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1. Full Text Tumour suppressor RNF43 is a stem-cell E3 ligase that induces endocytosis of Wnt receptors
by Koo, B.K and Spit, M and Jordens, I and Low, T.Y and Stange, D.E and van de Wetering, M and van Es, J.H and Mohammed, S and Heck, A.J.R and Maurice, M.M and Clevers, H
Nature, ISSN 0028-0836, 2012, Volume 488, Issue 7413, pp. 665 - 669
LGR5+ stem cells reside at crypt bottoms, intermingled with Paneth cells that provide Wnt, Notch and epidermal growth factor signals. Here we find that the... 
IN-VITRO | INHIBITION | MULTIDISCIPLINARY SCIENCES | TRANSCRIPTION | UBIQUITYLATION | SMALL-INTESTINE | COLON | BETA-CATENIN | LGR5 | CANCER | NEGATIVE REGULATOR | Oncogene Proteins - genetics | Receptors, Wnt - antagonists & inhibitors | Cell Proliferation | Receptors, G-Protein-Coupled - metabolism | Humans | Ubiquitin - metabolism | Paneth Cells - pathology | Stem Cells - cytology | Receptors, Wnt - metabolism | Stem Cells - metabolism | DNA-Binding Proteins - deficiency | Adenoma - metabolism | DNA-Binding Proteins - metabolism | Endocytosis | Ubiquitination | Lysosomes - metabolism | Stem Cells - enzymology | Tumor Suppressor Proteins - deficiency | Organoids - metabolism | Tumor Suppressor Proteins - genetics | HEK293 Cells | Colorectal Neoplasms - metabolism | Paneth Cells - metabolism | Tumor Suppressor Proteins - metabolism | Organoids - pathology | Oncogene Proteins - metabolism | Organoids - cytology | Ubiquitin-Protein Ligases - metabolism | Frizzled Receptors - metabolism | DNA-Binding Proteins - genetics | beta Catenin - metabolism | Animals | Wnt Signaling Pathway - drug effects | Adenoma - pathology | Ubiquitin-Protein Ligases - deficiency | Oncogene Proteins - deficiency | Mice | Receptors, G-Protein-Coupled - genetics | Colorectal Neoplasms - pathology | Ubiquitin-Protein Ligases - genetics | Ubiquitin | Colorectal cancer | Physiological aspects | Development and progression | Research | Gene expression | Risk factors | Proteins | Epidermal growth factor | Mutation | Kinases | Rodents | Stem cells | Index Medicus
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2. Full Text Structure of the DDB1-CRBN E3 ubiquitin ligase in complex with thalidomide
by Fischer, Eric S and Böhm, Kerstin and Lydeard, John R and Yang, Haidi and Stadler, Michael B and Cavadini, Simone and Nagel, Jane and Serluca, Fabrizio and Acker, Vincent and Lingaraju, Gondichatnahalli M and Tichkule, Ritesh B and Schebesta, Michael and Forrester, William C and Schirle, Markus and Hassiepen, Ulrich and Ottl, Johannes and Hild, Marc and Beckwith, Rohan E. J and Harper, J. Wade and Jenkins, Jeremy L and Thomä, Nicolas H
Nature, ISSN 0028-0836, 2014, Volume 512, Issue 1, pp. 49 - 53
In the 1950s, the drug thalidomide, administered as a sedative to pregnant women, led to the birth of thousands of children with multiple defects. Despite the... 
DNA-Binding Proteins - antagonists & inhibitors | Thalidomide - metabolism | Homeodomain Proteins - metabolism | Humans | Thalidomide - chemistry | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Substrate Specificity | Ubiquitin-Protein Ligases - antagonists & inhibitors | Crystallography, X-Ray | Structure-Activity Relationship | Ubiquitin-Protein Ligases - chemistry | DNA-Binding Proteins - chemistry | Peptide Hydrolases - chemistry | Multiprotein Complexes - antagonists & inhibitors | DNA-Binding Proteins - metabolism | Transcription Factors - metabolism | Multiprotein Complexes - metabolism | Thalidomide - analogs & derivatives | Multiprotein Complexes - chemistry | DNA-Binding Proteins - agonists | Protein Binding | Multiprotein Complexes - agonists | Peptide Hydrolases - metabolism | Protein research | Research | Properties | Ubiquitin-proteasome system | Ligases | Immunity | Proteins | Solvents | Transcription factors | Ligands | Mutation | Drug resistance | Pharmaceuticals | Index Medicus
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3. Full Text RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation
by Geoffroy, Marie-Claude and Hay, Ronald T and Hattersley, Neil and Jaffray, Ellis G and Palvimo, Jorma J and Shen, Linnan and Plechanovova, Anna and Tatham, Michael H
Nature Cell Biology, ISSN 1465-7392, 05/2008, Volume 10, Issue 5, pp. 538 - 546
In acute promyelocytic leukaemia (APL), the promyelocytic leukaemia (PML) protein is fused to the retinoic acid receptor a (RAR). This disease can be treated... 
