JOURNAL OF BIOMEDICAL SCIENCE, ISSN 1021-7770, 10/2019, Volume 26, Issue 1, pp. 1 - 12
Autophagy is a major degradation pathway that utilizes lysosome hydrolases to degrade cellular constituents and is often induced under cellular stress...
MEDICINE, RESEARCH & EXPERIMENTAL | POLYUBIQUITIN | DAMAGED LYSOSOMES | Ubiquitin E3 ligase | Autophagy | Protein ubiquitination | CELL BIOLOGY | CHAIN | PARKIN | Deubiquitinating enzyme | PINK1/PARKIN-MEDIATED MITOPHAGY | UBIQUITYLATION | ULK1 | Selective autophagy | INHIBITS AUTOPHAGY | PROTEASOME SYSTEM | Ubiquitin | Ligases | Delivery services
MEDICINE, RESEARCH & EXPERIMENTAL | POLYUBIQUITIN | DAMAGED LYSOSOMES | Ubiquitin E3 ligase | Autophagy | Protein ubiquitination | CELL BIOLOGY | CHAIN | PARKIN | Deubiquitinating enzyme | PINK1/PARKIN-MEDIATED MITOPHAGY | UBIQUITYLATION | ULK1 | Selective autophagy | INHIBITS AUTOPHAGY | PROTEASOME SYSTEM | Ubiquitin | Ligases | Delivery services
Journal Article
BMC Genomics, ISSN 1471-2164, 01/2019, Volume 20, Issue 1, pp. 38 - 13
BackgroundThe process of gene fusion involves the formation of a single chimeric gene from multiple complete or partial gene sequences. Gene fusion is...
Ubiquitin | Ubiquitin fusion proteins | Plastid evolution | Endosymbiosis | Algae | ACTIN | POLYUBIQUITIN GENE | SIGNALP | CONCERTED EVOLUTION | FAMILY | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | GENETICS & HEREDITY | TREE | FISSION | BIRTH | Symbiosis | Ubiquitins - classification | Cercozoa - genetics | Cryptophyta - genetics | Ubiquitins - genetics | Mutant Chimeric Proteins - genetics | Gene Fusion | Phylogeny | Evolution, Molecular | Physiological aspects | Genetic aspects | Research | Photosynthesis | Trees | Peptides | Genes | Biological evolution | Amino acids | Superoxide dismutase | Superoxide | Genomes | Biology | Gene fusion | Gene sequencing | Proteins | Phylogenetics | Nickel | Fusion protein | Plastids
Ubiquitin | Ubiquitin fusion proteins | Plastid evolution | Endosymbiosis | Algae | ACTIN | POLYUBIQUITIN GENE | SIGNALP | CONCERTED EVOLUTION | FAMILY | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | GENETICS & HEREDITY | TREE | FISSION | BIRTH | Symbiosis | Ubiquitins - classification | Cercozoa - genetics | Cryptophyta - genetics | Ubiquitins - genetics | Mutant Chimeric Proteins - genetics | Gene Fusion | Phylogeny | Evolution, Molecular | Physiological aspects | Genetic aspects | Research | Photosynthesis | Trees | Peptides | Genes | Biological evolution | Amino acids | Superoxide dismutase | Superoxide | Genomes | Biology | Gene fusion | Gene sequencing | Proteins | Phylogenetics | Nickel | Fusion protein | Plastids
Journal Article
Structure, ISSN 0969-2126, 10/2019
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 10/2019, Volume 294, Issue 41, pp. 14860 - 14875
The human papillomavirus (HPV) oncoprotein E6 specifically binds to E6AP (E6-associated protein), a HECT (homologous to the E6AP C terminus)-type ubiquitin...
Index Medicus | Editors' Picks | E6-associated protein | linkage specificity | polyubiquitin chain | E3 ubiquitin ligase | in vitro reconstitution | human papillomavirus (HPV) oncoprotein E6 | enzyme mechanism | Lys48-linked ubiquitin chain | p53 | mass spectrometry (MS)
Index Medicus | Editors' Picks | E6-associated protein | linkage specificity | polyubiquitin chain | E3 ubiquitin ligase | in vitro reconstitution | human papillomavirus (HPV) oncoprotein E6 | enzyme mechanism | Lys48-linked ubiquitin chain | p53 | mass spectrometry (MS)
Journal Article
SCIENTIFIC REPORTS, ISSN 2045-2322, 10/2019, Volume 9
The ubiquitin-proteasome system (UPS) is responsible for the bulk of protein degradation in eukaryotic cells, but the factors that cause different substrates...
