相关参考文献
注意：仅列出部分参考文献，下载原文获取全部文献信息。Cryo-EM structures reveal multiple stages of bacterial outer membrane protein folding
Matthew Thomas Doyle et al.
CELL (2022)
The Escherichia coli outer membrane protein OmpA acquires secondary structure prior to its integration into the membrane
Xu Wang et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2022)
Chaperones Skp and SurA dynamically expand unfolded OmpX and synergistically disassemble oligomeric aggregates
Neharika Chamachi et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2022)
The assembly of β-barrel membrane proteins by BAM and SAM
Karl Lundquist et al.
MOLECULAR MICROBIOLOGY (2021)
Substrate-dependent arrangements of the subunits of the BAM complex determined by neutron reflectometry
Xiaoyu Chen et al.
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES (2021)
Plasticity within the barrel domain of BamA mediates a hybrid-barrel mechanism by BAM
Runrun Wu et al.
NATURE COMMUNICATIONS (2021)
The antibiotic darobactin mimics a β-strand to inhibit outer membrane insertase
Hundeep Kaur et al.
NATURE (2021)
Highly accurate protein structure prediction with AlphaFold
John Jumper et al.
NATURE (2021)
Critical assessment of methods of protein structure prediction (CASP)-Round XIV
Andriy Kryshtafovych et al.
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS (2021)
The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding
Paul White et al.
NATURE COMMUNICATIONS (2021)
Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients
Antonio N. Calabrese et al.
NATURE COMMUNICATIONS (2020)
Conformational Dynamics of the Periplasmic Chaperone SurA
Moye Jia et al.
BIOCHEMISTRY (2020)
The transmembrane supercomplex mediating the biogenesis of OMPs in Gram-negative bacteria assumes a circular conformational change upon activation
Feng Jin
FEBS OPEN BIO (2020)
Role of the lipid bilayer in outer membrane protein folding in Gram-negative bacteria
Jim E. Horne et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2020)
Structure of a nascent membrane protein as it folds on the BAM complex
David Tomasek et al.
NATURE (2020)
PyXlinkViewer: A flexible tool for visualization of protein chemical crosslinking data within thePyMOLmolecular graphics system
Bob Schiffrin et al.
PROTEIN SCIENCE (2020)
Domain interactions determine the conformational ensemble of the periplasmic chaperoneSurA
Dagan C. Marx et al.
PROTEIN SCIENCE (2020)
SurA is a cryptically grooved chaperone that expands unfolded outer membrane proteins
Dagan C. Marx et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2020)
Hydrogen-deuterium exchange mass spectrometry captures distinct dynamics upon substrate and inhibitor binding to a transporter
Ruyu Jia et al.
NATURE COMMUNICATIONS (2020)
Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs
Matthew G. Iadanza et al.
COMMUNICATIONS BIOLOGY (2020)
Inter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesis
Sara Alvira et al.
ELIFE (2020)
The Role of SurA PPlase Domains in Preventing Aggregation of the Outer-Membrane Proteins tOmpA and OmpT
Julia R. Humes et al.
JOURNAL OF MOLECULAR BIOLOGY (2019)
First Community-Wide, Comparative Cross-Linking Mass Spectrometry Study
Claudio Iacobucci et al.
ANALYTICAL CHEMISTRY (2019)
Plasticity and transient binding are key ingredients of the periplasmic chaperone network
Aaron P. Chum et al.
PROTEIN SCIENCE (2019)
Recommendations for performing, interpreting and reporting hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments
Glenn R. Masson et al.
NATURE METHODS (2019)
Bacterial outer membrane proteins assemble via asymmetric interactions with the BamA β-barrel
Matthew T. Doyle et al.
NATURE COMMUNICATIONS (2019)
Profiling the Escherichia coli membrane protein interactome captured in Peptidisc libraries
Michael Luke Carlson et al.
