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61. Full Text Direct activation of protein kinases by unanchored polyubiquitin chains
by Xia, Zong-Ping and Sun, Lijun and Chen, Xiang and Pineda, Gabriel and Jiang, Xiaomo and Adhikari, Anirban and Zeng, Wenwen and Chen, Zhijian J
Nature, ISSN 0028-0836, 09/2009, Volume 461, Issue 7260, pp. 114 - 119
TRAF6 is a ubiquitin ligase that is essential for the activation of NF-kappa B and MAP kinases in several signalling pathways, including those emanating from... 
LYS63-LINKED POLYUBIQUITINATION | UBIQUITIN-CONJUGATING ENZYME | TAK1 | IL-1 | TRAF6 | MULTIDISCIPLINARY SCIENCES | IKK | NF-KAPPA-B | BINDING | NEMO | AUTOUBIQUITINATION | Polyubiquitin - metabolism | Cell Line | DEAD Box Protein 58 | Interleukin-1beta - pharmacology | Phosphorylation | Tumor Suppressor Proteins - metabolism | Deubiquitinating Enzyme CYLD | Polyubiquitin - biosynthesis | Humans | MAP Kinase Kinase Kinases - metabolism | Enzyme Activation - drug effects | Ubiquitination | I-kappa B Kinase - metabolism | TNF Receptor-Associated Factor 6 - metabolism | Lysine - metabolism | HeLa Cells | Ubiquitin-Conjugating Enzymes | Adaptor Proteins, Signal Transducing - metabolism | DEAD-box RNA Helicases - metabolism | Ubiquitin | Physiological aspects | Genetic aspects | Research | Protein kinases | Proteins | Enzymes | Kinases | Cells
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62. Full Text Regulation of NF-κB by ubiquitination
by Chen, Jueqi and Chen, Zhijian J
Current Opinion in Immunology, ISSN 0952-7915, 2013, Volume 25, Issue 1, pp. 4 - 12
Highlights ► Polyubiquitination activates TAK1 and IKK through proteasome-independent mechanisms. ► Unanchored ubiquitin chains have signaling functions in... 
Allergy and Immunology | ACTIVATION | UNANCHORED POLYUBIQUITIN CHAINS | LINEAR POLYUBIQUITIN | RIG-I | ZINC-FINGER 7 | TNF-ALPHA | IMMUNOLOGY | NEMO | BINDING | EDITING ENZYME A20 | LIGASE | Signal Transduction - immunology | Ubiquitination | Animals | Ubiquitins - immunology | Gene Expression Regulation - immunology | Humans | Protein Binding | NF-kappa B - metabolism | Structure-Activity Relationship | Transcriptional Activation - immunology
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63. Full Text Parkin overexpression during aging reduces proteotoxicity, alters mitochondrial dynamics, and extends lifespan
by Anil Rana and Michael Rera and David W. Walker
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 5/2013, Volume 110, Issue 21, pp. 8638 - 8643
Aberrant protein aggregation and mitochondrial dysfunction have each been linked to aging and a number of age-onset neurodegenerative disorders, including... 
Aggregation | Brain | Mitochondria | Quantification | Neurodegenerative diseases | Neurons | Drosophila | Parkinson disease | Longevity | Adulthood | Neuronal aging | Energy metabolism | Healthspan | Proteostasis | Mitophagy | neuronal aging | UBIQUITIN-PROTEASOME SYSTEM | MULTIDISCIPLINARY SCIENCES | MUSCLE | QUALITY-CONTROL | healthspan | proteostasis | DROSOPHILA PGC-1 HOMOLOG | mitophagy | PINK1 | MITOFUSIN | DISEASE | STRESS | EXPRESSION | energy metabolism | Polyubiquitin - metabolism | Membrane Proteins - genetics | Gene Expression Regulation - physiology | Neurodegenerative Diseases - genetics | Neurons - cytology | Mitochondria - metabolism | Neurodegenerative Diseases - metabolism | Drosophila Proteins - metabolism | Ubiquitin-Protein Ligases - biosynthesis | Polyubiquitin - genetics | Drosophila Proteins - biosynthesis | Organ Specificity - genetics | Animals | Mitochondria - genetics | Membrane Proteins - metabolism | Neurons - metabolism | Drosophila Proteins - genetics | Ubiquitin-Protein Ligases - genetics | Drosophila melanogaster | Longevity - physiology | Life spans (Biology) | Ubiquitin | Aging | Physiological aspects | Genetic aspects | Mitochondrial DNA | Ubiquitin-proteasome system | Life Sciences | Biological Sciences
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64. Full Text Insights into the Molecular Composition of Endogenous Unanchored Polyubiquitin Chains
by Strachan, Joanna and Roach, Lucy and Sokratous, Kleitos and Tooth, David and Long, Jed and Garner, Thomas P and Searle, Mark S and Oldham, Neil J and Layfield, Robert
Journal of Proteome Research, ISSN 1535-3893, 03/2012, Volume 11, Issue 3, pp. 1969 - 1980
The diverse influences of ubiquitin, mediated by its post-translational covalent modification of other proteins, have been extensively investigated. However,... 
