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Molecular Cell, ISSN 1097-2765, 11/2006, Volume 24, Issue 3, pp. 341 - 354
Small ubiquitin-like modifier (SUMO) modification has emerged as an important posttranslational control of protein functions. Daxx, a transcriptional... 
CELLBIO | PROTEINS | PROMYELOCYTIC LEUKEMIA PROTEIN | CONJUGATION | GLUCOCORTICOID-RECEPTOR | ISOFORMS | ENZYME UBC9 | BIOCHEMISTRY & MOLECULAR BIOLOGY | BINDING-PROTEIN | NUCLEAR-BODY FORMATION | IDENTIFICATION | SUMO-1-MODIFIED PML | UBIQUITIN-RELATED MODIFIER-1 | CELL BIOLOGY | Adaptor Proteins, Signal Transducing - chemistry | Transcription, Genetic - drug effects | Humans | Cercopithecus aethiops | Molecular Sequence Data | Intracellular Signaling Peptides and Proteins - metabolism | Receptors, Glucocorticoid - metabolism | Neoplasm Proteins - metabolism | Cell Nucleus - metabolism | Dexamethasone - pharmacology | Carrier Proteins - chemistry | Repressor Proteins - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Tumor Suppressor Proteins - metabolism | Small Ubiquitin-Related Modifier Proteins - metabolism | Arsenicals - pharmacology | Nuclear Proteins - metabolism | Nuclear Proteins - chemistry | Amino Acid Motifs | Protein Transport | Transcription Factors - metabolism | Oxides - pharmacology | Animals | Carrier Proteins - metabolism | Intracellular Signaling Peptides and Proteins - chemistry | Protein Binding | Mice | HeLa Cells | Adaptor Proteins, Signal Transducing - metabolism | COS Cells | Promyelocytic Leukemia Protein | Cellular proteins | Sumo | Corticosteroids | Arsenic | Genetic research | DNA binding proteins | Gene expression | Index Medicus
Journal Article
by Chu, Y and Yang, X
Oncogene, ISSN 0950-9232, 03/2011, Volume 30, Issue 9, pp. 1108 - 1116
SUMOylation governs numerous cellular processes and is essential to most eukaryotic life. Despite increasing recognition of the importance of this process, an... 
Mdm2 | TRIM proteins | sumoylation | SUMOE3 ligase | PML | p53 | BIOCHEMISTRY & MOLECULAR BIOLOGY | PML NUCLEAR-BODIES | DNA-DAMAGE | REGULATES P53 | FAMILY PROTEINS | SUMO E3 ligase | UBIQUITIN LIGASES | CELL BIOLOGY | RET FINGER PROTEIN | ONCOLOGY | GENETICS & HEREDITY | TUMOR-SUPPRESSOR | C-JUN | Immunoprecipitation | Transcription Factors - chemistry | Humans | Tumor Suppressor Protein p53 - genetics | DNA-Binding Proteins - metabolism | Small Ubiquitin-Related Modifier Proteins - genetics | Tumor Suppressor Proteins - chemistry | Tumor Suppressor Proteins - genetics | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Proto-Oncogene Proteins c-mdm2 - metabolism | Cell Line | Tumor Suppressor Proteins - metabolism | Small Ubiquitin-Related Modifier Proteins - metabolism | Tumor Suppressor Protein p53 - metabolism | Ubiquitin-Protein Ligases - metabolism | Nuclear Proteins - metabolism | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Nuclear Proteins - chemistry | DNA-Binding Proteins - chemistry | Transcription Factors - metabolism | Animals | Small Ubiquitin-Related Modifier Proteins - chemistry | Ubiquitin-Conjugating Enzymes - metabolism | Protein Binding | Sumoylation | RNA, Small Interfering | Ubiquitin-Protein Ligases - genetics | Microscopy, Fluorescence | Promyelocytic Leukemia Protein | Physiological aspects | Tumor suppressor genes | Research | Tumor proteins | Ligases | Proteins | Enzymes | Biochemistry | Cellular biology | Gene expression | Index Medicus
Journal Article
Oncogene, ISSN 0950-9232, 04/2018, Volume 37, Issue 16, pp. 2165 - 2180
Prostate cancer growth is promoted by the gene regulatory action of androgen receptor (AR) and its downstream signals. The aberrant dysfunction of tumor... 
