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S100 calcium binding protein A5

S100A5, S100D
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 has a Ca2+ affinity 20- to 100-fold higher than the other S100 proteins studied under identical conditions. This protein also binds Zn2+ and Cu2+, and Cu2+ strongly which impairs the binding of Ca2+. This protein is expressed in very restricted regions of the adult brain. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: S-100, calcyclin, S100A4, S100A3, S100A2
Papers on S100A5
HuR regulates alternative splicing of the TRA2β gene in human colon cancer cells under oxidative stress.
Rokutan et al., Tokushima, Japan. In Mol Cell Biol, 2014
In endogenous HuR knockdown cells, the overexpression of a HuR mutant that could not be phosphorylated (with changes of serine to alanine at position 88 [S88A], S100A, and T118A) blocked the associated TRA2β4 interaction and TRA2β4 generation, while the overexpression of a phosphomimetic HuR (with mutations S88D, S100D, and T118D) restored the TRA2β4-related activities.
The membrane proteome of sensory cilia to the depth of olfactory receptors.
Warscheid et al., Bochum, Germany. In Mol Cell Proteomics, 2014
Quantitative data evaluation revealed four ciliary membrane-associated candidate proteins (the annexins ANXA1, ANXA2, ANXA5, and S100A5) with a suggested function in the regulation of olfactory signal transduction, and their presence in ciliary structures was confirmed by immunohistochemistry.
Activity-dependent genes in mouse olfactory sensory neurons.
McClintock et al., Lexington, United States. In Chem Senses, 2014
Both unilateral naris occlusion of mice for 6 days and genetic silencing of OSNs decreased S100A5, Lrrc3b, Kirrel2, Slc17a6, Rasgrp4, Pcp4l1, Plcxd3, and Kcnn2 while increasing Kirrel3.
Modulation of quaternary structure of S100 proteins by calcium ions.
Makhatadze et al., Troy, United States. In Biophys Chem, 2010
To this end we performed equilibrium analytical ultracentrifugation experiments for 16 S100 proteins (S100A1, S100A2, S100A3, S100A4, S100A5, S100A6, S100A7, S100A8, S100A9, S100A10, S100A11, S100A12, S100A13, S100B, S100P, and S100Z) under reducing conditions in the absence and presence of calcium ions.
Epidermal growth factor receptor ligands as new extracellular targets for the metastasis-promoting S100A4 protein.
Lukanidin et al., Copenhagen, Denmark. In Febs J, 2009
Structured digital abstract: * MINT-7256556: EGF (uniprotkb:P01133) binds (MI:0407) to S100A4 (uniprotkb:P26447) by far western blotting (MI:0047) * MINT-7256512: BC (uniprotkb:P35070) binds (MI:0407) to S100A4 (uniprotkb:P26447) by far western blotting (MI:0047) * MINT-7256485, MINT-7256618, MINT-7256636: AR (uniprotkb:P15514) binds (MI:0407) to S100A4 (uniprotkb:P26447) by far western blotting (MI:0047) * MINT-7256494: HB-EGF (uniprotkb:Q99075) binds (MI:0407) to S100A4 (uniprotkb:P26447) by far western blotting (MI:0047) * MINT-7256502: P53 (uniprotkb:P04637) binds (MI:0407) to S100A4 (uniprotkb:P26447) by far western blotting (MI:0047) * MINT-7256654: S100A2 (uniprotkb:P29034) binds (MI:0407) to AR (uniprotkb:P15514) by far western blotting (MI:0047) * MINT-7256693: S100A5 (uniprotkb:P33763) binds (MI:0407) to AR (uniprotkb:P15514) by far western blotting (MI:0047) * MINT-7256593: S100A4 (uniprotkb:P26447) binds (MI:0407) to BC (uniprotkb:P35070) by pull down (MI:0096) * MINT-7256567: S100A4 (uniprotkb:P26447) binds (MI:0407) to AR (uniprotkb:P15514) by pull down (MI:0096).
