Mechanism of coupled folding and binding of an intrinsically disordered protein
By K. Sugase, H. J. Dyson, Peter E. Wright. Nature, 2007
1,009 citations recorded by the source corpus.
Subfields: Materials Chemistry, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/4d81e297796227492eb68f114e4adf4efdd117c1
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Materials Chemistry
- Burkhard Rost
- Avner Schlessinger
- Guy Yachdav
- Frank No'e
- Marco Punta
- Douglas E. V. Pires
- David B. Ascher
- László Kaján
In Molecular Biology
- Burkhard Rost
- Frank No'e
- Avner Schlessinger
- Guy Yachdav
- Lukasz Kurgan
- David B. Ascher
- Douglas E. V. Pires
- Marco Punta
Citations in the corpus
- DUET: a server for predicting effects of mutations on protein stability using an integrated computational approach (2014, background): “Users are encouraged to submit PDB files with a single chain with the exception of cases of proteins that fold upon binding (coupled folding and binding of intrinsically disordered proteins (24)).”
- Improved Disorder Prediction by Combination of Orthogonal Approaches (2009, background): “This simplification ignores the important roles that some disordered regions play in target recognition by forming highly specific electrostatic interactions and hydrogen bonds upon folding and binding to substrates [40,41], and through the use of conserved motifs [33,34].”
- Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies (2016, methodology): “The NMR techniques used to study these interactions can identify the unbound disordered IDP, the fully bound complex structure, and in some cases, stable intermediates (36, 37).”
- Identification of slow molecular order parameters for Markov model construction. (2013, background): “The entry represent the folded configuration of the pKID-CBP bound structure, determined through NMR [89].”
- Linking Folding and Binding (2009, background): “6 10(6) M 1 s (1)) followed by a slower structural rearrangement of the partly folded intermediate [32].”
- Continuous Distributed Representation of Biological Sequences for Deep Proteomics and Genomics (2015, neutral): “y play in cell biology, disordered proteins are considered to be an important class of proteins [19]. Several studies have focused on disordered peptides and their functional analysis in recent years [20, 21, 22]. In the present work, we introduce ProtVec for the visualization and characterization o”