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

Combinatorial mutagenesis analysis of residues in the channel constriction loop L3 and neighbouring beta-strands in the LamB glycoporin of Escherichia coli.

Molecular membrane biology - 1 Jan 2000

Chan W C, Schirmer T, Ferenci T

Abstract excerpt

Members of the LamB family of sugar-selective porins (glycoporins) are beta-barrel proteins in the outer membrane of Gram-negative bacteria. To study the determinants of structure and sugar selectivity, 68 non-identical single amino acid substitutions were introduced into the stretch of sequence consisting of residues 106 through 125 in Escherichia coli LamB. This region includes all bar one residue of the...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Antibodies, Monoclonal

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

Share to Binding Sites

Share to Escherichia coli

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Conformation

Share to Sequence Homology, Amino Acid

Source

Identifiers

PMID: 9147661
DOI: 10.3109/09687689609160573

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

Combinatorial mutagenesis analysis of residues in the channel constriction loop L3 and neighbouring beta-strands in the LamB glycoporin of Escherichia coli.PMID 9147661Read ↗

Combinatorial mutagenesis of the lamB gene: residues 41 through 43, which are conserved in Escherichia coli outer membrane proteins, are informationally important in maltoporin structure and function.Semantic proximity Read ↗

In vivo and in vitro studies of major surface loop deletion mutants of the Escherichia coli K-12 maltoporin: contribution to maltose and maltooligosaccharide transport and binding.Semantic proximity Read ↗

Further genetic analysis of the C-terminal external loop region in Escherichia coli maltoporin.Semantic proximity Read ↗

Site-directed mutagenesis of tyrosine 118 within the central constriction site of the LamB (maltoporin) channel of Escherichia coli. II. Effect on maltose and maltooligosaccharide binding kinetics.Semantic proximity Read ↗

In vivo and in vitro studies of transmembrane beta-strand deletion, insertion or substitution mutants of the Escherichia coli K-12 maltoporin.Semantic proximity Read ↗

Generation and evaluation of a large mutational library from the Escherichia coli mechanosensitive channel of large conductance, MscL: implications for channel gating and evolutionary design.Semantic proximity Read ↗

Phenotypic characterization of pore mutants of the Vibrio cholerae porin OmpU.Semantic proximity Read ↗

Sucrose transport through maltoporin mutants of Escherichia coli.Semantic proximity Read ↗

Sugar transport through maltoporin of Escherichia coli: role of the greasy slide.Semantic proximity Read ↗

Distinct patterns of mutational sensitivity for λ resistance and maltodextrin transport in Escherichia coli LamB.Semantic proximity Read ↗

Fine-Tuning of σE Activation Suppresses Multiple Assembly-Defective Mutations in Escherichia coli.Semantic proximity Read ↗

Mutational analysis supports a role for multiple structural features in the C-terminal secretion signal of Escherichia coli haemolysin.Semantic proximity Read ↗

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