The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Improving protein disorder prediction by deep bidirectional long short-term memory recurrent neural networks
Abstract
Motivation: Capturing long-range interactions between structural but not sequence neighbors of proteins is a long-standing challenging problem in bioinformatics. Recently, long short-term memory (LSTM) networks have significantly improved the accuracy of speech and image classification problems by remembering useful past information in long sequential events. Here, we have implemented deep bidirectional LSTM recurrent neural networks in the problem of protein intrinsic disorder prediction. Results: The new method, named SPOT-Disorder, has steadily improved over a similar method using a traditional, window-based neural network (SPINE-D) in all datasets tested without separate training on short and long disordered regions. Independent tests on four other datasets including the datasets from critical assessment of structure prediction (CASP) techniques and >10 000 annotated proteins from MobiDB, confirmed SPOT-Disorder as one of the best methods in disorder prediction. Moreover, initial studies indicate that the method is more accurate in predicting functional sites in disordered regions. These results highlight the usefulness combining LSTM with deep bidirectional recurrent neural networks in capturing non-local, long-range interactions for bioinformatics applications. Availability and Implementation: SPOT-disorder is available as a web server and as a standalone program at: http://sparks-lab.org/server/SPOT-disorder/index.php. Supplementary information: Supplementary data is available at Bioinformatics online.
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Cites
Hochreiter, S., & Schmidhuber, J. (1997) · Neural Computation · doi:10.1162/neco.1997.9.8.1735 · Cited by 102,318
Bidirectional recurrent neural networks
Schuster, M., & Paliwal, K. K. (1997) · IEEE Transactions on Signal Processing · doi:10.1109/78.650093 · Cited by 10,172
Self-citationShow and tell: A neural image caption generator
Vinyals, O., Toshev, A., Bengio, S., & Erhan, D. (2015) · 2015 IEEE Conference on Computer Vision and Pattern Recognition (CVPR) · doi:10.1109/cvpr.2015.7298935 · Cited by 6,318
Comparison of the predicted and observed secondary structure of T4 phage lysozyme
Matthews, B. W. (1975) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(75)90109-9 · Cited by 5,399 · cited 12×
“For CASP9, SPOT-disorder has the best performance in AUC, S w and MCC values.”
MethodInfluentialIntrinsically unstructured proteins and their functions
Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871
Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2005) · Journal of Molecular Recognition · doi:10.1002/jmr.747 · Cited by 847
Cited by
Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2
Alderson, T. R., Pritišanac, I., Kolarić, Đ., Moses, A. M., & Forman-Kay, J. D. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2304302120 · Cited by 240
AlphaFold2: A Role for Disordered Protein/Region Prediction?
Wilson, C. J., Choy, W.-Y., & Karttunen, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094591 · Cited by 173
“We selected the top 10 performing on the DisProt and DisProt-PDB giving a combined non-redundant set of 11 (fIDPnn [34], SPOT-Disorder2 [35], RawMSA [36], fIDPlr [34], PreDisorder [37], AUCpreD [38], SPOT-Disorder1 [39], SPOT-Disorder-Single (SPOT-Disorder-S) [40] , DisoMine [41], AUCpreD-np [38] and ESpritz-D [42]).”
MethodSPOT-Disorder2: Improved Protein Intrinsic Disorder Prediction by Ensembled Deep Learning
Hanson, J., Paliwal, K. K., Litfin, T., & Zhou, Y. (2019) · Genomics, Proteomics & Bioinformatics · doi:10.1016/j.gpb.2019.01.004 · Cited by 165
Self-citationProtein generation with evolutionary diffusion: sequence is all you need
Alamdari, S., Thakkar, N., van den Berg, R., Tenenholtz, N., Strome, R., Moses, A. M., Lu, A. X., Fusi, N., Amini, A. P., & Yang, K. K. (2023) · doi:10.1101/2023.09.11.556673 · Cited by 154
Lv, X., Chen, J., Lu, Y., Chen, Z., Xiao, N., & Yang, Y. (2020) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c00064 · Cited by 26
Self-citationZheng, S. (2025) · PLOS ONE · doi:10.1371/journal.pone.0313812 · Cited by 4
Metadata
- Authors
- Hanson, J., Yang, Y., Paliwal, K., & Zhou, Y.
- Venue
- Bioinformatics
- Publisher
- Oxford University Press (OUP)
- Published
- 2016-12-05
- Volume
- 33
- Issue
- 5
- Pages
- 685-692
- ISSN
- 1367-4803 (ISSN-L)
- 1367-4811
- OpenAlex
- W2566370974
- Cited by
- 292
- References
- 6
- FWCI
- 13.69
- Type
- journal article
- Language
- en
- Open access
- closed
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