Solution structure and dynamics of S100A5 in the apo and Ca2+-bound states.
Yuan et al., Sesto Fiorentino, Italy. In J Biol Inorg Chem, 2009
Homodimeric solution structures of S100A5 in both apo & Ca(II)-loaded forms were obtained & show conformational rearrangement on Ca binding. Also, large mobility was observed in hinge loop of apo-S100A5; this mobility was not quenched in Ca form.
Expression of S100 protein family members in the pathogenesis of bladder tumors.
Cheng et al., Saint Louis, United States. In Anticancer Res, 2007
Thirteen members of the S100 gene family were confirmed by real-time PCR to be differentially expressed in human bladder cancers, with overexpression of S100A2, S100A3, S100A5, S100A7, S100A8, S100A9, S100A14, S100A15, S100A16 and S100P, and underexpression of S100A1, S100A4 and S100B.
Effect of hypoxic preconditioning on brain genomic response before and following ischemia in the adult mouse: identification of potential neuroprotective candidates for stroke.
Bernaudin et al., Davis, United States. In Neurobiol Dis, 2006
A second wave of changes occurred 24 h after reoxygenation (S100A5, TH, Calretinin, PBX3).
S100-mediated signal transduction in the nervous system and neurological diseases.
Rast et al., College Station, United States. In Cell Mol Biol (noisy-le-grand), 2005
A total of ten S100 family members are reported in the literature to be expressed in brain -S100A1, S100A2, S100A4, S100A5, S100A6, S100A10, S100A11, S100A13, S100B, and S100Z.
Calcium-modulated S100 protein-phospholipid interactions. An NMR study of calbindin D9k and DPC.
Chazin et al., Nashville, United States. In Biochemistry, 2005
The interactions between calbindin D(9k) (S100D) and the detergent dodecyl phosphocholine (DPC) were studied using NMR spectroscopy.
Differentially expressed transcripts from phenotypically identified olfactory sensory neurons.
McClintock et al., Lexington, United States. In J Comp Neurol, 2005
S100A5, Ddit3, Sirt2, CD81, Sdc2, Omp, and Ptpla.
Meningioma: an update.
Gutmann et al., Saint Louis, United States. In Curr Opin Neurol, 2004
In addition to histologic grading and estimates of the extent of resection, biomarkers, such as progesterone receptor, cyclooxygenase 2, S100A5 and ornithine decarboxylase may be useful in predicting tumor recurrence and/or progression potential in patients with meningioma.
Detection of S100B, S100A6 and galectin-3 ligands in meningiomas as markers of aggressiveness.
Decaestecker et al., Brussels, Belgium. In Int J Oncol, 2004
Using 63 meningiomas (39 benign and 24 atypical), we performed a semi-quantitative histochemical analysis of both the expression of galectin-3 and its ligand profile and the Ca2+-binding proteins S100A5, S100A6 and S100B.
S100A5: a marker of recurrence in WHO grade I meningiomas.
Decaestecker et al., Brussels, Belgium. In Neuropathol Appl Neurobiol, 2004
The fixed tumour material from each meningioma was submitted to histochemical analyses targeting galectin-3 and its binding sites, the S100A5, S100A6 and S100B proteins, and cathepsin-B and -D.
Expression analysis of S100 proteins and RAGE in human tumors using tissue microarrays.
Heizmann et al., Zürich, Switzerland. In Biochem Biophys Res Commun, 2003
In contrast, S100A5 and S100A12 were not significantly expressed in any of the tumor tissues tested.
Differential expression of S100 proteins in the developing human hippocampus and temporal cortex.
Yew et al., Hong Kong, Hong Kong. In Microsc Res Tech, 2003
Strongly expressed at 12 weeks gestation in the cells and fibers of the hippocampus, and then decreased with age. In the temporal cortex, detected from 12 weeks onwards, peaked at 20 to 24 weeks, and then decreased with age.
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