RESPONSIVE FINGER PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | NUCLEAR EXPORT | EFP | CELL BIOLOGY | BREAST-CANCER | NONCODING RNA | ONCOLOGY | 14-3-3-SIGMA | GENETICS & HEREDITY | MUTANT P53 | ANDROGEN RECEPTOR GENE | TUMOR-GROWTH | E3 UBIQUITIN LIGASE | Prostatic Neoplasms - metabolism | Protein Binding - genetics | Tripartite Motif Proteins - physiology | Humans | Middle Aged | Cell Survival - genetics | Male | Ubiquitin-Protein Ligases - physiology | Tumor Suppressor Protein p53 - genetics | Cell Nucleus - metabolism | Prostatic Neoplasms - genetics | HEK293 Cells | Prostatic Neoplasms - pathology | Cell Proliferation - genetics | Transcription Factors - physiology | Cells, Cultured | Tumor Suppressor Protein p53 - metabolism | Ubiquitin-Protein Ligases - metabolism | Tripartite Motif Proteins - genetics | Signal Transduction - genetics | Transcription Factors - genetics | Protein Transport | Transcription Factors - metabolism | Animals | Carrier Proteins - metabolism | Mice, Nude | Aged | Mice | Tripartite Motif Proteins - metabolism | Ubiquitin-Protein Ligases - genetics | Cell proliferation | Cell survival | p53 Protein | Nuclear transport | SUMO protein | Proteins | Androgens | Cell growth | Cell activation | GTPase-activating protein | Medical prognosis | Cell cycle | Xenografts | Ran-binding protein | Tumor suppressor genes | Prostate cancer | Prostate | Ubiquitin-protein ligase | Cytoplasm | Apoptosis | Guanosinetriphosphatase | Index Medicus
Journal Article
Molecular Cell, ISSN 1097-2765, 01/2015, Volume 57, Issue 1, pp. 150 - 164
We show that central components of the Fanconi anemia (FA) DNA repair pathway, the tumor suppressor proteins FANCI and FANCD2 (the ID complex), are SUMOylated... 
E3 LIGASE | REPAIR | SEGREGASE | PROTEIN | FANCD2 | PATHWAY | BIOCHEMISTRY & MOLECULAR BIOLOGY | DVC1 C1ORF124 | RNF4 | IDENTIFICATION | SUMOYLATION | CELL BIOLOGY | Hydroxyurea - pharmacology | Ataxia Telangiectasia Mutated Proteins - metabolism | Fanconi Anemia Complementation Group D2 Protein - genetics | Humans | Ubiquitin - metabolism | Protein Inhibitors of Activated STAT - metabolism | Recombinant Fusion Proteins - metabolism | Small Ubiquitin-Related Modifier Proteins - genetics | Poly-ADP-Ribose Binding Proteins | Fanconi Anemia Complementation Group Proteins - metabolism | Ubiquitination | Cysteine Endopeptidases - metabolism | HEK293 Cells | Protein Inhibitors of Activated STAT - genetics | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Signal Transduction | Small Ubiquitin-Related Modifier Proteins - metabolism | Fanconi Anemia Complementation Group Proteins - genetics | Gene Expression Regulation | Nuclear Proteins - metabolism | Ubiquitin - genetics | Transcription Factors - genetics | Transcription Factors - metabolism | Fanconi Anemia Complementation Group D2 Protein - metabolism | Cysteine Endopeptidases - genetics | Cell Line, Tumor | Protein Binding | Recombinant Fusion Proteins - genetics | Sumoylation | DNA Damage | Ataxia Telangiectasia Mutated Proteins - genetics | Ubiquitin | Sumo | Proteases | Ligases | DNA damage | DNA | Molecular biology | Fanconi's anemia | Index Medicus
Journal Article
Journal of Cell Science, ISSN 0021-9533, 08/2008, Volume 121, Issue 16, pp. 2731 - 2743
PML nuclear bodies (NBs) are involved in the regulation of key nuclear pathways but their biochemical function in nuclear metabolism is unknown. In this study... 
Promyelocytic leukemia | SP100 | SUMO | Nuclear body | FCS | RARα | Kineticss modeling | FRAP | Assembly | DNA-DAMAGE | INTERACTING PROTEIN KINASE-2 | PHOTOBLEACHING RECOVERY | MAMMALIAN-CELLS | RECEPTOR-ALPHA | CELL BIOLOGY | CAJAL BODY COMPONENTS | nuclear body | kinetics modeling | ANOMALOUS DIFFUSION | GREEN FLUORESCENT PROTEIN | CELL-NUCLEUS | promyelocytic leukemia | assembly | RAR alpha | ACUTE PROMYELOCYTIC LEUKEMIA | Oncogene Proteins, Fusion - metabolism | Autoantigens - metabolism | Transcription Factors - chemistry | Antigens, Nuclear - metabolism | Humans | Substrate Specificity | Protein Transport - physiology | Green Fluorescent Proteins - genetics | Recombinant Fusion Proteins - metabolism | Cell Nucleus - metabolism | Protein Isoforms - metabolism | Tumor Suppressor Proteins - chemistry | Tumor Suppressor Proteins - genetics | Diffusion | Nuclear Proteins - genetics | Green Fluorescent Proteins - metabolism | Tumor Suppressor Proteins - metabolism | Cells, Cultured | Nuclear Proteins - metabolism | Transcription Factors - genetics | Nuclear Proteins - chemistry | Protein Processing, Post-Translational - physiology | Transcription Factors - metabolism | Models, Biological | Protein Binding | Recombinant Fusion Proteins - genetics | SUMO-1 Protein - metabolism | HeLa Cells | Kinetics | Intranuclear Inclusion Bodies - metabolism | Promyelocytic Leukemia Protein | Protein Structure, Tertiary - physiology | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2016, Volume 291, Issue 9, pp. 4417 - 4428
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2012, Volume 287, Issue 7, pp. 4740 - 4751
Journal Article
PLoS ONE, ISSN 1932-6203, 07/2014, Volume 9, Issue 7, pp. e102957 - e102957
Gene silencing by small RNAs has emerged as a powerful post-transcriptional regulator of gene expression, however processes underlying regulation of the small... 
