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S100 calcium binding protein A4

S100A4, 42 A
The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein may function in motility, invasion, and tubulin polymerization. Chromosomal rearrangements and altered expression of this gene have been implicated in tumor metastasis. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: S-100, CAN, HAD, V1a, E-cadherin
Papers using S100A4 antibodies
Heparanase enhances syndecan-1 shedding: a novel mechanism for stimulation of tumor growth and metastasis
Wrenshall Lucile E. et al., In Immunology and Cell Biology, 2006
... antibody recognizing a smooth muscle cell actin, a rabbit polyclonal antibody against cytokeratin 19, a rabbit polyclonal recognizing S100A4, and a biotinylated goat polyclonal anti-GFP antibody were from Abcam (Cambridge, MA) ...
Papers on S100A4
S100A4 and P53 in myocardial collagen fibers of hypertrophic cardiomyopathy : Expression and clinical significance.
Gong et al., Qingdao, China. In Herz, Feb 2016
OBJECTIVE: The purpose of this work is to investigate the expression of S100A4 and P53 and their correlation with myocardial collagen fibers in hypertrophic cardiomyopathy (HCM).
Propofol suppresses invasion, angiogenesis and survival of EC-1 cells in vitro by regulation of S100A4 expression.
Zhuang et al., Guangzhou, China. In Eur Rev Med Pharmacol Sci, Dec 2015
EC-1 cells were explored to 100 μmol/L propofol for 24 h, then was transiently transfected into PcDNA3.1-S100A4
Downregulation of AKT3 Increases Migration and Metastasis in Triple Negative Breast Cancer Cells by Upregulating S100A4.
Jücker et al., Hamburg, Germany. In Plos One, Dec 2015
Screening for promigratory proteins revealed that downregulation of AKT3 increases the expression of S100A4 protein.
Cekirdekci, Çorlu, Turkey. In Eur Rev Med Pharmacol Sci, Dec 2015
Reply letter "More appropriate study design is need for confirm diagnostic utility of S100A4 protein", by E.I. Cekirdekci, published in the Eur Rev Med Pharmacol Sci 2015; 19(22): 4212-4213, PMID 26636504.
Clinical significance of the integrin α6β4 in human malignancies.
O'Connor et al., Lexington, United States. In Lab Invest, Sep 2015
Furthermore, it dramatically alters the transcriptome toward a more invasive phenotype by controlling promoter DNA demethylation of invasion and metastasis-associated proteins, such as S100A4 and autotaxin, and upregulates and activates key tumor-promoting transcription factors such as the NFATs and NF-κB.
An oxazetidine amino acid for chemical protein synthesis by rapid, serine-forming ligations.
Bode et al., Zürich, Switzerland. In Nat Chem, Aug 2015
The utility of the reaction was demonstrated by the synthesis of S100A4, a 12 kDa calcium-binding protein not easily accessible by NCL or other amide-forming reactions due to its primary sequence and properties.
Molecular targets and pathways involved in liver metastasis of colorectal cancer.
Krüger et al., München, Germany. In Clin Exp Metastasis, Aug 2015
In addition, the functional role and validation of targets such as PRL3, Trop-2, L1CAM, S100A4, S100P, CD133, LIPC, and APOBEC3G are summarized.
Use of proteins as biomarkers and their role in carcinogenesis.
Zarogoulidis et al., Thessaloníki, Greece. In J Cancer, 2014
Other members of this family of proteins include S100A4, which has been associated with several malignancies and S100A2, which has been found to be decreased in some cancers.
Correction: More appropriate study design needs to confirm the diagnostic utility of S100A4 protein.
Cekirdekci, Çorlu, Turkey. In Eur Rev Med Pharmacol Sci, 2014
UNASSIGNED: [This corrects the title for article PMID 26636504].
S100 family signaling network and related proteins in pancreatic cancer (Review).
Xiao et al., Nantong, China. In Int J Mol Med, 2014
The expression of S100A4 and S100P is associated with drug resistance, differentiation, metastasis and clinical outcome.
Antioxidative dietary compounds modulate gene expression associated with apoptosis, DNA repair, inhibition of cell proliferation and migration.
Huang et al., Beijing, China. In Int J Mol Sci, 2013
Inhibition of hypoxia-inducible factor-1 by saponin extracts of ginsenoside (Ginsen) and Gynostemma and inhibition of S100A4 by coix polysaccharides inhibited cancer cell migration and invasion.
High prognostic impact of flow cytometric minimal residual disease detection in acute myeloid leukemia: data from the HOVON/SAKK AML 42A study.
Schuurhuis et al., Nieuwegein, Netherlands. In J Clin Oncol, 2013
PATIENTS AND METHODS: In adults (younger than age 60 years) with AML enrolled onto the Dutch-Belgian Hemato-Oncology Cooperative Group/Swiss Group for Clinical Cancer Research Acute Myeloid Leukemia 42A study, MRD was evaluated in bone marrow samples in CR (164 after induction cycle 1, 183 after cycle 2, 124 after consolidation therapy).
The oncoprotein HBXIP uses two pathways to up-regulate S100A4 in promotion of growth and migration of breast cancer cells.
Ye et al., Tianjin, China. In J Biol Chem, 2012
HBXIP up-regulates S100A4 through activating S100A4 promoter involving STAT4 and inducing PTEN/PI3K/AKT signaling to promote growth and migration of breast cancer cells.
Regulation of S100A4 expression via the JAK2-STAT3 pathway in rhomboid-phenotype pulmonary arterial smooth muscle cells exposure to hypoxia.
Wang et al., Chongqing, China. In Int J Biochem Cell Biol, 2012
Data show that S100A4 is predominantly expressed in hypoxic rhomboid smooth muscle cells, and regulated by the activation of JAK2-STAT3 signal pathway, which is dependent on hypoxia-induced HIF-1alpha expression.
Crystal structure of the S100A4-nonmuscle myosin IIA tail fragment complex reveals an asymmetric target binding mechanism.
Nyitray et al., Budapest, Hungary. In Proc Natl Acad Sci U S A, 2012
Data suggest that the complex will facilitate the design of specific drugs that interfere with the S100A4-NMIIA interaction.
Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling.
Barsukov et al., Liverpool, United Kingdom. In Structure, 2012
Asymmetric mode of Ca-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling in epithelial carcinoma cells.
Evaluation of plasma and tissue S100A4 protein and mRNA levels as potential markers of metastasis and prognosis in clear cell renal cell carcinoma.
Li et al., Tianjin, China. In J Int Med Res, 2011
S100A4 and VEGF mRNA levels were up-regulated in clear cell renal cell carcinoma (CCRCC), tissue compared with control; upregulated tumour S100A4 and VEGF mRNA levels were independent risk factors for the presence of invasion and/or metastasis
Differential expression of S100A2 and S100A4 during progression of human prostate adenocarcinoma.
Mukhtar et al., Cleveland, United States. In J Clin Oncol, 2003
PURPOSE: To establish the clinical significance of calcium binding proteins S100A2 and S100A4 during progression of human prostate adenocarcinoma.
Analysis of a drosophila tRNA gene cluster: two tRNALeu genes contain intervening sequences.
Davidson et al., In Cell, 1981
The remaining five genes are identical tRNAIle genes, which are also identical to a tRNAIle gene from chromosomal region 42A.
The gross anatomy of a tRNA gene cluster at region 42A of the D. melanogaster chromosome.
Davidson et al., In Cell, 1980
The sequence organization and positions of the tRNA genes in a tRNA gene cluster at chromosomal region 42A of the D. melanogaster (Dm) genome have been studied by recombinant DNA methods.
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