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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
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2019, Volume 116, Issue 28, pp. 13952 - 13957
...)-family proteins are essential for membrane fusion in exocytic and endocytic trafficking... 
COMPLEX | YEAST VACUOLE | DOCKING | MULTIDISCIPLINARY SCIENCES | HOPS | RELEASE | SACCHAROMYCES-CEREVISIAE | REGULATORY LIPIDS | membrane fusion | SNARE | yeast vacuoles | MEMBRANE-FUSION | SEC17P | PROTEINS | Membrane Fusion Proteins - chemistry | Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins - genetics | Saccharomyces cerevisiae - genetics | Membrane Fusion - genetics | Exocytosis - genetics | Glutathione Peroxidase - chemistry | Membrane Fusion Proteins - genetics | Protein Multimerization - genetics | Vacuoles - chemistry | Phosphatidylinositols - metabolism | Endocytosis - genetics | Vacuoles - genetics | Phosphatidylinositols - chemistry | R-SNARE Proteins - genetics | Vesicular Transport Proteins - genetics | Recombinant Proteins - chemistry | Vesicular Transport Proteins - chemistry | Saccharomyces cerevisiae Proteins - genetics | R-SNARE Proteins - chemistry | Glutathione Peroxidase - genetics | Protein Transport - genetics | Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins - chemistry | Adenosine Triphosphatases - chemistry | Adenosine Triphosphatases - genetics | Adenosine Triphosphate - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Yeasts | Membrane fusion | Phosphoinositides | Membranes | Yeast | SNAP receptors | Tethering | Proteins | Domains | Fusion protein | Protein transport | Dismantling | Ethylmaleimide | ATP | Assembly | Adenosine triphosphate | N-Ethylmaleimide | Biological Sciences
Journal Article
Protein expression and purification, ISSN 1046-5928, 2015, Volume 116, pp. 42 - 49
•We present a set of protein expression vectors to screen for optimal fusion tags... 
Scytovirin | SUMO system | Solubility enhancement tag | TonB | Protein ligation | Fusion proteins | Ulp1 protease | SPLICING ELEMENT | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | AFFINITY TAGS | BIOCHEMICAL RESEARCH METHODS | LIGATION | IN-VITRO | MULTIDOMAIN PROTEIN | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | RECOMBINANT PROTEINS | C-TERMINAL DOMAIN | INTEIN | Cyanobacteria - genetics | Cysteine Endopeptidases - chemistry | Recombinant Fusion Proteins - isolation & purification | Small Ubiquitin-Related Modifier Proteins - isolation & purification | Saccharomyces cerevisiae - genetics | Cyanobacteria - chemistry | Bacterial Proteins - chemistry | Helicobacter pylori - genetics | Lectins - isolation & purification | Small Ubiquitin-Related Modifier Proteins - genetics | Proteolysis | Base Sequence | Cloning, Molecular - methods | Carrier Proteins - chemistry | Saccharomyces cerevisiae Proteins - isolation & purification | Lectins - chemistry | Pseudomonas - genetics | Membrane Proteins - isolation & purification | Genetic Vectors - chemistry | Helicobacter pylori - chemistry | Membrane Proteins - genetics | Bacterial Proteins - genetics | Solubility | Recombinant Fusion Proteins - chemistry | Saccharomyces cerevisiae Proteins - genetics | Escherichia coli - chemistry | Genetic Vectors - genetics | Saccharomyces cerevisiae - chemistry | Carrier Proteins - genetics | Membrane Proteins - chemistry | Cysteine Endopeptidases - isolation & purification | Escherichia coli - genetics | Small Ubiquitin-Related Modifier Proteins - chemistry | Carrier Proteins - isolation & purification | Cysteine Endopeptidases - genetics | Recombinant Fusion Proteins - genetics | Lectins - genetics | Bacterial Proteins - isolation & purification | Pseudomonas - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Antiviral agents | Sumo | Proteases | Glutathione transferase | Escherichia coli | Nuclear magnetic resonance spectroscopy | Sugars | Protein binding
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
Science (American Association for the Advancement of Science), ISSN 0036-8075, 3/2012, Volume 335, Issue 6074, pp. 1355 - 1359
Journal Article
PLoS ONE, ISSN 1932-6203, 10/2012, Volume 7, Issue 10, p. e46039
...(2) adrenergic receptor (beta(2)AR), a G-protein coupled receptor (GPCR) for catecholamines. We demonstrate that the N-terminal fused T4L is sufficiently rigid... 
COMPLEX | ANTAGONIST | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | GPCR | BETA-ADRENERGIC RECEPTOR | MUSCARINIC ACETYLCHOLINE-RECEPTOR | Protein Engineering - methods | Receptors, G-Protein-Coupled - metabolism | Humans | Molecular Sequence Data | Crystallography, X-Ray | Tritium | Recombinant Fusion Proteins - metabolism | Viral Proteins - metabolism | Receptors, Adrenergic, beta-2 - chemistry | Sf9 Cells | Bacteriophage T4 - enzymology | Binding Sites | Binding, Competitive | Protein Structure, Tertiary | Amino Acid Sequence | Protein Structure, Secondary | Muramidase - chemistry | Receptors, Adrenergic, beta-2 - genetics | Viral Proteins - chemistry | Muramidase - genetics | Crystallization | Models, Molecular | Viral Proteins - genetics | Muramidase - metabolism | Recombinant Fusion Proteins - chemistry | Receptors, Adrenergic, beta-2 - metabolism | Animals | Dihydroalprenolol - metabolism | Protein Binding | Recombinant Fusion Proteins - genetics | Dihydroalprenolol - chemistry | Protein Conformation | Receptors, G-Protein-Coupled - genetics | Mutation | Receptors, G-Protein-Coupled - chemistry | Proteins | Lysozyme | G proteins | Protein engineering | G protein-coupled receptors | Crystal lattices | Science | Catecholamines | Crystallography | Medicine | Signaling | N-Terminus | Chemical bonds | Adrenergic receptors | Physiology | Crystal structure
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
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