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Science (American Association for the Advancement of Science), ISSN 1095-9203, 11/2018, Volume 362, Issue 6416, pp. 829 - 834
Membrane proteins reside in lipid bilayers and are typically extracted from this environment for study, which often compromises their integrity... 
adenine nucleotide translocase | protein interaction | bacterial outer membrane | porin | proton transporting adenosine triphosphate synthase | Escherichia coli | porosity | mitochondrial membrane | fatty acid | lipid | beta sheet | protein assembly | article | taurine cattle | protein localization | chaperone | membrane protein | lipid bilayer | mass spectrometry | nonhuman | priority journal | membrane binding | Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Molecular Chaperones - metabolism | Bacterial Proteins - chemistry | Porins - metabolism | Molecular Chaperones - chemistry | Proteome - chemistry | Adenine Nucleotide Translocator 1 - chemistry | Cattle | Mass Spectrometry | Mitochondrial Membranes - chemistry | Porins - chemistry | Membrane Proteins - metabolism | SEC Translocation Channels - chemistry | SEC Translocation Channels - metabolism | Bacterial Outer Membrane Proteins - chemistry | Escherichia coli Proteins - metabolism | Adenine Nucleotide Translocator 1 - metabolism | Mitochondrial Proton-Translocating ATPases - chemistry | Mitochondrial Proton-Translocating ATPases - metabolism | Mitochondrial Membranes - metabolism | Animals | Bacterial Outer Membrane Proteins - metabolism | Membrane Proteins - chemistry | Protein Conformation, beta-Strand | Bacterial Proteins - metabolism | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Escherichia coli Proteins - chemistry | Proteome - metabolism | Physiological aspects | Mass spectrometry | Methods | Membrane proteins | Stoichiometry | Membranes | Outer membranes | Lipids | Translocase | Chaperones | Lipid bilayers | Proteins | Mitochondria | E coli | Bacteria | Assemblies | Adenosine triphosphate | Efflux | Inner membranes | Adenosine | Adenosine diphosphate | Membrane vesicles | Mass spectroscopy | Electron microscopy | Fatty acids | Organic chemistry | Scientific imaging | Dimers | Disruption | Proteomes | ATP | Ejection | Index Medicus
Journal Article
Annual review of biochemistry, ISSN 0066-4154, 6/2017, Volume 86, Issue 1, pp. 685 - 714
.... The protein import machineries of the mitochondrial membranes and aqueous compartments reveal a remarkable variability of mechanisms for protein recognition, translocation, and sorting... 
outer membrane | mitochondrial architecture | inner membrane | protein sorting | translocase | preprotein | Inner membrane | Preprotein | Protein sorting | Translocase | Outer membrane | Mitochondrial architecture | Protein Precursors - chemistry | Humans | Eukaryotic Cells - metabolism | Isoenzymes - chemistry | Mitochondrial Proteins - genetics | Mitochondria - ultrastructure | Mitochondrial Membrane Transport Proteins - genetics | Organelle Biogenesis | Isoenzymes - metabolism | Mitochondrial Proteins - metabolism | Eukaryotic Cells - ultrastructure | Carrier Proteins - chemistry | Protein Conformation, alpha-Helical | Gene Expression | Mitochondrial Membrane Transport Proteins - chemistry | Mitochondrial Membrane Transport Proteins - metabolism | Protein Precursors - genetics | Isoenzymes - genetics | Mitochondria - metabolism | Mitochondrial Membranes - metabolism | Protein Precursors - metabolism | Protein Transport | Carrier Proteins - genetics | Carrier Proteins - metabolism | Protein Conformation, beta-Strand | Mitochondrial Membranes - ultrastructure | Mitochondrial Proteins - chemistry | Physiological aspects | Mitochondria | Genetic aspects | Research | Carrier proteins | Translocation | Membranes | Integration | Homeostasis | Imports | Metabolism | Organelles | Cytosol | Proteins | Molecular modelling | Compartments | Quality control | Protein transport | Index Medicus
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 10/2018, Volume 293, Issue 43, pp. 16778 - 16790
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... 
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | 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 | Index Medicus | 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
The Journal of biological chemistry, ISSN 1083-351X, 02/2018, Volume 293, Issue 8, pp. 2959 - 2973
Journal Article