PROVIDES INSIGHTS | SITE | RECOGNITION | PROTEIN-DEGRADATION | MULTIDISCIPLINARY SCIENCES | POLYUBIQUITIN CHAIN | RPN13 | 26S PROTEASOME | ATP | BINDING | MASS-SPECTROMETRY
PROVIDES INSIGHTS | SITE | RECOGNITION | PROTEIN-DEGRADATION | MULTIDISCIPLINARY SCIENCES | POLYUBIQUITIN CHAIN | RPN13 | 26S PROTEASOME | ATP | BINDING | MASS-SPECTROMETRY
Journal Article
Tetrahedron Letters, ISSN 0040-4039, 10/2019, Volume 60, Issue 41, p. 151123
Atypical ubiquitin (Ub) chains are generally involved in intracellular physiological processes, while the molecular mechanisms underlying their regulation...
Atypical ubiquitin chains | Acid-sensitive auxiliary handles | Thiol-ene coupling | Protein chemical synthesis | PEPTIDE LIGATION | TOTAL CHEMICAL-SYNTHESIS | UBIQUITIN CHAINS | SEMISYNTHESIS | POLYUBIQUITIN | CHEMISTRY, ORGANIC | CLICK | PROTEINS
Atypical ubiquitin chains | Acid-sensitive auxiliary handles | Thiol-ene coupling | Protein chemical synthesis | PEPTIDE LIGATION | TOTAL CHEMICAL-SYNTHESIS | UBIQUITIN CHAINS | SEMISYNTHESIS | POLYUBIQUITIN | CHEMISTRY, ORGANIC | CLICK | PROTEINS
Journal Article
Molecular Cell, ISSN 1097-2765, 10/2019
Journal Article
CELL DEATH & DISEASE, ISSN 2041-4889, 09/2019, Volume 10, Issue 10, pp. 1 - 16
The cytokine TNF promotes inflammation either directly by activating the MAPK and NF-kappa B signaling pathways, or indirectly by triggering cell death. A20 is...
CYLD | ACTIVATION | COMPLEX | POLYUBIQUITIN | PHOSPHORYLATION | INFLAMMATION | DEATH | CHAINS | NF-KAPPA-B | BINDING | CELL BIOLOGY | Tumor necrosis factor receptors | Ubiquitin | NF-κB protein | Cytotoxicity | MAP kinase | Inflammation | Molecular modelling | Clonal deletion | Cell death | Tumor necrosis factor | A20 protein | Zinc finger proteins | Ubiquitin-protein ligase | Apoptosis
CYLD | ACTIVATION | COMPLEX | POLYUBIQUITIN | PHOSPHORYLATION | INFLAMMATION | DEATH | CHAINS | NF-KAPPA-B | BINDING | CELL BIOLOGY | Tumor necrosis factor receptors | Ubiquitin | NF-κB protein | Cytotoxicity | MAP kinase | Inflammation | Molecular modelling | Clonal deletion | Cell death | Tumor necrosis factor | A20 protein | Zinc finger proteins | Ubiquitin-protein ligase | Apoptosis
Journal Article
Protein Science, ISSN 0961-8368, 10/2019, Volume 28, Issue 10, pp. 1758 - 1770
Protein ubiquitination is a fundamental regulatory component in eukaryotic cell biology, where a cascade of ubiquitin activating (E1), conjugating (E2), and...
E2–E3 specificity | RING E3 | structural basis of specificity | ubiquitination | DOMAIN | POLYUBIQUITIN | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | COMPLEX REVEALS | E2-E3 specificity | UBIQUITYLATION | CONJUGATING ENZYME | CHAIN ELONGATION | BINDING | LIGASE | Proteins | Ubiquitin | Ubiquitination | Substrates
E2–E3 specificity | RING E3 | structural basis of specificity | ubiquitination | DOMAIN | POLYUBIQUITIN | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | COMPLEX REVEALS | E2-E3 specificity | UBIQUITYLATION | CONJUGATING ENZYME | CHAIN ELONGATION | BINDING | LIGASE | Proteins | Ubiquitin | Ubiquitination | Substrates
Journal Article
BBA - General Subjects, ISSN 0304-4165, 10/2019, Volume 1863, Issue 10, pp. 1568 - 1574
UBQLN proteins regulate proteostasis by facilitating clearance of misfolded proteins through the proteasome and autophagy degradation pathways. Consistent with...
Ubiquilin | UBQLN1 | Polyubiquitin | UBA domain | UBL domain | PROTEIN | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CHAPERONE | IDENTIFICATION | FAMILY | BIOPHYSICS | MUTATION | PROTEASOME | DEGRADATION | ENDOPLASMIC-RETICULUM | ASSOCIATION | Ubiquitin | Medical colleges | Lysine | Proteolysis | Biomedical engineering | Protein binding
Ubiquilin | UBQLN1 | Polyubiquitin | UBA domain | UBL domain | PROTEIN | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CHAPERONE | IDENTIFICATION | FAMILY | BIOPHYSICS | MUTATION | PROTEASOME | DEGRADATION | ENDOPLASMIC-RETICULUM | ASSOCIATION | Ubiquitin | Medical colleges | Lysine | Proteolysis | Biomedical engineering | Protein binding
Journal Article
11.
