The synucleins are a family of intrinsically disordered proteins involved in various human
diseases. α‐Synuclein has been extensively characterized due to its role in Parkinson's …

Most known pathogenic mutations occur in protein-coding regions of DNA and change the
way proteins are made. Taking protein structure into account has therefore provided great …

The assembly of individual proteins into functional complexes is fundamental to nearly all
biological processes. In recent decades, many thousands of homomeric and heteromeric …

Intrinsically disordered proteins (IDPs), which lack folded structure and are disordered
under nondenaturing conditions, have been shown to perform important functions in a large …

Do young and old protein molecules have the same probability to be degraded? We addressed
this question using metabolic pulse-chase labeling and quantitative mass spectrometry …

Is the order in which proteins assemble into complexes important for biological function?
Here, we seek to address this by searching for evidence of evolutionary selection for ordered …

INTRODUCTION The assembly of proteins into complexes is crucial for most biological
processes. The three-dimensional structures of many thousands of homomeric and heteromeric …

Heterozygous missense mutations in coatomer protein subunit α, COPA, cause a syndrome
overlapping clinically with type I IFN-mediated disease due to gain-of-function in STING, a …

Protein interactions are often accompanied by significant changes in conformation. We have
analyzed the relationships between protein structures and the conformational changes they …

Most known disease-causing mutations occur in protein-coding regions of DNA. While some
of these involve a loss of protein function (eg, through premature stop codons or missense …