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

In vitro reconstitution, functional dissection, and mutational analysis of metal ion transport by mitoferrin-1.

The Journal of biological chemistry - 9 Mar 2018

Christenson Eric T, Gallegos Austin S, Banerjee Anirban

Abstract excerpt

Iron is universally important to cellular metabolism, and mitoferrin-1 and -2 have been proposed to be the iron importers of mitochondria, the cell's assembly plant of heme and iron-sulfur clusters. These iron-containing prosthetic groups are critical for a host of physiological processes ranging from oxygen transport and energy consumption to maintaining protein structural integrity. Mitoferrin-1 (Mfrn1) belongs...

Read the complete abstract on PubMed

Topics

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

Share to Cichlids
Share to Cobalt
Share to Fish Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Liposomes

Share to Manganese

Share to Nickel

Share to Pichia

Source

Open in PubMed Open full text

Identifiers

PMID: 29305420
DOI: 10.1074/jbc.M117.817478
PMCID: PMC5846140

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

In vitro reconstitution, functional dissection, and mutational analysis of metal ion transport by mitoferrin-1.PMID 29305420Read ↗

Ins and Outs: Recent Advancements in Membrane Protein-Mediated Prokaryotic Ferrous Iron TransportSemantic proximity Read ↗

Iron-sulfur cluster biosynthesis and trafficking - impact on human disease conditions.Semantic proximity Read ↗

Iron transport across biologic membranes.Semantic proximity Read ↗

Iron TransportSemantic proximity Read ↗

Recent progress in structure-function analyses of Nramp proton-dependent metal-ion transporters.Semantic proximity Read ↗

H(+)-coupled divalent metal-ion transporter-1: functional properties, physiological roles and therapeutics.Semantic proximity Read ↗

Analysis of NFU-1 metallocofactor binding-site substitutions-impacts on iron-sulfur cluster coordination and protein structure and function.Semantic proximity Read ↗

Understanding the binding properties of an unusual metal-binding protein--a study of bacterial frataxin.Semantic proximity Read ↗

Structure-function analysis of NEET proteins uncovers their role as key regulators of iron and ROS homeostasis in health and disease.Semantic proximity Read ↗

Genetic, Biochemical, and Biophysical Methods for Studying FeS Proteins and Their Assembly.Semantic proximity Read ↗

The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins.Semantic proximity Read ↗

MICU1 modulates MCU ion selectivity and tolerance to manganese stressSemantic proximity Read ↗

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