unanchored polyubiquitin | ZNF216 | top-down mass spectrometry | ubiquitin | UBIQUITIN-BINDING DOMAINS | QUANTIFICATION | BIOCHEMICAL RESEARCH METHODS | QUANTITATIVE-ANALYSIS | MASS-SPECTROMETRY | 26 S PROTEASOME | PATHWAY | IN-VIVO | DEGRADATION | PROTEINS | REVEALS | Polyubiquitin - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Ubiquitinated Proteins - chemistry | Polyubiquitin - isolation & purification | Immobilized Proteins - chemistry | Peptide Fragments - isolation & purification | Humans | Rats | Male | Muscle, Skeletal - metabolism | DNA-Binding Proteins - chemistry | Ubiquitinated Proteins - isolation & purification | Tandem Mass Spectrometry | Peptide Fragments - chemistry | Animals | Protein Binding | Ubiquitinated Proteins - metabolism | Chromatography, Affinity - methods | Polyubiquitin - chemistry
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65. Full Text Innate immune signaling in Drosophila is regulated by transforming growth factor β (TGFβ)-activated kinase (Tak1)-triggered ubiquitin editing
by Chen, Li and Paquette, Nicholas and Mamoor, Shahan and Rus, Florentina and Nandy, Anubhab and Leszyk, John and Shaffer, Scott A and Silverman, Neal
Journal of Biological Chemistry, ISSN 0021-9258, 05/2017, Volume 292, Issue 21, pp. 8738 - 8749
Coordinated regulation of innate immune responses is necessary in all metazoans. In Drosophila the Imd pathway detects Gram-negative bacterial infections... 
Imd | ACTIVATION | Drosophila | BIOCHEMISTRY & MOLECULAR BIOLOGY | NF-B (NF-B) | ubiquitin editing | PGRP-LC | ubiquitylation (ubiquitination) | IMD-PATHWAY | PEPTIDOGLYCAN | Tak1 | CONJUGATING ENZYMES | POLYUBIQUITIN CHAINS | phosphorylation | NF-KAPPA-B | BINDING | antimicrobial peptide (AMP) | mass spectrometry (MS) | Inhibitor of Apoptosis Proteins - genetics | MAP Kinase Kinase Kinases - genetics | Ubiquitin-Conjugating Enzymes - genetics | Signal Transduction - genetics | Ubiquitination - immunology | Drosophila Proteins - immunology | Transcription Factors - genetics | Immunity, Innate | MAP Kinase Kinase Kinases - immunology | Polyubiquitin - genetics | Signal Transduction - immunology | Animals | Polyubiquitin - immunology | Inhibitor of Apoptosis Proteins - immunology | Drosophila Proteins - genetics | Ubiquitin-Conjugating Enzymes - immunology | Transcription Factors - immunology | Drosophila melanogaster | Ubiquitination - genetics | Signal Transduction | NF-κB (NF-κB)
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66. Full Text Isolation and initial characterization of GW5, a major QTL associated with rice grain width and weight
by Jianfeng Weng Suhai Gu Xiangyuan Wan He Gao Tao Guo Ning Su Cailin Lei Xin Zhang Zhijun Cheng Xiuping Guo Jiulin Wang Ling Jiang Huqu Zhai Jianmin Wan
细胞研究：英文版, ISSN 1001-0602, 2008, Volume 18, Issue 12, pp. 1199 - 1209
Grain weight is a major determinant of crop grain yield and is controlled by naturally occurring quantitative trait loci （QTLs）. We earlier identified a major... 
