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Cancer Cell, ISSN 1535-6108, 2010, Volume 17, Issue 6, pp. 609 - 621
MLL is involved in chromosomal rearrangements that generate fusion proteins with deregulated transcriptional activity... 
CELLCYCLE | DNA | HUMDISEASE | RNA-POLYMERASE-II | CHROMOSOMAL TRANSLOCATIONS | TARGET GENES | STEM-CELLS | HISTONE H2B | ONCOLOGY | H3 METHYLATION | TUMOR-SUPPRESSOR PROTEIN | LEUKEMIA | EXPRESSION | TRANSCRIPTIONAL ELONGATION | CELL BIOLOGY | Myeloid Cells - cytology | Myeloid-Lymphoid Leukemia Protein - metabolism | Oncogene Proteins, Fusion - metabolism | Transcriptional Activation - genetics | Protein Interaction Domains and Motifs - physiology | Humans | Leukemia - metabolism | Phosphoproteins - metabolism | DNA-Binding Proteins - metabolism | Cell Differentiation - genetics | Transfection | RNA Interference | Cell Transformation, Neoplastic - genetics | Tumor Suppressor Proteins - genetics | Neoplasm Proteins - genetics | Nuclear Proteins - genetics | Leukemia - genetics | Recombinant Proteins - metabolism | Cell Line | Tumor Suppressor Proteins - metabolism | Sequence Deletion - physiology | Mice, Inbred C57BL | Gene Expression Regulation | Nuclear Proteins - metabolism | Recombinant Proteins - genetics | DNA - metabolism | Phosphoproteins - genetics | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Cell Transformation, Neoplastic - metabolism | Down-Regulation - genetics | Homeodomain Proteins - genetics | Transcription Factors - metabolism | Carrier Proteins - genetics | Transcription, Genetic - physiology | Animals | Carrier Proteins - metabolism | Models, Biological | Myeloid-Lymphoid Leukemia Protein - genetics | Oncogene Proteins, Fusion - genetics | HL-60 Cells | Myeloid Cells - metabolism | Mice | HeLa Cells | Myeloid Ecotropic Viral Integration Site 1 Protein | Cell Transformation, Neoplastic - pathology | Protein Binding - physiology | Proteins | RNA | Gene expression
Journal Article
Cell (Cambridge), ISSN 0092-8674, 2017, Volume 168, Issue 5, pp. 904 - 915.e10
... membrane fusion proteins. We further show that targeting the segment corresponding to the fusion loop by mutagenesis or by antibodies blocks gamete fusion... 
Chlamydomonas reinhardtii | gamete fusion | crystal structure | sexual reproduction | virus entry | HAP2 | transmission-blocking malaria vaccine | lipid insertion | class II fusion protein | membrane fusion | SEXUAL REPRODUCTION | VIRUS ENVELOPE PROTEIN | FERTILIZATION | GENE | CRYSTAL-STRUCTURE | MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SEMLIKI-FOREST-VIRUS | GLYCOPROTEIN | GCS1 | CHLAMYDOMONAS | CELL BIOLOGY | Membrane Fusion Proteins - chemistry | Recombinant Proteins - metabolism | Amino Acid Sequence | Plasmodium - metabolism | Plasmodium - cytology | Recombinant Proteins - chemistry | Crystallography, X-Ray | Recombinant Proteins - genetics | Chlamydomonas - metabolism | Protozoan Proteins - genetics | Membrane Fusion Proteins - metabolism | Biological Evolution | Plant Proteins - genetics | Sequence Alignment | Protozoan Proteins - metabolism | Membrane Fusion Proteins - genetics | Plant Proteins - chemistry | Chlamydomonas - cytology | Germ Cells - chemistry | Protein Domains | Protozoan Proteins - chemistry | Plant Proteins - metabolism | Germ Cells - metabolism | Proteins | Viral antibodies | Antibodies | Plants | Cells | Malaria | Malaria vaccine | Crystals | Structure | Recombinant Proteins | Protozoan Proteins | Germ Cells | Membrane Fusion Proteins | Chlamydomonas | Life Sciences | Plasmodium | Plant Proteins
Journal Article
The Journal of experimental medicine, ISSN 1540-9538, 2013, Volume 210, Issue 6, pp. 1251 - 1263
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 37, pp. 15287 - 15300
A remarkable property of the machinery for import of peroxisomal matrix proteins is that it can accept already folded proteins as substrates... 
