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1. Full Text The K48-K63 Branched Ubiquitin Chain Regulates NF-κB Signaling
by Ohtake, Fumiaki and Saeki, Yasushi and Ishido, Satoshi and Kanno, Jun and Tanaka, Keiji
Molecular Cell, ISSN 1097-2765, 10/2016, Volume 64, Issue 2, pp. 251 - 266
Polyubiquitin chains of different topologies regulate diverse cellular processes. K48- and K63-linked chains, the two most abundant chain types, regulate... 
NF-κB | CYLD | AQUA | proteomics | Lys63 | inflammation | TRAF6 | HUWE1 | Lys48 | ACTIVATION | COMPLEX | INHIBITION | SPECIFICITY | ELONGATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | CYLD USP | DEGRADATION | POLYUBIQUITIN CHAIN | MECHANISMS | LIGASE | CELL BIOLOGY | Adaptor Proteins, Signal Transducing - chemistry | Interleukin-1beta - pharmacology | Deubiquitinating Enzyme CYLD | Humans | Ubiquitin - metabolism | Substrate Specificity | NF-kappa B - metabolism | NF-kappa B - chemistry | Polyubiquitin - genetics | Ubiquitination | Tumor Suppressor Proteins - chemistry | Tumor Suppressor Proteins - genetics | Lysine - metabolism | Protein Interaction Domains and Motifs | Osteoblasts - cytology | TNF Receptor-Associated Factor 6 - genetics | Binding Sites | Polyubiquitin - chemistry | Polyubiquitin - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Gene Expression | Tumor Suppressor Proteins - metabolism | Signal Transduction | Osteoblasts - drug effects | Ubiquitin - chemistry | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Ubiquitin - genetics | Ubiquitin-Protein Ligases - chemistry | Sequence Alignment | NF-kappa B - genetics | Protein Conformation, beta-Strand | Adaptor Proteins, Signal Transducing - genetics | TNF Receptor-Associated Factor 6 - chemistry | TNF Receptor-Associated Factor 6 - metabolism | Cell Line, Tumor | Protein Binding | Adaptor Proteins, Signal Transducing - metabolism | Lysine - chemistry | Osteoblasts - metabolism | Ubiquitin-Protein Ligases - genetics | Index Medicus
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2. Full Text Notch-1 signaling regulates microglia activation via NF-κB pathway after hypoxic exposure in vivo and in vitro
by Yao, Linli and Kan, Enci Mary and Kaur, Charanjit and Dheen, S. Thameem and Hao, Aijun and Lu, Jia and Ling, Eng-Ang
PLoS ONE, ISSN 1932-6203, 11/2013, Volume 8, Issue 11, p. e78439
Neuroinflammation mediated by the activated microglia is suggested to play a pivotal role in the pathogenesis of hypoxic brain injury; however, the underlying... 
MURINE BV-2 CELLS | MULTIDISCIPLINARY SCIENCES | NITRIC-OXIDE | RECEPTOR | NEURAL PROGENITOR CELLS | RAT-BRAIN | DIFFERENTIATION | INFLAMMATORY RESPONSE | EXPRESSION | AMEBOID MICROGLIA | INNATE IMMUNITY | Amyloid Precursor Protein Secretases - genetics | Microglia - metabolism | Transcription Factor HES-1 | Homeodomain Proteins - metabolism | NF-kappa B - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Hypoxia - metabolism | Basic Helix-Loop-Helix Transcription Factors - metabolism | Gene Expression Regulation, Developmental | Microglia - pathology | Membrane Proteins - metabolism | TNF Receptor-Associated Factor 6 - genetics | Immunoglobulin J Recombination Signal Sequence-Binding Protein - genetics | Intracellular Signaling Peptides and Proteins - genetics | Animals, Newborn | Immunoglobulin J Recombination Signal Sequence-Binding Protein - metabolism | Basic Helix-Loop-Helix Transcription Factors - genetics | Signal Transduction | Membrane Proteins - genetics | Dipeptides - pharmacology | Enzyme Inhibitors - pharmacology | Myeloid Differentiation Factor 88 - genetics | Rats | Toll-Like Receptor 4 - genetics | Receptor, Notch1 - metabolism | Toll-Like Receptor 4 - metabolism | Homeodomain Proteins - genetics | Amyloid Precursor Protein Secretases - metabolism | Hypoxia - genetics | Animals | NF-kappa B - genetics | Hypoxia - pathology | TNF Receptor-Associated Factor 6 - metabolism | Cell Line, Tumor | Mice | Amyloid Precursor Protein Secretases - antagonists & inhibitors | Receptor, Notch1 - antagonists & inhibitors | Cell Hypoxia - genetics | Receptor, Notch1 - genetics | Myeloid Differentiation Factor 88 - metabolism | Brain | Mental disorders | Laboratories | Pathogenesis | Crosstalk | Activation | Neurogenesis | Signal transduction | Embryology | Head injuries | Pathways | Rodents | Cerebrum | Toll-like receptors | Microglial cells | Inhibition | Pretreatment | Casualties | Translocation | NF-κB protein | Adenosine | TRAF6 protein | Cytokines | Histology | Exposure | Inflammation | TLR4 protein | Gene expression | Microglia | Medicine | Studies | Signaling | Brain research | DELTA protein | Stem cells | MyD88 protein | Hypoxia | Ligands | Brain damage | Notch protein | Brain injury | Secretase
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3. Full Text Two antagonistic MALT1 auto-cleavage mechanisms reveal a role for TRAF6 to unleash MALT1 activation
by Ginster, Stefanie and Bardet, Maureen and Unterreiner, Adeline and Malinverni, Claire and Renner, Florian and Lam, Stephen and Freuler, Felix and Gerrits, Bertran and Voshol, Johannes and Calzascia, Thomas and Régnier, Catherine H and Renatus, Martin and Nikolay, Rainer and Israël, Laura and Bornancin, Frédéric
PLoS ONE, ISSN 1932-6203, 01/2017, Volume 12, Issue 1, p. e0169026
The paracaspase MALT1 has arginine-directed proteolytic activity triggered by engagement of immune receptors. Recruitment of MALT1 into activation complexes is... 
PARACASPASE MALT1 | REGULATOR | KAPPA-B ACTIVATION | UBIQUITIN LIGASE | PHOSPHORYLATION | CARMA1 | MULTIDISCIPLINARY SCIENCES | T-CELL-ACTIVATION | LYMPHOMA | BCL10 | PROTEASE ACTIVITY | Evaluation | Reports | MALT lymphoma | Research | Proteolysis | Phosphorylation | Biomedical research | Activation | Kinases | Protein turnover | Proteins | Receptors | Ubiquitination | Clonal deletion | Arginine | Lymphocytes | Deletion | Cleavage | NF-κB protein | Immunoglobulins | TRAF6 protein | Research & development--R&D | Cloning | T cell receptors | MALT1 protein | Signaling | Mutagenesis | Scaffolding | Plasmids | Isoforms | Bcl-10 protein | Lymphomas | Internet | Binding sites | Cancer | Research & development | R&D
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4. Full Text RBR E3 ubiquitin ligases: New structures, new insights, new questions
by Spratt, Donald E and Walden, Helen and Shaw, Gary S
Biochemical Journal, ISSN 0264-6021, 03/2014, Volume 458, Issue 3, pp. 421 - 437
The RBR (RING-BetweenRING-RING) or TRIAD [two RING fingers and a DRIL (double RING finger linked)] E3 ubiquitin ligases comprise a group of 12 complex... 
