ArticleJournal of molecular biology2009
Structure and activity of human mitochondrial peptide deformylase, a novel cancer target.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 52 citations in OpenAlex.
- N-terminal formylmethionine as a degron and a specific signal in proteostasis and stress adaptation.Experimental & molecular medicine · 2026Review
- Activation ofACS chemical biology · 2025Article
- Structures of Legionella pneumophila serogroup 1 peptide deformylase bound to nickel(II) and actinonin.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Hypoxia-induced tRF-3Frontiers in pharmacology · 2025Article
- Structural insights into N-terminal methionine cleavage by the human mitochondrial methionine aminopeptidase, MetAP1D.Scientific reports · 2023Article
- Maternally inherited peptides as strain-specific chemosignals.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Targeting Metalloenzymes for Therapeutic Intervention.Chemical reviews · 2019Review
- Expedient on-resin synthesis of peptidic benzimidazoles.Bioorganic & medicinal chemistry letters · 2018Article
- Validation of Putative Apicoplast-Targeting Drugs Using a Chemical Supplementation Assay in Cultured Human Malaria Parasites.Antimicrobial agents and chemotherapy · 2018Article
- The C-terminal residue of phage Vp16 PDF, the smallest peptide deformylase, acts as an offset element locking the active conformation.Scientific reports · 2017Article
- A unique peptide deformylase platform to rationally design and challenge novel active compounds.Scientific reports · 2016Article
- Structure-Based Drug Design of Small Molecule Peptide Deformylase Inhibitors to Treat Cancer.Molecules (Basel, Switzerland) · 2016Article
- The role of formylated peptides and formyl peptide receptor 1 in governing neutrophil function during acute inflammation.The American journal of pathology · 2015Review
- Inhibition of human mitochondrial peptide deformylase causes apoptosis in c-myc-overexpressing hematopoietic cancers.Cell death & disease · 2014Article
- Article
- Successful COG8 and PDF overlap is mediated by alterations in splicing and polyadenylation signals.Human genetics · 2012Article
- Genome-wide identification and in silico analysis of poplar peptide deformylases.International journal of molecular sciences · 2012Article
- Identification of benzofuran-4,5-diones as novel and selective non-hydroxamic acid, non-peptidomimetic based inhibitors of human peptide deformylase.Bioorganic & medicinal chemistry letters · 2011Article
- Inhibition of human peptide deformylase disrupts mitochondrial function.Molecular and cellular biology · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Peptide deformylase proteins (PDFs) participate in the N-terminal methionine excision pathway of newly synthesized peptides. We show that the human PDF (HsPDF) can deformylate its putative substrates derived from mitochondrial DNA-encoded proteins. The first structural model of a mammalian PDF (1.7 A), HsPDF, shows a dimer with conserved topology of the catalytic residues and fold as non-mammalian PDFs. The HsPDF C-terminus topology and the presence of a helical loop (H2 and H3), however, shape a characteristic active site entrance. The structure of HsPDF bound to the peptidomimetic inhibitor actinonin (1.7 A) identified the substrate-binding site. A defined S1' pocket, but no S2' or S3' substrate-binding pockets, exists. A conservation of PDF-actinonin interaction across PDFs was observed. Despite the lack of true S2' and S3' binding pockets, confirmed through peptide binding modeling, enzyme kinetics suggest a combined contribution from P2'and P3' positions of a formylated peptide substrate to turnover.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.