ELIFE (2019)
A new antibiotic selectively kills Gram-negative pathogens
Yu Imai et al.
NATURE (2019)
Formation of a β-barrel membrane protein is catalyzed by the interior surface of the assembly machine protein BamA
James Lee et al.
ELIFE (2019)
Deuteros: software for rapid analysis and visualization of data from differential hydrogen deuterium exchange-mass spectrometry
Andy M. C. Lau et al.
BIOINFORMATICS (2019)
Protein interaction networks revealed by proteome coevolution
Qian Cong et al.
SCIENCE (2019)
Single-Molecule Detection Reveals Different Roles of Skp and SurA as Chaperones
Geng Li et al.
ACS CHEMICAL BIOLOGY (2018)
The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition
Sunyia Hussain et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2018)
Mass spectrometry-enabled structural biology of membrane proteins
Antonio N. Calabrese et al.
METHODS (2018)
Membrane protein insertion through a mitochondrial β-barrel gate
Alexandra I. C. Hohr et al.
SCIENCE (2018)
The WD40 Protein BamB Mediates Coupling of BAM Complexes into Assembly Precincts in the Bacterial Outer Membrane
Sachith D. Gunasinghe et al.
CELL REPORTS (2018)
Sequence-Specific Solution NMR Assignments of the β-Barrel Insertase BamA to Monitor Its Conformational Ensemble at the Atomic Level
Jean-Baptiste Hartmann et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2018)
C-terminal kink formation is required for lateral gating in BamA
Karl Lundquist et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2018)
Bacterial machineries for the assembly of membrane-embedded beta-barrel proteins
David Ranava et al.
FEMS MICROBIOLOGY LETTERS (2018)
Effects of Periplasmic Chaperones and Membrane Thickness on BamA-Catalyzed Outer-Membrane Protein Folding
Bob Schiffrin et al.
JOURNAL OF MOLECULAR BIOLOGY (2017)
Structural basis for substrate selection by the translocation and assembly module of the -barrel assembly machinery
Rebecca S. Bamert et al.
MOLECULAR MICROBIOLOGY (2017)
Flexibility in the Periplasmic Domain of BamA Is Important for Function
Lisa R. Warner et al.
STRUCTURE (2017)
Folding of a bacterial integral outer membrane protein is initiated in the periplasm
Rakesh Sikdar et al.
NATURE COMMUNICATIONS (2017)
BamA β16C strand and periplasmic turns are critical for outer membrane protein insertion and assembly
Yinghong Gu et al.
BIOCHEMICAL JOURNAL (2017)
Outer membrane protein folding from an energy landscape perspective
Bob Schiffrin et al.
BMC BIOLOGY (2017)
The Activity of Escherichia coli Chaperone SurA Is Regulated by Conformational Changes Involving a Parvulin Domain
Garner R. Soltes et al.
JOURNAL OF BACTERIOLOGY (2016)
A Supercomplex Spanning the Inner and Outer Membranes Mediates the Biogenesis of β-Barrel Outer Membrane Proteins in Bacteria
Yan Wang et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2016)
Structural basis of outer membrane protein insertion by the BAM complex
Yinghong Gu et al.
NATURE (2016)
Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins
Long Han et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2016)
The type III secretion system apparatus determines the intracellular niche of bacterial pathogens
Juan Du et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2016)
The structure of the β-barrel assembly machinery complex
Jeremy Bakelar et al.
SCIENCE (2016)
Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM
Matthew G. Iadanza et al.
NATURE COMMUNICATIONS (2016)
Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins
Long Han et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2016)
TtOmp85, a β-Barrel Assembly Protein, Functions by Barrel Augmentation
Luisa Estrada Mallarino et al.
BIOCHEMISTRY (2015)
Protein-protein interactions and the spatiotemporal dynamics of bacterial outer membrane proteins
Colin Kleanthous et al.