籼型非巨品系 | QTL | 胚重 | 籼型巨胚稻品系 | GW5 | 细胞 | Domestication | Rice (Oryza sativa L.) | Polyubiquitin | Grain width and weight | ENCODES | TOMATO FRUIT | grain width and weight | SIZE | polyubiquitin | CELL BIOLOGY | ORYZA-SATIVA L | rice (Oryza sativa L.) | EVOLUTION | DWARF MUTANT | GENE | domestication | SEED | QUALITY TRAITS | Polyubiquitin - metabolism | Oryza - growth & development | Oryza - genetics | Genes, Plant | Gene Deletion | Chromosome Mapping | Chromosomes, Plant - metabolism | Quantitative Trait Loci
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67. Full Text A single MIU motif of MINDY‐1 recognizes K48‐linked polyubiquitin chains
by Kristariyanto, Yosua Adi and Abdul Rehman, Syed Arif and Weidlich, Simone and Knebel, Axel and Kulathu, Yogesh
EMBO reports, ISSN 1469-221X, 03/2017, Volume 18, Issue 3, pp. 392 - 402
The eight different types of ubiquitin (Ub) chains that can be formed play important roles in diverse cellular processes. Linkage‐selective recognition of Ub... 
ubiquitin binding domain | motif interacting with ubiquitin | polyubiquitin | MINDY deubiquitinase | ubiquitin signaling | RABEX-5 | PROTEIN-TURNOVER | UBIQUITIN-BINDING DOMAINS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | DISTINCT | MODEL | CELL BIOLOGY | STRUCTURAL BASIS | TANDEM UIMS | LYS48-LINKED TETRAUBIQUITIN | REVEALS | Polyubiquitin - metabolism | Amino Acid Sequence | Models, Molecular | Tandem Repeat Sequences | Amino Acid Motifs | Ubiquitination | Models, Biological | Conserved Sequence | Protein Binding | Ubiquitin Thiolesterase - metabolism | Protein Conformation | Protein Interaction Domains and Motifs | Polyubiquitin - chemistry | Ubiquitin Thiolesterase - chemistry | Enzymes | Cellular biology | Binding sites | Crystal structure | Signal Transduction | Post-translational Modifications, Proteolysis & Proteomics | Structural Biology | Scientific Report
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68. Full Text Assembly and structure of Lys33-linked polyubiquitin reveals distinct conformations
by Kristariyanto, Yosua Adi and Choi, Soo-Youn and Rehman, Syed Arif Abdul and Ritorto, Maria Stella and Campbell, David G and Morrice, Nicholas A and Toth, Rachel and Kulathu, Yogesh
The Biochemical journal, ISSN 0264-6021, 04/2015, Volume 467, Issue 2, pp. 345 - 352
Ubiquitylation regulates a multitude of biological processes and this versatility stems from the ability of ubiquitin (Ub) to form topologically different... 
Polyubiquitin - metabolism | Protein Structure, Tertiary | Humans | Ubiquitin-Protein Ligases - metabolism | Ubiquitin-Protein Ligases - chemistry | Polyubiquitin - genetics | Protein Folding | Lysine - genetics | Animals | Protein Structure, Quaternary | Lysine - metabolism | Lysine - chemistry | Ubiquitin-Protein Ligases - genetics | Polyubiquitin - chemistry | PTM, post-translational modification | Crn7, coronin-7 | RBR, RING-between-RING | RING, really interesting new gene | HECT, homologous to the E6–AP C-terminus | Accelerated Publication | polyubiquitin | ubiquitin linkage | deubiquitinase | DUB, deubiquitinase | pRM, parallel reaction monitoring | homologous to the E6–AP C-terminus (HECT) E3 ligase | Ub, ubiquitin | ASU, asymmetric unit | UBD, ubiquitin-binding domain | AREL1, apoptosis-resistant E3 ubiquitin protein ligase 1 | TCR, T-cell antigen receptor
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69. Full Text Ubiquitin-Induced Oligomerization of the RNA Sensors RIG-I and MDA5 Activates Antiviral Innate Immune Response
by Jiang, Xiaomo and Kinch, Lisa N and Brautigam, Chad A and Chen, Xiang and Chen, Zhijian J and Du, Fenghe and Grishin, Nick V
Immunity, ISSN 1074-7613, 06/2012, Volume 36, Issue 6, pp. 959 - 973
RIG-I and MDA5 detect viral RNA in the cytoplasm and activate signaling cascades leading to the production of type-I interferons. RIG-I is activated through... 
