Prediction of protein function from protein sequence and structure
By James C. Whisstock, Arthur M. Lesk. 2003
461 citations recorded by the source corpus.
Subfields: Molecular Biology
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In Molecular Biology
- Lim Heo
- Janet M. Thornton
- Bercem Dutagaci
- Roman A. Laskowski
- Lenore J. Cowen
- Michael Feig
- Alex Smola
- Karsten M. Borgwardt
Citations in the corpus
- Protein Secondary Structure Prediction Using Deep Convolutional Neural Fields (2015, neutral): “ first for CRF and then for DCNN. The gradient of the log-likelihood with respect to the parameters � and � is given by, 𝛻� �,� =[∑Å𝑖=1𝛿(�𝑖=�)𝛿(�𝑖+1=�)]−𝐸�𝑃𝑃(�|�,�,�,�)[∑ 𝛿(�𝑖=�)𝛿(�𝑖+1=�) Å 𝑖=1 ] (6) 𝛻� �,� =[∑Å𝛿(�𝑖=�)𝐻�(�,𝑖,�) 𝑖=1 ]−𝐸�𝑃𝑃(�|�,�,�,�)[∑ 𝛿(�𝑖=�)𝐻�(�,𝑖,�) Å 𝑖”
- Computational protein structure refinement: Almost there, yet still so far to go (2017, background): “3 Accurate protein structures are necessary as starting points for rational drug design, 4 protein engineering applications, 5 and to understand functional implications of mutations associated with genomic variations within populations.”
- Protein function prediction via graph kernels (2005, background): “Exceptions are also numerous if similarity is measured by means other than structure (Whisstock and Lesk, 2003).”
- Predicting protein function from sequence and structure (2007, unknown): “However, as the volume of data has increased, so too have the number and sophistication of computational methods for predicting functio”
- The biological impact of mass-spectrometry-based proteomics (2007, background): “jpg" NDATA ITEM> ]> Of the many fascinating discoveries made by genome-sequencing projects, perhaps none is more provocative than the prediction that all prokaryotes and eukaryotes produce numerous proteins with uncharacterized or pleiotropic function”
- Predicting protein function from sequence and structural data. (2005, background): “The more similar the sequence, the more similar the function is likely to be, although there are cases of proteins having 100% sequence identity yet performing different roles according to where they are expressed [1].”
- Matt: Local Flexibility Aids Protein Multiple Structure Alignment (2008, background): “Structural information can align the residues in this common core, even after the sequences have diverged too far for successful sequence-based alignment, because structural similarity is typically more evolutionarily conserved [5–7].”
- Structure Refinement of Membrane Proteins via Molecular Dynamics Simulations (2018, background): “Proteins have evolved over billions of years to form highly complex structures, which give rise to a diverse range of functions.(1,2) The atomistic details of their structure are of great importance to develop a deeper understanding of their function as well as to develop novel pharmaceutical strate”
- Structure-based Systems Biology for Analyzing Off-target Binding (2011, background): “Tremendous efforts have been made in detecting global sequence and structure similar proteins to infer their functional relationship [30].”