Hagan, Christine, Thomas Silhavy, and Daniel Kahne. 2011. “β-Barrel Membrane Protein Assembly by the Bam Complex”. Annu Rev Biochem 80: 189-210. doi:10.1146/annurev-biochem-061408-144611. Reference Link
Chng, Shu-Sin, Natividad Ruiz, Gitanjali Chimalakonda, Thomas Silhavy, and Daniel Kahne. (2010) 2010. “Characterization of the Two-Protein Complex in Escherichia Coli Responsible for Lipopolysaccharide Assembly at the Outer Membrane”. Proc Natl Acad Sci U S A 107 (12): 5363-8. doi:10.1073/pnas.0912872107. Reference Link
Kim, Seokhee, Juliana Malinverni, Piotr Sliz, Thomas Silhavy, Stephen Harrison, and Daniel Kahne. (2007) 2007. “Structure and Function of an Essential Component of the Outer Membrane Protein Assembly Machine”. Science 317 (5840): 961-4. doi:10.1126/science.1143993. Reference Link
Rigel, Nathan, Dante Ricci, and Thomas Silhavy. (2013) 2013. “Conformation-Specific Labeling of BamA and Suppressor Analysis Suggest a Cyclic Mechanism for β-Barrel Assembly in Escherichia Coli”. Proc Natl Acad Sci U S A 110 (13): 5151-6. doi:10.1073/pnas.1302662110. Reference Link
Grabowicz, Marcin, Jennifer Yeh, and Thomas Silhavy. (2013) 2013. “Dominant Negative LptE Mutation That Supports a Role for LptE As a Plug in the LptD Barrel”. J Bacteriol 195 (6): 1327-34. doi:10.1128/JB.02142-12. Reference Link
Ricci, Dante, Christine Hagan, Daniel Kahne, and Thomas Silhavy. (2012) 2012. “Activation of the Escherichia Coli β-Barrel Assembly Machine (Bam) Is Required for Essential Components to Interact Properly With Substrate”. Proc Natl Acad Sci U S A 109 (9): 3487-91. doi:10.1073/pnas.1201362109. Reference Link
Konovalova, Anna, David Perlman, Charles Cowles, and Thomas Silhavy. (2014) 2014. “Transmembrane Domain of Surface-Exposed Outer Membrane Lipoprotein RcsF Is Threaded through the Lumen of β-Barrel Proteins”. Proc Natl Acad Sci U S A 111 (41). doi:10.1073/pnas.1417138111. Reference Link
Soltes, Garner, Jaclyn Schwalm, Dante Ricci, and Thomas Silhavy. (2016) 2016. “The Activity of Escherichia Coli Chaperone SurA Is Regulated by Conformational Changes Involving a Parvulin Domain”. J Bacteriol 198 (6): 921-9. doi:10.1128/JB.00889-15. Reference Link
