Structural and functional insights into the role of BamD and BamE within the β-barrel assembly machinery inNeisseria gonorrhoeae

Deciphering the Function of New Gonococcal Vaccine Antigens Using Phenotypic Microarrays

(2017) Benjamin I. Baarda et al.   JOURNAL OF BACTERIOLOGY

The β-barrel assembly machinery in motion

(2017) Nicholas Noinaj et al.   NATURE REVIEWS MICROBIOLOGY

Functional and structural studies on theNeisseria gonorrhoeaeGmhA, the first enzyme in theglycero-manno-heptose biosynthesis pathways, demonstrate a critical role in lipooligosaccharide synthesis and gonococcal viability

(2017) Igor H. Wierzbicki et al.   MicrobiologyOpen

Proteomics-driven Antigen Discovery for Development of Vaccines Against Gonorrhea

(2016) Ryszard A. Zielke et al.   MOLECULAR & CELLULAR PROTEOMICS

Structural basis of outer membrane protein insertion by the BAM complex

(2016) Yinghong Gu et al.   NATURE

Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins

(2016) Long Han et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

The structure of the  -barrel assembly machinery complex

(2016) J. Bakelar et al.   SCIENCE

The Structure of a BamA-BamD Fusion Illuminates the Architecture of the β-Barrel Assembly Machine Core

(2016) Hans Thor Bergal et al.   STRUCTURE

Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM

(2016) Matthew G. Iadanza et al.   Nature Communications

Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins

(2016) Long Han et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Fitting the Pieces of the β-Barrel Assembly Machinery Complex

(2015) Patrick K. O’Neil et al.   BIOCHEMISTRY

The Neisseria gonorrhoeae Obg protein is an essential ribosome-associated GTPase and a potential drug target

(2015) Ryszard A. Zielke et al.   BMC MICROBIOLOGY

A Metalloprotease Secreted by the Type II Secretion System Links Vibrio cholerae with Collagen

(2015) Bo R. Park et al.   JOURNAL OF BACTERIOLOGY

Outer membrane protein biogenesis in Gram-negative bacteria

(2015) Sarah E. Rollauer et al.   PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES

Global Estimates of the Prevalence and Incidence of Four Curable Sexually Transmitted Infections in 2012 Based on Systematic Review and Global Reporting

(2015) Lori Newman et al.   PLoS One

Structural and functional analysis of the β-barrel domain of BamA from Escherichia coli

(2014) Dongchun Ni et al.   FASEB JOURNAL

Crystal Structure of BamB Bound to a Periplasmic Domain Fragment of BamA, the Central Component of the β-Barrel Assembly Machine

(2014) Katarina Bartoš Jansen et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Quantitative Proteomics of theNeisseria GonorrhoeaeCell Envelope and Membrane Vesicles for the Discovery of Potential Therapeutic Targets

(2014) Ryszard A. Zielke et al.   MOLECULAR & CELLULAR PROTEOMICS

Lateral Opening and Exit Pore Formation Are Required for BamA Function

(2014) Nicholas Noinaj et al.   STRUCTURE

Reconstitution of bacterial autotransporter assembly using purified components

(2014) Giselle Roman-Hernandez et al.   eLife

Structure of BamA, an essential factor in outer membrane protein biogenesis

(2014) Reinhard Albrecht et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Structural insight into the biogenesis of β-barrel membrane proteins

(2013) Nicholas Noinaj et al.   NATURE

Distinct Binding and Immunogenic Properties of the Gonococcal Homologue of Meningococcal Factor H Binding Protein

(2013) Ilse Jongerius et al.   PLoS Pathogens

Structure ofEscherichia coliBamD and its functional implications in outer membrane protein assembly

(2012) Cheng Dong et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Dynamic Association of BAM Complex Modules Includes Surface Exposure of the Lipoprotein BamC

(2012) Chaille T. Webb et al.   JOURNAL OF MOLECULAR BIOLOGY

Structural basis for iron piracy by pathogenic Neisseria

(2012) Nicholas Noinaj et al.   NATURE

Activation of the Escherichia coli  -barrel assembly machine (Bam) is required for essential components to interact properly with substrate

