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Science (American Association for the Advancement of Science), ISSN 1095-9203, 2018, Volume 362, Issue 6416, pp. 829 - 834
...-barrel assembly machinery. We observed efflux pumps bridging inner and outer membranes, and from inner membranes we identified a pentameric pore of TonB, as well as the protein-conducting channel SecYEG in association with F F... 
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 | OUTER-MEMBRANE | NMR | OXIDASE | STRUCTURAL BASIS | MULTIDISCIPLINARY SCIENCES | LIPIDS | SUBUNIT | 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
Journal Article
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 2018, Volume 293, Issue 43, pp. 16778 - 16790
Cytochromes c are ubiquitous proteins, essential for life in most organisms. Their distinctive characteristic is the covalent attachment of heme to their polypeptide chain... 
post-translational modification (PTM) | CHAPERONE CCME | cytochrome c maturation | BACTERIA | APOCYTOCHROME-C | heme | NMR-SPECTROSCOPY | BIOCHEMISTRY & MOLECULAR BIOLOGY | CcmE | ESCHERICHIA-COLI | TRAFFICKING | CcmC | protein-protein interactions | BIOGENESIS SYSTEM | PATHWAY | nuclear magnetic resonance (NMR) | Gram-negative bacteria | System I | cytochrome c | BINDING SITE | LIGATION COMPLEX | Apoproteins - chemistry | Hemeproteins - genetics | Heme - metabolism | Crystallography, X-Ray | Cytochromes c - genetics | Cytochromes c - chemistry | Heme - chemistry | Heme - genetics | Hemeproteins - chemistry | Escherichia coli - metabolism | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Escherichia coli - growth & development | Binding Sites | Apoproteins - metabolism | Bacterial Outer Membrane Proteins - genetics | Mutagenesis, Site-Directed | Hemeproteins - metabolism | Membrane Proteins - genetics | Cytochromes c - metabolism | Bacterial Outer Membrane Proteins - chemistry | Escherichia coli Proteins - metabolism | Bacterial Outer Membrane Proteins - metabolism | Membrane Proteins - chemistry | Escherichia coli - genetics | Apoproteins - genetics | Escherichia coli Proteins - genetics | Protein Conformation | Escherichia coli Proteins - chemistry | Amino Acid Substitution | Index Medicus | Bioenergetics
Journal Article
Journal Article
Journal Article
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 2018, Volume 293, Issue 8, pp. 2959 - 2973
Most proteins that reside in the bacterial outer membrane (OM) have a distinctive "beta-barrel" architecture, but the assembly of these proteins is poorly understood... 
IN-VITRO | GRAM-NEGATIVE BACTERIA | CONFORMATIONAL-CHANGES | BETA-BARREL | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | AUTOTRANSPORTER | BARREL ASSEMBLY MACHINERY | YAET COMPLEX | SECRETION | MOLECULAR-BASIS | Protein Multimerization | Porins - metabolism | Recombinant Fusion Proteins - metabolism | Lipid-Linked Proteins - metabolism | Escherichia coli - metabolism | Serine Endopeptidases - genetics | Porins - chemistry | Protein Interaction Domains and Motifs | Peptide Fragments - genetics | Bacterial Outer Membrane Proteins - genetics | Protein Conformation, alpha-Helical | Peptide Fragments - metabolism | Porins - genetics | Bacterial Outer Membrane Proteins - chemistry | Escherichia coli Proteins - metabolism | Serine Endopeptidases - chemistry | Recombinant Fusion Proteins - chemistry | Escherichia coli - chemistry | Protein Folding | Protein Transport | Peptide Fragments - chemistry | Bacterial Outer Membrane Proteins - metabolism | Protein Conformation, beta-Strand | Escherichia coli Proteins - genetics | Serine Endopeptidases - metabolism | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Liposomes | Escherichia coli Proteins - chemistry | Lipid-Linked Proteins - genetics | Lipid-Linked Proteins - chemistry | outer membrane | molecular chaperone | beta-barrel proteins | Bam complex | protein-lipid interaction | Membrane Biology | membrane protein | protein folding | Gram-negative bacteria
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2009, Volume 106, Issue 4, pp. 1045 - 1050
Gram-negative bacteria use specific heme uptake systems, relying on outer membrane receptors and excreted heme-binding proteins (hemophores... 
Proteins | Molecules | Receptors | Carrier proteins | Serratia marcescens | Crystallization | Ligands | Titration | Binding sites | Crystal structure | Protein complex | Heme binding | Membrane protein | Membrane transport | Iron uptake | HEMOGLOBIN | PROTEIN | heme binding | HASA | MULTIDISCIPLINARY SCIENCES | iron uptake | ACQUISITION | IRON | SERRATIA-MARCESCENS | protein complex | HAEMOPHORE | TRANSPORT | PURIFICATION | membrane protein | membrane transport | BINDING | Apoproteins - chemistry | Heme - metabolism | Protein Structure, Secondary | Hemeproteins - metabolism | Bacterial Proteins - chemistry | Models, Molecular | Receptors, Cell Surface - metabolism | Crystallography, X-Ray | Serratia marcescens - chemistry | Carrier Proteins - metabolism | Biological Transport | Heme - chemistry | Membrane Proteins - chemistry | Hemeproteins - chemistry | Surface Properties | Bacterial Proteins - metabolism | Calorimetry | Carrier Proteins - chemistry | Receptors, Cell Surface - chemistry | Cell Membrane - metabolism | Membrane Proteins - metabolism | Apoproteins - metabolism | Hemoproteins | Physiological aspects | Gram-negative bacteria | Research | Properties | Structure | Membrane proteins | Protein binding | Cell Membrane | Receptors, Cell Surface | Bacterial Proteins | Membrane Proteins | Life Sciences | Microbiology and Parasitology | Apoproteins | Heme | Hemeproteins | Carrier Proteins | Biological Sciences
Journal Article