Building bigger beta-barrels by Vikas Nanda

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Molecular modelling of beta-barrel outer membrane proteins by Pongprayoon, P

Phospholipids are imported into mitochondria by VDAC, a dimeric beta barrel scramblase by Helene Jahn, Ladislav Bartoš, Grace I. Dearden, Jeremy S. Dittman, Joost C. M. Holthuis, Robert Vácha, Anant K. Menon

“…Thus, VDAC isoforms, members of a superfamily of beta barrel proteins, moonlight as a class of phospholipid scramblases - distinct from alpha-helical scramblase proteins - that act to import lipids into mitochondria.…”
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NN approach and its comparison with NN-SVM to beta-barrel prediction by Kazemian, Hassan, Yusuf, Syed A., White, Kenneth, Grimaldi, Cédric Maxime

“…This paper is concerned with applications of a dual Neural Network (NN) and Support Vector Machine (SVM) to prediction and analysis of beta barrel trans membrane proteins. The prediction and analysis of beta barrel proteins usually offer a host of challenges to the research community, because of their low presence in genomes. …”
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Cascading classifier application for topology prediction of transmembrane beta-barrel proteins by Kazemian, Hassan, Grimaldi, Cédric Maxime

“…Membrane proteins are a major focus for new drug discovery. Transmembrane beta-barrel proteins play key roles in the translocation machinery, pore formation, membrane anchoring and ion exchange. …”
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Machine learning applications for the topology prediction of transmembrane beta-barrel proteins by Grimaldi, Cédric Maxime

“…The two most predominant classes are alpha-helix bundles and beta-barrel transmembrane proteins. Alpha-helix proteins are present in larger numbers than beta-barrel transmembrane proteins in structure databases. …”
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The Functional Significance of Hydrophobic Residue Distribution in Bacterial Beta-Barrel Transmembrane Proteins by Irena Roterman, Katarzyna Stapor, Piotr Fabian, Leszek Konieczny

“…The present analysis allowed us to compare the ways in which the different proteins interact with antibiotics and helped us understand their relative importance in the development of the resistance mechanism. We showed that beta barrel membrane proteins with a hydrophobic core interact less strongly with the molecules they transport.…”
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Transmembrane beta-barrel of staphylococcal alpha-toxin forms in sensitive but not in resistant cells. by Valeva, A, Walev, I, Pinkernell, M, Walker, B, Bayley, H, Palmer, M, Bhakdi, S

“…Thus, every other residue in the sequence 126-140 entered a nonpolar environment in a striking display of an amphipathic transmembrane beta-barrel. In contrast, human granulocytes were found to bind alpha-toxin to a similar extent as lymphocytes, but the heptamers forming on these cells failed to insert their pore-forming domain into the membrane. …”

Beta-Barrel Channel Response to High Electric Fields: Functional Gating or Reversible Denaturation? by Ekaterina M. Nestorovich, Sergey M. Bezrukov

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Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR by Eddy, Matthew Thomas, Su, Yongchao, Andreas, Loren, Clark, Lindsay, Wagner, Gerhard, Pintacuda, Guido, Emsley, Lyndon, Griffin, Robert Guy, Silvers, Robert, 1968-

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Genetically engineered metal ion binding sites on the outside of a Channel's transmembrane beta-barrel. by Kasianowicz, J, Burden, D, Han, L, Cheley, S, Bayley, H

Towards Symmetry-Based Explanation of (Approximate) Shapes of Alpha-Helices and Beta-Sheets (and Beta-Barrels) in Protein Structure by Vladik Kreinovich, Jaime Nava

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Spontaneous oligomerization of a staphylococcal alpha-hemolysin conformationally constrained by removal of residues that form the transmembrane beta-barrel. by Cheley, S, Malghani, MS, Song, L, Hobaugh, M, Gouaux, J, Yang, J, Bayley, H

“…Based on these findings, the deletion is proposed to constrain the central domain and thereby force the creation of a shortened beta barrel, which in turn induces the additional structural changes that normally accompany pore formation. …”

Structural bioinformatics studies of bacterial outer membrane beta-barrel transporters and their AlphaFold2 predicted water-soluble QTY variants. by Akash Sajeev-Sheeja, Eva Smorodina, Shuguang Zhang

“…Beta-barrel outer membrane proteins (OMP) are integral components of Gram-negative bacteria, eukaryotic mitochondria, and chloroplasts. …”
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Evolutionary pathways of repeat protein topology in bacterial outer membrane proteins by Meghan Whitney Franklin, Sergey Nepomnyachyi, Ryan Feehan, Nir Ben-Tal, Rachel Kolodny, Joanna SG Slusky

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A Deep Dive into VDAC1 Conformational Diversity Using All-Atom Simulations Provides New Insights into the Structural Origin of the Closed States by Jordane Preto, Hubert Gorny, Isabelle Krimm

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Structural plasticity in the loop region of engineered lipocalins with novel ligand specificities, so-called Anticalins by S. Achatz, A. Jarasch, A. Skerra

Subjects: “…Beta-barrel…”
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Curcumin Blocks Cytotoxicity of Enteroaggregative and Enteropathogenic Escherichia coli by Blocking Pet and EspC Proteolytic Release From Bacterial Outer Membrane by Javier I. Sanchez-Villamil, Fernando Navarro-Garcia, Araceli Castillo-Romero, Filiberto Gutierrez-Gutierrez, Daniel Tapia, Gabriela Tapia-Pastrana

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Targeting BAM for Novel Therapeutics against Pathogenic Gram-Negative Bacteria by Claire Overly Cottom, Robert Stephenson, Lindsey Wilson, Nicholas Noinaj

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The Role of Extracellular Loops in the Folding of Outer Membrane Protein X (OmpX) of Escherichia coli by Simen Hermansen, David Ryoo, Marcella Orwick-Rydmark, Athanasios Saragliadis, James C. Gumbart, Dirk Linke

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