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Nature Cell Biology, ISSN 1465-7392, 05/2008, Volume 10, Issue 5, pp. 538 - 546
Journal Article
Nature Immunology, ISSN 1529-2908, 02/2016, Volume 17, Issue 2, pp. 140 - 149
Innate sensing of pathogens initiates inflammatory cytokine responses that need to be tightly controlled. We found here that after engagement of Toll-like... 
PATHWAYS | INTERFERON | ACTIVATION | SUMO | BETA-GENE | IFN-GAMMA | NEGATIVE REGULATION | ENHANCER | MICE | IMMUNOLOGY | UP-REGULATION | Chromatin - metabolism | Dendritic Cells - immunology | Gene Expression Profiling | Genetic Loci | Shock, Septic - immunology | Lipopolysaccharides - immunology | Shock, Septic - metabolism | Inflammation - metabolism | Inflammation Mediators - metabolism | Toll-Like Receptors - metabolism | Dendritic Cells - metabolism | Disease Models, Animal | Receptor, Interferon alpha-beta - metabolism | Shock, Septic - genetics | Sumoylation - genetics | Disease Resistance | Disease Susceptibility | Cytokines - metabolism | Signal Transduction | Immunomodulation | Gene Expression Regulation | Inflammation - virology | Inflammation - immunology | Immunity, Innate | Mice, Knockout | Animals | Enhancer Elements, Genetic | Interferon-beta - metabolism | Regulatory Elements, Transcriptional | Sumoylation - immunology | Inflammation - genetics | Protein Binding | Mice | SUMO-1 Protein - metabolism | Chromatin - genetics | Analysis | Influence | Interferon | Inflammation | Research | Biological response modifiers | Gene expression | Health aspects | Risk factors | Shock, Septic/metabolism | Inflammation Mediators/metabolism | Sumoylation/immunology | Interferon-beta/metabolism | Dendritic Cells/metabolism | Inflammation/virology | Inflammation/immunology | Life Sciences | Immunology | Receptor, Interferon alpha-beta/metabolism | Inflammation/genetics | SUMO-1 Protein/metabolism | Cytokines/metabolism | Sumoylation/genetics | Chromatin/metabolism | Inflammation/metabolism | Toll-Like Receptors/metabolism | Lipopolysaccharides/immunology | Shock, Septic/immunology | Chromatin/genetics | Shock, Septic/genetics | Dendritic Cells/immunology
Journal Article
Nature Cell Biology, ISSN 1465-7392, 05/2013, Volume 15, Issue 5, pp. 526 - +
Cdc48 (also known as p97), a conserved chaperone-like ATPase, plays a strategic role in the ubiquitin system(1-3). Empowered by ATP-driven conformational... 
UBIQUITIN-SELECTIVE SEGREGASE | COMPLEX | PROTEIN | RAD51 | PCNA | AAA-ATPASE | HOMOLOGOUS RECOMBINATION | DNA-REPAIR | BRCA2 | SUMOYLATION | CELL BIOLOGY | Immunoprecipitation | DNA, Fungal - genetics | Saccharomyces cerevisiae - genetics | Humans | Valosin Containing Protein | DNA Breaks, Double-Stranded | Saccharomyces cerevisiae - metabolism | Multiprotein Complexes - metabolism | Rad52 DNA Repair and Recombination Protein - metabolism | Proteolysis | Recombination, Genetic | Cell Cycle Proteins - genetics | Rad51 Recombinase - metabolism | Recombinant Proteins - metabolism | Rad51 Recombinase - genetics | Small Ubiquitin-Related Modifier Proteins - metabolism | Electrophoresis, Polyacrylamide Gel | Cell Cycle Proteins - metabolism | Adenosine Triphosphatases - metabolism | Recombinant Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Blotting, Western | Rad52 DNA Repair and Recombination Protein - genetics | Protein Interaction Mapping - methods | Two-Hybrid System Techniques | Animals | Ubiquitin-Conjugating Enzymes - metabolism | DNA Repair | DNA, Fungal - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Cell Line, Tumor | Protein Binding | Sumoylation | Adenosine Triphosphatases - genetics | SUMO-1 Protein - metabolism | Enzyme Activation | Cellular control mechanisms | Research | Ubiquitin-proteasome system | Observations | Properties | Adenosine triphosphatase | Testing
Journal Article
Cell Host & Microbe, ISSN 1931-3128, 11/2017, Volume 22, Issue 5, pp. 627 - 638.e7
TRIM25 is an E3 ubiquitin ligase that activates RIG-I to promote the antiviral interferon response. The NS1 protein from all strains of influenza A virus binds... 