Full Text
A TRIM32-AMBRA1-ULK1 complex initiates the autophagy response in atrophic muscle cells
Autophagy, ISSN 1554-8627, 09/2019, Volume 15, Issue 9, pp. 1674 - 1676
The Ser/Thr protein kinase ULK1 is an upstream macroautophagy/autophagy regulator that is rapidly activated to ensure a proper adaptive response to stress...
muscular dystrophy | unanchored polyubiquitin | ULK1 | AMBRA1 | muscle atrophy | TRIM32 | Tripartite Motif Protein | CELL BIOLOGY
muscular dystrophy | unanchored polyubiquitin | ULK1 | AMBRA1 | muscle atrophy | TRIM32 | Tripartite Motif Protein | CELL BIOLOGY
Journal Article
PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS, ISSN 1000-3282, 09/2019, Volume 46, Issue 9, pp. 845 - 857
Protein ubiquitination is one of the most versatile post-translational modifications, and is widely involved in multiple cellular processes including protein...
LOCALIZATION | ACTIVATION | POLYUBIQUITIN | SPECIFICITY | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | antibody library technique | ubiquitin | MASS-SPECTROMETRY | ubiquitin chains | BIOPHYSICS | ubiquitination | UBIQUITYLATION | ubiquitin linkage-specific antibodies | DEGRADATION | CHEMICAL-SYNTHESIS | PROTEINS
LOCALIZATION | ACTIVATION | POLYUBIQUITIN | SPECIFICITY | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | antibody library technique | ubiquitin | MASS-SPECTROMETRY | ubiquitin chains | BIOPHYSICS | ubiquitination | UBIQUITYLATION | ubiquitin linkage-specific antibodies | DEGRADATION | CHEMICAL-SYNTHESIS | PROTEINS
Journal Article
Journal of Neurochemistry, ISSN 0022-3042, 09/2019, Volume 150, Issue 6, pp. 776 - 786
The SH3 and multiple ankyrin repeat domains 3 (Shank3) proteins are core organizers of the postsynaptic density in neuronal excitatory synapses, and their...
Lys63‐linked polyubiquitin chain | Shank3 | striatum | Cyld | deubiquitinase | Proteins | Nervous system diseases | Genetic engineering | Analysis | Mental disorders | Synaptogenesis | Disorders | Transgenic mice | Chains | Neurodevelopmental disorders | Density | Substrates | Domains | Neostriatum | Ankyrin | Postsynaptic density | Synapses
Lys63‐linked polyubiquitin chain | Shank3 | striatum | Cyld | deubiquitinase | Proteins | Nervous system diseases | Genetic engineering | Analysis | Mental disorders | Synaptogenesis | Disorders | Transgenic mice | Chains | Neurodevelopmental disorders | Density | Substrates | Domains | Neostriatum | Ankyrin | Postsynaptic density | Synapses
Journal Article
Trends in Cell Biology, ISSN 0962-8924, 09/2019, Volume 29, Issue 9, pp. 704 - 716
Ubiquitin chains of distinct topologies control the stability, interactions, or localization of many proteins in eukaryotic cells, and thus play an essential...
protein quality control | ubiquitin code | ubiquitin | branched ubiquitin chain | ANAPHASE-PROMOTING COMPLEX | ACTIVATION | MULTIUBIQUITIN CHAIN | MECHANISM | SPECIFICITY | RECOGNITION | DEGRADATION | POLYUBIQUITIN CHAIN | BINDING | REVEALS | CELL BIOLOGY | Ubiquitin | Cells | Signaling | Information transfer | Chain branching | Control stability | Topology | Localization
protein quality control | ubiquitin code | ubiquitin | branched ubiquitin chain | ANAPHASE-PROMOTING COMPLEX | ACTIVATION | MULTIUBIQUITIN CHAIN | MECHANISM | SPECIFICITY | RECOGNITION | DEGRADATION | POLYUBIQUITIN CHAIN | BINDING | REVEALS | CELL BIOLOGY | Ubiquitin | Cells | Signaling | Information transfer | Chain branching | Control stability | Topology | Localization
Journal Article
Seminars in Cell and Developmental Biology, ISSN 1084-9521, 09/2019, Volume 93, pp. 125 - 135
The balance between cell survival and cell death is often lost in human pathologies such as inflammation and cancer. Autophagy plays a critical role in cell...
