Structure and function of bacterial outer membrane proteins: barrels in a nutshell

By R. Koebnik, K. Locher, P. Van Gelder. Molecular Microbiology, 2000

1,210 citations recorded by the source corpus.

Subfields: Genetics, Infectious Diseases, Molecular Medicine

View Paper: https://www.semanticscholar.org/paper/ae37c655f337adb472077b5541cd15af960791af

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In Genetics

1. J. Pagés
2. Ian R. Henderson
3. A. Vorobieva
4. D. Rapaport
5. C. Godornes
6. L. Giacani
7. H. Nikaido
8. Burkhard Rost

In Infectious Diseases

1. H. Nikaido

In Molecular Medicine

1. H. Nikaido
2. J. Pagés
3. E. Dassa
4. C. Orelle
5. A. Davidson
6. Jue Chen
7. Burkhard Rost
8. Xian-Zhi Li

Citations in the corpus

• Molecular Basis of Bacterial Outer Membrane Permeability Revisited (2003, background): “Important conclusions from these studies include the following (there are recent minireviews on the structure of porins [343, 598, 599]).”
• The porin and the permeating antibiotic: a selective diffusion barrier in Gram-negative bacteria (2008, background): “Different types of porins have been characterized in Gram-negative bacteria and classified according to their activity (non-specific or specific channel or selective pore), their functional structure (monomeric or trimeric) and their regulation and expressio”
• B-Cell Epitope Mapping of TprC and TprD Variants of Treponema pallidum Subspecies Informs Vaccine Development for Human Treponematoses (2022, background): “Integral TpOMPs will necessarily contain a membrane-embedded b-barrel domain composed of antiparallel b-strands joined together by loops that alternatively protrude toward the extracellular environment or the periplasm (25).”
• The importance of the viable but non-culturable state in human bacterial pathogens (2014, background): “It consists of phospholipids, lipopolysaccharides and outer membrane proteins (OMPs) (Koebnik et al., 2000).”
• Predicting transmembrane beta-barrels in proteomes. (2004, methodology): “This was a natural extension from the observations of the `aromatic cuff' and `hydrophobic belt' (1,5,19).”
• Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems (2008, background): “A large loop folds back into the barrel, forming a constriction zone about halfway through the channel that contributes to the exclusion limit and ion selectivity of the pore (251).”
• Adaptive and Mutational Resistance: Role of Porins and Efflux Pumps in Drug Resistance (2012, background): “Together with hydrophilic amino acids from several -strands, this creates a constriction zone with an electrostatic field, created by acidic residues in loop 3 and basic residues in the opposite -strand, which plays an important role in the selectivity of the pore for the size and charge of permeati”
• Folding and assembly of β-barrel membrane proteins (2004, background): “Porins are extremely stable towards heat denaturation, protease digestion, and chemical denaturation with urea and GdnHCl [ 4 ].”
• Biogenesis of β-barrel membrane proteins in bacteria and eukaryotes: evolutionary conservation and divergence (2009, background): “While integral inner membrane proteins typically span the membrane in the form of hydrophobic a-helices, most integral outer membrane proteins (OMPs) are b-barrels consisting of antiparallel amphipathic b-strands [1] (see Fig.”
• Type V Protein Secretion Pathway: the Autotransporter Story (2004, background): “The -barrel architecture has been found in all integral outer membrane proteins whose structures have been solved (97); -helical bundles have been found only in the cytoplasmic membrane (257, 444).”