Special Issue "Metallothioneins in Bioinorganic Chemistry: Recent Developments"
Deadline for manuscript submissions: closed (16 April 2017)
PD. Dr. Eva Freisinger
Department of Chemistry, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland
Website | E-Mail
Phone: +41 44 63 546 21
Interests: structures and properties of plant metallothioneins; gene cloning, protein over-expression, and purification; spectroscopic and biochemical characterization of MTs; determination of metal ion binding affinities and redox states; structure determination of MTs by X-ray and NMR
“Metallothioneins”—this is the name of a superfamily combining proteins with two rather basic characteristics, a high percentage of thiolate groups in form of cysteine residues and the ability to coordinate certain metal ions via these thiolate ligands. There is, however, no requirement for a specific function or structure. While the name was initially invented 60 years ago for a class of proteins found in mammalians, all having very similar sequences and a common three-dimensional structure involving metal-thiolate clusters, nowadays, proteins from nearly all kingdoms of life, among them vertebrates, molluscs, nematodes, prokaryotes, fungi, and plants are included. Often the classification as metallothionein is solely based on the respective gene sequence without further knowledge about the metal ion binding ability of the encoded protein. The elucidation of the metal ion binding modes including cluster formation, the spectroscopic properties and last not least the three-dimensional structures of the members of this very variable superfamily belongs to the classical research fields of Bioinorganic Chemistry. Beyond this basic characterisation, unravelling the diversity of functions including, but not being restricted to, metal ion homeostasis and detoxification as well as redox activities, investigating the role of MTs in certain diseases, and inventing biotechnological applications are hot topics in MT research.
It is the aim of this Special Issue to highlight the recent developments in the field in form of Topical Reviews, Articles, and Short Communications. I invite you all to make this Special Issue a valuable source of new and exciting information about this very unique protein superfamily.
PD. Dr. Eva Freisinger
Manuscript Submission Information
Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.
Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access monthly journal published by MDPI.
Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.
• metal clusters
• metal ion homeostasis
• heavy metal detoxification
• reactive oxygen species (ROS) scavenging
The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.
Proteomic Zn2+ Trafficking: Where Does Metallothionein Fit in?
Petering et al.
Mammalian metallothionein-3: new functional and structural insights
Vasak et al.
In depth analysis of the metal binding abilities of Ll-MT (Litorina littorea metallothionein) and two truncated mutants
Capdevila et al.
In depth analysis of the metal binding abilities of BgMT (Biomphalaria glabrata metallothionein) and two crucial, natural (CY and KN) mutants
Capdevila et al.
cDNA sequence, protein expression and metal binding properties of metallothionein from wild populations of the catfish Clarias gariepinus: Potential as biomarker for metal pollution of Zambia’s Kafue River
Blindauer et al.
The structures of human metallothioneins and their functions in human zinc metabolism
Maret et al.
Regulation of MT3 by a variety of metal ions in human neuronal cell cultures
Austin et al.
Höckner et al.