SMALL RNAS | SUMO | PML DEGRADATION | BIOGENESIS | PATHWAY | PHOSPHORYLATION | MULTIDISCIPLINARY SCIENCES | POSTTRANSLATIONAL MODIFICATIONS | PROTEINS | CANCER | E3 UBIQUITIN LIGASE | RNA, Small Interfering - genetics | Molecular Chaperones - metabolism | Humans | Protein Processing, Post-Translational - genetics | Nuclear Pore Complex Proteins - genetics | Small Ubiquitin-Related Modifier Proteins - genetics | Phosphorylation - genetics | SUMO-1 Protein - genetics | Lysine - metabolism | Argonaute Proteins - metabolism | Sumoylation - genetics | Argonaute Proteins - genetics | Nuclear Pore Complex Proteins - metabolism | Small Ubiquitin-Related Modifier Proteins - metabolism | Molecular Chaperones - genetics | Ubiquitin-Protein Ligases - metabolism | Ubiquitin-Conjugating Enzymes - genetics | Lysine - genetics | Animals | Ubiquitin-Conjugating Enzymes - metabolism | Cell Line, Tumor | Mice | SUMO-1 Protein - metabolism | HeLa Cells | Ubiquitin-Protein Ligases - genetics | Gene Silencing - physiology | Post-translational modification | RNA | Lysine | Ligases | Post-transcription | Phosphorylation | Arsenic | Laboratories | Genes | Biosynthesis | Tissues | DNA repair | Proteins | SUMO protein | Post-translation | Ran-binding protein | Localization | Ubiquitin-protein ligase | Deoxyribonucleic acid--DNA | Enzymes | Translation | Stability | Extinction | RNA-mediated interference | Hot spots | siRNA | Argonaute 2 protein | Gene expression | Gene silencing | Ribonucleic acids | Cancer | Index Medicus | Life Sciences | Molecular biology | Biochemistry, Molecular Biology | Deoxyribonucleic acid | DNA
Journal Article
Scientific Reports, ISSN 2045-2322, 12/2019, Volume 9, Issue 1, pp. 2050 - 8
The molecular dissociation constant, K-d, is a well-established parameter to quantitate the affinity of protein-protein or other molecular interactions.... 
ENERGY-TRANSFER ANALYSIS | BINDING | MULTIDISCIPLINARY SCIENCES | SUMO protein | Proteins | Affinity | Fluorescence resonance energy transfer
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 | Index Medicus
Journal Article
Molecular Cell, ISSN 1097-2765, 2006, Volume 24, Issue 1, pp. 77 - 89
Journal Article
Science, ISSN 0036-8075, 09/2017, Volume 357, Issue 6358, pp. 1412 - 1416
Topoisomerase 2 (TOP2) DNA transactions proceed via formation of the TOP2 cleavage complex (TOP2cc), a covalent enzyme-DNA reaction intermediate that is... 
REPAIR | SUMO | STRUCTURAL BASIS | TDP2 | PATHWAY | UBIQUITIN | MULTIDISCIPLINARY SCIENCES | PHOSPHODIESTERASE | INHIBITORS | DAMAGE | COVALENT COMPLEXES | Immunoprecipitation | Humans | Gene Knockdown Techniques | HEK293 Cells | Nuclear Proteins - genetics | Recombinant Proteins - metabolism | DNA Topoisomerases, Type II - metabolism | Catalytic Domain | Biocatalysis | Small Ubiquitin-Related Modifier Proteins - metabolism | Bacterial Proteins - genetics | Ubiquitin-Protein Ligases - metabolism | Etoposide - pharmacology | Nuclear Proteins - metabolism | Recombinant Proteins - genetics | Topoisomerase II Inhibitors - pharmacology | DNA - metabolism | Saccharomyces cerevisiae Proteins - genetics | Transcription Factors - genetics | DNA - genetics | Transcription Factors - metabolism | Animals | DNA Repair | Saccharomyces cerevisiae Proteins - metabolism | Sumoylation | Bacterial Proteins - metabolism | DNA Topoisomerases, Type II - genetics | Luminescent Proteins - genetics | Mice | DNA Damage | Ubiquitin-Protein Ligases - genetics | Luminescent Proteins - metabolism | Proteins | Topoisomerases | Physiological aspects | Genetic research | Crosslinking | Genetic aspects | Research | Zinc finger proteins | DNA repair | Ubiquitin | Drugs | Hydrolase | Transcription | DNA damage | Genotoxicity | Phosphoesterase | Topology | Recruitment | Coordination compounds | Ubiquitin-protein ligase | Deoxyribonucleic acid--DNA | Phosphodiesterase | Index Medicus
Journal Article