COREGULATOR | APOPTOSIS | CELLS | NUCLEAR-BODIES | TRIOXIDE | SNURF RNF4 | DNA-REPAIR | PROTEINS | IDENTIFICATION | ACUTE PROMYELOCYTIC LEUKEMIA | CELL BIOLOGY | RNA, Small Interfering - genetics | Oncogene Proteins, Fusion - metabolism | Humans | Ubiquitin - metabolism | Molecular Sequence Data | Neoplasm Proteins - metabolism | Arsenic - metabolism | Leukemia, Promyelocytic, Acute - metabolism | SUMO-1 Protein - genetics | Tumor Suppressor Proteins - genetics | Neoplasm Proteins - genetics | Nuclear Proteins - genetics | Amino Acid Sequence | Cell Line | Tumor Suppressor Proteins - metabolism | Ubiquitin-Protein Ligases - metabolism | Rats | Nuclear Proteins - metabolism | Transcription Factors - genetics | Transcription Factors - metabolism | Sequence Alignment | Animals | Oncogene Proteins, Fusion - genetics | SUMO-1 Protein - metabolism | Leukemia, Promyelocytic, Acute - genetics | Proteasome Endopeptidase Complex - metabolism | Ubiquitin-Protein Ligases - genetics | Promyelocytic Leukemia Protein | RNA, Small Interfering - metabolism | Arsenic | Research | DNA binding proteins | Index Medicus
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4. Full Text Functional Targeting of DNA Damage to a Nuclear Pore-Associated SUMO-Dependent Ubiquitin Ligase
by Shigeki Nagai and Karine Dubrana and Monika Tsai-Pflugfelder and Marta B. Davidson and Tania M. Roberts and Grant W. Brown and Elisa Varela and Florence Hediger and Susan M. Gasser and Nevan J. Krogan
Science, ISSN 0036-8075, 10/2008, Volume 322, Issue 5901, pp. 597 - 602
Recent findings suggest important roles for nuclear organization in gene expression. In contrast, little is known about how nuclear organization contributes to... 
Yeasts | Medical research | Nuclear pore | DNA damage | Ubiquitins | DNA | Imaging | Genetic loci | Reports | DNA repair | Genetic mutation | ORGANIZATION | RECOMBINATION | REPAIR | REPLICATION | LIVING YEAST | MULTIDISCIPLINARY SCIENCES | DYNAMICS | DOUBLE-STRAND BREAKS | PROTEIN COMPLEXES | SACCHAROMYCES-CEREVISIAE | SUMOYLATION | Immunoprecipitation | DNA, Fungal - genetics | Saccharomyces cerevisiae - genetics | Intracellular Signaling Peptides and Proteins - metabolism | DNA Breaks, Double-Stranded | DNA-Binding Proteins - metabolism | Nuclear Pore Complex Proteins - genetics | Saccharomyces cerevisiae - metabolism | Chromatin Immunoprecipitation | Recombination, Genetic | Genes, Fungal | Protein-Serine-Threonine Kinases - metabolism | Zinc Fingers | Nuclear Pore Complex Proteins - metabolism | Small Ubiquitin-Related Modifier Proteins - metabolism | Ubiquitin-Protein Ligases - metabolism | Saccharomyces cerevisiae Proteins - genetics | DNA-Binding Proteins - genetics | Nuclear Pore - metabolism | Gene Conversion | Deoxyribonucleases, Type II Site-Specific - metabolism | DNA Repair | DNA, Fungal - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Kinetics | Physiological aspects | Cellular proteins | Genetic aspects | Research | Ligases | Biomedical research | Yeast | Gene expression | Genomics | Index Medicus
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5. Full Text Immunomodulatory agents lenalidomide and pomalidomide co-stimulate T cells by inducing degradation of T cell repressors Ikaros and Aiolos via modulation of the E3 ubiquitin ligase complex CRL4(CRBN)
by Gandhi, AK and Kang, J and Havens, CG and Conklin, T and Ning, YH and Wu, L and Ito, T and Ando, H and Waldman, MF and Thakurta, A and Klippel, A and Handa, H and Daniel, TO and Schafer, PH and Chopra, R
BRITISH JOURNAL OF HAEMATOLOGY, ISSN 0007-1048, 03/2014, Volume 164, Issue 6, pp. 811 - 821
Cereblon (CRBN), the molecular target of lenalidomide and pomalidomide, is a substrate receptor of the cullin ring E3 ubiquitin ligase complex, CRL4(CRBN). T... 
