Speeding molecular recognition by using the folding funnel: the fly-casting mechanism.

By Benjamin A. Shoemaker, J. Portman, Peter G. Wolynes. Proceedings of the National Academy of Sciences of the United States of America, 2000

976 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/0a6147cd4f042202d0f55e5c8d593d886db16740

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Citations in the corpus

Identification of slow molecular order parameters for Markov model construction. (2013, background): “…much interest (e.g. for the druggability of protein-protein interactions) to investigate whether the presence of pre-formed elements causes folded conformations to be selected from the ensemble (conformational selection) [54], or whether the binding rather occurs through induced-ﬁt mechanics [85].”
The interplay between structure and function in intrinsically unstructured proteins (2005, background): “noted that both may be interpreted in terms of the current ‘‘fly-casting’’ [76] model of IUP recognition, which suggests that IUPs make use of their folding funnel in binding to their partner.”
Water mediation in protein folding and molecular recognition. (2006, background): “recognition via the fly-casting mechanism (134), in which the water acts as a molecular glue that increases structural adaptability.”
Integrin structure, activation, and interactions. (2011, background): “Because they are extended and flexible, the cytoplasmic tails, especially b, can “flycast” (Shoemaker et al. 2000) and reach out to form “hub” interactions with a number of proteins (Wegener and Campbell 2008; Legate and Fassler 2009).”
Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics (2019, background): “In this model, functional protein interaction with its partners resembles fitting a specifically shaped key into a unique lock, where only the substrate with the correct shape/size (key) is able to fit into the specifically shaped active site (key-hole) of the particular protein (lock), and where a ”
Linking Folding and Binding (2009, background): “Folding and binding kinetics It has been suggested that the rate of macromolecular association is enhanced by the presence of disorder [36,48].”
Analysis of molecular recognition features (MoRFs). (2006, background): “The open, extended structure of MoRFs may enable an increased speed of interaction; macromolecular association rates are thought to be substantially improved by an initial, relatively non-specific association enabled by flexible (disordered) recognition segments, mechanistically describe as the ‘‘fl”