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

Metabolic and chaperone gene loss marks the origin of animals: evidence for Hsp104 and Hsp78 chaperones sharing mitochondrial enzymes as clients.

PloS one - 1 Jan 2015

Erives Albert J, Fassler Jan S

Abstract excerpt

The evolution of animals involved acquisition of an emergent gene repertoire for gastrulation. Whether loss of genes also co-evolved with this developmental reprogramming has not yet been addressed. Here, we identify twenty-four genetic functions that are retained in fungi and choanoflagellates b...

Read the complete abstract on PubMed

Topics

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

Share to Aconitate Hydratase
Share to Bayes Theorem
Share to Endopeptidase Clp

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Heat-Shock Proteins

Share to Likelihood Functions

Share to Mitochondria

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 25710177
DOI: 10.1371/journal.pone.0117192
PMCID: PMC4339202

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-25710177-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Metabolic and chaperone gene loss marks the origin of animals: evidence for Hsp104 and Hsp78 chaperones sharing mitochondrial enzymes as clients.PMID 25710177Read ↗

Tuning the Hsp70 Chaperone Cycle: Emerging Roles of GrpE-Like NEFs in Proteostasis and Organelle FunctionSemantic proximity Read ↗

CLPX regulates erythroid heme synthesis by control of mitochondrial heme synthesis enzymes and iron utilizationSemantic proximity Read ↗

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

The Bacterial ClpXP-ClpB Family is Enriched with RNA-Binding Protein ComplexesSemantic proximity Read ↗

Diving into the Evolutionary History of HSC70-Linked Selective Autophagy Pathways: Endosomal Microautophagy and Chaperone-Mediated AutophagySemantic proximity Read ↗

Proteostatic tuning underpins the evolution of novel multicellular traits.Semantic proximity Read ↗

The stress of protein misfolding: from single cells to multicellular organisms.Semantic proximity Read ↗

[Iron and sulfur in proteins. How does the cell build Fe-S clusters, cofactors essential for life?].Semantic proximity Read ↗

Cell biology. "Pumping" iron: the proteins.Semantic proximity Read ↗

Guardians of the Genome: Iron–Sulfur Proteins in the NucleusSemantic proximity Read ↗

Energy transduction anchors genes in organelles.Semantic proximity Read ↗

The final stage of gene expression: chaperones and the regulation of protein fate.Semantic proximity Read ↗

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