Christopher W. V. Hogue

Associate Professor, Department of Biological Sciences
Principal Investigator, Research Center of Excellence in Mechanobiology

Contact Information
RCE in Mechanobiology
National University of Singapore
T-Lab #05-04
5A Engineering Drive 1
Singapore 117411

E-mail: dbshcwv (at)
Phone: (65) 9487 5537
Office: (65) 6516 7066
fax: (65) 6774 2540


2007-Associate Professor, Dept. of Biological Sciences, National University of Singapore
2004-2007 Adjunct Professor, Dept. of Biological Sciences, National University of Singapore
2004-2007 Associate Professor, Dept. of Biochemistry, University of Toronto
1997-2004 Assistant Professor, Dept. of Biochemistry, University of Toronto
1997-2005 Scientist, Bioinformatcs. Samuel Lunenfeld Research Institute, Mount Sinai Hospital.
1995-1997 Postdoctoral Fellow, National Center for Biotechnology Information, NIH
1995 Ph.D. NRC-CNRC-IBS/University of Ottawa 1990 B.Sc. University of Windsor


2004 Sun Microsystems Center of Excellence in Systems Biology
2001 Canada's TOP 40 UNDER 40 Award
1999 Canada Foundation for Innovation Researcher
1997 Max Bell Scientist, SLRI Toronto
1995 NSERC Postdoctoral Research Fellowship
1995 GenBank Scholar Fellowship, NCBI, NIH
1993 NSERC Postgraduate Scholarship

Research Areas:

Molecular Structure, Evolution and Assembly, Bioinformatics and Mechanobiology

Research Interests:

We are interested in a systems approach to understanding the basis of mechanobiological function at the molecular level. We use both bioinformatics and experimental techniques focusing on purified molecular systems involving proteins and RNA and biophysical techniques like mass spectrometry, intrinsic fluorescence and FRET. We are studying a variety of systems including the mechanical relationship between ATPases and hexameric helicases, the mechanical origin of ribosomal protein synthesis, and the mechanical transitions that may be present in a defined class of protein domains we call 'scaffold-style domains' (SSD) that have to date been difficult to study as they do not fold into a single structure. We have patented software (TraDES) that is used to sample these ensemble conformational states. My group is also responsible for delivery of the RCE in Mechanobiology effort to construct an online resource of information known as the Manual for Cellular and Molecular Function (MCMF) which can be found at

Selected Publications

Betel D, Breitkreuz KE, Isserlin R, Dewar-Darch D, Tyers M, and Hogue CWV. Structure-templated predictions of novel protein interactions from sequence information. PLOS Computational Biology 2007 3:1783-9.

Snyder, K.A. Feldman, H.J., Dumontier, M., Salama J.J., and Hogue CWV. Domain-based Small Molecule Binding Site Annotation .BMC Bioinformatics. 2006 7:152

Feldman, H.J., Snyder, K.A, Ticoll, A., Pintilie, G., and Hogue CWV. A Complete Small Molecule Dataset from the Protein Data Bank. FEBS Lett. 2006 580:1649-53.

Dumontier, M., Yao, R., Feldman, HJ, Hogue, CWV. Armadillo: Domain Boundary Prediction by Amino Acid Composition. 2005. Journal of Molecular Biology. 350: 1061-1073..

Alfarano C, Andrade CE, Anthony K, Bahroos N, Bajec M, Bantoft K, Betel D, Bobechko B, Boutilier K, Burgess E, Buzadzija K, Cavero R, D'Abreo C, Donaldson I, Dorairajoo D, Dumontier MJ, Dumontier MR, Earles V, Farrall R, Feldman H, Garderman E, Gong Y, Gonzaga R, Grytsan V, Gryz E, Gu V, Haldorsen E, Halupa A, Haw R, Hrvojic A, Hurrell L, Isserlin R, Jack F, Juma F, Khan A, Kon T, Konopinsky S, Le V, Lee E, Ling S, Magidin M, Moniakis J, Montojo J, Moore S, Muskat B, Ng I, Paraiso JP, Parker B, Pintilie G, Pirone R, Salama JJ, Sgro S, Shan T, Shu Y, Siew J, Skinner D, Snyder K, Stasiuk R, Strumpf D, Tuekam B, Tao S, Wang Z, White M, Willis R, Wolting C, Wong S, Wrong A, Xin C, Yao R, Yates B, Zhang S, Zheng K, Pawson T, Ouellette BF, Hogue CW. 2005. The Biomolecular Interaction Network Database and related tools 2005 update. Nucleic Acids Research. 33(Database Issue):D418-D424.

Bader, G.D., Hogue, CW 2003. An automated method for finding molecular complexes in large protein interaction networks.  BMC Bioinformatics. 4(1): 2

Salama JJ, Donaldson I, Hogue CW Automatic annotation of BIND molecular interactions from three-dimensional structures. Biopolymers 2001-2002, 61:111-20

Ho Y, Gruhler A, Heilbut A, Bader GD, Moore L, Adams SL, Millar A, Taylor P, Bennett K, Boutilier K, Yang L, Wolting C, Donaldson I, Schandorff S, Shewnarane J, Vo M, Taggart J, Goudreault M, Muskat B, Alfarano C, Dewar D, Lin Z, Michalickova K, Willems AR, Sassi H, Nielsen PA, Rasmussen KJ, Andersen JR, Johansen LE, Hansen LH, Jespersen H, Podtelejnikov A, Nielsen E, Crawford J, Poulsen V, Sorensen BD, Matthiesen J, Hendrickson RC, Gleeson F, Pawson T, Moran MF, Durocher D, Mann M, Hogue CW, Figeys D, Tyers M Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 2002 415:180-3

Feldman HJ, Hogue CW Probabilistic sampling of protein conformations: new hope for brute force? Proteins 2002 46:8-23

Bader, GD, and Hogue, CWV (2000) BIND - A data specification for storing and describing biomolecular interactions, molecular complexes and pathways.  Bioinformatics, 16: 465-477.

Feldman, HJ, and Hogue, CWV (2000) A fast method to sample real protein conformational space. Proteins 39:112-131.

Ross, JBA., Szabo, AG and Hogue, CWV. (1997) Enhancement of protein spectra with tryptophan analogs: Exposing the molecular details of protein-protein and protein-nucleic acid interactions. Methods in Enzymology, Editors: L. Brand and M. L. Johnson. 278:151-190.

Hogue, CWV. (1997) Cn3D: a new generation of three-dimensional molecular structure viewer. Trends in Biochemical Sciences 22:314-316.

Hogue, CWV., Rasquinha, I., Szabo, AG, and MacManus, JP (1992) A new intrinsic probe for proteins - biosynthetic incorporation of 5-hydroxytryptophan into oncomodulin FEBS Letters 310, 269-272.

Hogue, CWV., MacManus, JP., Banville, D., and Szabo, AG. (1992) Comparison of terbium(III) luminescence enhancement in mutants of EF-hand calcium-binding J. Biol. Chem. 267, 13340-13348.