S100A1 is a member of the S100 family of calcium-binding proteins. As with most S100
proteins, S100A1 undergoes a large conformational change upon binding calcium as …

Molecular docking has become a valuable technique for structure-based drug discovery,
including fragment-based approaches. This review summarizes the latest development in …

The S100P protein is a member of the S100 family of calcium-binding proteins and
possesses both intracellular and extracellular functions. Extracellular S100P binds to the cell …

Protein-protein and protein-nucleic acid interactions are involved in many regulatory cellular
pathways, playing a key role in cell growth and proliferation, as well as in the progression …

The unique ability of intrinsically disordered proteins (IDPs) to fold upon binding to partner
molecules makes them functionally well-suited for cellular communication networks. For …

Giardiasis is a gastrointestinal diarrheal illness caused by the protozoan parasite Giardia
duodenalis, which affects annually over 200 million people worldwide. The limited …

The rapid increase of antimicrobial resistance against conventional antibiotics has resulted
in a significant focus on the use of peptides as antimicrobial agents. Understanding the …

Weak interactions form the core basis of a vast number of biological processes, in particular,
those involving intrinsically disordered proteins. Here, we establish a new technique …

Structural studies are part of a rational drug design program aimed at inhibiting the S100B−
p53 interaction and restoring wild-type p53 function in malignant melanoma. To this end …

The interaction between human S100 calcium-binding protein B (S100B) and the tumor
suppressor protein p53 is considered to be a possible therapeutic target for malignant …