(2012) D. P. Ricci et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

β-Barrel Membrane Protein Assembly by the Bam Complex

(2011) Christine L. Hagan et al.   Annual Review of Biochemistry

Structural Characterization ofEscherichia coliBamE, a Lipoprotein Component of the β-Barrel Assembly Machinery Complex

(2011) Kelly H. Kim et al.   BIOCHEMISTRY

The Bam machine: A molecular cooper

(2011) Dante P. Ricci et al.   BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES

BIGSdb: Scalable analysis of bacterial genome variation at the population level

(2011) Keith A Jolley et al.   BMC BIOINFORMATICS

The structural biology of β-barrel membrane proteins: a summary of recent reports

(2011) James W Fairman et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY

Structure and function of BamE within the outer membrane and the β-barrel assembly machine

(2011) Timothy J Knowles et al.   EMBO REPORTS

BamE Modulates the Escherichia coli Beta-Barrel Assembly Machine Component BamA

(2011) N. W. Rigel et al.   JOURNAL OF BACTERIOLOGY

Structural Basis of Outer Membrane Protein Biogenesis in Bacteria

(2011) Reinhard Albrecht et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Crystal Structure of β-Barrel Assembly Machinery BamCD Protein Complex

(2011) Kelly H. Kim et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Crystal Structure of BamD: An Essential Component of the β-Barrel Assembly Machinery of Gram-Negative Bacteria

(2011) Cristina M. Sandoval et al.   JOURNAL OF MOLECULAR BIOLOGY

The Crystal Structure of BamB Suggests Interactions with BamA and Its Role within the BAM Complex

(2011) Nicholas Noinaj et al.   JOURNAL OF MOLECULAR BIOLOGY

Augmenting β-Augmentation: Structural Basis of How BamB Binds BamA and May Support Folding of Outer Membrane Proteins

(2011) Alexander Heuck et al.   JOURNAL OF MOLECULAR BIOLOGY

Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega

(2011) F. Sievers et al.   Molecular Systems Biology

Features and development ofCoot

(2010) P. Emsley et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

PHENIX: a comprehensive Python-based system for macromolecular structure solution

(2010) Paul D. Adams et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Biological Functions and Biogenesis of Secreted Bacterial Outer Membrane Vesicles

(2010) Adam Kulp et al.   Annual Review of Microbiology

Crystal Structure of Escherichia coli BamB, a Lipoprotein Component of the β-Barrel Assembly Machinery Complex

(2010) Kelly H. Kim et al.   JOURNAL OF MOLECULAR BIOLOGY

A Modular BAM Complex in the Outer Membrane of the α-Proteobacterium Caulobacter crescentus

(2010) Khatira Anwari et al.   PLoS One

Automated minimization of steric clashes in protein structures

(2010) Srinivas Ramachandran et al.   PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS

Reconstitution of Outer Membrane Protein Assembly from Purified Components

(2010) C. L. Hagan et al.   SCIENCE

MolProbity: all-atom structure validation for macromolecular crystallography

(2009) Vincent B. Chen et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

xia2: an expert system for macromolecular crystallography data reduction

(2009) G. Winter   JOURNAL OF APPLIED CRYSTALLOGRAPHY

The  -Barrel Outer Membrane Protein Assembly Complex of Neisseria meningitidis

(2009) E. B. Volokhina et al.   JOURNAL OF BACTERIOLOGY

The BAM complex subunit BamE (SmpA) is required for membrane integrity, stalk growth and normal levels of outer membrane  -barrel proteins in Caulobacter crescentus

(2009) K. R. Ryan et al.   MICROBIOLOGY-SGM

Membrane protein architects: the role of the BAM complex in outer membrane protein assembly

(2009) Timothy J. Knowles et al.   NATURE REVIEWS MICROBIOLOGY

Small outer-membrane lipoprotein, SmpA, is regulated by  E and has a role in cell envelope integrity and virulence of Salmonella enterica serovar Typhimurium

(2008) C. Lewis et al.   MICROBIOLOGY-SGM

Crystal Structure of YaeT: Conformational Flexibility and Substrate Recognition

(2008) Petia Z. Gatzeva-Topalova et al.   STRUCTURE