TARGET | ACTIVATION | ISOFORMS | DNA-BINDING PROTEINS | IDENTIFICATION | pomalidomide | Aiolos | Ikaros | Cereblon | lenalidomide | INHIBITORS | HEMATOLOGY | EXPRESSION | Peptide Hydrolases - genetics | Humans | Ubiquitin-Protein Ligases - metabolism | Angiogenesis Inhibitors - pharmacology | Thalidomide - pharmacology | Transcription Factors - genetics | Ikaros Transcription Factor - genetics | Proteasome Endopeptidase Complex - genetics | Transcription Factors - metabolism | Thalidomide - analogs & derivatives | Ubiquitination | Transfection | T-Lymphocytes - metabolism | T-Lymphocytes - drug effects | Ikaros Transcription Factor - metabolism | Proteasome Endopeptidase Complex - metabolism | Ubiquitin-Protein Ligases - genetics | Immunologic Factors - pharmacology | Peptide Hydrolases - metabolism | Index Medicus
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6. Full Text Human BRCA1-BARD1 ubiquitin ligase activity counteracts chromatin barriers to DNA resection
by Densham, Ruth M and Garvin, Alexander J and Stone, Helen R and Strachan, Joanna and Baldock, Robert A and Daza-Martin, Manuel and Fletcher, Alice and Blair-Reid, Sarah and Beesley, James and Johal, Balraj and Pearl, Laurence H and Neely, Robert and Keep, Nicholas H and Watts, Felicity Z and Morris, Joanna R
Nature Structural and Molecular Biology, ISSN 1545-9993, 07/2016, Volume 23, Issue 7, pp. 647 - 655
The opposing activities of 53BP1 and BRCA1 influence pathway choice in DNA double-strand-break repair. How BRCA1 counteracts the inhibitory effect of 53BP1 on... 
STRAND BREAK REPAIR | RING-RING COMPLEX | TUMOR SUPPRESSION | BIOCHEMISTRY & MOLECULAR BIOLOGY | REPAIR PATHWAY CHOICE | BRCA1 | REMODELING ENZYME | CELL BIOLOGY | E3 LIGASE | BIOPHYSICS | END RESECTION | HOMOLOGOUS RECOMBINATION | FUN30 | Chromatin - metabolism | DNA, Neoplasm - metabolism | Humans | Gene Expression Regulation, Neoplastic | Ubiquitin - metabolism | DNA Breaks, Double-Stranded | Ubiquitination - drug effects | BRCA1 Protein - metabolism | Tumor Suppressor Proteins - genetics | Cloning, Molecular | Escherichia coli - metabolism | Binding Sites | Chromatin - drug effects | DNA Helicases - genetics | Chromatin - chemistry | Tumor Suppressor p53-Binding Protein 1 - metabolism | Recombinant Proteins - metabolism | Gene Expression | Recombinational DNA Repair | Tumor Suppressor Proteins - metabolism | Tumor Suppressor p53-Binding Protein 1 - genetics | Signal Transduction | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Recombinant Proteins - genetics | Ubiquitin - genetics | Piperazines - pharmacology | DNA Cleavage - drug effects | BRCA1 Protein - genetics | DNA Helicases - metabolism | Phthalazines - pharmacology | Histones - genetics | Escherichia coli - genetics | Protein Binding | DNA, Neoplasm - genetics | HeLa Cells | Histones - metabolism | Ubiquitin-Protein Ligases - genetics | Camptothecin - pharmacology | Breast cancer | BRCA mutations | DNA repair | Analysis | Risk factors | Enzymes | Protein expression | Chromatin | DNA damage | Index Medicus
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7. Full Text Ubiquitin Ligase Nedd4L Targets Activated Smad2/3 to Limit TGF-β Signaling
by Gao, Sheng and Alarcón, Claudio and Sapkota, Gopal and Rahman, Sadia and Chen, Pan-Yu and Goerner, Nina and Macias, Maria J and Erdjument-Bromage, Hediye and Tempst, Paul and Massagué, Joan
Molecular Cell, ISSN 1097-2765, 11/2009, Volume 36, Issue 3, pp. 457 - 468
TGF-β induces phosphorylation of the transcription factors Smad2 and Smad3 at the C terminus as well as at an interdomain linker region. TGF-β-induced linker... 
