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Protein Science : a Publication of the Protein Society|February 18, 2014
Advantages of proteins being disorderedZhirong Liu, Yongqi HuangPlos One|November 17, 2010
Nonnative interactions in coupled folding and binding processes of intrinsically disordered proteinsYongqi Huang, Zhirong LiuInternational Journal of Molecular Sciences|May 5, 2011
Anchoring intrinsically disordered proteins to multiple targets: lessons from N-terminus of the p53 proteinYongqi Huang, Zhirong LiuProtein Science : a Publication of the Protein Society|December 15, 2012
Evidences for the unfolding mechanism of three-dimensional domain swappingZhirong Liu, Yongqi HuangProteins|October 16, 2010
Smoothing molecular interactions: the "kinetic buffer" effect of intrinsically disordered proteinsYongqi Huang, Zhirong LiuJournal of Molecular Biology|September 15, 2009
Kinetic advantage of intrinsically disordered proteins in coupled folding-binding process: a critical assessment of the "fly-casting" mechanismYongqi Huang, Zhirong LiuChemistry (Weinheim an Der Bergstrasse, Germany)|February 26, 2013
Do intrinsically disordered proteins possess high specificity in protein-protein interactions?Yongqi Huang, Zhirong LiuProteins|March 14, 2012
Three-dimensional domain swapping in the protein structure spaceYongqi Huang, Huaiqing Cao, Zhirong LiuProteins|March 29, 2016
Interplay between binding affinity and kinetics in protein-protein interactionsHuaiqing Cao, Yongqi Huang, Zhirong LiuPlos Computational Biology|October 3, 2012
Binding of two intrinsically disordered peptides to a multi-specific protein: a combined Monte Carlo and molecular dynamics studyIskra Staneva, Yongqi Huang, Zhirong Liu, et al.Pageof 40