To accomplish this, cells have evolved a sophisticated network of protein quality control machines consisting of molecular chaperones and energy-dependent proteases, which monitor the protein folding ...

Molecular chaperones have long been heralded as machines for folding and salvaging proteins. However, not every attempt to fold or refold a protein can be successful. Chaperones are known to ...

Figure 1: The molecular chaperone network. Client proteins rely on sequential interactions with chaperones, cochaperones, and chaperonins to fold into an active, native, state. Thus, functional ...

Previous studies have shown that mammalian cells express several hundreds of molecular chaperones, proteins that preserve or ...

Funding from FightMND enables Professor Heath Ecroyd and team to continue cutting-edge research Professor Heath Ecroyd and ...

Yet, despite their crucial role, the precise molecular mechanism of Hsp70 chaperones has remained elusive for decades. Using a cutting-edge nanopore single-molecule technique, a team has now made ...

A new review was published in Oncotarget's Volume 15 on October 1, 2024, entitled, "Molecular chaperones: Guardians of tumor ...

The main job of HSF1 is to regulate the induction of molecular chaperones and other heat shock proteins—permitting cell survival under stressful, protein-damaging conditions. HSF1 is activated ...

Dr. Francis T.F. Tsai was awarded the 2008 Hackerman Award for his innovative work on determining three-dimensional structures of molecular chaperones and multi-component protein assemblies involved ...

There are five APs (AP1-5) in mammalian cells. We found that the assembly of AP2 is assisted by two chaperones: AAGAB and CCDC32. Our current research focuses on unraveling the molecular mechanisms by ...