Shiptide free download

Affiliations 1 author 1. Share this article Share with email Share with twitter Share with linkedin Share with facebook. Abstract The lipid phosphatase Ship2 is a protein that intervenes in several diseases such as diabetes, cancer, neurodegeneration, and atherosclerosis. It is made up of a catalytic domain and several protein docking modules such as a C-terminal Sam Sterile alpha motif domain.

Here we investigated the conformational features of this peptide, through solution CD and NMR studies in different conditions. These studies reveal that the peptide is highly flexible in aqueous buffer, while it adopts a helical conformation in presence of 2,2,2-trifluoroethanol.

The discovered structural insights and in particular the identification of a helical motif, may lead to the design of more constrained and possibly cell permeable Shiptide analogs that could work as efficient antagonists of Ship2-Sam heterotypic interactions and embrace therapeutic applications.

Full text links Read article at publisher's site DOI : References Articles referenced by this article 71 The role of the inositol polyphosphate 5-phosphatases in cellular function and human disease. Lipid phosphatases as drug discovery targets for type 2 diabetes. SHIP2 and its involvement in various diseases. Identification of a second SH2-domain-containing protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP. The lipid phosphatase SHIP2 controls insulin sensitivity.

A human sterile alpha motif domain polymerizome. SAM domains: uniform structure, diversity of function. Identifying polymer-forming SAM domains. Show 10 more references 10 of Smart citations by scite. The number of the statements may be higher than the number of citations provided by EuropePMC if one paper cites another multiple times or lower if scite has not yet processed some of the citing articles.

Explore citation contexts and check if this article has been supported or disputed. The Sam-Sam interaction between Ship2 and the EphA2 receptor: design and analysis of peptide inhibitors. Similar Articles To arrive at the top five similar articles we use a word-weighted algorithm to compare words from the Title and Abstract of each citation.

Structural investigation of a C-terminal EphA2 receptor mutant: Does mutation affect the structure and interaction properties of the Sam domain? Funding Funders who supported this work. Joining Europe PMC. Tools Tools overview. ORCID article claiming. Journal list. Roboto has a dual nature. It has a mechanical skeleton and the forms are largely geometric.

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