Proteome-wide microarray-based screening of PAR-binding proteins

Poly (ADP-ribose) (PAR) plays a crucial role in intracellular signaling and scaffolding through covalent modification or non-covalent binding to target proteins. The non-covalent PAR binding proteome (PARylome) has not been extensively characterized. Here, we performed a PAR-binding screen using a human protein microarray that covers most of the human proteome to characterize the non-covalent binding PARylome. A total of 356 PAR-binding proteins were identified. The PAR-binding PARylome suggests that PAR binding regulates a variety of biological processes beyond DNA damage signaling and DNA repair. Proteins that may be reprogrammed by PAR binding include signaling molecules, transcription factors, nucleic acid-binding proteins, calcium-binding proteins, ligases, oxidoreductases, enzymes, transferases, hydrolases, and receptors. The global database of PAR-binding proteins that we established will be a valuable tool for further in-depth analysis of the role of PARylation in a wide range o..., , # Proteome-wide microarray-based screening of PAR-binding proteins

Dataset DOI: [10.5061/dryad.zw3r228k1](https://doi.org/10.5061/dryad.zw3r228k1)

## Description of the data and file structure

We performed a large-scale PAR-binding screen using a human protein microarray to identify proteins that interact non-covalently with poly(ADP-ribose) (PAR). This experiment characterized the PAR-binding proteome (PARylome) and identified 356 PAR-binding proteins involved in diverse biological processes beyond DNA damage and repair, providing a global resource for studying PAR-mediated regulation.

Files are labeled by figure and include imaging files, data sets in Excel, and graphs in GraphPad. All files included in this submission are raw data files generated from experiments performed for this manuscript. 

### Files and variables

**File: Microarray_Source.zip**

**Description:** The file \"Protein information of the protein chip.txt\" contains information on all of the proteins spotted in th...,