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

Phosphate binding protein as the biorecognition element in a biosensor for phosphate.

Sensors and actuators. B, Chemical - 1 Jan 2004

Salins Lyndon L E, Deo Sapna K, Daunert Sylvia

Abstract excerpt

This work explores the potential use of a member of the periplasmic family of binding proteins, the phosphate binding protein (PBP), as the biorecognition element in a sensing scheme for the detection of inorganic phosphate (Pi). The selectivity of this protein originates from its natural role which, in Escherichia coli, is to serve as the initial receptor for the highly specific translocation of Pi to the...

Read the complete abstract on PubMed

Topics

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

Share to Biosensing Techniques
Share to Coumarins
Share to Cysteine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Environmental Monitoring

Share to Fluorescence

Share to Ligands

Share to Phosphate-Binding Proteins

Share to Phosphates

Source

Identifiers

PMID: 14997877
DOI: 10.1016/j.snb.2003.07.019

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Phosphate binding protein as the biorecognition element in a biosensor for phosphate.PMID 14997877Read ↗

A dynamical investigation of acrylodan-labeled mutant phosphate binding protein.Semantic proximity Read ↗

Direct, real-time measurement of rapid inorganic phosphate release using a novel fluorescent probe and its application to actomyosin subfragment 1 ATPase.Semantic proximity Read ↗

The X-ray crystal structures of two constitutively active mutants of the Escherichia coli PhoB receiver domain give insights into activation.Semantic proximity Read ↗

Probing of the substrate binding domain of lactose permease by a proton pulse.Semantic proximity Read ↗

Role of citrate and phosphate anions in the mechanism of iron(III) sequestration by ferric binding protein: kinetic studies of the formation of the holoprotein of wild-type FbpA and its engineered mutants.Semantic proximity Read ↗

Relative binding affinities of OmpR and OmpR-phosphate at the ompF and ompC regulatory sites.Semantic proximity Read ↗

Dominant role of local dipolar interactions in phosphate binding to a receptor cleft with an electronegative charge surface: equilibrium, kinetic, and crystallographic studies.Semantic proximity Read ↗

Detecting protein analytes that modulate transmembrane movement of a polymer chain within a single protein pore.Semantic proximity Read ↗

ATP hydrolysis-driven structural changes in the gamma-subunit of Escherichia coli ATPase monitored by fluorescence from probes bound at introduced cysteine residues.Semantic proximity Read ↗

Modulation of KdpD phosphatase implicated in the physiological expression of the kdp ATPase of Escherichia coli.Semantic proximity Read ↗

Influence of K+-dependent membrane lipid composition on the expression of the kdpFABC operon in Escherichia coli.Semantic proximity Read ↗

Substitutions of glycine residues Gly100 and Gly147 in conservative loops decrease rates of conformational rearrangements of Escherichia coli inorganic pyrophosphatase.Semantic proximity Read ↗

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