Ubiquitination | Catalysis | Ubiquitin ligase | Structure | ubiquitin ligase | INDUCED CELL-DEATH | ANDROGEN RECEPTOR TRANSACTIVATION | KAPPA-B ACTIVATION | LINEAR POLYUBIQUITIN CHAINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | catalysis | CHAIN ASSEMBLY COMPLEX | AMYOTROPHIC-LATERAL-SCLEROSIS | ALPHA-SYNUCLEIN | structure | ubiquitination | RING-FINGER PROTEINS | CONJUGATING ENZYME | FAMILIAL PARKINSONS-DISEASE | Animals | DNA Repair | Humans | Ubiquitin-Protein Ligases - metabolism | Protein Conformation | Membrane Proteins - metabolism | Enzyme Activation | Ubiquitin-Protein Ligases - chemistry | Protein Interaction Maps | RNA - metabolism | HECT, homologous with E6-associated protein C-terminus | Ubl, ubiquitin-like | IBR, InBetweenRING | ANKIB1, ankyrin repeat- and IBR domain-containing 1 | SH3, Src homology 3 | Eps15, epidermal growth factor receptor pathway substrate 15 | UBA, ubiquitin-associated | RWD, RING finger and WD repeat-containing | CCCP, carbonyl cyanide m-chlorophenylhydrazone | CRL, Cul-RING-ligase | TOMM70A, translocase of outer mitochondrial membrane 70 homologue A | NF-κB, nuclear factor κB | NZF, Npl4 ZNF | cIAP2, cellular inhibitor of apoptosis 2 | MIRO, mitochondrial Rho GTPase | TRAF6, tumour-necrosis-factor-receptor-associated factor 6 | NEMO, NF-κB essential modulator | MDM2, murine double minute 2 | TRIAD, two RING fingers and a DRIL (double RING finger linked) | HOIP, HOIL-1-interacting protein | BRcat, benign-catalytic | SHARPIN, SHANK-associated RH domain interactor | Review | RING1-BRcat-Rcat | Parc, parkin-like cytoplasmic p53-binding protein | SUMO, small ubiquitin-related modifier | LUBAC, linear ubiquitin chain assembly complex | HOIL-1, haem-oxidized IRP2 ubiquitin ligase 1 | RNF, RING finger protein | CPH, Cul7, Parc and HERC2 proteins | HDAC, histone deacetylase | RBR, RING-BetweenRING-RING | Cdk5, cyclin-dependent kinase 5 | SILAC, stable isotope labelling by amino acids in cell culture | RanBP2, RAN-binding protein 2 | FANCL, Fanconi anaemia, complementation group L | PINK1, PTEN-induced putative kinase 1 | PKC, protein kinase C | CK1, casein kinase 1 | NEDD, neural-precursor-cell-expressed developmentally down-regulated | ZNF, zinc finger | UBE2L, ubiquitin-conjugating enzyme E2L | UIM, ubiquitin-interacting motif | Cul, cullin | Rcat, required-for-catalysis
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5. Full Text Negative Regulation of Mitochondrial Antiviral Signaling Protein–Mediated Antiviral Signaling by the Mitochondrial Protein LRPPRC During Hepatitis C Virus Infection
by Refolo, Giulia and Ciccosanti, Fabiola and Di Rienzo, Martina and Basulto Perdomo, Ariel and Romani, Marta and Alonzi, Tonino and Tripodi, Marco and Ippolito, Giuseppe and Piacentini, Mauro and Fimia, Gian Maria
Hepatology, ISSN 0270-9139, 01/2019, Volume 69, Issue 1, pp. 34 - 50
Hepatitis C virus (HCV) is highly efficient in establishing a chronic infection, having evolved multiple strategies to suppress the host antiviral responses.... 
INTERFERON RESPONSE | MAVS | ACTIVATE | REPLICATION | NLRX1 | BLOCKS | KINASE | TOLL-LIKE RECEPTORS | CLEAVAGE | GASTROENTEROLOGY & HEPATOLOGY | INNATE IMMUNITY | Proteins | Hepatitis | Mitochondria | TRAF6 protein | Chronic infection | Infections | Interferon | Hepatitis C
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6. Full Text The Architecture of the TIR Domain Signalosome in the Toll-like Receptor-4 Signaling Pathway
by Guven-Maiorov, Emine and Keskin, Ozlem and Gursoy, Attila and VanWaes, Carter and Chen, Zhong and Tsai, Chung-Jung and Nussinov, Ruth
Scientific Reports, ISSN 2045-2322, 08/2015, Volume 5, Issue 1, p. 13128
Activated Toll-like receptors (TLRs) cluster in lipid rafts and induce pro-and anti-tumor responses. The organization of the assembly is critical to the... 
