Yaoqi Zhou
Yaoqi Zhou
Senior Principal Investigator, Institute for Systems & Physical Biology, Shenzhen Bay Laboratory
Verified email at - Homepage
Cited by
Cited by
Distance‐scaled, finite ideal‐gas reference state improves structure‐derived potentials of mean force for structure selection and stability prediction
H Zhou, Y Zhou
Protein science 11 (11), 2714-2726, 2002
Improving prediction of secondary structure, local backbone angles and solvent accessible surface area of proteins by iterative deep learning
R Heffernan, K Paliwal, J Lyons, A Dehzangi, A Sharma, J Wang, A Sattar, ...
Scientific reports 5 (1), 1-11, 2015
Improving protein fold recognition and template-based modeling by employing probabilistic-based matching between predicted one-dimensional structural properties of query and …
Y Yang, E Faraggi, H Zhao, Y Zhou
Bioinformatics 27 (15), 2076-2082, 2011
Interpreting the folding kinetics of helical proteins
Y Zhou, M Karplus
Nature 401 (6751), 400-403, 1999
Real-time reliable determination of binding kinetics of DNA hybridization using a multi-channel graphene biosensor
S Xu, J Zhan, B Man, S Jiang, W Yue, S Gao, C Guo, H Liu, Z Li, J Wang, ...
Nature communications 8 (1), 14902, 2017
A knowledge-based energy function for protein-ligand, protein-protein, and protein-DNA complexes
C Zhang, S Liu, Q Zhu, Y Zhou
Journal of medicinal chemistry 48 (7), 2325-2335, 2005
Protein binding site prediction using an empirical scoring function
S Liang, C Zhang, S Liu, Y Zhou
Nucleic acids research 34 (13), 3698-3707, 2006
Capturing non-local interactions by long short-term memory bidirectional recurrent neural networks for improving prediction of protein secondary structure, backbone angles …
R Heffernan, Y Yang, K Paliwal, Y Zhou
Bioinformatics 33 (18), 2842-2849, 2017
SPINE X: improving protein secondary structure prediction by multistep learning coupled with prediction of solvent accessible surface area and backbone torsion angles
E Faraggi, T Zhang, Y Yang, L Kurgan, Y Zhou
Journal of computational chemistry 33 (3), 259-267, 2012
Fold recognition by combining sequence profiles derived from evolution and from depth‐dependent structural alignment of fragments
H Zhou, Y Zhou
Proteins: Structure, Function, and Bioinformatics 58 (2), 321-328, 2005
Specific interactions for ab initio folding of protein terminal regions with secondary structures
Y Yang, Y Zhou
Proteins: Structure, Function, and Bioinformatics 72 (2), 793-803, 2008
The distance fluctuation criterion for melting: Comparison of square-well and Morse potential models for clusters and homopolymers
Y Zhou, M Karplus, KD Ball, RS Berry
The Journal of chemical physics 116 (5), 2323-2329, 2002
Improving protein disorder prediction by deep bidirectional long short-term memory recurrent neural networks
J Hanson, Y Yang, K Paliwal, Y Zhou
Bioinformatics 33 (5), 685-692, 2017
Equilibrium thermodynamics of homopolymers and clusters: molecular dynamics and Monte Carlo simulations of systems with square-well interactions
Y Zhou, M Karplus, JM Wichert, CK Hall
The Journal of chemical physics 107 (24), 10691-10708, 1997
Sixty-five years of the long march in protein secondary structure prediction: the final stretch?
Y Yang, J Gao, J Wang, R Heffernan, J Hanson, K Paliwal, Y Zhou
Briefings in bioinformatics 19 (3), 482-494, 2018
Single‐body residue‐level knowledge‐based energy score combined with sequence‐profile and secondary structure information for fold recognition
H Zhou, Y Zhou
Proteins: Structure, Function, and Bioinformatics 55 (4), 1005-1013, 2004
Structural insights into the histone H1-nucleosome complex
BR Zhou, H Feng, H Kato, L Dai, Y Yang, Y Zhou, Y Bai
Proceedings of the National Academy of Sciences 110 (48), 19390-19395, 2013
Folding rate prediction using total contact distance
H Zhou, Y Zhou
Biophysical journal 82 (1), 458-463, 2002
First-order disorder-to-order transition in an isolated homopolymer model
Y Zhou, CK Hall, M Karplus
Physical review letters 77 (13), 2822, 1996
Folding thermodynamics of a model three-helix-bundle protein
Y Zhou, M Karplus
Proceedings of the National Academy of Sciences 94 (26), 14429-14432, 1997
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