• Special Issue Topic

    Posttranslational Modifications in Health and Disease

    Submission Deadline: May 31, 2024

    Guest Editor

    Prof. Oliver Krämer E-Mail

    Institute of Toxicology, Johannes-Gutenberg University of Mainz, Mainz, Germany


    About the Special Issue

    Posttranslational modifications increase the functions of proteins and thereby regulate key biological functions. Examples of posttranslational modifications are acetylation, ubiquitinylation, and sumoylation of lysine residues and phosphorylation of serine, threonine, and tyrosine residues. The balance between the attachment and removal of posttranslational modifications is dysregulated in severe diseases including cancers, neurodegeneration, and immune failure. Therefore, enzymes modulating posttranslational modifications are in the focus of current research and drug development. Increasing evidence indicates that inhibitors of dysregulated posttranslational modification patterns are useful to treat humans.
    In this Special Issue, short and long original research articles, reviews, and case reports are welcome. Submitted articles should be pertinent to the analysis of posttranslational modifications that are dysregulated in tumor cells. This also applies to drugs that correct aberrant modifications to combat cancer. Basic research articles as well as reports with a strong clinical focus are welcome.

    Keywords: acetylation; cancer; posttranslational modification acetylation; health and disease; inhibitor(s); methylation; SUMO; tumorigenesis; phosphorylation; posttranslational modification(s); ubiquitin

    Call for Papers

    Published Articles

    Open Access
    Review
    Post-translational modulation of cell signalling through protein succinylation
    Cells need to adapt their activities to extra- and intracellular signalling cues. To translate a received extracellular signal, cells have specific receptors that transmit the signal to downstream p [...] Read more.
    Katharina F. Kubatzky ... Dayoung Yu
    Published: December 27, 2023 Explor Target Antitumor Ther. 2023;4:1260–1285
    DOI: https://doi.org/10.37349/etat.2023.00196
    View:1064
    Download:35
    Times Cited: 0
    Open Access
    Review
    Recent advancements in targeted protein knockdown technologies—emerging paradigms for targeted therapy
    A generalized therapeutic strategy for various disease conditions, including cancer, is to deplete or inactivate harmful protein targets. Various forms of protein or gene silencing molecules, e.g.,  [...] Read more.
    Mansi Joshi ... Abhijit De
    Published: December 26, 2023 Explor Target Antitumor Ther. 2023;4:1227–1248
    DOI: https://doi.org/10.37349/etat.2023.00194
    View:962
    Download:40
    Times Cited: 0
    Open Access
    Review
    Medicinal chemistry advances in targeting class I histone deacetylases
    Histone deacetylases (HDACs) are a class of zinc (Zn)-dependent metalloenzymes that are responsible for epigenetic modifications. HDACs are largely associated with histone proteins that regulate gen [...] Read more.
    Diaaeldin I. Abdallah ... Patrick T. Gunning
    Published: August 31, 2023 Explor Target Antitumor Ther. 2023;4:757–779
    DOI: https://doi.org/10.37349/etat.2023.00166
    View:1328
    Download:50
    Open Access
    Review
    Protein ISGylation: a posttranslational modification with implications for malignant neoplasms
    Interferon (IFN)-stimulated gene 15 (ISG15) is a member of the ubiquitin-like (UBL) protein family that can modify specific proteins via a catalytic process called ISGylation. This posttranslational [...] Read more.
    Angeles C. Tecalco-Cruz, Jesús Zepeda-Cervantes
    Published: August 31, 2023 Explor Target Antitumor Ther. 2023;4:699–715
    DOI: https://doi.org/10.37349/etat.2023.00162