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

Further insights into the metal ion binding abilities and the metalation pathway of a plant metallothionein from Musa acuminata.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry - 1 Jan 2018

Cabral Augusto C S, Jakovleska Jovana, Deb Aniruddha, Penner-Hahn James E, Pecoraro Vincent L, Freisinger Eva

Abstract excerpt

The superfamily of metallothioneins (MTs) combines a diverse group of metalloproteins, sharing the characteristics of rather low molecular weight and high cysteine content. The latter provides MTs with the capability to coordinate thiophilic metal ions, in particular those with a d 10 electron configuration. The sub-family of plant MT3 proteins is only poorly characterized and there is a complete lack of...

Read the complete abstract on PubMed

Topics

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

Share to Cadmium
Share to Cobalt

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Histidine

Share to Hydrolysis

Share to Metallothionein

Share to Peptide Fragments

Source

Open in PubMed Open full text

Identifiers

PMID: 29218632
DOI: 10.1007/s00775-017-1513-9
PMCID: PMC5756683

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

Further insights into the metal ion binding abilities and the metalation pathway of a plant metallothionein from Musa acuminata.PMID 29218632Read ↗

Uncovering the copper(I) binding abilities of a unique fungal metallothionein: characterization of Yarrowia lipolytica MT and its Y54C mutant.Semantic proximity Read ↗

Investigating the influence of histidine residues on the metal ion binding ability of the wheat metallothionein γ-Ec-1 domain.Semantic proximity Read ↗

Molecular strategies to replace the structural metal site in the prokaryotic zinc finger domain.Semantic proximity Read ↗

Contributions of primary coordination ligands and importance of outer sphere interactions in UFsc, a de novo designed protein with high affinity for metal ions.Semantic proximity Read ↗

Sunflower metallothionein family characterisation. Study of the Zn(II)- and Cd(II)-binding abilities of the HaMT1 and HaMT2 isoforms.Semantic proximity Read ↗

A histidine-rich Pseudomonas metallothionein with a disordered tail displays higher binding capacity for cadmium than zinc.Semantic proximity Read ↗

Histidine ligands in bacterial metallothionein enhance cluster stability.Semantic proximity Read ↗

Asymmetric functions of a binuclear metal center within the transport pathway of a human zinc transporter ZIP4.Semantic proximity Read ↗

Human metallothionein metallomicsSemantic proximity Read ↗

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

Crystal structures of a ZIP zinc transporter reveal a binuclear metal center in the transport pathway.Semantic proximity Read ↗

Diversity and distribution of plant metallothioneins: a review of structure, properties and functions.Semantic proximity Read ↗

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