TRAP1 is a Novel Interaction Partner of PML, Localized with PML in Nuclear Bodies and Relocating with PML to the Cytoplasm Following Stress

References (28)

1. 1 Targeting the dynamic HSP90 complex in cancer [DOI]
2. 2 Pml Is Critical for Nd10 Formation and Recruits the Pml-Interacting Protein Daxx to This Nuclear Structure When Modified by Sumo-1 [DOI]
3. 3 PINK1 Protects against Oxidative Stress by Phosphorylating Mitochondrial Chaperone TRAP1 [DOI]
4. 4 Regulation of proliferation, survival and apoptosis by members of the TNF superfamily [DOI]
5. 5 Pml is essential for multiple apoptotic pathways [DOI]
6. 6 PML Regulates Apoptosis at Endoplasmic Reticulum by Modulating Calcium Release [DOI]
7. 7 The hsp90-related Protein TRAP1 Is a Mitochondrial Protein with Distinct Functional Properties [DOI]
8. 8 Cytoplasmic PML function in TGF-β signalling [DOI]
9. 9 Pondering the Promyelocytic Leukemia Protein (PML) Puzzle: Possible Functions for PML Nuclear Bodies [DOI]
10. 10 Identification of a Protein with Homology to hsp90 That Binds the Type 1 Tumor Necrosis Factor Receptor [DOI]
11. 11 Heat Shock Protein 75 (TRAP1) Antagonizes Reactive Oxygen Species Generation and Protects Cells from Granzyme M-mediated Apoptosis [DOI]
12. 12 TRAP-1, the mitochondrial Hsp90 [DOI]
13. 13 Tumor necrosis factor-associated protein 1 (TRAP-1) protects cells from oxidative stress and apoptosis [DOI]
14. 14 Regulation of apoptosis by PML and the PML-NBs [DOI]
15. 15 TRAP1, a novel mitochondrial chaperone responsible for multi-drug resistance and protection from apoptotis in human colorectal carcinoma cells [DOI]
16. 16 Cytoprotective Mitochondrial Chaperone TRAP-1 As a Novel Molecular Target in Localized and Metastatic Prostate Cancer [DOI]
17. 17 PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia.
18. 18 A New Member of the hsp90 Family of Molecular Chaperones Interacts with the Retinoblastoma Protein during Mitosis and after Heat Shock [DOI]
19. 19 The molecular pathogenesis of acute promyelocytic leukaemia: implications for the clinical management of the disease [DOI]
20. 20 Involvement of Tumor Necrosis Factor Receptor-associated Protein 1 (TRAP1) in Apoptosis Induced by β-Hydroxyisovalerylshikonin [DOI]
21. 21 Size, position and dynamic behavior of PML nuclear bodies following cell stress as a paradigm for supramolecular trafficking and assembly [DOI]
22. 22 Immunoelectron Microscopy Provides Evidence That Tumor Necrosis Factor Receptor-Associated Protein 1 (TRAP-1) Is a Mitochondrial Protein Which also Localizes at Specific Extramitochondrial Sites [DOI]
23. 23 TRAP1 and the proteasome regulatory particle TBP7/Rpt3 interact in the endoplasmic reticulum and control cellular ubiquitination of specific mitochondrial proteins [DOI]
24. 24 The nuclear bodies inside out: PML conquers the cytoplasm [DOI]
25. 25 A Role for Cytoplasmic PML in Cellular Resistance to Viral Infection [DOI]
26. 26 Nuclear domain 10 (ND10) associated proteins are also present in nuclear bodies and redistribute to hundreds of nuclear sites after stress [DOI]
27. 27 Characterization of a new monoclonal antibody (PG-M3) directed against the aminoterminal portion of the PML gene product: immunocytochemical evidence for high expression of PML proteins on activated macrophages, endothelial cells, and epithelia [DOI]
28. 28 The puzzling multiple lives of PML and its role in the genesis of cancer [DOI]

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