ADAPTER RECRUITMENT | STRUCTURAL BASIS | TRAF3 | CRYSTAL-STRUCTURE | INFLAMMATION | MULTIDISCIPLINARY SCIENCES | PROTEIN-PROTEIN INTERACTIONS | NF-KAPPA-B | MOLECULAR-BASIS | CANCER | MYD88 | Protein Structure, Tertiary | Multiprotein Complexes - metabolism | Multiprotein Complexes - chemistry | Signal Transduction | Models, Biological | Humans | Protein Multimerization | Models, Molecular | Protein Binding | Myeloid Differentiation Factor 88 | Imaging, Three-Dimensional | Toll-Like Receptor 4 - metabolism | Cell culture | Antiviral agents | TRAF6 protein | Lipid rafts | Inflammation | TLR4 protein | FADD protein | Signal transduction | MyD88 protein | Toll-like receptors | Receptor density | Binding sites | Cancer
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7. Full Text Autophagy-dependent PELI3 degradation inhibits proinflammatory IL1B expression
by Giegerich, Annika Klara and Kuchler, Laura and Sha, Lisa Katharina and Knape, Tilo and Heide, Heinrich and Wittig, Ilka and Behrends, Christian and Brüne, Bernhard and Knethen, Andreas von
Autophagy, ISSN 1554-8627, 11/2014, Volume 10, Issue 11, pp. 1937 - 1952
Lipopolysaccharide (LPS)-induced activation of TLR4 (toll-like receptor 4) is followed by a subsequent overwhelming inflammatory response, a hallmark of the... 
ACTB, actin, beta | MYD88, myeloid differentiation primary response 88 | PELI3 | CHX, cycloheximide | BECN1, Beclin 1, autophagy related | TICAM1, toll-like receptor adaptor molecule 1 | LPS | RIPK1, receptor (TNFRSF)-interacting serine-threonine kinase 1 | TUBB, tubulin, beta class I | PRRs, pattern recognition receptors | UBB, ubiquitin B | IRAKs, interleukin-1 receptor-associated kinases | HBSS, Hank's balanced salt solution | ATG7, autophagy-related 7 | MAP1LC3B, microtubule-associated protein 1 light chain 3 beta | TLRs, toll-like receptors | Baf A1, bafilomycin A | WT, wildtype | autophagy | TNF, tumor necrosis factor | MAPK14, mitogen-activated protein kinase 14 | NFKB, nuclear factor of kappa light polypeptide gene enhancer in B-cells | MAPK1/3, mitogen-activated protein kinase 1/3 | Epoxo, epoxomycin | TRAF6, TNF receptor-associated factor 6, E3 ubiquitin protein ligase | IL1B, interleukin 1, beta | MTOR, mechanistic target of rapamycin (serine/threonine kinase) | TABs, TGF-beta activated kinase 1/MAP3K7 binding protein 1/2/3 | Wortm, wortmannin | 1 | PELI3, pellino E3 ubiquitin protein ligase family member 3 | MAPK8/9, mitogen-activated protein kinase 8/9 | SQSTM1, sequestosome 1 | NFE2L2, nuclear factor, erythroid 2-like 2 | NLRP3, NLR family, pyrin domain containing 3 | LAMP2, lysosomal-associated membrane protein 2 | LPS, lipopolysaccharide | MAP3K14, mitogen-activated protein kinase kinase kinase 14 | MΦ, macrophages | Rapa, rapamycin | SQSTM1 | TBK1, TANK-binding kinase 1 | Torin2 | MAP3K7, mitogen-activated protein kinase kinase kinase 7 | Autophagy | TOLL-LIKE-RECEPTORS | ACTIVATION | BECLIN 1 | RECOGNITION | SELECTIVE AUTOPHAGY | CELL BIOLOGY | UBIQUITINATION | IL-1-BETA PRODUCTION | INFLAMMASOME | SCAFFOLD PROTEINS | INNATE IMMUNITY | Cell Line | Cytokines - metabolism | Signal Transduction | Ubiquitin - metabolism | Ubiquitin-Protein Ligases - metabolism | Adenosine Triphosphatases - metabolism | Lipopolysaccharides - metabolism | Inflammation | Immunity, Innate | RNA, Messenger - metabolism | Toll-Like Receptor 4 - metabolism | Point Mutation | Macrophages - metabolism | Animals | Interleukin-1beta - metabolism | Sepsis - metabolism | Mice | Naphthyridines - metabolism | RNA, Small Interfering - metabolism
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8. Full Text Inhibition of TRAF6-Ubc13 interaction in NFkB inflammatory pathway by analyzing the hotspot amino acid residues and protein–protein interactions using molecular docking simulations
by Biswas, Ria and Bagchi, Angshuman
Computational Biology and Chemistry, ISSN 1476-9271, 10/2017, Volume 70, pp. 116 - 124
Protein–protein interactions (PPIs) are important in most of the biochemical processes. Hotspot amino acid residues in proteins are the most important... 
