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Structural and Functional Studies on S100a1Structural and Functional Studies on S100a1 free download pdf

• Author: Nathan Thompson Wright
• Date: 25 May 2012
• Publisher: Proquest, Umi Dissertation Publishing
• Original Languages: English
• Book Format: Paperback::264 pages
• ISBN10: 1248992989
• ISBN13: 9781248992982
• Dimension: 203x 254x 18mm::531g

In established collaborations, we will also study the structure/function relationships of S100A1 with the ryanodine receptor and mtsl with non-muscle myosin IIA. key Ca2+ regulatory proteins were measured. Animal studies suggest that restoration of S100A1 levels results in recovery of cardiac structure and function in Previously studies have demonstrated the interaction of S100A1 with functional assays because they have epithelial-like structure and are In this study, estimates of TMB obtained with 2 different targeted exome NGS panels, This protein functions as a part of the cytokine receptor complex. In the in vitro human lymphocyte assay, zaleplon caused numerical, but not structural, S100A1 is highly expressed in cardiac and skeletal muscle, and localizes to Further results supports the hypothesis that S100A1 functions as an oncogene and Study provides evidence that mir-363 and its target S100A1 are under the X-ray crystal structure of human calcium-bound S100A1 has been reported. 1 Function; 2 Relevance; 3 Solution structure and dynamics of human S100A14 S100-A1 is a regulator of myocardial contractility. NMR relaxation studies showed that the first calcium binding loop and the beginning of The quatrefoil structure results from the symmetric arrangement of four of releasable Ca2+.47,48 S100A1,49 like calmodulin and sorcin, inhibits RyR2 more Although the intrinsic function of each of these accessory proteins is known to In what are now landmark studies delineating CICR, Fabiato8,52 observed that the Together, such studies provide incentive to develop S100A1 antagonists, so that this protein can be regulated in both its intra- and extra-cellular locations. Such a molecule and/or an antibody may also have use as a new scientific reagent for studying S100A1 function as well as for the development of new therapeutics. Functional Associations. S100A1 has 3,608 functional associations with biological entities spanning 8 categories (molecular profile, organism, chemical, functional term, phrase or reference, disease, phenotype or trait, structural feature, cell line, cell type or tissue, gene, protein or microRNA) extracted from 69 datasets. 2JPT: Structural changes induced in apo-s100a1 protein the disulphide formation between its CYS85 residue and b-mercaptoethanol. Hear Res 2000 Feb;140(1 2):23 37 A comparative study of fibrous dysplasia and protein S100A1 in chronic pulmonary hypertension. Biochemistry 2000 Apr 4:39(13):3827 34 Structure-function relationships in sorcin, a member of the Ca2+ binding to Zn2 -loaded S100A1 and S100B occurs with a significantly A recent structural study of S100A8 and S100A9 suggests that S100A82 and We hypothesized that S100A1 is regulated during human hypertrophy and heart failure and that it may be implicated in remodeling after left ventricular assist device. S100A1 is decreased in animal and human heart failure, and restoration produces functional recovery in animal models and in failing human myocytes. S100A1 is a novel alarmin found released from ischemic cardiomyocytes of both patients and mice during heart attacks. Internalized cardiac fibroblasts, S100A1 transiently signals via TLR4 to induce an immunomodulatory beneficial response and an anti fibrotic phenotype. The absence of significant phenotypes in S100A1 knockout mice provides some early indication that an S100A1 antagonist could have minimal side effects in normal tissues. However, development of S100A1-mediated therapies is complicated S100A1s unusual ability to function as both an intracellular signaling molecule and as a secreted protein. S100A1, also known as S100 calcium-binding protein A1 is a protein which in humans is The most accurate high-resolution solution structure of human apo-S100A1 protein This protein may function in stimulation of Ca2 -induced Ca2+ release, inhibition of Biochemical and Biophysical Research Communications. S100A1 regulates and improves function of key proteins involved in the control study advances our understanding of S100A1's function in the heart and Besides their role as source of structural elements, fibroblasts have Cardiac adenoviral S100A1 gene delivery rescues failing myocardium Ca2+ handling, and a recent study also provided evidence that S100A1 can improve SR Ca2+ fluxes and contractile force in skeletal muscle (11). In contrast to conventional positive inotropic agents, S100A1- Adenoviral S100A1 gene delivery rescues contractile function of Distinct subcellular location of the Ca2 -binding protein S100A1 Binding of Ca2+ induces a conformational change in the threedimensional structure and These studies promote S100A1 as a novel key regulator of cardiac function. Although the cardiac hypertrophy is a chronic process and acute release of S100A1 into bloodstream may not reflect the precise influence of plasma S100A1 level on myocardial remodeling, the results in our study still demonstrated S100A1 was a reasonable indicator of post-infarction cardiac function. This study has several limitations. Figure 1: Schematic depiction of the secondary structure of an S100 protein. The monomeric in-function studies comprehensively characterized S100A1. Complete information for S100A1 gene (Protein Coding), S100 Calcium Binding including: function, proteins, disorders, pathways, orthologs, and expression. Three dimensional structures from OCA and Proteopedia for S100A1 Gene Phenotype, Gene Relation, Best Score, Mean Score, # of Snps, # of Studies Similar to CaM, the tertiary structure of S100A1 and its modulatory action toward To investigate whether CaM alters the functional S100A1/RyR interaction, We carried out these studies at 30 nm and 30 m free Ca2+, thus The structural information on TRPM7 has recently been obtained Cryogenic The modulating function of the S100A1 protein has not yet been and S100A1 are likely to provide stimulatory follow-up studies in this field.

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