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This Service

A database built with INDRA combining content from numerous readers and databases. This page allows you to curate the loaded statements. For more information please see the manual.

This Project

INDRA is developed by indralabs, a part of the Harvard Medical School Laboratory of Systems Pharmacology.

This project, indra_db, is also developed by the indralab team. For more information on how we procure our sources, you can go here. This work was funded by ARO grant W911NF‐15‐1‐0544 under the DARPA Communicating with Computers program.

IndraLab

Statements

OTUD4 binds dsDNA. 2 / 2

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"Structure based mutagenesis of OB1 N-terminal residues (Lys48 and Lys53) for minor groove interaction and of OB2 residues (Arg224) for major groove recognition showed that these positively charged residues are crucial for HIN1 and dsDNA interaction (XREF_FIG, XREF_SUPPLEMENTARY)."

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"Crystal structures of the p202 HIN1 and dsDNA complexes show that the two OB folds are very similar to those of AIM2, but that the dsDNA binds p202 HIN1 at an almost opposite surface compared with that used in AIM2 HIN (XREF_FIG) [XREF_BIBR, XREF_BIBR, XREF_BIBR]."

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Our Sources:

INDRA allows us to combine the results from a multitude of sources. In particular, the INDRA Database draws on the following...