Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Methods to Characterize Folding and Function of BamA Cross-Link Mutants.

Methods in molecular biology (Clifton, N.J.) - 1 Jan 2015

Kuszak Adam J, Noinaj Nicholas, Buchanan Susan K

Abstract excerpt

The utility of protein engineering, both the mutation and deletion of specific amino acids, to investigate protein structure and function has been demonstrated time and time again, and intermolecular and intramolecular interactions within the BAM complex and its individual components are no exception. Extensive efforts have probed conserved and unique amino acid sequences of the Bam proteins to define their...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacterial Outer Membrane Proteins
Share to Blotting, Western
Share to Cloning, Molecular

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Electrophoresis, Polyacrylamide Gel

Share to Endopeptidase K

Share to Hot Temperature

Share to Mutagenesis

Share to Protein Folding

Source

Open in PubMed Open full text

Identifiers

PMID: 26427681
DOI: 10.1007/978-1-4939-2871-2_10
PMCID: PMC4880027

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Methods to Characterize Folding and Function of BamA Cross-Link Mutants.PMID 26427681Read ↗

Functions of the BamBCDE Lipoproteins Revealed by Bypass Mutations in BamA.Semantic proximity Read ↗

Formation of a β-barrel membrane protein is catalyzed by the interior surface of the assembly machine protein BamA.Semantic proximity Read ↗

Lateral opening and exit pore formation are required for BamA function.Semantic proximity Read ↗

Outer membrane protein assembly mediated by BAM-SurA complexes.Semantic proximity Read ↗

The Structure of a BamA-BamD Fusion Illuminates the Architecture of the β-Barrel Assembly Machine Core.Semantic proximity Read ↗

The BAM complex subunit BamE (SmpA) is required for membrane integrity, stalk growth and normal levels of outer membrane {beta}-barrel proteins in Caulobacter crescentus.Semantic proximity Read ↗

Sequential and spatially restricted interactions of assembly factors with an autotransporter beta domain.Semantic proximity Read ↗

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

Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway.Semantic proximity Read ↗

BamA β16C strand and periplasmic turns are critical for outer membrane protein insertion and assembly.Semantic proximity Read ↗

Plasticity within the barrel domain of BamA mediates a hybrid-barrel mechanism by BAM.Semantic proximity Read ↗

Probing interactions of the Escherichia coli F0F1 ATP synthase beta and gamma subunits with disulphide cross-links.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.