Post-translational modifications are at the apex of cellular communication and eventually
regulate every aspect of life. The identification of new post-translational modifiers is opening …

Post-translational modifications of cellular substrates with ubiquitin and ubiquitin-like
proteins (UBLs), including ubiquitin, SUMOs, and neural precursor cell–expressed …

Ubiquitin-fold modifier 1 (UFM1) is a ubiquitin-like protein covalently conjugated with
intracellular proteins through ufmylation, similar to ubiquitylation. Ufmylation is involved in …

UFMylation involves the covalent modification of substrate proteins with UFM1 (Ubiquitin‐
fold modifier 1) and is important for maintaining ER homeostasis. Stalled translation triggers …

Post-translational modifications (PTMs) add a major degree of complexity to the proteome
and are essential controllers of protein homeostasis. Amongst the hundreds of PTMs …

Protein UFMylation, ie, post‐translational modification with ubiquitin‐fold modifier 1 (UFM1),
is essential for cellular and endoplasmic reticulum homeostasis. Despite its biological …

Besides ubiquitin (Ub), humans have a set of ubiquitin-like proteins (UBLs) that can also
covalently modify target proteins. To date, less is known about UBLs than Ub and even less …

An essential first step in the post-translational modification of proteins with UFM1,
UFMylation, is the proteolytic cleavage of pro-UFM1 to expose a C-terminal glycine. Of the …

Stalled ribosomes at the endoplasmic reticulum (ER) are covalently modified with the
ubiquitin-like protein UFM1 on the 60S ribosomal subunit protein RPL26 (also known as …

Reversible modification of target proteins by ubiquitin and ubiquitin-like proteins (UBLs) is
widely used by eukaryotic cells to control protein fate and cell behaviour. UFM1 is a UBL that …