The FDR control in the newer versions looks much better. DIA-NN is an excellent tool. We use it a lot in our lab.
25.07.2025 18:48 β π 3 π 0 π¬ 0 π 0@bo-wen.bsky.social
The FDR control in the newer versions looks much better. DIA-NN is an excellent tool. We use it a lot in our lab.
25.07.2025 18:48 β π 3 π 0 π¬ 0 π 0Cascadia from @wnoble.bsky.social is a mass spec-based de novo sequencing model that uses a transformer architecture to handle data-independent acquisition data and achieves substantially improved performance across a range of instruments and experimental protocols. www.nature.com/articles/s41...
07.07.2025 22:31 β π 10 π 3 π¬ 0 π 0The FDR control in the newer version of DIA-NN is much improved on the datasets I have looked at.
04.07.2025 02:42 β π 2 π 0 π¬ 0 π 0(1/2) We have always validated FDR internally on several datasets. Bo Wen and colleagues discovered that FDR of DIA-NN 1.8.1 was anti-conservative on some (but not other) datasets - for some unknown reason. So we fixed it in 2.0 :) Now q-values are more accurate and fluctate less across datasets.
02.07.2025 22:24 β π 16 π 1 π¬ 2 π 0Error control in proteomics mass spectrometry analysis is hard. We came up with a way to evaluate error control. Upshot: for old-school DDA data, not so bad. For DIA data, no existing tool successfully controls the false discovery rate!
www.nature.com/articles/s41...
Excited to see this published! It is a good step in the process for people to assess their FDR control in proteomics experiments. Great work from @bo-wen.bsky.social and @urikeich.bsky.social in particular who drove this.
16.06.2025 18:52 β π 41 π 9 π¬ 1 π 1Assessing error control is fundamental in mass spectrometry-based proteomics. @bo-wen.bsky.social @maccoss.bsky.social @urikeich.bsky.social et al introduce a theoretical foundation for entrapment along with a method for more accurate evaluation of FDR control.
www.nature.com/articles/s41...