CURRENT OPINION IN STRUCTURAL BIOLOGY (2015)
Cross-species chimeras reveal BamA POTRA and -barrel domains must be fine-tuned for efficient OMP insertion
Douglas F. Browning et al.
MOLECULAR MICROBIOLOGY (2015)
Supramolecular assemblies underpin turnover of outer membrane proteins in bacteria
Patrice Rassam et al.
NATURE (2015)
Impact of holdase chaperones Skp and SurA on the folding of β-barrel outer-membrane proteins
Johannes Thoma et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2015)
Inhibition of the β-barrel assembly machine by a peptide that binds BamD
Christine L. Hagan et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2015)
Impact of holdase chaperones Skp and SurA on the folding of β-barrel outer-membrane proteins
Johannes Thoma et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2015)
Folding mechanisms of periplasmic proteins
Camille Goemans et al.
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH (2014)
The amyloid state and its association with protein misfolding diseases
Tuomas P. J. Knowles et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2014)
Outer membrane β-barrel protein folding is physically controlled by periplasmic lipid head groups and BamA
Dennis Gessmann et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2014)
Distance restraints from crosslinking mass spectrometry: Mining a molecular dynamics simulation database to evaluate lysine-lysine distances
Eric D. Merkley et al.
PROTEIN SCIENCE (2014)
Lateral Opening and Exit Pore Formation Are Required for BamA Function
Nicholas Noinaj et al.
STRUCTURE (2014)
Reconstitution of bacterial autotransporter assembly using purified components
Giselle Roman-Hernandez et al.
ELIFE (2014)
The Lipid Bilayer-Inserted Membrane Protein BamA of Escherichia coli Facilitates Insertion and Folding of Outer Membrane Protein A from Its Complex with Skp
Geetika J. Patel et al.
BIOCHEMISTRY (2013)
Barn Lipoproteins Assemble BamA in Vitro
Christine L. Hagan et al.
BIOCHEMISTRY (2013)
Demarcating SurA Activities Required for Outer Membrane Targeting of Yersinia pseudotuberculosis Adhesins
Ikenna R. Obi et al.
INFECTION AND IMMUNITY (2013)
Dissecting the Effects of Periplasmic Chaperones on the In Vitro Folding of the Outer Membrane Protein PagP
Lindsay M. McMorran et al.
JOURNAL OF MOLECULAR BIOLOGY (2013)
Structural insight into the biogenesis of β-barrel membrane proteins
Nicholas Noinaj et al.
NATURE (2013)
Conformation-specific labeling of BamA and suppressor analysis suggest a cyclic mechanism for β-barrel assembly in Escherichia coli
Nathan W. Rigel et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2013)
Substitutions in the BamA β-Barrel Domain Overcome the Conditional Lethal Phenotype of a ΔbamB ΔbamE Strain of Escherichia coli
Rene Tellez et al.
JOURNAL OF BACTERIOLOGY (2012)
BamE Modulates the Escherichia coli Beta-Barrel Assembly Machine Component BamA
Nathan W. Rigel et al.
JOURNAL OF BACTERIOLOGY (2012)
Genetic, Biochemical, and Molecular Characterization of the Polypeptide Transport-Associated Domain of Escherichia coli BamA
Patricia Workman et al.
JOURNAL OF BACTERIOLOGY (2012)
Dynamic Association of BAM Complex Modules Includes Surface Exposure of the Lipoprotein BamC
Chaille T. Webb et al.
JOURNAL OF MOLECULAR BIOLOGY (2012)
Activation of the Escherichia coli β-barrel assembly machine (Bam) is required for essential components to interact properly with substrate
Dante P. Ricci et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2012)
Hydrogen exchange mass spectrometry for studying protein structure and dynamics
Lars Konermann et al.
CHEMICAL SOCIETY REVIEWS (2011)
The Fimbrial Usher FimD Follows the SurA-BamB Pathway for Its Assembly in the Outer Membrane of Escherichia coli
Carmen Palomino et al.
