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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 of cellular and molecular medicine, ISSN 1582-1838, 2018, Volume 22, Issue 12, pp. 6039 - 6054
...; however, the pathogenic mechanism of this organism remains unclear. Tp92 is the only T. pallidum outer membrane protein that has structural features similar to the outer membrane proteins of other Gram... 
pyroptosis | Tp92 | apoptosis | membrane protein | CD14 | IL‐8 | TLR2 | Treponema pallidum | IL-8 | MEDICINE, RESEARCH & EXPERIMENTAL | ACTIVATION | RECEPTOR | MONOCYTIC CELLS | CELL BIOLOGY | BORRELIA-BURGDORFERI LIPOPROTEINS | INNATE IMMUNE-RESPONSES | NF-KAPPA-B | TLR4 | PATHWAY DISTINCT | Interleukin-8 - genetics | Toll-Like Receptor 2 - genetics | Leukemia, Monocytic, Acute - pathology | Humans | Antigens, Surface - genetics | Bacterial Proteins - genetics | Leukemia, Monocytic, Acute - microbiology | Recombinant Proteins - genetics | Signal Transduction - genetics | Leukemia, Monocytic, Acute - genetics | Leukocytes, Mononuclear - pathology | Syphilis - microbiology | Cell Death - genetics | Host-Pathogen Interactions - genetics | NF-kappa B - genetics | Caspase 1 - genetics | Treponema pallidum - genetics | Syphilis - genetics | Syphilis - pathology | Cell Line, Tumor | Lipopolysaccharide Receptors - genetics | Cytokines - genetics | Leukocytes, Mononuclear - microbiology | Treponema pallidum - pathogenicity | Interleukins | Cell death | Syphilis | Leukemia | Biochemistry | Protein kinases | Membrane proteins | Sexually transmitted diseases--STD | Mortality | Interleukin | Outer membrane proteins | Globus pallidus | Caspase | Leukocytes (mononuclear) | Kinases | CD14 antigen | Proteins | Monocytes | Protein kinase | Tumor necrosis factor | TLR2 protein | Toll-like receptors | Peripheral blood mononuclear cells | Monocyte chemoattractant protein 1 | Tumors | Immune system | Apoptosis | Original
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 0027-8424, 2/2011, Volume 108, Issue 6, pp. 2486 - 2491
Journal Article