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Articles by Laszlo Dobson
Regularly updated benchmark sets for statistically correct evaluations of AlphaFold applications
Abstract AlphaFold2 changed structural biology by providing high-quality structure predictions for all possible proteins. Since its inception, a plethora of applications were built on AlphaFold2, expediting discoveries in virtually all areas related to protein science. In many cases, however, optimism seems to have made scientists forget about data leakage, a serious issue that needs to be addressed when evaluating machine learning methods.
Importance of updated benchmark sets for statistically correct AlphaFold applications
Abstract AlphaFold2 changed structural biology by providing high-quality structure prediction for all possible proteins. Since that a plethora of applications were built on AlphaFold2, expediting discoveries on virtually all fields related to protein science. In many cases it seems like optimism made scientists forget about data leakage, a serious issue that needs to be addressed when evaluating machine learning methods.
Linear motifs regulating protein secretion, sorting and autophagy in Leishmania parasites are diverged with respect to their host equivalents
Loading metrics Open Access Peer-reviewed Research Article ? This is an uncorrected proof. Citation: Zeke A, Gibson TJ, Dobson L (2024) Linear motifs regulating protein secretion, sorting and autophagy in Leishmania parasites are diverged with respect to their host equivalents. PLoS Comput Biol 20(2): e1011902.
How AlphaFold shaped the structural coverage of the human transmembrane proteome
Abstract AlphaFold2 (AF2) provides structures for every protein, opening up prospects for virtually every field in structural biology. However, transmembrane proteins pose a challenge for experimental scientists, resulting in a limited number of solved structures. Consequently, algorithms trained on this finite training set also face difficulties.
Exploring Leishmania linear motifs directing protein secretion, sorting and autophagy
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How AlphaFold shaped the structural coverage of the human transmembrane proteome
Thank you for your interest in spreading the word about bioRxiv. NOTE: Your email address is requested solely to identify you as the sender of this article. Your Email * Your Name * Send To * Enter multiple addresses on separate lines or separate them with commas. Message Subject (Your Name) has forwarded a page to you from bioRxiv Message Body (Your Name) thought you would like to see this page from the bioRxiv website.
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