DOUBLE-STRANDED-RNA | UNANCHORED POLYUBIQUITIN CHAINS | RECOGNITION | PATHWAY | COMPLEXES | IMMUNOLOGY | RECEPTORS | BINDING | REVEALS | Encephalomyocarditis virus - genetics | Humans | Multiprotein Complexes | Recombinant Fusion Proteins - physiology | Structure-Activity Relationship | Interferon-Induced Helicase, IFIH1 | DEAD-box RNA Helicases - physiology | Ubiquitination | Interferon-beta - genetics | RNA, Viral - metabolism | DEAD-box RNA Helicases - chemistry | Encephalomyocarditis virus - physiology | Fibroblasts - metabolism | Fibroblasts - virology | Polyubiquitin - metabolism | Protein Structure, Tertiary | DEAD Box Protein 58 | Mutagenesis, Site-Directed | Interferon-beta - biosynthesis | Recombinant Fusion Proteins - chemistry | HEK293 Cells - virology | Protein Interaction Mapping | DEAD-box RNA Helicases - genetics | Animals | Cell-Free System | Interferon Regulatory Factor-3 - metabolism | Protein Binding | Signal Transduction - physiology | Mice | Protein Processing, Post-Translational | HEK293 Cells - metabolism | Oligomers | Ubiquitin | Sensors | RNA | Lysine | Proteins | Experiments | Immune system
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70. Full Text Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains
by Licchesi, Julien D F and Wilkinson, Keith D and Odenwaelder, Peter and Barford, David and Reyes-Turcu, Francisca and Komander, David
EMBO reports, ISSN 1469-221X, 05/2009, Volume 10, Issue 5, pp. 466 - 473
At least eight types of ubiquitin chain exist, and individual linkages affect distinct cellular processes. The only distinguishing feature of differently... 
TAK1/IKK/NEMO/NF‐κB | ubiquitin binding domain | NF‐κB signalling | ubiquitin linkage | deubiquitinase | ACTIVATION | DOMAIN | NF-kappa B signalling | RECOGNITION | SPECIFICITY | TAK1/IKK/NEMO/NF-kappa B | BIOCHEMISTRY & MOLECULAR BIOLOGY | SIGNALS | IKK | CELL BIOLOGY | UBIQUITIN CHAINS | NF-KAPPA-B | BINDING | NEMO | DNA-Binding Proteins - metabolism | Polyubiquitin - metabolism | Protein Structure, Tertiary | Endopeptidases - metabolism | Endopeptidases - chemistry | Protein Structure, Secondary | Models, Molecular | Protein Binding | Crystallography, X-Ray | Lysine - chemistry | DNA-Binding Proteins - chemistry | Polyubiquitin - chemistry | Proteins | Signal transduction | Cellular biology | Molecular biology | Binding sites | NF-κB | TAK1 | NF-κB signalling | Scientific Report
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71. Full Text USP38 Inhibits Type I Interferon Signaling by Editing TBK1 Ubiquitination through NLRP4 Signalosome
by Lin, Meng and Zhao, Zhiyao and Yang, Zhifen and Meng, Qingcai and Tan, Peng and Xie, Weihong and Qin, Yunfei and Wang, Rong-Fu and Cui, Jun
Molecular Cell, ISSN 1097-2765, 10/2016, Volume 64, Issue 2, pp. 267 - 281
TBK1 is a component of the type I interferon (IFN) signaling pathway, yet the mechanisms controlling its activity and degradation remain poorly understood.... 