JOURNAL OF BACTERIOLOGY (2011)
Crystal Structure of β-Barrel Assembly Machinery BamCD Protein Complex
Kelly H. Kim et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2011)
A Diversity of Assembly Mechanisms of a Generic Amyloid Fold
Timo Eichner et al.
MOLECULAR CELL (2011)
Molecular chaperones in protein folding and proteostasis
F. Ulrich Hartl et al.
NATURE (2011)
Sequential and spatially restricted interactions of assembly factors with an autotransporter β domain
Raffaele Ieva et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2011)
The role of SurA factor in outer membrane protein transport and virulence
Susanne Behrens-Kneip
INTERNATIONAL JOURNAL OF MEDICAL MICROBIOLOGY (2010)
Dissection of β-barrel outer membrane protein assembly pathways through characterizing BamA POTRA 1 mutants of Escherichia coli
Drew Bennion et al.
MOLECULAR MICROBIOLOGY (2010)
Self-Association of Unfolded Outer Membrane Proteins
Alexandra Ebie Tan et al.
MACROMOLECULAR BIOSCIENCE (2010)
Reconstitution of Outer Membrane Protein Assembly from Purified Components
Christine L. Hagan et al.
SCIENCE (2010)
The Bacterial Cell Envelope
Thomas J. Silhavy et al.
COLD SPRING HARBOR PERSPECTIVES IN BIOLOGY (2010)
Characterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics
Didier Vertommen et al.
PROTEOMICS (2009)
β-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro
Nancy K. Burgess et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2008)
Fold and function of polypeptide transport-associated domains responsible for delivering unfolded proteins to membranes
Timothy J. Knowles et al.
MOLECULAR MICROBIOLOGY (2008)
Analysis of YfgL and YaeT interactions through bioinformatics, mutagenesis, and biochemistry
Phu Vuong et al.
JOURNAL OF BACTERIOLOGY (2008)
The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues
Xiaohua Xu et al.
JOURNAL OF MOLECULAR BIOLOGY (2007)
Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli
Joseph G. Sklar et al.
GENES & DEVELOPMENT (2007)
Inference of macromolecular assemblies from crystalline state
Evgeny Krissinel et al.
JOURNAL OF MOLECULAR BIOLOGY (2007)
Structure and function of an essential component of the outer membrane protein assembly machine
Seokhee Kim et al.
SCIENCE (2007)
Kinetic analysis of the assembly of the outer membrane protein LamB in Escherichia coli mutants each lacking a secretion or targeting factor in a different cellular compartment
Alejandro R. Ureta et al.
JOURNAL OF BACTERIOLOGY (2007)
Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif
Viviane Robert et al.
PLOS BIOLOGY (2006)
YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli
Juliana C. Malinverni et al.
MOLECULAR MICROBIOLOGY (2006)
Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli
SS Justice et al.
JOURNAL OF BACTERIOLOGY (2005)
Characterization of six lipoproteins in the σE regulon
C Onufryk et al.
JOURNAL OF BACTERIOLOGY (2005)
The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition
G Hennecke et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2005)
Omp85, an evolutionarily conserved bacterial protein involved in outer-membrane-protein assembly
R Voulhoux et al.
RESEARCH IN MICROBIOLOGY (2004)
Molecular basis of bacterial outer membrane permeability revisited
H Nikaido
MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS (2003)
Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli
AE Rizzitello et al.
JOURNAL OF BACTERIOLOGY (2001)
The SurA periplasmic PPlase lacking its parvulin domains functions in vivo and has chaperone activity
S Behrens et al.
EMBO JOURNAL (2001)
Structure and function of bacterial outer membrane proteins: barrels in a nutshell
R Koebnik et al.
MOLECULAR MICROBIOLOGY (2000)
High-resolution structure of the OmpA membrane domain
A Pautsch et al.
JOURNAL OF MOLECULAR BIOLOGY (2000)
分享论文
