Physical, chemical and biological stress factors, such as microbial infection, upregulate the
transcription levels of a number of plant genes, coding for the so‐called pathogenesis …

Recent years have witnessed major advances in our understanding of the structural basis of
protein aggregation on several fronts. Firstly, high-resolution structural information that …

The all-α helix multi-domain protein bovine serum albumin (BSA) aggregates at elevated
temperatures. Here we show that these thermal aggregates have amyloid properties. They …

Although intermediates have long been recognised as fascinating species that form during
the folding of large proteins, the role that intermediates play in the folding of small, single …

We have established a time-resolved fluorescence assay to study fibrillation of the 29
residue peptide hormone glucagon under a variety of different conditions in a high …

Recent years have seen the publication of both empirical and theoretical relationships
predicting the rates with which proteins fold. Our ability to test and refine these relationships …

Many neurodegenerative diseases are linked with formation of amyloid aggregates. It is
increasingly accepted that not the fibrils but rather oligomeric species are responsible for …

Polyclonal stimuli like phorbol myristate acetate (PMA) plus calcium ionophore (Ca-I),
concanavalin A (ConA) or anti-CD3 plus anti-CD28 (αCD3/αCD28) are widely used T cell …

Theoretical and experimental studies of protein folding have suggested that the topology of
the native state may be the most important factor determining the folding pathway of a …

Mutations in the human TGFBI gene encoding TGFBIp have been linked to protein deposits
in the cornea leading to visual impairment. The protein consists of an N-terminal Cys-rich …