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

Molecular basis of claudin-17 anion selectivity.

Cellular and molecular life sciences : CMLS - 1 Jan 2016

Conrad Marcel P, Piontek Jörg, Günzel Dorothee, Fromm Michael, Krug Susanne M

Abstract excerpt

Claudin-17 is a paracellular channel-forming tight junction protein. Unlike the cation channels claudin-2 and -15, claudin-17 forms a distinct anion-selective channel. Aim of this study was to determine the molecular basis of channel formation and charge selectivity of this protein. To achieve this, residues located in the extracellular loops (ECL) 1 and 2 of claudin-17 were substituted, preferably those whose...

Read the complete abstract on PubMed

Topics

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

Share to HEK293 Cells
Share to Claudins
Share to Dogs

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

Share to Anions

Share to Madin Darby Canine Kidney Cells

Share to Models, Molecular

Share to Protein Conformation

Share to Sequence Alignment

Source

Open in PubMed Open full text

Identifiers

PMID: 26194246
DOI: 10.1007/s00018-015-1987-y
PMCID: PMC11108356

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Molecular basis of claudin-17 anion selectivity.PMID 26194246Read ↗

Conserved aromatic residue confers cation selectivity in claudin-2 and claudin-10b.Semantic proximity Read ↗

Determinants contributing to claudin ion channel formation.Semantic proximity Read ↗

Claudins create charge-selective channels in the paracellular pathway between epithelial cells.Semantic proximity Read ↗

Channel functions of claudins in the organization of biological systems.Semantic proximity Read ↗

Polar and charged extracellular residues conserved among barrier-forming claudins contribute to tight junction strand formation.Semantic proximity Read ↗

Claudins in Renal Physiology and PathologySemantic proximity Read ↗

Assembly of Tight Junction Strands: Claudin-10b and Claudin-3 Form Homo-Tetrameric Building Blocks that Polymerise in a Channel-Independent Manner.Semantic proximity Read ↗

Molecular dynamics analyses of CLDN15 pore size and charge selectivitySemantic proximity Read ↗

Biochemical and biophysical analyses of tight junction permeability made of claudin-16 and claudin-19 dimerizationSemantic proximity Read ↗

Molecular dynamics analyses of CLDN15 pore size and charge selectivity.Semantic proximity Read ↗

Claudins and epithelial paracellular transport.Semantic proximity Read ↗

A multi-pore model of the blood-brain barrier tight junction strands recapitulates the permeability features of wild-type and mutant claudin-5.Semantic proximity Read ↗

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