nuclear TRIM25 | viral RNA synthesis | Influenza virus | viral ribonucleoproteins | CELLS | UBIQUITIN LIGASE | POLYMERASE | RIG-I | MICROBIOLOGY | NS1 PROTEINS | B VIRUS | A VIRUS | VIROLOGY | STRUCTURAL BASIS | NUCLEOPROTEIN | ANTIVIRAL ACTIVITY | PARASITOLOGY | Transcription, Genetic - drug effects | DEAD Box Protein 58 - metabolism | Humans | Influenza A Virus, H3N2 Subtype - metabolism | Ubiquitin-Protein Ligases - antagonists & inhibitors | Antiviral Agents - metabolism | RNA, Messenger - metabolism | Ubiquitination | SUMO-1 Protein - genetics | HEK293 Cells | Ribonucleoproteins - drug effects | Influenza A virus - pathogenicity | RNA, Viral - metabolism | A549 Cells | Cell Line | Influenza, Human - metabolism | Virus Replication - drug effects | Tripartite Motif Proteins - antagonists & inhibitors | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Tripartite Motif Proteins - genetics | Transcription Factors - antagonists & inhibitors | Transcription Factors - genetics | Host-Pathogen Interactions | Transcription Factors - metabolism | Carrier Proteins - genetics | Carrier Proteins - metabolism | Influenza A virus - metabolism | Ubiquitin-Protein Ligases - drug effects | Interferons - metabolism | Protein Binding | Viral Nonstructural Proteins - metabolism | SUMO-1 Protein - metabolism | Tripartite Motif Proteins - metabolism | RNA, Viral - drug effects | Ubiquitin-Protein Ligases - genetics | Viral Nonstructural Proteins - antagonists & inhibitors | Influenza viruses | Ubiquitin | Synthesis | Messenger RNA | RNA | Developmental biology | Ligases | Influenza | Interferon | Biological response modifiers
Journal Article
Journal Article
Journal Article
Science, ISSN 0036-8075, 4/2004, Volume 304, Issue 5667, pp. 100 - 104
Journal Article
PLoS Pathogens, ISSN 1553-7366, 09/2011, Volume 7, Issue 9, p. e1002245
Intrinsic antiviral resistance represents the first line of intracellular defence against virus infection. During herpes simplex virus type-1 (HSV-1) infection... 
MUTANT | SIMPLEX-VIRUS TYPE-1 | BINDING MOTIF | MICROBIOLOGY | REGULATORY PROTEIN ICP0 | MUTATIONAL ANALYSIS | PML | E3 LIGASE | NUCLEAR-BODIES | VIROLOGY | RING FINGER | INFECTION | PARASITOLOGY | Humans | Substrate Specificity | Viral Proteins - metabolism | Immediate-Early Proteins - metabolism | Ubiquitination | Protein Isoforms - metabolism | Basic Helix-Loop-Helix Transcription Factors - metabolism | SUMO-1 Protein - genetics | Immediate-Early Proteins - chemistry | Herpesvirus 1, Human - immunology | Protein Interaction Domains and Motifs | Repressor Proteins - metabolism | Tumor Suppressor Proteins - metabolism | Herpesvirus 1, Human - metabolism | Trans-Activators | Cells, Cultured | Ubiquitin-Protein Ligases - metabolism | Viral Proteins - genetics | Nuclear Proteins - metabolism | Ubiquitin-Protein Ligases - chemistry | Transcription Factors - metabolism | Immediate-Early Proteins - genetics | Gene Expression Regulation, Viral | Herpesvirus 1, Human - genetics | SUMO-1 Protein - metabolism | Proteasome Endopeptidase Complex - metabolism | Ubiquitin-Protein Ligases - genetics | Herpesvirus 1, Human - pathogenicity | Promyelocytic Leukemia Protein | Antiviral agents | Ligases | Herpesvirus diseases | Physiological aspects | Herpes | Research | Drug therapy | Health aspects | Proteins | Enzymes | Viruses | Genomes | Mutation | Gene expression
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2014, Volume 111, Issue 46, pp. 16586 - 16591
Intracellular accumulation of the abnormally modified tau is hall-mark pathology of Alzheimer's disease (AD), but the mechanism leading to tau aggregation is... 
Aggregation | Phosphorylation | HEK293 cells | Neurons | Ubiquitins | Microtubules | Antibodies | Alzheimers disease | Tau proteins | Western blotting | PROTEIN-TAU | PHOSPHATASE 2A | MULTIDISCIPLINARY SCIENCES | GLYCOGEN-SYNTHASE KINASE-3 | tau | degradation | ABNORMAL PHOSPHORYLATION | SUMO-1 MODIFICATION | HYPERPHOSPHORYLATED-TAU | ubiquitination | DISEASE | PAIRED HELICAL FILAMENTS | SUMOylation | phosphorylation | ALZHEIMER NEUROFIBRILLARY DEGENERATION | AGGREGATION | Amyloid beta-Peptides - pharmacology | Humans | Middle Aged | Cerebral Cortex - pathology | Maleimides - pharmacology | tau Proteins - metabolism | Glycogen Synthase Kinase 3 beta | Male | Peptide Fragments - pharmacology | Mutation, Missense | Recombinant Fusion Proteins - metabolism | Cerebral Cortex - metabolism | Alzheimer Disease - pathology | Salicylates - pharmacology | Ubiquitination | tau Proteins - genetics | SUMO-1 Protein - genetics | Proteolysis | HEK293 Cells | Female | Indoles - pharmacology | Mutagenesis, Site-Directed | Solubility | Rats | Glycogen Synthase Kinase 3 - metabolism | Nerve Tissue Proteins - genetics | Rats, Sprague-Dawley | Nerve Tissue Proteins - metabolism | Hippocampus - metabolism | Point Mutation | Animals | Androstadienes - pharmacology | Alzheimer Disease - metabolism | Sumoylation | Protein Processing, Post-Translational | SUMO-1 Protein - metabolism | Proteasome Endopeptidase Complex - metabolism | Amino Acid Substitution | Protein research | Research | Protein-protein interactions | Biological Sciences
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 12/2007, Volume 282, Issue 50, pp. 36177 - 36189
As a multifunctional protein, KRAB domain-associated protein 1 (KAP1) is reportedly subjected to multiple protein posttranslational modifications, including... 