TBK1 ubiquitination | K33 ubiquitination | USP38 deubiquitination | innate immune signaling | type I interferon response | TBK1 degradation | ANTIVIRAL RESPONSE | IMMUNITY | ACTIVATION | IFN-BETA PRODUCTION | RECOGNITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | CYTOSOLIC DNA | SENSOR | DEGRADATION | BINDING KINASE 1 | NF-KAPPA-B | CELL BIOLOGY | Phosphorylation | Ubiquitin-Specific Proteases - genetics | Vesiculovirus - immunology | Intracellular Signaling Peptides and Proteins - immunology | Intracellular Signaling Peptides and Proteins - metabolism | Interferon Type I - immunology | Polyubiquitin - genetics | DNA-Binding Proteins - metabolism | Bone Marrow Cells - virology | Signal Transduction - immunology | Ubiquitination | Macrophages - virology | Eukaryotic Initiation Factors - immunology | Herpesvirus 1, Human - growth & development | Bone Marrow Cells - immunology | Interferon Type I - metabolism | Herpesvirus 1, Human - immunology | Ubiquitin-Specific Proteases - metabolism | Intracellular Signaling Peptides and Proteins - genetics | Macrophages - immunology | Protein-Serine-Threonine Kinases - metabolism | Eukaryotic Initiation Factors - genetics | Eukaryotic Initiation Factors - metabolism | Polyubiquitin - metabolism | Amino Acid Sequence | DNA-Binding Proteins - immunology | Gene Expression Regulation | Protein-Serine-Threonine Kinases - genetics | DNA-Binding Proteins - genetics | Immunity, Innate | Proteins - immunology | Mice, Knockout | Host-Pathogen Interactions | Proteins - genetics | Macrophages - metabolism | Animals | Proteins - metabolism | Polyubiquitin - immunology | Vesiculovirus - growth & development | Ubiquitin-Specific Proteases - immunology | Interferon Type I - genetics | Protein-Serine-Threonine Kinases - immunology | Mice | Bone Marrow Cells - metabolism | Ubiquitin | Epigenetic inheritance | Medical colleges | Biological control | Genetically modified organisms | Genetic engineering | Interferon | Pests | Biological response modifiers
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72. Full Text Deubiquitinase-based analysis of ubiquitin chain architecture using Ubiquitin Chain Restriction (UbiCRest)
by Hospenthal, Manuela K and Mevissen, Tycho E. T and Komander, David
Nature Protocols, ISSN 1754-2189, 01/2015, Volume 10, Issue 2, pp. 349 - 361
Protein ubiquitination is a versatile protein modification that regulates virtually all cellular processes. This versatility originates from polyubiquitin... 
LOCALIZATION | ACTIVATION | COMPLEX | POLYUBIQUITIN | RECOGNITION | MECHANISM | PROTEIN-DEGRADATION | BIOCHEMICAL RESEARCH METHODS | CROSS-REACTIVITY | BINDING | REVEALS | Ubiquitin - analysis | Ubiquitin-Specific Proteases - chemistry | Ubiquitinated Proteins - chemistry | Ubiquitination | Biochemistry - methods | Ubiquitin - chemistry | Ubiquitin - metabolism | Ubiquitin-Specific Proteases - metabolism | Ubiquitinated Proteins - analysis | Blotting, Western | Medical equipment | Enzymes | Protein research | Usage | Regulation | Research | Ubiquitin-proteasome system | Observations | Physiological apparatus | branched ubiquitin | mixed linkage chain | deubiquitinating enzyme | ubiquitin | polyubiquitin chain type
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73. Full Text Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation
by Babu, Jeganathan Ramesh and Geetha, Thangiah and Wooten, Marie W
Journal of Neurochemistry, ISSN 0022-3042, 07/2005, Volume 94, Issue 1, pp. 192 - 203
Inclusions isolated from several neurodegenerative diseases, including Alzheimer's disease (AD), are characterized by ubiquitin‐positive proteinaceous... 
neurodegeneration | proteasome | tau | ubiquitin | Ubiquitin | Tau | Neurodegeneration | Proteasome | SYSTEM | UBIQUITIN LIGASE | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BINDING-PROTEIN | ALPHA-SYNUCLEIN | NEUROSCIENCES | SH2 DOMAIN | PHOSPHOTYROSINE-INDEPENDENT LIGAND | IN-VITRO | INTERACTING PROTEIN P62 | LEWY BODIES | Polyubiquitin - metabolism | Cell Line | Proteins - physiology | Sequestosome-1 Protein | Humans | Proteasome Endopeptidase Complex - chemistry | Rats | tau Proteins - metabolism | Male | PC12 Cells | Polyubiquitin - genetics | tau Proteins - chemistry | Proteasome Endopeptidase Complex - genetics | Proteins - genetics | Adaptor Proteins, Signal Transducing | Animals | tau Proteins - genetics | Female | Aged | Proteasome Endopeptidase Complex - metabolism | Proteins - chemistry | Genetic Vectors | Polyubiquitin - chemistry | Neurology | Biochemistry | Alzheimers disease | Proteases
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