Direct observation of catch bonds involving cell-adhesion molecules

By B. Marshall, M. Long, J. W. Piper, T. Yago, R. McEver, Cheng-Long Zhu. Nature, 2003

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High-resolution atomic force microscopy and spectroscopy of native membrane proteins (2011, background): “However, compared with the His6–NTA bond, most receptor–ligand interactions are considerably weaker [26, 28, 205], such as the bond between the Strep-tagII and Strep-Tactin, a streptavidin variant optimized for Strep-tagII binding, which withstands only 37 pN (at 337 pN s−1) [27].”
The physics of cancer: the role of physical interactions and mechanical forces in metastasis (2011, positive): “The development of sophisticated biophysical tools for measuring the kinetic and micromechanical properties of single ligand–receptor bonds have allowed single-molecule affinity to be distinguished from multi-molecular avidit”
Demonstration of catch bonds between an integrin and its ligand (2009, positive): “The effects of dimeric bonds are to shift the lifetime versus force curve of the monomeric bond rightward toward doubling the force and upward toward doubling the lifetime (Marshall et al., 2003).”
Theory, analysis, and interpretation of single-molecule force spectroscopy experiments (2008, background): “In fact, in experiments, so-called catch-bonds have been reported in which force initially slows down rupture, before accelerating it at high force (37, 38).”