We con-dense if we want to; We can't leave AZUL outside.

[1]  H. Matsuo,et al.  E6AP AZUL interaction with UBQLN1/2 in cells, condensates, and an AlphaFold-NMR integrated structure. , 2023, Structure.

[2]  S. Martens,et al.  Reconstitution defines the roles of p62, NBR1 and TAX1BP1 in ubiquitin condensate formation and autophagy initiation , 2021, Nature Communications.

[3]  M. Rosen,et al.  A framework for understanding the functions of biomolecular condensates across scales , 2020, Nature Reviews Molecular Cell Biology.

[4]  R. Chari,et al.  Structure of E3 ligase E6AP with a proteasome-binding site provided by substrate receptor hRpn10 , 2020, Nature Communications.

[5]  B. Pugh,et al.  Phase separation directs ubiquitination of gene-body nucleosomes , 2020, Nature.

[6]  W. Baumeister,et al.  Stress- and ubiquitylation-dependent phase separation of the proteasome , 2020, Nature.

[7]  C. Castañeda,et al.  Single Amino Acid Substitutions in Stickers, but Not Spacers, Substantially Alter UBQLN2 Phase Transitions and Dense Phase Material Properties. , 2019, The journal of physical chemistry. B.

[8]  K. Lindorff-Larsen,et al.  Cancer Mutations of the Tumor Suppressor SPOP Disrupt the Formation of Active, Phase-Separated Compartments. , 2018, Molecular cell.

[9]  J. Taylor,et al.  Ubiquitin Modulates Liquid-Liquid Phase Separation of UBQLN2 via Disruption of Multivalent Interactions. , 2018, Molecules and Cells.

[10]  J. Heath,et al.  Nbr1 Is a Novel Inhibitor of Ligand-Mediated Receptor Tyrosine Kinase Degradation , 2010, Molecular and Cellular Biology.