Harris D Bernstein

Protein targeting: getting into the groove.

Membrane protein biogenesis: the exception explains the rules.

The structure of multiple polypeptide domains determines the signal recognition particle targeting requirement of Escherichia coli inner membrane proteins.

The biogenesis and assembly of bacterial membrane proteins.

Physiological basis for conservation of the signal recognition particle targeting pathway in Escherichia coli.

The targeting pathway of Escherichia coli presecretory and integral membrane proteins is specified by the hydrophobicity of the targeting signal.

Evidence for a novel GTPase priming step in the SRP protein targeting pathway.

Trigger factor retards protein export in Escherichia coli.

DnaK promotes the selective export of outer membrane protein precursors in SecA-deficient Escherichia coli.

Signal recognition particle (SRP)-mediated targeting and Sec-dependent translocation of an extracellular Escherichia coli protein.

Basic amino acids in a distinct subset of signal peptides promote interaction with the signal recognition particle.

Conserved tertiary base pairing ensures proper RNA folding and efficient assembly of the signal recognition particle Alu domain.

An unusual signal peptide facilitates late steps in the biogenesis of a bacterial autotransporter.

Efficient secretion of a folded protein domain by a monomeric bacterial autotransporter.

An unusual signal peptide extension inhibits the binding of bacterial presecretory proteins to the signal recognition particle, trigger factor, and the SecYEG complex.

Translation arrest requires two-way communication between a nascent polypeptide and the ribosome.

The surprising complexity of signal sequences.

Characterization of a novel two-partner secretion system in Escherichia coli O157:H7.

Cleavage of a bacterial autotransporter by an evolutionarily convergent autocatalytic mechanism.

Protein secretion in gram-negative bacteria via the autotransporter pathway.

Are bacterial 'autotransporters' really transporters?

Autotransporter structure reveals intra-barrel cleavage followed by conformational changes.

Incorporation of a polypeptide segment into the beta-domain pore during the assembly of a bacterial autotransporter.

Identification of a post-targeting step required for efficient cotranslational translocation of proteins across the Escherichia coli inner membrane.

The plasticity of a translation arrest motif yields insights into nascent polypeptide recognition inside the ribosome tunnel.

Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane.

Sequential translocation of an Escherchia coli two-partner secretion pathway exoprotein across the inner and outer membranes.

Molecular basis for the structural stability of an enclosed β-barrel loop.

The conformation of a nascent polypeptide inside the ribosome tunnel affects protein targeting and protein folding.

Secretion of a bacterial virulence factor is driven by the folding of a C-terminal segment.

The double life of a bacterial lipoprotein.

The translational regulatory function of SecM requires the precise timing of membrane targeting.

Residues in a conserved α-helical segment are required for cleavage but not secretion of an Escherichia coli serine protease autotransporter passenger domain.

Sequential and spatially restricted interactions of assembly factors with an autotransporter beta domain.

Molecular basis for the activation of a catalytic asparagine residue in a self-cleaving bacterial autotransporter.

Cell biology: All clear for ribosome landing.

Mechanistic link between β barrel assembly and the initiation of autotransporter secretion.

Mutations in the Escherichia coli ribosomal protein L22 selectively suppress the expression of a secreted bacterial virulence factor.

Charge-dependent secretion of an intrinsically disordered protein via the autotransporter pathway.

Stepwise folding of an autotransporter passenger domain is not essential for its secretion.

Reconstitution of bacterial autotransporter assembly using purified components.

Of linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion.

Analysis of the outer membrane proteome and secretome of Bacteroides fragilis reveals a multiplicity of secretion mechanisms.

Looks can be deceiving: recent insights into the mechanism of protein secretion by the autotransporter pathway.

An In Vitro Assay for Outer Membrane Protein Assembly by the BAM Complex.

Type V Secretion: the Autotransporter and Two-Partner Secretion Pathways.

Surface-Exposed Lipoproteins: An Emerging Secretion Phenomenon in Gram-Negative Bacteria.

Enterohemorrhagic reduce mucus and intermicrovillar bridges in human stem cell-derived colonoids.

Genomic Diversity of Enterotoxigenic Strains of Bacteroides fragilis.

Selective pressure for rapid membrane integration constrains the sequence of bacterial outer membrane proteins.

Folding of a bacterial integral outer membrane protein is initiated in the periplasm.

The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition.

Identification of a novel post-insertion step in the assembly of a bacterial outer membrane protein.