ProNIT statistics

info info

Citations per year


Tool usage distribution map

info info

Associated diseases


Popular tool citations

chevron_left Protein-RNA interaction databases Protein-DNA interaction databases chevron_right
Want to access the full stats & trends on this tool?

ProNIT specifications


Unique identifier OMICS_00541
Name ProNIT
Restrictions to use None
Community driven No
Data access File download, Browse
User data submission Not allowed
Maintained No

Publications for ProNIT

ProNIT citations


Mapping genetic variations to three dimensional protein structures to enhance variant interpretation: a proposed framework

Genome Med
PMCID: 5735928
PMID: 29254494
DOI: 10.1186/s13073-017-0509-y

[…] m wild-type and mutant protein pairs, often using protein stability data from the ProTherm database [], protein–protein binding affinities from SKEMPI [], protein–nucleic acid binding affinities from ProNIT [], and protein–ligand binding affinities from Platinum [].A second set of methods [, , , –] predicts the phenotypic effect (pathogenicity) of mutations, most often as a binary classification: […]


Functional Annotation of Putative Regulatory Elements at Cancer Susceptibility Loci

Cancer Inform
PMCID: 4179605
PMID: 25288875
DOI: 10.4137/CIN.S13789

[…] f annotating specific variants for functional effect. Similarly, nonsynonymous SNPs (nsSNPs) can be assigned function based on their impact on structural stability through databases like ProTherm and ProNit. In contrast, noncoding SNP annotations are constrained by a dearth of knowledge pertaining to the phenotypic impact of regulatory variation. However, the number of genome annotations relevant […]


Using protein design algorithms to understand the molecular basis of disease caused by protein–DNA interactions: the Pax6 example

Nucleic Acids Res
PMCID: 2995082
PMID: 20685816
DOI: 10.1093/nar/gkq683

[…] mutations in the interface with DNA and the other made of wild-type proteins interacting with different DNA sequences.The set of protein mutants in protein–DNA complexes was initially taken from the ProNIT database (). However, due to internal inconsistencies of the database, the actual data (physical data of the experiments and the change in interaction energy due to the mutation, ΔΔGint) were t […]

Want to access the full list of citations?
ProNIT institution(s)
Department of Bioscience and Bioinformatics, Kyushu Institute of Technology (KIT), Iizuka, Japan; Advanced Technology Institute, Inc. (ATI), Saitama, Japan; Computational Biology Research Center (CBRC), National Institute of Advanced Industrial Science and Technology (AIST), Tokyo, Japan; Laboratory of Experimental and Computational Biology, NCI, NIH, Frederick, MD, USA; Tsukuba Materials Information Laboratory, Tsukuba, Japan
ProNIT funding source(s)
Partially supported by a Grant-inAid for Publication Scientific Research Results from the Japan Society for the Promotion of Sciences (JSPS).

ProNIT reviews

star_border star_border star_border star_border star_border
star star star star star

Be the first to review ProNIT