Pages that link to "Q27679204"
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The following pages link to Structure and Activity of the Peptidyl-Prolyl Isomerase Domain from the Histone Chaperone Fpr4 toward Histone H3 Proline Isomerization (Q27679204):
Displaying 11 items.
- Crystal structure of Plasmodium vivax FK506-binding protein 25 reveals conformational changes responsible for its noncanonical activity (Q27687798) (← links)
- Quantitative proteomic analysis of histone modifications (Q30375585) (← links)
- The pentameric nucleoplasmin fold is present in Drosophila FKBP39 and a large number of chromatin-related proteins (Q30917202) (← links)
- Prolyl isomerases in gene transcription (Q35561852) (← links)
- Basic surface features of nuclear FKBPs facilitate chromatin binding (Q41095709) (← links)
- Lysine acetylation controls local protein conformation by influencing proline isomerization (Q42868563) (← links)
- Prolyl isomerization of the CENP-A N-terminus regulates centromeric integrity in fission yeast (Q47294808) (← links)
- The prolyl isomerase FKBP25 regulates microtubule polymerization impacting cell cycle progression and genomic stability. (Q52735215) (← links)
- FKBP25 participates in DNA double-strand break repair (Q64388239) (← links)
- Histone Chaperone Paralogs Have Redundant, Cooperative, and Divergent Functions in Yeast (Q90661943) (← links)
- AtFKBP53: a chimeric histone chaperone with functional nucleoplasmin and PPIase domains (Q91743530) (← links)