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EMBO reports, ISSN 1469-221X, 02/2009, Volume 10, Issue 2, pp. 173 - 179
Ubiquilins (UBQLNs) are adaptor proteins thought to deliver ubiquitinated substrates to proteasomes. Here, we show a role for UBQLN in autophagy: enforced... 
ubiquitin‐like | PLIC | autophagy | ubiquilin | autophagosomes | APOPTOSIS | ubiquitin-like | BIOCHEMISTRY & MOLECULAR BIOLOGY | MITOCHONDRIAL AUTOPHAGY | MITOPHAGY | DEATH | MATURATION | HUNTINGTIN | INCLUSION-BODY FORMATION | CELL BIOLOGY | PROTEASOME | DEGRADATION | PROMOTES | Ubiquitin-Activating Enzymes - physiology | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Ubiquitins - genetics | Humans | Adaptor Proteins, Vesicular Transport - genetics | Recombinant Fusion Proteins - physiology | Autophagy - physiology | Autophagy - drug effects | Microscopy, Immunoelectron | Cell Cycle Proteins - antagonists & inhibitors | Recombinant Fusion Proteins - antagonists & inhibitors | RNA Interference | Cell Cycle Proteins - genetics | Carrier Proteins - physiology | Protein Structure, Tertiary | Ubiquitin-Activating Enzymes - genetics | Adaptor Proteins, Vesicular Transport - physiology | Adaptor Proteins, Vesicular Transport - antagonists & inhibitors | Phagosomes - metabolism | Carrier Proteins - antagonists & inhibitors | RNA, Small Interfering - physiology | Microtubule-Associated Proteins - antagonists & inhibitors | Ubiquitins - physiology | HeLa Cells - drug effects | Microtubule-Associated Proteins - physiology | Protein Interaction Mapping | Carrier Proteins - genetics | Autophagy-Related Protein 7 | Animals | Autophagy-Related Protein 5 | Ubiquitin-Activating Enzymes - antagonists & inhibitors | Culture Media - pharmacology | Mice | HeLa Cells - cytology | Cell Cycle Proteins - physiology | Ubiquitins - antagonists & inhibitors | Proteins | Genetics | Nutrients | Molecular biology | Substrates | Index Medicus | Scientific Report
Journal Article
Nucleic Acids Research, ISSN 0305-1048, 2017, Volume 45, Issue 1, pp. 215 - 230
Replication across damaged DNA templates is accompanied by transient formation of sister chromatid junctions (SCJs). Cells lacking Esc2, an adaptor protein... 
STRUCTURE-SPECIFIC ENDONUCLEASE | STALLED REPLICATION | REPLICATION FORKS | BUDDING YEAST | SACCHAROMYCES-CEREVISIAE MUS81-MMS4 | BIOCHEMISTRY & MOLECULAR BIOLOGY | GENOME INTEGRITY | UBIQUITIN-LIKE MODIFIER | HOMOLOGOUS RECOMBINATION | STIMULATES FLAP ENDONUCLEASE-1 | HOLLIDAY JUNCTIONS | Genomic Instability | Endonucleases - genetics | DNA, Fungal - genetics | Saccharomyces cerevisiae - genetics | DNA, Cruciform - metabolism | Endonucleases - metabolism | Chromatids - metabolism | DNA-Binding Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Small Ubiquitin-Related Modifier Proteins - genetics | Cloning, Molecular | Escherichia coli - metabolism | Protein Domains | Nuclear Proteins - genetics | Gene Expression Regulation, Fungal | Recombinant Proteins - metabolism | Small Ubiquitin-Related Modifier Proteins - metabolism | Recombinant Proteins - chemistry | DNA Replication | Nuclear Proteins - metabolism | Recombinant Proteins - genetics | Chromatids - chemistry | Saccharomyces cerevisiae Proteins - genetics | DNA-Binding Proteins - genetics | Nuclear Proteins - chemistry | DNA-Binding Proteins - chemistry | Endonucleases - chemistry | Escherichia coli - genetics | Small Ubiquitin-Related Modifier Proteins - chemistry | DNA, Fungal - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | DNA Damage | DNA, Cruciform - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Index Medicus | Genome Integrity, Repair and
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 06/2017, Volume 292, Issue 24, pp. 10230 - 10238
Small ubiquitin-like modifier (SUMO) conjugation is a reversible post-translational modification process implicated in the regulation of gene transcription,... 
