Abundance of Intrinsically Unstructured Proteins ( IUPs ) in P . 4 falciparum and other Apicomplexan Parasite Proteomes

Tight regulation of unstructured proteins: from transcript synthesis to protein degradation.

Altered abundance of several intrinsically unstructured proteins (IUPs) has been associated with perturbed cellular signaling that may lead to pathological conditions such as cancer. Therefore, it is important to understand how cells precisely regulate the availability of IUPs. We observed that regulation of transcript clearance, proteolytic degradation, and translational rate contribute to con...

A novel two-dimensional electrophoresis technique for the identification of intrinsically unstructured proteins.

Intrinsically unstructured proteins (IUPs) lack a well defined three-dimensional structure under physiological conditions. They constitute a significant fraction of various proteomes, but only a handful of them have so far been identified. Here we report the development of a two-dimensional electrophoresis technique for their de novo recognition and characterization. This technique consists of ...

The interplay between structure and function in intrinsically unstructured proteins.

Intrinsically unstructured proteins (IUPs) are common in various proteomes and occupy a unique structural and functional niche in which function is directly linked to structural disorder. The evidence that these proteins exist without a well-defined folded structure in vitro is compelling, and justifies considering them a separate class within the protein world. In this paper, novel advances in...

Prediction of binding sites on Nucleic acid Binding Intrinsically Unstructured Proteins Using an Improved Prediction Algorithm Introduction: Intrinsically unstructured proteins (IUPs) are a novel class of proteins that, until a decade

Operational definition of intrinsically unstructured protein sequences based on susceptibility to the 20S proteasome.

Intrinsically unstructured proteins (IUPs), also known as natively unfolded proteins, lack well-defined secondary and tertiary structure under physiological conditions. In recent years, growing experimental and theoretical evidence has accumulated, indicating that many entire proteins and protein sequences are unstructured under physiological conditions, and that they play significant roles in ...