CELLS | DEPENDENT TRANSCRIPTION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ZINC-FINGER PROTEINS | DNA-DAMAGE | MDM2 INTERACTION | SUMO MODIFICATION | G CHECKPOINT | C-JUN | CANCER | P53 | Transcription, Genetic - drug effects | Antibiotics, Antineoplastic - pharmacology | Apoptosis - drug effects | Humans | bcl-2-Associated X Protein - biosynthesis | Mutation, Missense | Proto-Oncogene Proteins - biosynthesis | Tripartite Motif-Containing Protein 28 | DNA-Binding Proteins - metabolism | Cyclin-Dependent Kinase Inhibitor p21 - genetics | DNA Damage - physiology | SUMO-1 Protein - genetics | Tumor Suppressor Proteins - genetics | Apoptosis Regulatory Proteins - genetics | Cell Cycle Proteins - genetics | Cyclin-Dependent Kinase Inhibitor p21 - metabolism | Phosphorylation - drug effects | Nuclear Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | Repressor Proteins - metabolism | bcl-2-Associated X Protein - genetics | Apoptosis Regulatory Proteins - biosynthesis | DNA Damage - drug effects | Cell Line | Cysteine Endopeptidases | Endopeptidases - metabolism | Tumor Suppressor Proteins - metabolism | Cell Cycle Proteins - metabolism | Protein-Serine-Threonine Kinases - genetics | Repressor Proteins - genetics | Serine - genetics | Nuclear Proteins - metabolism | Proto-Oncogene Proteins - genetics | Ataxia Telangiectasia Mutated Proteins | DNA-Binding Proteins - genetics | Proto-Oncogene Proteins c-bcl-2 - biosynthesis | Serine - metabolism | Transcription, Genetic - physiology | Endopeptidases - genetics | Cell Cycle - physiology | SUMO-1 Protein - metabolism | Apoptosis - physiology | Cell Cycle - drug effects | Proto-Oncogene Proteins c-bcl-2 - genetics | Doxorubicin - pharmacology
Journal Article
PLoS Pathogens, ISSN 1553-7366, 07/2011, Volume 7, Issue 7, p. e1002123
Components of promyelocytic leukaemia (PML) nuclear bodies (ND10) are recruited to sites associated with herpes simplex virus type 1 (HSV-1) genomes soon after... 
DOMAIN 10 | PML NUCLEAR-BODIES | DNA-DAMAGE | SP100 PROTEINS | MICROBIOLOGY | CYTOMEGALOVIRUS GENE-EXPRESSION | MEDIATED REPRESSION | ANTIVIRAL DEFENSE | VIROLOGY | VIRAL GENOMES | BODY FORMATION | INTERACTING MOTIF | PARASITOLOGY | Autoantigens - metabolism | Antigens, Nuclear - metabolism | Humans | Protein Inhibitors of Activated STAT - metabolism | Autoantigens - genetics | Herpes Simplex - genetics | Cell Nucleus - metabolism | SUMO-1 Protein - genetics | Tumor Suppressor Proteins - genetics | Cell Nucleus - virology | HEK293 Cells | Protein Inhibitors of Activated STAT - genetics | Nuclear Proteins - genetics | Simplexvirus - metabolism | Repressor Proteins - metabolism | Genome, Viral | Sumoylation - genetics | Tumor Suppressor Proteins - metabolism | Simplexvirus - genetics | DNA, Viral - metabolism | Ubiquitin-Protein Ligases - metabolism | Repressor Proteins - genetics | Nuclear Proteins - metabolism | Transcription Factors - genetics | Amino Acid Motifs | Herpes Simplex - metabolism | Transcription Factors - metabolism | Antigens, Nuclear - genetics | Cell Nucleus - genetics | SUMO-1 Protein - metabolism | DNA, Viral - genetics | Ubiquitin-Protein Ligases - genetics | Promyelocytic Leukemia Protein | Myelocytic leukemia | Genetic aspects | Genomes | Nonlymphoid leukemia | Research | Health aspects | Herpes simplex virus | Risk factors | Proteins | Medical research | Cytokines | Microscopy | Infections | Viral infections | Recruitment
Journal Article