CONJUGATION | COMPLEX | TOPOISOMERASE-II | MITOTIC CHROMOSOMES | UBC9 | RECOGNITION | SUMO-INTERACTION MOTIFS | BIOCHEMISTRY & MOLECULAR BIOLOGY | BINDING SURFACE | SUMOYLATION | INSIGHTS | Xenopus Proteins - genetics | Ubiquitins - genetics | Humans | Ubiquitins - chemistry | Protein Inhibitors of Activated STAT - metabolism | Nitrogen Isotopes | Recombinant Fusion Proteins - metabolism | Xenopus Proteins - chemistry | Small Ubiquitin-Related Modifier Proteins - genetics | Gene Deletion | Protein Inhibitors of Activated STAT - genetics | Protein Interaction Domains and Motifs | Peptide Fragments - genetics | Ubiquitins - metabolism | Repressor Proteins - metabolism | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Repressor Proteins - chemistry | Mutagenesis, Site-Directed | Small Ubiquitin-Related Modifier Proteins - metabolism | Xenopus laevis | Models, Molecular | Recombinant Proteins - chemistry | Repressor Proteins - genetics | Recombinant Fusion Proteins - chemistry | Amino Acid Motifs | Peptide Fragments - chemistry | Animals | Small Ubiquitin-Related Modifier Proteins - chemistry | Protein Inhibitors of Activated STAT - chemistry | Hydrophobic and Hydrophilic Interactions | Sumoylation | Ligands | Xenopus Proteins - metabolism | Mutation | Index Medicus | Protein Structure and Folding | sumoylation | SUMO | PARP1 | TopoIIa | nuclear magnetic resonance (NMR) | SIM | PIASy | small ubiquitin-like modifier (SUMO) | SUMO-interacting motif (SIM)
Journal Article
eLife, ISSN 2050-084X, 11/2016, Volume 5, Issue 2016
Selective autophagy is mediated by cargo receptors that link the cargo to the isolation membrane via interactions with Atg8 proteins. Atg8 proteins are... 
MOLECULAR-DYNAMICS | ATG12-ATG5 CONJUGATE | SWISS-MODEL WORKSPACE | STRUCTURAL BASIS | MEMBRANE | IN-VIVO | BIOLOGY | SCAFFOLD PROTEIN | UBIQUITIN-LIKE PROTEINS | SACCHAROMYCES-CEREVISIAE | LIPIDATION | Saccharomyces cerevisiae - genetics | Vesicular Transport Proteins - metabolism | Humans | Transcription Factor TFIIIA - genetics | Autophagy-Related Protein 5 - chemistry | Autophagy-Related Protein 5 - genetics | Autophagy-Related Protein 8 Family - metabolism | Transcription Factor TFIIIA - metabolism | Autophagy-Related Proteins - chemistry | Saccharomyces cerevisiae - metabolism | Biological Transport | Cloning, Molecular | Escherichia coli - metabolism | Protein Interaction Domains and Motifs | Autophagy - genetics | Autophagy-Related Protein 8 Family - genetics | Nuclear Proteins - genetics | Autophagy-Related Proteins - genetics | Binding Sites | Sequestosome-1 Protein - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Autophagy-Related Protein 12 - genetics | Protein Structure, Secondary | Signal Transduction | Vesicular Transport Proteins - genetics | Gene Expression Regulation | Receptors, Cell Surface - metabolism | Recombinant Proteins - chemistry | Nuclear Proteins - metabolism | Receptors, Cytoplasmic and Nuclear - genetics | Recombinant Proteins - genetics | Autophagy-Related Protein 8 Family - chemistry | Saccharomyces cerevisiae Proteins - genetics | Autophagy-Related Protein 12 - metabolism | Sequestosome-1 Protein - genetics | Escherichia coli - genetics | Saccharomyces cerevisiae Proteins - metabolism | Autophagy-Related Protein 5 - metabolism | Protein Binding | Molecular Docking Simulation | HeLa Cells | Autophagy-Related Proteins - metabolism | Receptors, Cell Surface - genetics | Receptors, Cytoplasmic and Nuclear - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Observations | Autophagy (Cytology) | Ubiquitin | Proteins | Enzymes | Membranes | Peptides | Laboratories | Kinases | Autophagy | Phagocytosis | Binding sites | Recruitment | Index Medicus
Journal Article
2005, Methods in enzymology, ISBN 0121828042, Volume 399, xli, 907
Book
Methods in Enzymology, ISSN 0076-6879, 2017, Volume 587, pp. 377 - 390
Macroautophagy, hereafter autophagy, is a major degradation pathway in eukaryotic systems that allows the removal of large intracellular structures such as... 
Phosphatidylethanolamine | Atg8 lipidation | Isolation membrane | SUVs | GUVs | Reconstitution | Autophagy | Ubiquitin-like system | TARGET | GATE-16 | PROTEIN LIPIDATION | MEMBRANE-BINDING | BIOGENESIS | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | AUTOPHAGOSOME FORMATION | SELECTIVE AUTOPHAGY | LC3 | CELL BIOLOGY | Autophagy-Related Proteins - isolation & purification | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Autophagy-Related Protein 7 - metabolism | Multiprotein Complexes | Unilamellar Liposomes - chemistry | Green Fluorescent Proteins - genetics | Autophagy-Related Protein 8 Family - metabolism | Ubiquitin-Conjugating Enzymes - isolation & purification | Recombinant Proteins - isolation & purification | Autophagy-Related Protein 7 - isolation & purification | Saccharomyces cerevisiae Proteins - isolation & purification | Microtubule-Associated Proteins - isolation & purification | Autophagy-Related Protein 8 Family - genetics | Autophagy-Related Proteins - genetics | Recombinant Proteins - metabolism | Green Fluorescent Proteins - metabolism | Ubiquitin-Conjugating Enzymes - genetics | Recombinant Proteins - genetics | Autophagy-Related Protein 8 Family - chemistry | Saccharomyces cerevisiae Proteins - genetics | Autophagy-Related Protein 12 - metabolism | Autophagy-Related Protein 7 - genetics | Unilamellar Liposomes - metabolism | Ubiquitin-Conjugating Enzymes - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Autophagy-Related Protein 5 - metabolism | Luminescent Proteins - genetics | Phosphatidylethanolamines - metabolism | Autophagy-Related Proteins - metabolism | Luminescent Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Index Medicus
Journal Article
FEBS Letters, ISSN 0014-5793, 2005, Volume 579, Issue 22, pp. 5007 - 5012
Human Topors, which was originally identified as cellular binding partner of DNA topoisomerase I and of p53, has recently been shown to function as an... 
