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Protein engineering, ISSN 0269-2139, 1986
Journal
Immunotechnology, ISSN 1380-2933, 1995
Journal
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
Nature structural & molecular biology, ISSN 1545-9993, 08/2011, Volume 18, Issue 8, pp. 941 - 946
.... Recent studies indicate that the same SNARE-binding protein, complexin (CPX), can act either as a facilitator or as an inhibitor of membrane fusion, constituting a controversial dilemma... 
BIOPHYSICS | FORCE | NEUROTRANSMITTER RELEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | DISTINCT DOMAINS | SWITCH | BINDING | CELL BIOLOGY | Adaptor Proteins, Signal Transducing - chemistry | Humans | Vesicle-Associated Membrane Protein 2 - physiology | Syntaxin 1 - metabolism | Adaptor Proteins, Vesicular Transport - metabolism | Nerve Tissue Proteins - chemistry | SNARE Proteins - chemistry | Vesicle-Associated Membrane Protein 2 - chemistry | Adaptor Proteins, Vesicular Transport - chemistry | Syntaxin 1 - chemistry | Binding Sites | Protein Structure, Tertiary | Nerve Tissue Proteins - physiology | Adaptor Proteins, Vesicular Transport - physiology | SNARE Proteins - physiology | Models, Molecular | Rats | Synaptosomal-Associated Protein 25 - chemistry | Nerve Tissue Proteins - metabolism | Adaptor Proteins, Signal Transducing - physiology | Animals | Synaptosomal-Associated Protein 25 - physiology | Mice | Synaptosomal-Associated Protein 25 - metabolism | Lipid Bilayers - metabolism | Adaptor Proteins, Signal Transducing - metabolism | Membrane Fusion - physiology | Vesicle-Associated Membrane Protein 2 - metabolism | SNARE Proteins - metabolism | Syntaxin 1 - physiology | Cell hybridization | Physiological aspects | Research | Exocytosis | Membrane proteins | Proteins | Neurotransmitters | Membranes | Molecular biology | Vesicle-Associated Membrane Protein 2 | Membrane Fusion | Biochemistry, Molecular Biology | Nerve Tissue Proteins | Biophysics | Cellular Biology | Adaptor Proteins, Vesicular Transport | Life Sciences | Adaptor Proteins, Signal Transducing | Lipid Bilayers | Syntaxin 1 | Synaptosomal-Associated Protein 25 | SNARE Proteins
Journal Article
Molecular and Cellular Biology, ISSN 0270-7306, 10/2007, Volume 27, Issue 19, pp. 6581 - 6592
Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
YEAST | GENE | ATPASE | NUCLEAR EXPORT | GLOBAL ANALYSIS | REQUIRES | MATURATION | RIBOSOMAL-SUBUNIT BIOGENESIS | SACCHAROMYCES-CEREVISIAE | PRE-RIBOSOME | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL BIOLOGY | Ribosomes - metabolism | Cytoplasm - metabolism | Phosphoproteins - metabolism | GTP-Binding Proteins - genetics | Recombinant Fusion Proteins - metabolism | Ribosome Subunits, Large, Eukaryotic - metabolism | Intermediate Filament Proteins - genetics | Nuclear Proteins - genetics | Ribosome Subunits, Large, Eukaryotic - genetics | Protein Precursors - genetics | Ribosomes - chemistry | Adenosine Triphosphatases - metabolism | Nuclear Proteins - metabolism | Phosphoproteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Protein Precursors - metabolism | Peptide Initiation Factors - metabolism | Carrier Proteins - genetics | Peptide Initiation Factors - genetics | Carrier Proteins - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Recombinant Fusion Proteins - genetics | Saccharomyces cerevisiae - enzymology | Adenosine Triphosphatases - genetics | Biological Transport - physiology | Intermediate Filament Proteins - metabolism | GTP-Binding Proteins - metabolism | Ribosomal Proteins | Quantitative Methods | Peptide Initiation Factors | Biochemistry, Molecular Biology | Ribosomes | Cellular Biology | Recombinant Fusion Proteins | Nuclear Proteins | Life Sciences | Biological Transport | Adenosine Triphosphatases | Phosphoproteins | Protein Precursors | Saccharomyces cerevisiae Proteins | Ribosome Subunits, Large, Eukaryotic | Genetics | GTP-Binding Proteins | Subcellular Processes | Molecular biology | Saccharomyces cerevisiae | Intermediate Filament Proteins | Cytoplasm | Carrier Proteins
Journal Article
Cell Death and Differentiation, ISSN 1350-9047, 01/2007, Volume 14, Issue 1, pp. 128 - 136
All BH3-only proteins, key initiators of programmed cell death, interact tightly with multiple binding partners and have sequences of low complexity, properties that are the hallmark of intrinsically... 
