研究领域
We perform research in different areas of computational biology, in a comparative, evolutionary fashion. With an emphasis on understanding how protein structure and function have shaped the genomic sequence library of today, we pursue projects aimed at elucidating novel mechanisms of molecular evolution that contribute to biological divergence among and within a species. Thus, we travel back in time reconstructing the evolutionary history of protein families. As we gain insights from the past, we look to the future.
Currently, we are investigating how intrinsic disorder evolves, the evolutionary dynamics of protein structure, and how the interplay between different structural properties influences the evolutionary amino acid substitution rate per site. We are studying how the genomes of Corona viruses, such as SARS and MERS virus, and of Flavivirus, such as Zika, Dengue and West Nile Virus, evolve on the proteome level in order to inform the development of broadly neutralizing antibodies and antivirals for present day and emerging viral strains.
We are also developing novel applications for an integrated analysis of protein sequence data illuminating biophysical and functional charateristics in an evolutionary context, targeted to the non-bioinformatician user.
近期论文
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Avoiding regions symptomatic of conformational and functional flexibility to identify antiviral targets in current and future coronaviruses.
Rahaman J, Siltberg-Liberles J.
Genome Biol Evol 2016; 8 (11): 3471-3484. doi: 10.1093/gbe/evw246
Paralog-specific Patterns of Structural Disorder and Phosphorylation in the Vertebrate SH3-SH2-Tyrosine Kinase Protein Family.
Dos Santos HG, Siltberg-Liberles J.
Genome Biol Evol 2016; 8 (9):2806-2825. doi: 10.1093/gbe/evw194
The Nuanced Interplay of Intrinsic Disorder and other Structural Properties Driving Protein Evolution.
Ahrens J, Dos Santos, HG, Siltberg-Liberles J.
Mol Biol Evol 2016; 33 (9): 2248-2256. doi: 10.1093/molbev/msw092
Functional diversification after gene duplication: paralog specific regions of structural disorder and phosphorylation in p53, p63, and p73.
Dos Santos HG, Nunez-Castilla J, Siltberg-Liberles J.
PLoS ONE 2016;11(3): e0151961. doi: 10.1371/journal.pone.0151961
Engineering adenylate cyclases regulated by near-infrared window light.
Ryu MH, Kang IH, Nelson MD, Jensen TM, Lyuksyutova AI, Siltberg-Liberles J, Raizen DM, Gomelsky M.
PNAS. 2014;111(28):10167-10172.
Did the prion protein become vulnerable to misfolding after an evolutionary divide and conquer event?
Richmond K, Masterson P, Ortiz JF, Siltberg-Liberles J.
J Biomol Struct Dyn. 2014;32(7):1074-1084.
Metazoan innovation: from aromatic amino acids to extracellular signaling.
Kutchko KM, Siltberg-Liberles J.
Amino Acids. 2013;45(2):359-67.
Rapid evolutionary dynamics of structural disorder as a potential driving force for biological divergence in flaviviruses.
Ortiz JF, MacDonald ML, Masterson P, Uversky VN, Siltberg-Liberles J.
Genome Biol Evol. 2013;5(3):504-13.