PDF Antibody

1. compound M7594_0037 exhibited potent anticancer activities against HeLa, A549 and MCF-7 cell lines with IC50s of 35.26, 29.63 and 24.63 muM, respectively. Molecular docking studies suggested that M7594_0037 and its three derivatives could interact with Human peptide deformylase by several conserved hydrogen bonds. PMID: 27023495
2. c-myc regulated the expression of human PDF. PMID: 24675470
3. This is the first report showing that PDF is over-expressed in breast, colon, and lung cancers PMID: 23815882
4. these data reveals that PDF has several transcription start sites, the most important of which only 18 bp from the initiation codon. PMID: 22554513
5. the origin, evolution and preservation of the COG8/PDF same-strand overlap follow similar mechanistic steps as those documented for antisense overlaps where gain and/or loss of splice sites and polyadenylation signals seems to drive the process. PMID: 21805148
6. The inhibition of HsPDF may provide an explanation for the mechanism by which actinonin is cytotoxic against various human tumor cell lines. PMID: 14637138
7. 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. PMID: 19236878

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HGNC: 30012

KEGG: hsa:64146

STRING: 9606.ENSP00000288022

UniGene: Hs.130849