Role of SUMO-1-modified PML in nuclear body formation.
By S. Zhong, Stefan Müller, S. Ronchetti, P. Freemont, A. Dejean, P. Pandolfi. Blood, 2000
599 citations recorded by the source corpus.
Subfields: Immunology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/956d42b789c79a730c7ecdce8014c71d7fe2dd5f
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In Immunology
In Molecular Biology
Citations in the corpus
- PML regulates p53 acetylation and premature senescence induced by oncogenic Ras (2000, background): “Ras failed to induce CBP aggregates in PML -/- MEFs, in which the nuclear bodies are disrupte”
- Modification of proteins by ubiquitin and ubiquitin-like proteins. (2006, background): “The PML protein must be sumoylated for PML bodies to form and for a number of other sumoylated proteins to concentrate there as well (Zhong et al. 2000).”
- The role of PML in tumor suppression. (2002, unknown): “which have been variably named PML nuclear bodies PML-NB component so far analyzed acquires an aber- (PML-NBs), Kremer bodies, ND10 (nuclear domain 10) rant nuclear localization pattern and PML add-back is or POD (for PML oncogenic domains) (Jensen et al., able to rescue normal localization ( Zhong ”
- Compositional Control of Phase-Separated Cellular Bodies (2016, unknown): “SUMO-SIM interactions also appear to be critical for the recruitment of many PML NB clients (e.g., Daxx and Sp100) (Lin et al., 2006; Van Damme et al., 2010; Zhong et al., 2000).”
- The promise of retinoids to fight against cancer (2001, background): “PML–RARα interacts with the PML expressed from the intact allele, causing nuclear bodies to disintegrate, and leading to the relocalization of nuclear body proteins in aberrant nuclear structure”