Role of a Highly Conserved Bacterial Protein in Outer Membrane Protein Assembly
By R. Voulhoux, M. Bos, Jeroen Geurtsen, M. Mols, J. Tommassen. Science, 2003
771 citations recorded by the source corpus.
Subfields: Genetics, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/d13a4ef10fa57643217329baaba3827d96835177
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In Genetics
- D. Rapaport
- C. Onufryk
- Ian R. Henderson
- F. Fang
- Carol A. Gross
- D. Kahne
- T. Silhavy
- Marie-Laure V. Crouch
In Molecular Biology
- D. Rapaport
- C. Onufryk
- Ian R. Henderson
- F. Fang
- William C. Wimley
- Carol A. Gross
- D. Kahne
- T. Silhavy
Citations in the corpus
- Folding and assembly of β-barrel membrane proteins (2004, background): “meningitidis, which is an integral protein of the outer membranes of most if not all Gram-negative organisms [57].”
- Type V Protein Secretion Pathway: the Autotransporter Story (2004, background): “Recently, the involvement the surface antigen Omp85 challenged the idea of a spontaneous assembly of outer membrane proteins into the outer membrane (517).”
- The versatile β-barrel membrane protein (2003, background): “In the Escherichia coli genome, there are about 60 proteins, or 1.5% of the total, annotated as known, ‘probable’ or ‘putative’ outer membrane proteins (OMPs).”
- Biogenesis of β-barrel membrane proteins in bacteria and eukaryotes: evolutionary conservation and divergence (2009, background): “Omp85 was suggested to consist of two domains [32], a C-terminal membrane-embedded b-barrel and an N-termi-”
- Importing Mitochondrial Proteins: Machineries and Mechanisms (2009, background): “Sam50 is homologous to BamA, also termed Omp85 or YaeT, which forms the core of the β-barrel assembly machinery of the bacterial outer membrane (Kozjak et al., 2003; Paschen et al., 2003; Voulhoux et al., 2003; Gentle et al., 2004; Kim et al., 2007).”
- Characterization of Six Lipoproteins in the σE Regulon (2005, background): “) (46), Tob55 (mitochondria) (16, 33), and Toc75 (chloroplasts) (33), are also necessary for the insertion of -barrel proteins into the outer membrane.”
- Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. (2005, positive): “Mistargeting n m should result in decreased levels of folded OmpA and LamB and increased levels of the unfolded proteins in t s unheated samples (Voulhoux et al., 2003).”