{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Reay DP"],"funding":["NIDDK NIH HHS","NIA NIH HHS","NCRR NIH HHS"],"pagination":["442-52"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4559531"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["21"],"pubmed_abstract":["In Duchenne muscular dystrophy (DMD) patients and the mdx mouse model of DMD, chronic activation of the classical nuclear factor-κB (NF-κB) pathway contributes to the pathogenesis that causes degeneration of muscle fibers, inflammation and fibrosis. Prior studies demonstrate that inhibition of inhibitor of κB kinase (IKK)-mediated NF-κB activation using L-isomer NF-κB essential modulator (NEMO)-binding domain (NBD) peptide-based approaches reduce muscle pathology in the mdx mouse. For our studies, the NBD peptide is synthesized as a fusion peptide with an eight-lysine (8K) protein transduction domain to facilitate intracellular delivery. We hypothesized that the d-isoform peptide could have a greater effect than the naturally occurring L-isoform peptide due to the longer persistence of the"],"journal":["Molecular medicine (Cambridge, Mass.)"],"pubmed_title":["D-Amino Acid Substitution of Peptide-Mediated NF-κB Suppression in mdx Mice Preserves Therapeutic Benefit in Skeletal Muscle, but Causes Kidney Toxicity."],"pmcid":["PMC4559531"],"funding_grant_id":["P30-DK079307","T32 DK061296","P30 DK079307","1S10RR019003-01","P01 AG043376","S10 RR019003"],"pubmed_authors":["Wack KE","Bastacky SI","Robbins PD","Reay DP","Clemens PR","Stolz DB"],"additional_accession":[]},"is_claimable":false,"name":"D-Amino Acid Substitution of Peptide-Mediated NF-κB Suppression in mdx Mice Preserves Therapeutic Benefit in Skeletal Muscle, but Causes Kidney Toxicity.","description":"In Duchenne muscular dystrophy (DMD) patients and the mdx mouse model of DMD, chronic activation of the classical nuclear factor-κB (NF-κB) pathway contributes to the pathogenesis that causes degeneration of muscle fibers, inflammation and fibrosis. Prior studies demonstrate that inhibition of inhibitor of κB kinase (IKK)-mediated NF-κB activation using L-isomer NF-κB essential modulator (NEMO)-binding domain (NBD) peptide-based approaches reduce muscle pathology in the mdx mouse. For our studies, the NBD peptide is synthesized as a fusion peptide with an eight-lysine (8K) protein transduction domain to facilitate intracellular delivery. We hypothesized that the d-isoform peptide could have a greater effect than the naturally occurring L-isoform peptide due to the longer persistence of the","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 May","modification":"2025-04-26T04:07:57.838Z","creation":"2019-03-27T01:57:49Z"},"accession":"S-EPMC4559531","cross_references":{"pubmed":["26018805"],"doi":["10.2119/molmed.2013.00141"]}}