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

The dynamics of assembly of a cytoplasmic membrane protein in Escherichia coli.

The Journal of biological chemistry - 15 Mar 1992

Traxler B, Lee C, Boyd D, Beckwith J

Abstract excerpt

The topology of integral cytoplasmic membrane proteins can be analyzed using alkaline phosphatase fusions by determining which constructs have low and which have high specific activity. We show that in all cases the enzymatic activity is due to the fraction of the alkaline phosphatase moiety of the fusion protein localized to the periplasm. We present evidence that these fusions can also be used to analyze the...

Read the complete abstract on PubMed

Topics

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

Share to Carrier Proteins
Share to Escherichia coli
Share to Escherichia coli Proteins

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

Share to Genes, Bacterial

Share to Genotype

Share to Membrane Proteins

Share to Models, Biological

Share to Recombinant Fusion Proteins

Source

Identifiers

PMID: 1544915

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

The dynamics of assembly of a cytoplasmic membrane protein in Escherichia coli.PMID 1544915Read ↗

Synthetic competition between cytoplasmic folding and translocation of a soluble membrane protein domain.Semantic proximity Read ↗

The protein translocation apparatus contributes to determining the topology of an integral membrane protein in Escherichia coli.Semantic proximity Read ↗

Folding and assembly of bacterial alkaline phosphatase in vitro and in vivo.Semantic proximity Read ↗

A topological analysis of subunit alpha from Escherichia coli F1F0-ATP synthase predicts eight transmembrane segments.Semantic proximity Read ↗

Targeting of signal sequenceless proteins for export in Escherichia coli with altered protein translocase.Semantic proximity Read ↗

A simple screen for permissive sites in proteins: analysis of Escherichia coli lac permease.Semantic proximity Read ↗

Essential features of the pathway for protein translocation across the Escherichia coli cytoplasmic membrane.Semantic proximity Read ↗

McsA and B mediate the delocalization of competence proteins from the cell poles of Bacillus subtilis.Semantic proximity Read ↗

Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli.Semantic proximity Read ↗

Molecular biology of the lactose carrier of Escherichia coli.Semantic proximity Read ↗

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.Semantic proximity Read ↗

Signal sequence processing is required for the assembly of LamB trimers in the outer membrane of Escherichia coli.Semantic proximity Read ↗

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