Assessing posttranslational modification (PTM) patterns within protein molecules and
reading their functional implications present grand challenges for plant biology. We combine …

Proteases enzymatically hydrolyze peptide bonds in substrate proteins, resulting in a
widespread, irreversible posttranslational modification of the protein's structure and …

Characterization of the chloroplast proteome is needed to understand the essential
contribution of the chloroplast to plant growth and development. Here we present a large …

The vast majority of eukaryotic proteins are N‐terminally modified by one or more
processing enzymes. Enzymes acting on the very first amino acid of a polypeptide include …

N-terminal methionine excision (NME) is the major proteolytic pathway responsible for the
diversity of N-terminal amino acids in proteins. Dedicated NME components have been …

N-terminal protein modifications correspond to the first modifications which in principle any
protein may undergo, before translation is completed by the ribosome. This class of …

The Arg/N-end rule pathway targets for degradation proteins that bear specific unacetylated
N-terminal residues while the Ac/N-end rule pathway targets proteins through their N α …

The N-end rule pathway of targeted proteolysis, which relates the stability of a protein to the
nature of its N-terminus, has emerged as a key regulator of diverse processes in eukaryotes …

This review will assess new features reported for the molecular and biochemical aspects of
cysteine and methionine biosynthesis in Arabidopsis thaliana with regards to early …

Nod-like receptors (NLRs) serve as immune receptors in plants and animals. The stability of
NLRs is tightly regulated, though its mechanism is not well understood. Here, we show the …