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

Interaction with Cfd1 increases the kinetic lability of FeS on the Nbp35 scaffold.

The Journal of biological chemistry - 9 Aug 2013

Pallesen Leif J, Solodovnikova Natalia, Sharma Anil K, Walden William E

Abstract excerpt

P-loop NTPases of the ApbC/Nbp35 family are involved in FeS protein maturation in nearly all organisms and are proposed to function as scaffolds for initial FeS cluster assembly. In yeast and animals, Cfd1 and Nbp35 are homologous P-loop NTPases that form a heterotetrameric complex essential for FeS protein maturation through the cytosolic FeS cluster assembly (CIA) pathway. Cfd1 is conserved in animals, fungi,...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphatases
Share to GTP-Binding Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Iron-Sulfur Proteins

Share to Models, Biological

Share to Protein Binding

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 23798678
DOI: 10.1074/jbc.M113.486878
PMCID: PMC3743505

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

Interaction with Cfd1 increases the kinetic lability of FeS on the Nbp35 scaffold.PMID 23798678Read ↗

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

Turning Saccharomyces cerevisiae into a Frataxin-Independent Organism.Semantic proximity Read ↗

Assembly, activation, and trafficking of the Fet3p.Ftr1p high affinity iron permease complex in Saccharomyces cerevisiae.Semantic proximity Read ↗

Functional link between ribosome formation and biogenesis of iron-sulfur proteins.Semantic proximity Read ↗

The iron-sulphur protein Ind1 is required for effective complex I assembly.Semantic proximity Read ↗

HLH-30/TFEB rewires the chaperone network to promote proteostasis under conditions of Coenzyme A and Iron-Sulfur Cluster DeficiencySemantic proximity Read ↗

Mitochondrial Iba57p is required for Fe/S cluster formation on aconitase and activation of radical SAM enzymes.Semantic proximity Read ↗

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

Human mitochondrial complex I assembly is mediated by NDUFAF1.Semantic proximity Read ↗

Major targets of iron-induced protein oxidative damage in frataxin-deficient yeasts are magnesium-binding proteins.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 ↗

Requirement of the N-terminal extension for vacuolar trafficking and transport activity of yeast Ycf1p, an ATP-binding cassette transporter.Semantic proximity Read ↗

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