1. Acute Promyelocytic Leukemia: A Paradigm for Oncoprotein-Targeted Cure
Hugues de Thé, Pier Paolo Pandolfi, Zhu Chen 
Cancer Cell 
Volume 32, Issue 5, Pages (November 2017)
DOI: /j.ccell
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2. Figure 1 Schematic Representation of PML/RARA-Driven APL Pathogenesis
PML/RARA exerts dominant-negative effects on PML nuclear bodies assembly (top) and RAR/RXR-dependent transcriptional control (bottom). The latter is achieved through the recruitment of co-repressor complexes (CoR). PML/RARA ultimately drives enhanced self-renewal and differentiation block.
Cancer Cell  , DOI: ( /j.ccell )
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3. Figure 2
Current Models for the Therapeutic Efficacy of Retinoic Acid or Arsenic in APL
(A) Dual effects of RA therapy on PML/RARA: activation of transcription and proteasome-mediated degradation. The latter allows NB reformation and loss of self-renewal, at least in part through p53 activation. As, arsenic.
(B) Effect RA or RA/arsenic therapy to reform PML NB reformation in APL cells in vivo from Ablain et al. (2014).
(C) Schematic representation of the dual effects of arsenic to degrade PML/RARA (similar to RA) and also to directly enhance PML nuclear body association.
Cancer Cell  , DOI: ( /j.ccell )
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4. Figure 3
Mutations in PML or PML/RARA Associated with Clinical Resistance to Arsenic Therapy
(A) Summary of the published mutations on the arsenic-binding region of PML and PML/RARA in the B2 box in therapy-resistant patients. The red line indicates a highly evolutionarily conserved region. The presumed arsenic-binding cysteine residues are in blue. The most commonly mutated residue is A216.
(B) Mutants of the arsenic-binding site show altered NB targeting in the basal state and the diffuse nuclear PML fails to aggregate onto NBs upon arsenic exposure (Jeanne et al., 2010).
Cancer Cell  , DOI: ( /j.ccell )
Copyright © 2017 Elsevier Inc. Terms and Conditions