Inhibits Metastasis of Triple Negative Breast Cancer Cells.Biomolecules · 2023Article
- Article
- The Role of the C-Terminal Lysine of S100P in S100P-Induced Cell Migration and Metastasis.Biomolecules · 2021Article
- Fsp1 cardiac embryonic expression delineates atrioventricular endocardial cushion, coronary venous and lymphatic valve development.Journal of anatomy · 2021Article
- Attenuation of cancer-initiating cells stemness properties by abrogating S100A4 calcium binding ability in head and neck cancers.Oncotarget · 2016Article
- Joining S100 proteins and migration: for better or for worse, in sickness and in health.Cellular and molecular life sciences : CMLS · 2014Review
- The C-terminal random coil region tunes the Ca²⁺-binding affinity of S100A4 through conformational activation.PloS one · 2014Article
- S100P dissociates myosin IIA filaments and focal adhesion sites to reduce cell adhesion and enhance cell migration.The Journal of biological chemistry · 2012Article
- Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling.Structure (London, England : 1993) · 2012Article
- Article
- Self-association of calcium-binding protein S100A4 and metastasis.The Journal of biological chemistry · 2010Article
- The Calcium-Dependent Interaction of S100B with Its Protein Targets.Cardiovascular psychiatry and neurology · 2010Article
- Calcium-dependent and -independent interactions of the S100 protein family.The Biochemical journal · 2006Review
- S100A4 downregulates filopodia formation through increased dynamic instability.Cell adhesion & migrationArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The EF-hand protein, S100A4, binds calcium ions and interacts specifically in vitro with protein targets. Elevated levels of S100A4 have been shown to produce a metastatic phenotype in independent models of breast cancer. The presence of S100A4 in the carcinoma cells of patients with different carcinomas is associated with reduced patient survival. In order to identify the region of the S100A4 molecule that is responsible for its metastasis-inducing properties, specific mutant S100A4 genes and proteins have been produced which contain targeted mutations to the two calcium-binding sites and a deletion of the last 15 amino-acid residues of the protein. The ability of the mutant proteins to bind to a potential specific target in vitro, nonmuscle myosin heavy chain, is correlated with their ability to cause motile, invasive and metastatic phenotypes. Mutation of the C-EF hand of S100A4 virtually abolished calcium binding, and motility/invasion in vitro, abolished interaction with a molecular target, and reduced metastasis induction by 2.5-3-fold. However, deletion of the last 15 amino acids of S100A4 reduced motility/invasion, target binding and metastasis-induction to similar extents as the C-EF-hand mutant, but reduced calcium binding by only 26%. The results suggest that the ability to interact with protein target(s) is important in S100A4-induced metastasis.
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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.