@inbook{14848,
  abstract     = {Regulating protein states is considered the core function of chaperones. However, despite their importance to all major cellular processes, the conformational changes that chaperones impart on polypeptide chains are difficult to study directly due to their heterogeneous, dynamic, and multi-step nature. Here, we review recent advances towards this aim using single-molecule manipulation methods, which are rapidly revealing new mechanisms of conformational control and helping to define a different perspective on the chaperone function.},
  author       = {Wruck, F. and Avellaneda Sarrió, Mario and Naqvi, M. M. and Koers, E. J. and Till, K. and Gross, L. and Moayed, F. and Roland, A. and Heling, L. W. H. J. and Mashaghi, A. and Tans, S. J.},
  booktitle    = {Biophysics of Molecular Chaperones},
  editor       = {Hiller, Sebastian and Liu, Maili and He, Lichun},
  isbn         = {9781839162824},
  pages        = {278--318},
  publisher    = {Royal Society of Chemistry},
  title        = {{Probing Single Chaperone Substrates}},
  doi          = {10.1039/bk9781839165986-00278},
  volume       = {29},
  year         = {2023},
}

@article{12085,
  abstract     = {Molecular catch bonds are ubiquitous in biology and essential for processes like leucocyte extravasion1 and cellular mechanosensing2. Unlike normal (slip) bonds, catch bonds strengthen under tension. The current paradigm is that this feature provides ‘strength on demand3’, thus enabling cells to increase rigidity under stress1,4,5,6. However, catch bonds are often weaker than slip bonds because they have cryptic binding sites that are usually buried7,8. Here we show that catch bonds render reconstituted cytoskeletal actin networks stronger than slip bonds, even though the individual bonds are weaker. Simulations show that slip bonds remain trapped in stress-free areas, whereas weak binding allows catch bonds to mitigate crack initiation by moving to high-tension areas. This ‘dissociation on demand’ explains how cells combine mechanical strength with the adaptability required for shape change, and is relevant to diseases where catch bonding is compromised7,9, including focal segmental glomerulosclerosis10 caused by the α-actinin-4 mutant studied here. We surmise that catch bonds are the key to create life-like materials.},
  author       = {Mulla, Yuval and Avellaneda Sarrió, Mario and Roland, Antoine and Baldauf, Lucia and Jung, Wonyeong and Kim, Taeyoon and Tans, Sander J. and Koenderink, Gijsje H.},
  issn         = {1476-4660},
  journal      = {Nature Materials},
  number       = {9},
  pages        = {1019--1023},
  publisher    = {Springer Nature},
  title        = {{Weak catch bonds make strong networks}},
  doi          = {10.1038/s41563-022-01288-0},
  volume       = {21},
  year         = {2022},
}