PROTEINS | DNA | SIGNALING | PATHWAYS | BMP | MECHANISM | STRUCTURAL BASIS | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | RECEPTOR | DEGRADATION | SUPERFAMILY | FAMILY | CELL BIOLOGY | Embryonic Stem Cells - metabolism | Embryonic Stem Cells - cytology | Humans | Endosomal Sorting Complexes Required for Transport - genetics | Molecular Sequence Data | Immunoblotting | Smad3 Protein - metabolism | Immediate-Early Proteins - metabolism | Smad3 Protein - genetics | RNA Interference | Smad2 Protein - genetics | Nedd4 Ubiquitin Protein Ligases | Phosphorylation - drug effects | Protein-Serine-Threonine Kinases - metabolism | Polyubiquitin - metabolism | Amino Acid Sequence | Cell Line | Signal Transduction | Cells, Cultured | Endosomal Sorting Complexes Required for Transport - metabolism | Protein-Serine-Threonine Kinases - genetics | Smad2 Protein - metabolism | Ubiquitin-Protein Ligases - metabolism | Sequence Homology, Amino Acid | Transforming Growth Factor beta - pharmacology | Animals | Immediate-Early Proteins - genetics | Embryonic Stem Cells - drug effects | Protein Binding | Mice | HeLa Cells | Ubiquitin-Protein Ligases - genetics | Index Medicus
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8. Full Text The ubiquitin ligase Mul1 induces mitophagy in skeletal muscle in response to muscle-wasting stimuli
by Lokireddy, Sudarsanareddy and Wijesoma, Isuru W and Teng, Serena and Bonala, Sabeera and Gluckman, Peter D and McFarlane, Craig and Sharma, Mridula and Kambadur, Ravi
Cell Metabolism, ISSN 1550-4131, 11/2012, Volume 16, Issue 5, pp. 613 - 624
Recent research reveals that dysfunction and subsequent loss of mitochondria (mitophagy) is a potent inducer of skeletal muscle wasting. However, the molecular... 
MITOCHONDRIAL FUSION | CANCER CACHEXIA | MECHANISM | ATROPHY | PATHWAY | SARCOMERIC PROTEINS | MYOSTATIN | ENDOCRINOLOGY & METABOLISM | DEGRADATION | AUTOPHAGY | CELL BIOLOGY | Cell Line | Up-Regulation | DNA, Mitochondrial - metabolism | Muscular Atrophy - metabolism | DNA, Mitochondrial - drug effects | Muscular Atrophy - pathology | Ubiquitin-Protein Ligases - metabolism | Mitochondria - metabolism | Membrane Potential, Mitochondrial - drug effects | Myoblasts - metabolism | Myostatin - pharmacology | Ubiquitination | Animals | Dexamethasone - pharmacology | GTP Phosphohydrolases - metabolism | Signal Transduction - drug effects | Forkhead Transcription Factors - metabolism | Mitochondrial Degradation - drug effects | Mitochondrial Proteins - metabolism | Glucocorticoids - pharmacology | Mice | Ubiquitin | Muscles | Medical colleges | Mitochondrial DNA | Ligases | Index Medicus
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9. Full Text Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
by Plechanovov, Anna and Jaffray, Ellis G and Tatham, Michael H and Naismith, James H and Hay, Ronald T
Nature, ISSN 0028-0836, 09/2012, Volume 489, Issue 7414, pp. 115 - 120
Ubiquitin modification is mediated by a large family of specificity determining ubiquitin E3 ligases. To facilitate ubiquitin transfer, RING E3 ligases bind... 
