Kathrin Lang

This paper designs de novo ligases that achieve site-specific ubiquitylation of a target protein with high selectivity and efficiency.

This paper introduces a modular genetic code expansion approach to install diverse lysine acylations on proteins, enabling systematic studies of their functional impacts.

This paper demonstrates single-molecule protein sequencing with single-amino-acid resolution using nanopores and an unfoldase, enabling detection of amino acid substitutions.

The paper maps the functional importance of site-specific ubiquitination across the human proteome by analyzing conservation, perturbation, and machine learning scores.

This paper introduces UbyW, a platform for site-specific ubiquitylation using UBE2W, enabling efficient production of ubiquitylated proteins and identifying USP15 as a deubiquitylase for Ran K71 monoubiquitylation.

The paper determines how the human 26S proteasome distinguishes between K48-linked and K11/K48-branched ubiquitin chains through structural analysis and functional studies.

This paper develops a one-pot dual protein labelling method using orthogonal reactions to enable simultaneous mechanical and fluorescent readouts in optical tweezers for studying protein conformational dynamics.

This paper improves genetic code expansion by engineering a bacterial transporter to enhance non-canonical amino acid uptake, enabling efficient incorporation of multiple ncAAs into proteins.