Ubc13 | Hotspot | TRAF6 | PDTC | Protein–protein interaction | Molecular docking | Protein-protein interaction | KAPPA-B | PREDICTION | COMPUTER SCIENCE, INTERDISCIPLINARY APPLICATIONS | DISEASE | BIOLOGY | INTERFACES | HOT-SPOT | BINDING-ENERGY | Humans | Computational Biology | Amino Acids - chemistry | NF-kappa B - metabolism | TNF Receptor-Associated Factor 6 - antagonists & inhibitors | Ubiquitin-Conjugating Enzymes - chemistry | Protein Interaction Maps | Pyrrolidines - pharmacology | Amino Acids - metabolism | Inflammation - metabolism | Thiocarbamates - pharmacology | Ubiquitin-Conjugating Enzymes - metabolism | Protein Binding - drug effects | TNF Receptor-Associated Factor 6 - chemistry | TNF Receptor-Associated Factor 6 - metabolism | Ligands | Molecular Docking Simulation | Ubiquitin-Conjugating Enzymes - antagonists & inhibitors | Analysis | Protein-protein interactions | Proteins | Medicine, Experimental | Medical research | Amino acids | Heterocyclic compounds
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9. Full Text MAVS recruits multiple ubiquitin E3 ligases to activate antiviral signaling cascades
by Liu, Siqi and Chen, Jueqi and Cai, Xin and Wu, Jiaxi and Chen, Xiang and Wu, You-Tong and Sun, Lijun and Chen, Zhijian J
eLife, ISSN 2050-084X, 2013, Volume 2, p. e00785
RNA virus infections are detected by the RIG-I family of receptors, which induce type-I interferons through the mitochondrial protein MAVS. MAVS forms large... 
Human | MAVS | signaling | innate immunity | Mouse | mitochondria | Viruses | virus | ubiquitin | IFN-BETA | COMPLEX | KINASE | BIOLOGY | RIG-I | IKK ACTIVATION | TNF-ALPHA | RNA RECOGNITION | NF-KAPPA-B | ADAPTER PROTEIN | NEMO | Adaptor Proteins, Signal Transducing - chemistry | Amino Acid Sequence | Cell Line | Signal Transduction | Humans | Ubiquitin-Protein Ligases - metabolism | Molecular Sequence Data | Polymerization | Sendai virus - metabolism | Sequence Homology, Amino Acid | Adaptor Proteins, Signal Transducing - physiology | Animals | I-kappa B Kinase - metabolism | Tumor Necrosis Factor Receptor-Associated Peptides and Proteins - physiology | Interferon Regulatory Factor-3 - metabolism | Protein Binding | Adaptor Proteins, Signal Transducing - metabolism | Ubiquitin | Pathogens | RNA viruses | NF-κB protein | Transcription factors | TRAF6 protein | Immune response | Amino acids | Infections | Kinases | Recruitment | Proteins | TRAF2 protein | Ubiquitination | Mitochondria | Interferon regulatory factor 3 | Search engines | Interferon | Polymers | Viral infections | Immune system
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10. 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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11. Full Text Major vault protein suppresses obesity and atherosclerosis through inhibiting IKK-NF-kappa B signaling mediated inflammation
by Ben, JJ and Jiang, B and Wang, DD and Liu, QL and Zhang, YJ and Qi, Y and Tong, X and Chen, LL and Liu, XZ and Zhang, Y and Zhu, XD and Li, XY and Zhang, HW and Bai, H and Yang, Q and Ma, JQ and Wiemer, EAC and Xu, Y and Chen, Q
NATURE COMMUNICATIONS, ISSN 2041-1723, 04/2019, Volume 10, Issue 1, pp. 1801 - 15
Macrophage-orchestrated, low-grade chronic inflammation plays a pivotal role in obesity and atherogenesis. However, the underlying regulatory mechanisms remain... 
