ArticleProceedings of the National Academy of Sciences of the United States of America1996
In vivo and in vitro characterization of the B1 and B2 zinc-binding domains from the acute promyelocytic leukemia protooncoprotein PML.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
40 citing papers in PubMed, 117 citations in OpenAlex.
- Discovery of novel murine PML isoforms.Nucleus (Austin, Tex.) · 2026Article
- Mex3a-dependent post-transcriptional silencing ensures olfactory receptor diversity and axon guidance specificity.Cell reports · 2025Article
- Mutation in the UnrearrangedResearch (Washington, D.C.) · 2025Article
- The tripartite motif-containing 24 is a multifunctional player in human cancer.Cell & bioscience · 2024Review
- Review
- Conformational exchange at a CStructure (London, England : 1993) · 2023Article
- SUMOylation regulates the number and size of promyelocytic leukemia-nuclear bodies (PML-NBs) and arsenic perturbs SUMO dynamics on PML by insolubilizing PML in THP-1 cells.Archives of toxicology · 2022Article
- Effects of arsenic on the topology and solubility of promyelocytic leukemia (PML)-nuclear bodies.PloS one · 2022Article
- PML nuclear body biogenesis and oligomerization-driven leukemogenesis.Blood science (Baltimore, Md.) · 2020Review
- B1 oligomerization regulates PML nuclear body biogenesis and leukemogenesis.Nature communications · 2019Article
- RING tetramerization is required for nuclear body biogenesis and PML sumoylation.Nature communications · 2018Article
- Visualization of PML nuclear import complexes reveals FG-repeat nucleoporins at cargo retrieval sites.Nucleus (Austin, Tex.) · 2017Article
- RFPL3 and CBP synergistically upregulate hTERT activity and promote lung cancer growth.Oncotarget · 2015Article
- TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly.Journal of cell science · 2014Article
- Structural insights into the TRIM family of ubiquitin E3 ligases.Cell research · 2014Article
- Review
- The role of PML in the nervous system.Molecular neurobiology · 2011Review
- PML3 Orchestrates the Nuclear Dynamics and Function of TIP60.The Journal of biological chemistry · 2009Article
- Pondering the puzzle of PML (promyelocytic leukemia) nuclear bodies: can we fit the pieces together using an RNA regulon?Biochimica et biophysica acta · 2008Review
- LZF1/SALT TOLERANCE HOMOLOG3, an Arabidopsis B-box protein involved in light-dependent development and gene expression, undergoes COP1-mediated ubiquitination.The Plant cell · 2008Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Acute promyelocytic leukemia (APL) has been ascribed to a chromosomal translocation event which results in a fusion protein comprising the PML protein and retinoic acid receptor alpha. PML is normally a component of a nuclear multiprotein complex which is disrupted in the APL disease state. Here, two newly defined cysteine/histidine-rich protein motifs called the B-box (B1 and B2) from PML have been characterized in terms of their effect on PML nuclear body formation, their dimerization, and their biophysical properties. We have shown that both peptides bind Zn2+, which induces changes in the peptides' structures. We demonstrate that mutants in both B1 and B2 do not form PML nuclear bodies in vivo and have a phenotype that is different from that observed in the APL disease state. Interestingly, these mutations do not affect the ability of wild-type PML to dimerize with mutant proteins in vitro, suggesting that the B1 and B2 domains are involved in an additional interaction central to PML nuclear body formation. This report in conjunction with our previous work demonstrates that the PML RING-Bl/B2 motif plays a fundamental role in formation of a large multiprotein complex, a function that may be common to those unrelated proteins which contain the motif.
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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.