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ProteomicsRepairing of isoaspartyl residues by PCMT1 alleviates renal fibrosis through the repression of TGF-β1/TGFBR2/Smad signaling pathway
Protein L-isoaspartyl/D-aspartyl Methyltransferase (PCMT1) plays a pivotal role in repairing a spontaneous post-translational modification (PTM) of L-isoaspartyl residues resulted from asparagine deamidation or aspartate isomerization. This PTM is particularly important for extracellular matrix (ECM...
ORGANISM(S): Mus musculus (Mouse) 
2025-03-18 | PXD047057 | Pride
Pcmt1 Tgf-β1-smad pathway Isoaspartyl residues Tgfbr2 Extracellular matrix Renal fibrosis 
GenomicsRepairing of isoaspartyl residues by PCMT1 alleviates renal fibrosis through the repression of TGF-β1/TGFBR2/Smad signaling pathway
Repairing of isoaspartyl residues by PCMT1 alleviates renal fibrosis through the repression of TGF-β1/TGFBR2/Smad signaling pathway
PRJNA1043803 | ENA
TranscriptomicsRepairing of isoaspartyl residues by PCMT1 alleviates renal fibrosis through the repression of TGF-β1/TGFBR2/Smad signaling pathway
Protein L-isoaspartyl/D-aspartyl Methyltransferase (PCMT1) plays a pivotal role in repairing a spontaneous post-translational modification (PTM) of L-isoaspartyl residues resulted from asparagine deamidation or aspartate isomerization. This PTM is particularly important for extracellular matrix (ECM...
ORGANISM(S): Mus musculus Homo sapiens 
2024-01-01 | GSE248435 | GEO
UnknownNon-repair pathways for minimizing protein isoaspartyl damage in the yeast Saccharomyces cerevisiae.
Not available
S-EPMC4059137 | biostudies-literature
ProteomicsInvestigation of isoAsp accumulation to antioxidative enzymes during thermal stress and their repair by PROTEIN L-ISOASPARTYL METHYLTRANSFERASE (PIMT).
The formation of isoAsp residues from Asp and Asn residues in proteins and peptides is accelerated under stressful environments and has detrimental effects on protein structure and function. PROTEIN L-ISOASPARTYL METHYLTRANSFERASE (PIMT) is a protein repairing enzyme which revert such deleterious is...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2019-12-18 | PXD016240 | Pride
Arabidopsis Pimt Isoasp Protein repair. Antioxidative enzyme 
UnknownCrystal structure of human L-isoaspartyl-O-methyl-transferase with S-adenosyl homocysteine at 1.6-A resolution and modeling of an isoaspartyl-containing peptide at the active site.
Not available
S-EPMC2373461 | biostudies-literature
UnknownArabidopsis protein l-ISOASPARTYL METHYLTRANSFERASE repairs isoaspartyl damage to antioxidant enzymes and increases heat and oxidative stress tolerance.
Not available
S-EPMC6970934 | biostudies-literature
ProteomicsInvestigation of interacting proteins of PROTEIN L-ISOASPARTYL METHYLTRANSFERASE (PIMT) during ShB pathogenesis and identification of isoAsp accumulation in ALDH and PBZ1.
1. The formation of isoAsp residues from Asp and Asn residues in proteins and peptides is accelerated under stressful environments and has detrimental effects on protein structure and function. PROTEIN L-ISOASPARTYL METHYLTRANSFERASE (PIMT) is a protein repairing enzyme which revert such deleterious...
ORGANISM(S): Oryza sativa (Rice) 
2026-09-14 | PXD080366 | Pride
Rice Ros homeostasis Ospbz1. Pimt Isoasp Sheath blight disease Osaldh Protein repair Rhizoctonia solani 
Unknownl-Isoaspartyl Methyltransferase Deficiency in Zebrafish Leads to Impaired Calcium Signaling in the Brain.
Not available
S-EPMC7859441 | biostudies-literature
UnknownStructural basis for L-isoaspartyl-containing protein recognition by the PCMTD1 cullin-RING E3 ubiquitin ligase.
Not available
S-EPMC12139721 | biostudies-literature
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