It has been 25 years since the concept of intrinsically disordered proteins (IDPs) was proposed [1]. IDPs with intrinsically disordered regions (IDRs) longer than 30 residues are abundant in eukaryotes, accounting for 44 % of the human proteome, and are involved in crucial cellular processes, including transcription, translation, and signal transduction [2,3]. Numerous recent studies have shown that IDPs are also involved in diverse biological phenomena such as liquid-liquid phase separation (LLPS) [4], viral infection and disease. To understand the role of IDPs in these processes, the structure and dynamics of IDRs in isolation and in full-length proteins, the interactions of IDPs with their partners, the intracellular behavior of IDPs, and the mechanisms of coupled folding and binding of IDPs have been extensively studied using state-of-the-art experimental and theoretical methods. These include nuclear magnetic resonance (NMR) [5••,6], single-molecule fluorescence [6], small-angle X-ray scattering [7,8], electron paramagnetic resonance (EPR) [5••], and high-speed atomic force microscopy [9], as well as molecular dynamics (MD) simulations [10] and artificial intelligence [11]. In addition, advances have been made in drug discovery targeting interactions involving IDPs. This review highlights some of the exciting findings on these topics, particularly in the last two years.