Published in Biomolecules on July 09, 2014
Protein Quality Control by Molecular Chaperones in Neurodegeneration. Front Neurosci (2017) 0.87
Degradation-mediated protein quality control at the inner nuclear membrane. Nucleus (2016) 0.76
Bioinformatics analysis identifies several intrinsically disordered human E3 ubiquitin-protein ligases. PeerJ (2016) 0.75
UBL/BAG-domain co-chaperones cause cellular stress upon overexpression through constitutive activation of Hsf1. Cell Stress Chaperones (2016) 0.75
Subcellular organization of UBE3A in neurons. J Comp Neurol (2016) 0.75
The exocyst subunit Sec3 is regulated by a protein quality control pathway. J Biol Chem (2017) 0.75
RING domain E3 ubiquitin ligases. Annu Rev Biochem (2009) 12.55
The roles of intracellular protein-degradation pathways in neurodegeneration. Nature (2006) 9.77
Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu Rev Biochem (2009) 8.83
One step at a time: endoplasmic reticulum-associated degradation. Nat Rev Mol Cell Biol (2008) 8.68
Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science (2002) 7.49
The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat Cell Biol (2001) 6.10
RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat Cell Biol (2008) 5.90
Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nat Rev Mol Cell Biol (2007) 5.79
Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. Cell (2006) 5.54
Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol (2009) 5.47
The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat Cell Biol (2001) 5.36
Biological and chemical approaches to diseases of proteostasis deficiency. Annu Rev Biochem (2009) 5.23
Enhancement of proteasome activity by a small-molecule inhibitor of USP14. Nature (2010) 5.08
Multiple associated proteins regulate proteasome structure and function. Mol Cell (2002) 4.97
Arsenic degrades PML or PML-RARalpha through a SUMO-triggered RNF4/ubiquitin-mediated pathway. Nat Cell Biol (2008) 4.68
The recognition component of the N-end rule pathway. EMBO J (1990) 4.55
Arsenic trioxide controls the fate of the PML-RARalpha oncoprotein by directly binding PML. Science (2010) 4.52
A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Cell (2006) 4.08
A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation. Genes Dev (2001) 3.82
Identification of aneuploidy-tolerating mutations. Cell (2010) 3.73
Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu. Proc Natl Acad Sci U S A (2002) 3.54
Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation. Cell (2006) 3.21
Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling. Curr Biol (2001) 3.21
Degradation-mediated protein quality control in the nucleus. Cell (2005) 3.10
CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70. Nature (2006) 2.90
Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities. Cell (2006) 2.87
Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways. EMBO J (2006) 2.58
Ubiquitin-dependent proteolytic control of SUMO conjugates. J Biol Chem (2007) 2.44
Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates. Mol Cell (2011) 2.36
The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation. J Biol Chem (2007) 2.14
Cdc48: a power machine in protein degradation. Trends Biochem Sci (2011) 2.08
Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1. Proc Natl Acad Sci U S A (2009) 2.05
The family of ubiquitin-conjugating enzymes (E2s): deciding between life and death of proteins. FASEB J (2009) 1.91
A proteasome for all occasions. FEBS Lett (2007) 1.84
Subcellular localization of proteasomes and their regulatory complexes in mammalian cells. Biochem J (2000) 1.80
Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase. Nature (2006) 1.78
Substrate binding site flexibility of the small heat shock protein molecular chaperones. Proc Natl Acad Sci U S A (2009) 1.78
PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone. Cell (2013) 1.76
Localization of the 26S proteasome during mitosis and meiosis in fission yeast. EMBO J (1998) 1.61
Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1. FEBS Lett (2008) 1.61
PML/RARA oxidation and arsenic binding initiate the antileukemia response of As2O3. Cancer Cell (2010) 1.60
Mechanism of ubiquitylation by dimeric RING ligase RNF4. Nat Struct Mol Biol (2011) 1.59
SUMO-targeted ubiquitin ligases. Biochim Biophys Acta (2013) 1.55
Comparative proteomic analysis identifies a role for SUMO in protein quality control. Sci Signal (2011) 1.54
Cooperation of molecular chaperones with the ubiquitin/proteasome system. Biochim Biophys Acta (2004) 1.53
Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins. Mol Biol Cell (2010) 1.53
BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP. Mol Biol Cell (2005) 1.52