INTERLEUKIN-1 | IMMUNITY | ACTIVATION | CYTOKINES | MACROPHAGES | TRAF6 | MULTIDISCIPLINARY SCIENCES | RESISTANCE | INCREASES ATHEROSCLEROSIS | INDUCTION | BETA | IRAK protein | Obesity | NF-κB protein | Atherogenesis | Oligomerization | TRAF6 protein | Liver | Inflammation | Metabolism | Macrophages | Insulin | High fat diet | Steatosis | Proteins | Signaling | Ubiquitination | Fatty liver | Arteriosclerosis | Atherosclerosis | Regulatory mechanisms (biology) | Infiltration | Microenvironments | Metabolic disorders
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12. Full Text Parkinson's disease DJ-1 l166p alters rrna biogenesis by exclusion of TTRAP from the nucleolus and sequestration into cytoplasmic aggregates via TRAF6
by Vilotti, Sandra and Codrich, Marta and dal Ferro, Marco and Pinto, Milena and Ferrer, Isidro and Collavin, Licio and Gustincich, Stefano and Zucchelli, Silvia
PLoS ONE, ISSN 1932-6203, 04/2012, Volume 7, Issue 4, p. e35051
Mutations in PARK7/DJ-1 gene are associated to autosomal recessive early onset forms of Parkinson's disease (PD). Although large gene deletions have been... 
PROTEIN | OXIDATIVE DAMAGE | UBIQUITIN | MULTIDISCIPLINARY SCIENCES | MITOCHONDRIAL-FUNCTION | PROTEASOME | DOPAMINERGIC-NEURONS | ALPHA-SYNUCLEIN | DYSFUNCTION | STRESS | LEWY BODIES | Oncogene Proteins - genetics | Cell Fractionation | Cell Proliferation | Humans | Intracellular Signaling Peptides and Proteins - metabolism | Substantia Nigra - metabolism | RNA, Ribosomal - genetics | Lewy Bodies - genetics | Cell Nucleolus - metabolism | Parkinson Disease - metabolism | Lewy Bodies - metabolism | TNF Receptor-Associated Factor 6 - genetics | Nuclear Proteins - genetics | Intracellular Signaling Peptides and Proteins - genetics | Cell Nucleolus - genetics | Oncogene Proteins - metabolism | RNA, Ribosomal - metabolism | Nuclear Proteins - metabolism | Parkinson Disease - genetics | Transcription Factors - genetics | Proteasome Endopeptidase Complex - genetics | Transcription Factors - metabolism | Protein Deglycase DJ-1 | TNF Receptor-Associated Factor 6 - metabolism | Cell Line, Tumor | Proteasome Endopeptidase Complex - metabolism | Genetic aspects | Biosynthesis | RNA | Ligases | Tumor necrosis factor receptors | Brain | Neurosciences | Parkinson's disease | Yeast | Neuropathology | Parkinsons disease | Neurobiology | Neuroblastoma cells | Recruitment | Proteins | Nucleoli | Signal transduction | Missense mutation | Neurodegeneration | Protein folding | Evolution | Physiology | Life sciences | Trends | Stress response | Localization | Ubiquitin-protein ligase | Deoxyribonucleic acid--DNA | Movement disorders | TRAF6 protein | Neurodegenerative diseases | rRNA | MAP kinase | JNK protein | Lewy bodies | PARK7 protein | Molecular modelling | Aggregates | Tumor necrosis factor | Quality control | Mutation | Alzheimers disease | Endoplasmic reticulum | Cytoplasm | Apoptosis | Deoxyribonucleic acid | DNA
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