Effective assembly of bacterial fimbriae depends on the TAM nanomachine
暂无分享,去创建一个
G. Waksman | T. Lithgow | A. Lo | I. Hay | Hsin-Hui Shen | R. Strugnell | C. Stubenrauch | M. Phan | K. Tuck | M. Belousoff | K. M. Peters | A. Mark | James | Lillington | Schembri | K. Peters
[1] T. Lithgow. The Assembly of Beta-Barrel Proteins into Bacterial Outer Membranes , 2017 .
[2] T. Lithgow,et al. Reconstitution of a nanomachine driving the assembly of proteins into bacterial outer membranes , 2014, Nature Communications.
[3] G. Waksman,et al. Biogenesis and adhesion of type 1 and P pili. , 2014, Biochimica et biophysica acta.
[4] S. Buchanan,et al. Lateral opening and exit pore formation are required for BamA function. , 2014, Structure.
[5] Björn M. Burmann,et al. The structural basis of autotransporter translocation by TamA , 2013, Nature Structural &Molecular Biology.
[6] Trevor Lithgow,et al. Structural insight into the biogenesis of β-barrel membrane proteins , 2013, Nature.
[7] J. Coon,et al. A proteomics search algorithm specifically designed for high-resolution tandem mass spectra. , 2013, Journal of proteome research.
[8] D. Baker,et al. Structural and energetic basis of folded protein transport by the FimD usher , 2013, Nature.
[9] Sri H. Ramarathinam,et al. Discovery of an archetypal protein transport system in bacterial outer membranes , 2012, Nature Structural &Molecular Biology.
[10] Michael J. MacCoss,et al. Platform-independent and Label-free Quantitation of Proteomic Data Using MS1 Extracted Ion Chromatograms in Skyline , 2012, Molecular & Cellular Proteomics.
[11] T. Lithgow,et al. MrkH, a Novel c-di-GMP-Dependent Transcriptional Activator, Controls Klebsiella pneumoniae Biofilm Formation by Regulating Type 3 Fimbriae Expression , 2011, PLoS pathogens.
[12] T. Silhavy,et al. β-Barrel membrane protein assembly by the Bam complex. , 2011, Annual review of biochemistry.
[13] Gabriel Waksman,et al. Crystal structure of the FimD usher bound to its cognate FimC:FimH substrate , 2011, Nature.
[14] R. Kelley,et al. Improved Quantitative Mass Spectrometry Methods for Characterizing Complex Ubiquitin Signals , 2010, Molecular & Cellular Proteomics.
[15] C. Pan,et al. Fluorescent mannose-functionalized hyperbranched poly(amido amine)s: synthesis and interaction with E. coli. , 2010, Biomacromolecules.
[16] M. Prevost,et al. Escherichia coli K-12 possesses multiple cryptic but functional chaperone-usher fimbriae with distinct surface specificities. , 2010, Environmental microbiology.
[17] I. Henderson,et al. Membrane protein architects: the role of the BAM complex in outer membrane protein assembly , 2009, Nature Reviews Microbiology.
[18] G. von Heijne,et al. Assembly of the cytochrome bo3 complex. , 2007, Journal of molecular biology.
[19] R. Misra,et al. YaeT (Omp85) affects the assembly of lipid‐dependent and lipid‐independent outer membrane proteins of Escherichia coli , 2005, Molecular microbiology.
[20] J. Glasner,et al. Gene replacement without selection: regulated suppression of amber mutations in Escherichia coli. , 2003, Gene.
[21] Ueli Aebi,et al. Exploring the 3D molecular architecture of Escherichia coli type 1 pili. , 2002, Journal of molecular biology.
[22] E. Sokurenko,et al. Functional Flexibility of the FimH Adhesin: Insights from a Random Mutant Library , 2000, Infection and Immunity.
[23] S Falkow,et al. Copyright © 1997, American Society for Microbiology Common Themes in Microbial Pathogenicity Revisited , 2022 .
[24] J. Tommassen,et al. In Vitro Insertion and Assembly of Outer Membrane Protein PhoE of Escherichia coli K-12 into the Outer Membrane , 1996, The Journal of Biological Chemistry.
[25] B. Finlay,et al. Common themes in microbial pathogenicity , 1989, Microbiological reviews.