Regulation of the cytoplasmic quality control protein degradation pathway by BAG2. J Biol Chem (2005) 1.46
Genetic analysis connects SLX5 and SLX8 to the SUMO pathway in Saccharomyces cerevisiae. Genetics (2005) 1.40
Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins. Nat Cell Biol (2011) 1.39
To be, or not to be--molecular chaperones in protein degradation. Cell Mol Life Sci (2007) 1.37
Transferring substrates to the 26S proteasome. Trends Biochem Sci (2003) 1.37
Fission yeast Rnf4 homologs are required for DNA repair. J Biol Chem (2007) 1.37
HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome. Curr Biol (2005) 1.33
Chaperone-assisted degradation: multiple paths to destruction. Biol Chem (2010) 1.32
Protein quality control and elimination of protein waste: the role of the ubiquitin-proteasome system. Biochim Biophys Acta (2013) 1.28
Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome. J Biol Chem (2002) 1.28
A nucleus-based quality control mechanism for cytosolic proteins. Mol Biol Cell (2010) 1.28
Intranuclear degradation of polyglutamine aggregates by the ubiquitin-proteasome system. J Biol Chem (2009) 1.26
Quality control of a transcriptional regulator by SUMO-targeted degradation. Mol Cell Biol (2009) 1.25
Interaction of the anaphase-promoting complex/cyclosome and proteasome protein complexes with multiubiquitin chain-binding proteins. J Biol Chem (2003) 1.20
Sorting out the trash: the spatial nature of eukaryotic protein quality control. Curr Opin Cell Biol (2014) 1.17
The cell biology of disease: Acute promyelocytic leukemia, arsenic, and PML bodies. J Cell Biol (2012) 1.17
Purification of the yeast Slx5-Slx8 protein complex and characterization of its DNA-binding activity. Nucleic Acids Res (2006) 1.17
Molecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradation. FEBS J (2012) 1.11
Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation: the N-terminal domail is important for oligomer assembly and the binding of unfolding proteins. J Biol Chem (2004) 1.11
The E3 ubiquitin ligase TEB4 mediates degradation of type 2 iodothyronine deiodinase. Mol Cell Biol (2009) 1.09
Molecular chaperone-like properties of an unfolded protein, alpha(s)-casein. J Biol Chem (1999) 1.09
Ubiquitin conjugation triggers misfolded protein sequestration into quality control foci when Hsp70 chaperone levels are limiting. Mol Biol Cell (2013) 1.07
The Type II Hsp40 Sis1 cooperates with Hsp70 and the E3 ligase Ubr1 to promote degradation of terminally misfolded cytosolic protein. PLoS One (2013) 1.06
Exposure of bipartite hydrophobic signal triggers nuclear quality control of Ndc10 at the endoplasmic reticulum/nuclear envelope. Mol Biol Cell (2011) 1.01
The ubiquitin ligase E6-AP is induced and recruited to aggresomes in response to proteasome inhibition and may be involved in the ubiquitination of Hsp70-bound misfolded proteins. J Biol Chem (2009) 1.00
Regulation of NF-kappaB activity and inducible nitric oxide synthase by regulatory particle non-ATPase subunit 13 (Rpn13). Proc Natl Acad Sci U S A (2010) 1.00
Arkadia, a novel SUMO-targeted ubiquitin ligase involved in PML degradation. Mol Cell Biol (2013) 0.99
BAG-1 haplo-insufficiency impairs lung tumorigenesis. BMC Cancer (2004) 0.99
The ubiquitin ligase Hul5 promotes proteasomal processivity. Mol Cell Biol (2009) 0.98
Hsp70 targets a cytoplasmic quality control substrate to the San1p ubiquitin ligase. J Biol Chem (2013) 0.98
The E3 ubiquitin ligase UBE3C enhances proteasome processivity by ubiquitinating partially proteolyzed substrates. J Biol Chem (2013) 0.93
Redox control of the ubiquitin-proteasome system: from molecular mechanisms to functional significance. Antioxid Redox Signal (2011) 0.93
Yeast deubiquitinase Ubp3 interacts with the 26 S proteasome to facilitate Rad4 degradation. J Biol Chem (2010) 0.92
Nuclear protein quality is regulated by the ubiquitin-proteasome system through the activity of Ubc4 and San1 in fission yeast. J Biol Chem (2011) 0.89
A chaperone-assisted degradation pathway targets kinetochore proteins to ensure genome stability. PLoS Genet (2014) 0.86
The Ubiquitin ligase Ubr11 is essential for oligopeptide utilization in the fission yeast Schizosaccharomyces pombe. Eukaryot Cell (2012) 0.83
The requirement for Cdc48/p97 in nuclear protein quality control degradation depends on the substrate and correlates with substrate insolubility. J Cell Sci (2014) 0.81
Means of self-preservation: how an intrinsically disordered ubiquitin-protein ligase averts self-destruction. Mol Biol Cell (2013) 0.80
The proteasome factor Bag101 binds to Rad22 and suppresses homologous recombination. Sci Rep (2013) 0.78
Misfolded proteins driven to destruction by Hul5. Nat Cell Biol (2011) 0.76