The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
PML Nuclear Bodies
Open accessAbstract
PML nuclear bodies are matrix-associated domains that recruit an astonishing variety of seemingly unrelated proteins. Since their discovery in the early 1960s, PML bodies have fascinated cell biologists because of their beauty and their tight association with cellular disorders. The identification of PML, a gene involved in an oncogenic chromosomal translocation, as the key organizer of these domains drew instant interest onto them. The multiple levels of PML body regulation by a specific posttranslational modification, sumoylation, have raised several unsolved issues. Functionally, PML bodies may sequester, modify or degrade partner proteins, but in many ways, PML bodies still constitute an enigma.
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Zhang, R., Poustovoitov, M. V., Ye, X., Santos, H. A., Chen, W., Daganzo, S. M., Erzberger, J. P., Serebriiskii, I. G., Canutescu, A. A., Dunbrack, R. L., et al. (2005) · Developmental Cell · doi:10.1016/j.devcel.2004.10.019 · Cited by 699
The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network
Song, M. S., Salmena, L., Carracedo, A., Egia, A., Lo-Coco, F., Teruya-Feldstein, J., & Pandolfi, P. P. (2008) · Nature · doi:10.1038/nature07290 · Cited by 548
Draskovic, I., Arnoult, N., Steiner, V., Bacchetti, S., Lomonte, P., & Londoño-Vallejo, A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907689106 · Cited by 175
Gupta, P., Ho, P.-C., Huq, M. M., Ha, S. G., Park, S. W., Khan, A. A., Tsai, N.-P., & Wei, L.-N. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0710561105 · Cited by 74
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Quinodoz, S. A., Ollikainen, N., Tabak, B., Palla, A., Schmidt, J. M., Detmar, E., Lai, M. M., Shishkin, A. A., Bhat, P., Takei, Y., et al. (2018) · Cell · doi:10.1016/j.cell.2018.05.024 · Cited by 892
Deciphering molecular interactions by proximity labeling
Qin, W., Cho, K. F., Cavanagh, P. E., & Ting, A. Y. (2021) · Nature Methods · doi:10.1038/s41592-020-01010-5 · Cited by 671
Differentiation therapy revisited
de Thé, H. (2018) · Nature reviews. Cancer · doi:10.1038/nrc.2017.103 · Cited by 462
Transportin 3 promotes a nuclear maturation step required for efficient HIV-1 integration
Zhou, L., Sokolskaja, E., Jolly, C., James, W., Cowley, S. A., & Fassati, A. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002194 · Cited by 130
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Metadata
- Authors
- Lallemand-Breitenbach, V., & de The, H.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2010-04-21
- Volume
- 2
- Issue
- 5
- Pages
- a000661-a000661
- ISSN
- 1943-0264 (ISSN-L)
- OpenAlex
- W2130090902
- Cited by
- 563
- References
- 4
- Type
- posted content
- Language
- en
- Open access
- bronze
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