CONSERVED CYSTEINE | HUMAN PTS1 RECEPTOR | DOCKING PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | CYCLING RECEPTOR | MACHINERY | MEMBRANE-PROTEIN | II SECRETION SYSTEM | AAA PEROXINS | TARGETING SIGNAL RECEPTOR | IMPORT RECEPTOR | Humans | Protein Multimerization | Mutation, Missense | Recombinant Fusion Proteins - metabolism | Biological Transport | Gene Deletion | Receptors, Cytoplasmic and Nuclear - chemistry | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Peptide Fragments - genetics | Repressor Proteins - metabolism | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Repressor Proteins - chemistry | Mutagenesis, Site-Directed | Membrane Proteins - genetics | Solubility | Recombinant Proteins - chemistry | Repressor Proteins - genetics | Receptors, Cytoplasmic and Nuclear - genetics | Recombinant Fusion Proteins - chemistry | Peroxisomes - metabolism | Amino Acid Motifs | Peptide Fragments - chemistry | Membrane Proteins - chemistry | Models, Biological | Peroxisome-Targeting Signal 1 Receptor | Endopeptidase K - metabolism | Mutation | Intracellular Membranes - metabolism | Amino Acid Substitution | Hydrogen-Ion Concentration | Receptors, Cytoplasmic and Nuclear - metabolism | ubiquitylation (ubiquitination) | docking | PEX5 | peroxisome | translocation module | protein import | protein sorting | receptor recycling | PEX14 | Cell Biology
Journal Article
Science (American Association for the Advancement of Science), ISSN 0036-8075, 3/2012, Volume 335, Issue 6074, pp. 1355 - 1359
Journal Article
Molecular cell, ISSN 1097-2765, 2009, Volume 36, Issue 1, pp. 39 - 50
In the largest E3 ligase subfamily, Cul3 binds a BTB domain, and an associated protein-interaction domain such as MATH recruits substrates for ubiquitination... 
PROTEINS | ACTIVATION | PROTEIN | NRF2 | BIOCHEMISTRY & MOLECULAR BIOLOGY | SCF | ADAPTER | DEGRADATION | KEAP1 | DIMERIZATION | BTB DOMAIN | HEDGEHOG | CELL BIOLOGY | Transcription Factors - chemistry | Humans | Crystallography, X-Ray | Drosophila Proteins - metabolism | Mutation - physiology | Protein Multimerization - physiology | Protein Structure, Quaternary - physiology | Ubiquitination - physiology | Peptide Fragments - genetics | Repressor Proteins - metabolism | Amino Acid Sequence | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Repressor Proteins - genetics | Recombinant Fusion Proteins - chemistry | Nuclear Proteins - chemistry | Ubiquitin-Protein Ligases - chemistry | DNA-Binding Proteins - chemistry | Cullin Proteins - chemistry | Peptide Fragments - chemistry | Phosphoprotein Phosphatases - genetics | Consensus Sequence - physiology | Recombinant Fusion Proteins - genetics | Histones - metabolism | Ubiquitin-Protein Ligases - genetics | Drosophila melanogaster | Phosphoprotein Phosphatases - chemistry | Protein Binding - physiology | Adaptor Proteins, Signal Transducing - chemistry | Histones - chemistry | Protein Interaction Domains and Motifs - physiology | Phosphoprotein Phosphatases - metabolism | Recombinant Fusion Proteins - metabolism | DNA-Binding Proteins - metabolism | Cullin Proteins - metabolism | Nuclear Proteins - genetics | Peptide Fragments - metabolism | Repressor Proteins - chemistry | Nuclear Proteins - metabolism | Drosophila Proteins - chemistry | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Cullin Proteins - genetics | Transcription Factors - metabolism | Animals | Histones - genetics | Adaptor Proteins, Signal Transducing - genetics | Drosophila Proteins - genetics | Adaptor Proteins, Signal Transducing - metabolism | Ubiquitin | Chromatin | Phosphatases | Ligases | CHROMATIN | BASIC BIOLOGICAL SCIENCES | SUBSTRATES | FLEXIBILITY | GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE | LIGASES | DIMERS | PHOSPHATASES
Journal Article
Structure, ISSN 0969-2126, 07/2019, Volume 27, Issue 7, pp. 1148 - 1155.e3
Solving protein structures by single-particle cryoelectron microscopy (cryo-EM) has become a crucial tool in structural biology... 
artificial protein | DARPin | aldolase | Electron cryo-microscopy | Single-particle analysis | protein design | CryoEM | platform | cryo-electron microscopy | SYSTEM | DESIGN | BIOPHYSICS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | RESOLUTION | BETA-GALACTOSIDASE | ANTIBODY | ANKYRIN REPEAT PROTEINS | CELL BIOLOGY | Protein Engineering - methods | Humans | Protein Multimerization | Green Fluorescent Proteins - genetics | Single Molecule Imaging | Recombinant Fusion Proteins - metabolism | Single-Chain Antibodies - metabolism | Fructose-Bisphosphate Aldolase - chemistry | Single-Chain Antibodies - genetics | Cloning, Molecular | Escherichia coli - metabolism | Muscle Proteins - metabolism | beta-Galactosidase - metabolism | Protein Interaction Domains and Motifs | beta-Galactosidase - chemistry | Fructose-Bisphosphate Aldolase - metabolism | Green Fluorescent Proteins - chemistry | Binding Sites | Recombinant Proteins - metabolism | Green Fluorescent Proteins - metabolism | Protein Conformation, alpha-Helical | Rabbits | Gene Expression | Genetic Vectors - chemistry | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Recombinant Fusion Proteins - chemistry | Muscle Proteins - genetics | Animals | Protein Conformation, beta-Strand | Escherichia coli - genetics | Protein Binding | Recombinant Fusion Proteins - genetics | Muscle Proteins - chemistry | Fructose-Bisphosphate Aldolase - genetics | beta-Galactosidase - genetics | Cryoelectron Microscopy - methods | Single-Chain Antibodies - chemistry | Proteins | Electron microscopy | Analysis
Journal Article
Molecular cell, ISSN 1097-2765, 2015, Volume 60, Issue 2, pp. 220 - 230
Journal Article