Bcl-2 | intrinsically unstructured | APOPTOSIS | EGL-1 | RECOGNITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | UNFOLDED PROTEINS | DISORDERED PROTEINS | BH3-only | FAMILY | MEMBER | CELL BIOLOGY | STRUCTURAL BASIS | ROLES | molecular recognition | PEPTIDE COMPLEX | Adaptor Proteins, Signal Transducing - chemistry | Recombinant Fusion Proteins - isolation & purification | Adaptor Proteins, Signal Transducing - isolation & purification | Apoptosis Regulatory Proteins - isolation & purification | Proto-Oncogene Proteins - chemistry | Recombinant Fusion Proteins - metabolism | Bcl-2-Like Protein 11 | Apoptosis Regulatory Proteins - genetics | Nuclear Magnetic Resonance, Biomolecular | bcl-Associated Death Protein - metabolism | Membrane Proteins - metabolism | Circular Dichroism | Proto-Oncogene Proteins - isolation & purification | Protein Structure, Tertiary | Proto-Oncogene Proteins - metabolism | bcl-Associated Death Protein - genetics | Membrane Proteins - isolation & purification | Protein Structure, Secondary | bcl-Associated Death Protein - chemistry | Membrane Proteins - genetics | bcl-Associated Death Protein - isolation & purification | Apoptosis Regulatory Proteins - chemistry | Proto-Oncogene Proteins - genetics | Recombinant Fusion Proteins - chemistry | Protein Folding | Apoptosis Regulatory Proteins - metabolism | Animals | Membrane Proteins - chemistry | Adaptor Proteins, Signal Transducing - genetics | Recombinant Fusion Proteins - genetics | Mice | Adaptor Proteins, Signal Transducing - metabolism
Journal Article
The Journal of biological chemistry, ISSN 0021-9258, 12/2010, Volume 285, Issue 52, pp. 40573 - 40580
Secretion of the Escherichia coli toxin hemolysin A (HlyA) is catalyzed by the membrane protein complex HlyB-HlyD-TolC and requires a secretion sequence located within the last 60 amino acids of HlyA... 
SIGNAL | ANTIFOLDING ACTIVITY | SECB CHAPERONE | TRANSPORTER | MALTOSE-BINDING PROTEIN | MEMBRANE TRANSLOCATION | PATHWAY | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | EXPORT | EXPRESSION | Hemolysin Proteins - genetics | Bacterial Proteins - genetics | Escherichia coli Proteins - metabolism | Hemolysin Proteins - secretion | Multiprotein Complexes - genetics | Mutation, Missense | Bacterial Secretion Systems - physiology | Protein Folding | Carrier Proteins - genetics | Multiprotein Complexes - metabolism | Carrier Proteins - metabolism | Bacterial Outer Membrane Proteins - metabolism | Escherichia coli - genetics | Membrane Transport Proteins - genetics | Escherichia coli - metabolism | Escherichia coli Proteins - genetics | Escherichia coli Proteins - secretion | Bacterial Proteins - metabolism | Membrane Transport Proteins - metabolism | Periplasmic Binding Proteins - genetics | Bacterial Outer Membrane Proteins - genetics | Hemolysin Proteins - metabolism | Amino Acid Substitution | Periplasmic Binding Proteins - metabolism | Bacterial Outer Membrane Proteins | Bacterial Secretion Systems | Hemolysin Proteins | Escherichia coli | Multiprotein Complexes | Biochemistry, Molecular Biology | Bacterial Proteins | Life Sciences | Microbiology and Parasitology | Escherichia coli Proteins | Membrane Transport Proteins | Periplasmic Binding Proteins | Carrier Proteins | Membrane Proteins | Fusion Protein | Secretion | Membrane Biology | ABC Transporter
Journal Article
Nature biotechnology, ISSN 1546-1696, 2002, Volume 20, Issue 6, pp. 619 - 622
Journal Article
Molecular cell, ISSN 1097-2765, 2016, Volume 64, Issue 2, pp. 236 - 250
Caspase-8 activation can be triggered by death receptor-mediated formation of the death-inducing signaling complex (DISC) and by the inflammasome adaptor ASC.... 
caspase-8 | DED | MC159 | cFLIP | DISC | Fas | death domain | FADD | vFLIP | filament | APOPTOSIS | ACTIVATION | IMMUNE-SYSTEM | INHIBITION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RECEPTOR | UNIFIED MODEL | EFFECTOR DOMAIN | CELL-DEATH | CELL BIOLOGY | Death Domain Receptor Signaling Adaptor Proteins - chemistry | Apoptosis - drug effects | Cytoskeletal Proteins - genetics | Humans | Caspase 8 - metabolism | Caspase 8 - chemistry | CASP8 and FADD-Like Apoptosis Regulating Protein - chemistry | Death Domain Receptor Signaling Adaptor Proteins - genetics | Recombinant Fusion Proteins - metabolism | Viral Proteins - metabolism | Caspase 8 - genetics | Transfection | Cytoskeletal Proteins - metabolism | Protein Interaction Domains and Motifs | Binding Sites | CASP8 and FADD-Like Apoptosis Regulating Protein - metabolism | Death Effector Domain | Fas-Associated Death Domain Protein - genetics | Amino Acid Sequence | Protein Conformation, alpha-Helical | Gene Expression | CASP8 and FADD-Like Apoptosis Regulating Protein - genetics | Jurkat Cells | Viral Proteins - chemistry | Fas-Associated Death Domain Protein - metabolism | Viral Proteins - genetics | fas Receptor - pharmacology | Cytoskeletal Proteins - chemistry | Recombinant Fusion Proteins - chemistry | Plasmids - metabolism | Fas-Associated Death Domain Protein - chemistry | Cryoelectron Microscopy | Sequence Homology, Amino Acid | Sequence Alignment | Protein Conformation, beta-Strand | CARD Signaling Adaptor Proteins | Plasmids - chemistry | Protein Binding | Recombinant Fusion Proteins - genetics | Death Domain Receptor Signaling Adaptor Proteins - metabolism | Autoimmunity | Medical colleges | Skin diseases | Molecular biology | Analysis | Index Medicus
Journal Article
The 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