Ubiquitin | Inflammation | E3 ligase | Cell death | Deubiquitinase | Autophagy | APOPTOSIS | SPATA2 LINKS CYLD | POLYUBIQUITIN | PROTEIN | LINEAR UBIQUITINATION | DEVELOPMENTAL BIOLOGY | CELL BIOLOGY | INDUCED GENE ACTIVATION | ULK1 UBIQUITYLATION | NF-KAPPA-B | MOLECULAR-BASIS | LIGASE | Post-translational modification | Biochemistry | Proteases | Ligases | USP, ubiquitin-specific protease | IAP, inhibitors of apoptosis proteins | TRAIL, TNF-related apoptosis inducing ligand | TNF, tumor necrosis factor | 1B-light chain 3 | UPS, ubiquitin-proteasome system | ATG, autophagy-related | PTM, posttranslational modification | DUB, deubiquitinase | CYLD, cylindromatosis | LC3, microtubule-associated protein 1 A | UBD, ubiquitin-binding domain | LUBAC, linear ubiquitin chain assembly complex
Ubiquitin | Inflammation | E3 ligase | Cell death | Deubiquitinase | Autophagy | APOPTOSIS | SPATA2 LINKS CYLD | POLYUBIQUITIN | PROTEIN | LINEAR UBIQUITINATION | DEVELOPMENTAL BIOLOGY | CELL BIOLOGY | INDUCED GENE ACTIVATION | ULK1 UBIQUITYLATION | NF-KAPPA-B | MOLECULAR-BASIS | LIGASE | Post-translational modification | Biochemistry | Proteases | Ligases | USP, ubiquitin-specific protease | IAP, inhibitors of apoptosis proteins | TRAIL, TNF-related apoptosis inducing ligand | TNF, tumor necrosis factor | 1B-light chain 3 | UPS, ubiquitin-proteasome system | ATG, autophagy-related | PTM, posttranslational modification | DUB, deubiquitinase | CYLD, cylindromatosis | LC3, microtubule-associated protein 1 A | UBD, ubiquitin-binding domain | LUBAC, linear ubiquitin chain assembly complex
Journal Article
BREEDING SCIENCE, ISSN 1344-7610, 2019, Volume 69, Issue 3, pp. 536 - 544
The chrysanthemum (Chrysanthemum morifolium) is one of the most popular ornamental plants in the world. Genetic transformation is a promising tool for...
promoter activity | parsley | AGRONOMY | POLYUBIQUITIN GENES | BETA-GLUCURONIDASE | ARABIDOPSIS | Chrysanthemum morifolium | gene expression | GENETIC-TRANSFORMATION | PLANT SCIENCES | Ubiquitin | Leaves | Genetic transformation | Plant physiology | Cultivation | Actin | Ornamental plants | Viruses | Durability | Genomes | Promoters | Note
promoter activity | parsley | AGRONOMY | POLYUBIQUITIN GENES | BETA-GLUCURONIDASE | ARABIDOPSIS | Chrysanthemum morifolium | gene expression | GENETIC-TRANSFORMATION | PLANT SCIENCES | Ubiquitin | Leaves | Genetic transformation | Plant physiology | Cultivation | Actin | Ornamental plants | Viruses | Durability | Genomes | Promoters | Note
Journal Article
NATURE, ISSN 0028-0836, 08/2019, Volume 572, Issue 7770, pp. 533 - 533
Protein ubiquitination is a multi-functional post-translational modification that affects all cellular processes. Its versatility arises from architecturally...
PARKIN | COMPLEX | POLYUBIQUITIN | MECHANISM | SPECIFICITY | PHOSPHORYLATION | ACETYLATION | MULTIDISCIPLINARY SCIENCES | SPECTROMETRY ENABLES CHARACTERIZATION | MOLECULAR-BASIS | REVEALS | Ubiquitin | Structure | Analysis | Proteomics | Post-translational modification | Proteases | Mass spectrometry | Residues | Enzymes | Phosphorylation | Peptides | Chain branching | Mass spectroscopy | Mapping | Substrates | Complexity | Depolarization | Proteins | Mitochondria | Ubiquitination | Post-translation | Clipping | Scientific imaging | Parkin protein | Acetylation | Polymers | Endoplasmic reticulum | Combinatorial analysis
PARKIN | COMPLEX | POLYUBIQUITIN | MECHANISM | SPECIFICITY | PHOSPHORYLATION | ACETYLATION | MULTIDISCIPLINARY SCIENCES | SPECTROMETRY ENABLES CHARACTERIZATION | MOLECULAR-BASIS | REVEALS | Ubiquitin | Structure | Analysis | Proteomics | Post-translational modification | Proteases | Mass spectrometry | Residues | Enzymes | Phosphorylation | Peptides | Chain branching | Mass spectroscopy | Mapping | Substrates | Complexity | Depolarization | Proteins | Mitochondria | Ubiquitination | Post-translation | Clipping | Scientific imaging | Parkin protein | Acetylation | Polymers | Endoplasmic reticulum | Combinatorial analysis
Journal Article