RING finger | E3 ligase | Topors | Small ubiquitin-like modifier | p53 | YFP | SUMO | UBC9 | HCMV | glutathione | GST | transferase | green fluorescent protein | human cytomegalovirus | PIAS | GFP | small ubiquitin-like modifier | yellow fluorescent protein | ubiquitin conjugating enzyme 9 | protein inhibitors of activated STAT | LOCALIZATION | COACTIVATOR | UBIQUITIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | BINDING-PROTEIN | TOPOISOMERASE-I | SUMOYLATION | CELL BIOLOGY | CONJUGATION | BIOPHYSICS | GENE-EXPRESSION | TUMOR-SUPPRESSOR | Humans | Neoplasm Proteins - metabolism | Recombinant Fusion Proteins - metabolism | Tumor Suppressor Protein p53 - genetics | DNA-Binding Proteins - metabolism | SUMO-1 Protein - genetics | Neoplasm Proteins - genetics | Nuclear Proteins - genetics | Zinc Fingers | DNA Topoisomerases, Type I - metabolism | DNA Topoisomerases, Type I - genetics | Tumor Suppressor Protein p53 - metabolism | Ubiquitin-Protein Ligases - metabolism | Nuclear Proteins - metabolism | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Transcription Factors - metabolism | Carrier Proteins - genetics | Carrier Proteins - metabolism | Protein Binding | Recombinant Fusion Proteins - genetics | SUMO-1 Protein - metabolism | HeLa Cells | In Vitro Techniques | Ubiquitin-Protein Ligases - genetics | Proteins | Sumo | Glutathione transferase | Ligases | DNA topoisomerase I | Fluorescence | Glutathione | Index Medicus
Journal Article
Oncogene, ISSN 0950-9232, 03/2013, Volume 32, Issue 13, pp. 1626 - 1637
Since the discovery of post-translational modification (PTM) by the small ubiquitin-related modifiers (SUMOs), a multitude of proteins have been described to... 
Phosphorylation | Transformation | SUMO | Oncoprotein | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTIONAL REPRESSION | E1B 55-KILODALTON PROTEIN | NUCLEAR EXPORT | transformation | UBIQUITIN-LIKE PROTEINS | REGION-1B 55-KDA ONCOPROTEIN | CELL BIOLOGY | CELL-TRANSFORMATION | ONCOLOGY | GENETICS & HEREDITY | TUMOR-SUPPRESSOR PROTEIN | INFECTED-CELLS | SUMO MODIFICATION | phosphorylation | E1B-55K ONCOPROTEIN | oncoprotein | Phosphorylation - physiology | Protein Kinases - metabolism | Humans | Protein Processing, Post-Translational - genetics | Molecular Sequence Data | Sumoylation - physiology | Phylogeny | Receptor Cross-Talk - physiology | Viral Proteins - metabolism | Tumor Suppressor Protein p53 - physiology | Phosphorylation - genetics | Cell Transformation, Neoplastic - genetics | HEK293 Cells | Viral Proteins - physiology | Adenoviridae - genetics | Animals, Newborn | Amino Acid Sequence | Sumoylation - genetics | Viral Proteins - chemistry | Cells, Cultured | Tumor Suppressor Protein p53 - metabolism | Rats | Viral Proteins - genetics | Nuclear Proteins - metabolism | Cell Transformation, Neoplastic - metabolism | Protein Processing, Post-Translational - physiology | Sequence Homology, Amino Acid | Adaptor Proteins, Signal Transducing - physiology | Animals | Models, Biological | Protein Kinases - physiology | Nuclear Proteins - physiology | Adenoviridae - metabolism | Adaptor Proteins, Signal Transducing - metabolism | Post-translational modification | Viral proteins | Adenovirus diseases | Physiological aspects | Genetic aspects | Research | Health aspects | Proteins | Enzymes | Oncology | Index Medicus
Journal Article
Structure, ISSN 0969-2126, 08/2016, Volume 24, Issue 8, pp. 1257 - 1270
Three receptors (Rpn1/S2/PSMD2, Rpn10/S5a, Rpn13/Adrm1) in the proteasome bind substrates by interacting with conjugated ubiquitin chains and/or shuttle... 
