scholarly article | Q13442814 |
P50 | author | Sheena Radford | Q17011933 |
Jean-francois Collet | Q43171484 | ||
Antonio N. Calabrese | Q56152927 | ||
Bogdan I Iorga | Q56805098 | ||
Seung-Hyun Cho | Q58126799 | ||
P2093 | author name string | Han Remaut | |
Juliette Létoquart | |||
Van Son Nguyen | |||
Gwennaelle Louis | |||
Raquel Rodríguez-Alonso | |||
P2860 | cites work | Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection | Q22122301 |
CHARMM: the biomolecular simulation program | Q24658108 | ||
Crystal Structure of the Outer Membrane Protein RcsF, a New Substrate for the Periplasmic Protein-disulfide Isomerase DsbC | Q27667359 | ||
A Disulfide Bridge Network within the Soluble Periplasmic Domain Determines Structure and Function of the Outer Membrane Protein RCSF | Q27667445 | ||
Structural and functional analysis of the β-barrel domain of BamA from Escherichia coli | Q27689468 | ||
Structure of BamA, an essential factor in outer membrane protein biogenesis | Q27690708 | ||
Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins | Q27704061 | ||
Structural basis of outer membrane protein insertion by the BAM complex | Q27704064 | ||
XDS | Q27860472 | ||
Coot: model-building tools for molecular graphics | Q27860505 | ||
VMD: visual molecular dynamics | Q27860554 | ||
Comparative protein modelling by satisfaction of spatial restraints | Q27860866 | ||
Phasercrystallographic software | Q27860930 | ||
Regulation and mode of action of the second small RNA activator of RpoS translation, RprA | Q28212671 | ||
OPM database and PPM web server: resources for positioning of proteins in membranes | Q28740946 | ||
An efficient recombination system for chromosome engineering in Escherichia coli | Q29615038 | ||
The β-barrel assembly machinery in motion | Q30152662 | ||
Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM. | Q30152721 | ||
BamA POTRA Domain Interacts with a Native Lipid Membrane Surface | Q30152768 | ||
Detecting envelope stress by monitoring β-barrel assembly. | Q30153263 | ||
Transmembrane domain of surface-exposed outer membrane lipoprotein RcsF is threaded through the lumen of β-barrel proteins | Q30153329 | ||
Reconstitution of bacterial autotransporter assembly using purified components | Q30153344 | ||
Lateral opening and exit pore formation are required for BamA function | Q30153373 | ||
Lipoprotein sorting in bacteria. | Q30155534 | ||
β-Barrel membrane protein assembly by the Bam complex | Q30155627 | ||
Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli | Q30158006 | ||
E. coli outer membrane and interactions with OmpLA. | Q33736483 | ||
The structure of the β-barrel assembly machinery complex | Q36942637 | ||
"Major Tom to ground control: how lipoproteins communicate extra-cytoplasmic stress to the decision center of the cell". | Q39412545 | ||
A comparative cross-linking strategy to probe conformational changes in protein complexes | Q42155930 | ||
Cooperative nature of gating transitions in K(+) channels as seen from dynamic importance sampling calculations | Q42182110 | ||
Activation of cryptic aminoglycoside resistance in Salmonella enterica | Q45792333 | ||
Outer membrane protein folding from an energy landscape perspective | Q47133897 | ||
The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition | Q47223018 | ||
BamA β16C strand and periplasmic turns are critical for outer membrane protein insertion and assembly | Q47703707 | ||
Computing ensembles of transitions from stable states: Dynamic importance sampling. | Q51627727 | ||
Monoclonal antibody targeting the β-barrel assembly machine of Escherichia coli is bactericidal. | Q52648015 | ||
Mass spectrometry-enabled structural biology of membrane proteins. | Q52803097 | ||
A genetically incorporated crosslinker reveals chaperone cooperation in acid resistance. | Q54353719 | ||
Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel. | Q54443529 | ||
Distinct domains of Escherichia coli IgaA connect envelope stress sensing and down-regulation of the Rcs phosphorelay across subcellular compartments. | Q55280613 | ||
Sequence-Specific Solution NMR Assignments of the β-Barrel Insertase BamA to Monitor Its Conformational Ensemble at the Atomic Level | Q57751797 | ||
Identification of a Multicomponent Complex Required for Outer Membrane Biogenesis in Escherichia coli | Q57809995 | ||
A cross-linking/mass spectrometry workflow based on MS-cleavable cross-linkers and the MeroX software for studying protein structures and protein-protein interactions | Q58090255 | ||
Optimization Workflow for the Analysis of Cross-Linked Peptides Using a Quadrupole Time-of-Flight Mass Spectrometer | Q64266090 | ||
Improper Coordination of BamA and BamD Results in Bam Complex Jamming by a Lipoprotein Substrate | Q64273901 | ||
The Synthetic Phenotype of Δ Δ Double Mutants Results from a Lethal Jamming of the Bam Complex by the Lipoprotein RcsF | Q64273907 | ||
A new antibiotic selectively kills Gram-negative pathogens | Q77704224 | ||
The Complex Rcs Regulatory Cascade | Q89089718 | ||
CHARMM-GUI Membrane Builder for Complex Biological Membrane Simulations with Glycolipids and Lipoglycans | Q90331251 | ||
A small-molecule inhibitor of BamA impervious to efflux and the outer membrane permeability barrier | Q90573513 | ||
Chimeric peptidomimetic antibiotics against Gram-negative bacteria | Q90911763 | ||
Identification of conformation-selective nanobodies against the membrane protein insertase BamA by an integrated structural biology approach | Q91904039 | ||
P921 | main subject | beta barrel | Q310424 |
P577 | publication date | 2020-06-22 | |
P1433 | published in | Nature Chemical Biology | Q904026 |
P1476 | title | Structural insight into the formation of lipoprotein-β-barrel complexes |
Q100308472 | Defining the function of OmpA in the Rcs stress response | cites work | P2860 |
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