ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2006
Towards genome-scale structure prediction for transmembrane proteins.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 35 citations in OpenAlex.
- Transmembrane START domain proteins: in silico identification, characterization and expression analysis under stress conditions in chickpea (Cicer arietinum L.).Plant signaling & behavior · 2016Article
- Membrane protein orientation and refinement using a knowledge-based statistical potential.BMC bioinformatics · 2013Article
- Accurate de novo structure prediction of large transmembrane protein domains using fragment-assembly and correlated mutation analysis.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Knowledge-based potential for positioning membrane-associated structures and assessing residue-specific energetic contributions.Structure (London, England : 1993) · 2012Article
- CREST--a large and diverse superfamily of putative transmembrane hydrolases.Biology direct · 2011Article
- Transmembrane helix prediction using amino acid property features and latent semantic analysis.BMC bioinformatics · 2008Article
- Assessing the ability of sequence-based methods to provide functional insight within membrane integral proteins: a case study analyzing the neurotransmitter/Na+ symporter family.BMC bioinformatics · 2007Article
- A generalized born implicit-membrane representation compared to experimental insertion free energies.Biophysical journal · 2007Article
- Introduction. Bioinformatics: from molecules to systems.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2006Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this paper we briefly review some of the recent progress made by ourselves and others in developing methods for predicting the structures of transmembrane proteins from amino acid sequence. Transmembrane proteins are an important class of proteins involved in many diverse biological functions, many of which have great impact in terms of disease mechanism and drug discovery. Despite their biological importance, it has proven very difficult to solve the structures of these proteins by experimental techniques, and so there is a great deal of pressure to develop effective methods for predicting their structure. The methods we discuss range from methods for transmembrane topology prediction to new methods for low resolution folding simulations in a knowledge-based force field. This potential is designed to reproduce the properties of the lipid bilayer. Our eventual aim is to apply these methods in tandem so that useful three-dimensional models can be built for a large fraction of the transmembrane protein domains in whole proteomes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.