proteasome | Rpn13 | Dsk2 | ubiquitin | Rpn1 | Rad23 | GENETIC POLYMORPHISMS | DEUBIQUITINATING ENZYME UCH37 | BIOCHEMISTRY & MOLECULAR BIOLOGY | EXCISION-REPAIR PATHWAY | AMYLOID PRECURSOR PROTEIN | SACCHAROMYCES-CEREVISIAE | QUANTITATIVE-ANALYSIS | CELL BIOLOGY | UBA DOMAIN | 26 S PROTEASOME | BIOPHYSICS | UBIQUITIN-LIKE DOMAIN | AMPLIFICATION TARGET | Membrane Glycoproteins - metabolism | Ubiquitins - genetics | Humans | Membrane Glycoproteins - chemistry | Substrate Specificity | Crystallography, X-Ray | Ubiquitins - chemistry | Cell Cycle Proteins - chemistry | DNA-Binding Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Thermodynamics | Cell Cycle Proteins - genetics | Protein Interaction Domains and Motifs | Binding Sites | Ubiquitins - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Gene Expression | Cell Cycle Proteins - metabolism | Proteasome Endopeptidase Complex - chemistry | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | Molecular Dynamics Simulation | Saccharomyces cerevisiae - chemistry | Membrane Glycoproteins - genetics | Proteasome Endopeptidase Complex - genetics | Sequence Homology, Amino Acid | Sequence Alignment | Protein Conformation, beta-Strand | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Molecular Docking Simulation | Mutation | Proteasome Endopeptidase Complex - metabolism | Amino Acid Substitution | Saccharomyces cerevisiae Proteins - chemistry | Ubiquitin | Molecular biology | Amino acids | Index Medicus | Proteasome
Journal Article
Genes and Development, ISSN 0890-9369, 12/2001, Volume 15, Issue 23, pp. 3104 - 3117
Journal Article
Biochemical Journal, ISSN 0264-6021, 11/2012, Volume 448, Issue 1, pp. 55 - 65
The ubiquitin-proteasome system targets selected proteins for degradation by the 26S proteasome. Rpn12 is an essential component of the 19S regulatory particle... 
Ubiquitin | X-ray crystallography | PCI domain | Proteasome | REGULATORY PARTICLE | proteasome | FISSION YEAST | BIOCHEMISTRY & MOLECULAR BIOLOGY | UBIQUITIN RECEPTOR | 26S PROTEASOME | SACCHAROMYCES-CEREVISIAE | ubiquitin | DOMAIN PROTEIN | COP9 SIGNALOSOME | PCI COMPLEXES | BINDING | SUBUNIT | Microtubule-Associated Proteins - chemistry | Schizosaccharomyces pombe Proteins - chemistry | Ubiquitin - metabolism | Crystallography, X-Ray | Structure-Activity Relationship | Schizosaccharomyces - genetics | Schizosaccharomyces pombe Proteins - metabolism | Carrier Proteins - chemistry | Circular Dichroism | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Mutagenesis, Site-Directed | Schizosaccharomyces pombe Proteins - genetics | Models, Molecular | COP9 Signalosome Complex | Winged-Helix Transcription Factors - chemistry | Drosophila Proteins - chemistry | Protein Interaction Mapping | Schizosaccharomyces - metabolism | Peptide Fragments - chemistry | Animals | Carrier Proteins - metabolism | Arabidopsis Proteins - chemistry | Protein Binding | Protein Conformation | Proteasome Endopeptidase Complex - metabolism | Index Medicus | Pad1 N-terminal | cryo-EM, cryo-electron microscopy | WT, wild-type | ORF, open reading frame | RP, regulatory particle | WH, winged helix | CSN, COP9 signalosome | eIF3, eukaryotic initiation factor 3 | UBL, ubiquitin-like | TPR, tetratrico peptide repeat | vWA, von Willebrand factor A | HSQC, heteronuclear single-quantum coherence | ESRF, European Synchrotron Radiation Facility | MPN, Mpr1 | PCI, proteasome, COP9 signalosome, initiation factor 3 | rmsd, root mean square deviation | DUB, deubiquitylating enzyme | UIM, ubiquitin-interacting motif
Journal Article
The EMBO Journal, ISSN 0261-4189, 07/1999, Volume 18, Issue 14, pp. 3888 - 3896
Journal Article