COMPLEX | MECHANISM | DETERMINANTS | PATHWAY | MULTIDISCIPLINARY SCIENCES | DNA-DAMAGE | UBIQUITYLATION | DEGRADATION | RNF4 | BINDING | INSIGHTS | Transcription Factors - chemistry | Humans | Ubiquitin - metabolism | Crystallography, X-Ray | Ubiquitin-Conjugating Enzymes - chemistry | Multiprotein Complexes - metabolism | Ubiquitination | Nuclear Proteins - genetics | Protein Structure, Tertiary | Catalytic Domain | Zinc Fingers | Biocatalysis | Ubiquitin - chemistry | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Rats | Nuclear Proteins - metabolism | Ubiquitin-Conjugating Enzymes - genetics | Ubiquitin - genetics | Transcription Factors - genetics | Nuclear Proteins - chemistry | Ubiquitin-Protein Ligases - chemistry | Hydrolysis | Transcription Factors - metabolism | Multiprotein Complexes - chemistry | Animals | Ubiquitin-Conjugating Enzymes - metabolism | Protein Binding | Mutation | Proteins | Enzymes | Index Medicus
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10. Full Text The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
by Lazarou, Michael and Sliter, Danielle A and Kane, Lesley A and Sarraf, Shireen A and Wang, Chunxin and Burman, Jonathon L and Sideris, Dionisia P and Fogel, Adam I and Youle, Richard J
Nature, ISSN 0028-0836, 08/2015, Volume 524, Issue 7565, pp. 309 - 314
Protein aggregates and damaged organelles are tagged with ubiquitin chains to trigger selective autophagy. To initiate mitophagy, the ubiquitin kinase PINK1... 
ACTIVATE PARKIN | OPEN-ANGLE GLAUCOMA | COMPLEX | PARKIN-MEDIATED MITOPHAGY | PHOSPHORYLATION | MULTIDISCIPLINARY SCIENCES | P62/SQSTM1 | DEPOLARIZED MITOCHONDRIA | OPTINEURIN | SELECTIVE AUTOPHAGY | BINDING | Protein Kinases - metabolism | Autophagy-Related Proteins | Phosphorylation | Signal Transduction | Microtubule-Associated Proteins - metabolism | Humans | Ubiquitin - metabolism | Ubiquitin-Protein Ligases - metabolism | Nuclear Proteins - metabolism | Autophagy - physiology | Intracellular Signaling Peptides and Proteins - metabolism | Mitochondria - metabolism | Mitochondrial Degradation - physiology | Transcription Factor TFIIIA - metabolism | Autophagy-Related Protein-1 Homolog | Carrier Proteins - metabolism | Mitochondrial Proteins - metabolism | Models, Biological | Membrane Proteins - metabolism | HeLa Cells | Protein-Serine-Threonine Kinases - metabolism | Ubiquitin | Mitochondrial DNA | Research | Ligases | Membrane proteins | Mitochondria | Mutation | Kinases | Autophagy | Index Medicus
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11. Full Text Orchestration of the DNA-Damage Response by the Rnf8 Ubiquitin Ligase
by Nadine K. Kolas and J. Ross Chapman and Shinichiro Nakada and Jarkko Ylanko and Richard Chahwan and Frédéric D. Sweeney and Stephanie Panier and Megan Mendez and Jan Wildenhain and Timothy M. Thomson and Laurence Pelletier and Stephen P. Jackson and Daniel Durocher
Science, ISSN 0036-8075, 12/2007, Volume 318, Issue 5856, pp. 1637 - 1640
Cells respond to DNA double-strand breaks by recruiting factors such as the DNA-damage mediator protein MDC1, the p53-binding protein 1 (53BP1), and the breast... 
Phosphorylation | Ubiquitins | DNA damage | DNA | Cell lines | HeLa cells | Small interfering RNA | Antibodies | Irradiation | Reports | Mice | MDC1 | RECOGNITION | 53BP1 | MULTIDISCIPLINARY SCIENCES | DOUBLE-STRAND BREAKS | NUCLEAR FOCI | HISTONE H2AX | ATM | CHECKPOINT | BRCA1 | CELLULAR-RESPONSE | Humans | Ubiquitin - metabolism | Molecular Sequence Data | Intracellular Signaling Peptides and Proteins - metabolism | Trans-Activators - chemistry | DNA Breaks, Double-Stranded | DNA-Binding Proteins - metabolism | Ubiquitination | BRCA1 Protein - metabolism | Protein-Serine-Threonine Kinases - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Tumor Suppressor Proteins - metabolism | Cell Nucleus Structures - genetics | Cell Cycle Proteins - metabolism | Ubiquitin-Protein Ligases - metabolism | Nuclear Proteins - metabolism | Ataxia Telangiectasia Mutated Proteins | Nuclear Proteins - chemistry | DNA-Binding Proteins - chemistry | Amino Acid Motifs | Ubiquitin-Conjugating Enzymes - metabolism | DNA Repair | Cell Line, Tumor | Trans-Activators - metabolism | RNA, Small Interfering | HeLa Cells | Tumor Suppressor p53-Binding Protein 1 | Ubiquitin | Physiological aspects | Genetic aspects | Proteins | Enzymes | Cellular biology | Deoxyribonucleic acid | Breast cancer | Mutation | Kinases | Index Medicus
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