Mass spectrometry (MS) has become one of the key technologies of structural biology. In this
review, the contributions of chemical cross-linking combined with mass spectrometry (XL …

Proteomics researchers today face an interesting challenge: how to choose among the
dozens of data processing and analysis pipelines available for converting tandem mass …

Herpesviruses assemble large enveloped particles that are difficult to characterize
structurally due to their size, fragility and complex multilayered proteome with partially …

Over the past decade, cross-linking mass spectrometry (CLMS) has developed into a robust
and flexible tool that provides medium-resolution structural information. CLMS data provide …

A better understanding of the molecular mechanisms underlying disease is key for
expediting the development of novel therapeutic interventions. Disease mechanisms are …

Defining protein–protein interactions (PPIs) in their native environment is crucial to
understanding protein structure and function. Cross-linking–mass spectrometry (XL-MS) has …

The ability of living systems to adapt to changing conditions originates from their capacity to
change their molecular constitution. This is achieved by multiple mechanisms that modulate …

Proteins adopt different higher-order structures (HOS) to enable their unique biological
functions. Understanding the complexities of protein higher-order structures and dynamics …

Protein-protein interactions are fundamental to the formation of intricate interaction networks
and the assembly of multisubunit protein complexes that represent the functional …

Chemical cross-linking in combination with mass spectrometric analysis of the created cross-
linked products is an emerging technology aimed at deriving valuable structural information …