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17 results for “protein language models”
Data for "SeaMoon: from protein language models to continuous structural heterogeneity"
<p>Datasets used for development of SeaMoon: <br><a href="https://github.com/PhyloSofS-Team/seamoon">https://github.com/PhyloSofS-Team/seamoon</a>.</p> <p>This upload contains the following data:</p> <ul> <li><strong>precomputed_emb.tar.gz</strong> is a compressed archive containing the precomputed data used for training and testing the models of the SeaMoon method, in Torch <strong>.pt </strong>format. <br>The file prefixes consist of two IDs, "ID1_ID2_", identifying the <a href="https://github.com/PhyloSofS-Team/DANCE">DANCE</a> [1] protein conformational collection used for its generation. "ID1" represents the first member of the collection in alphabetical order, while "ID2" is the reference conformation for the structural alignment. The "ESM_data" or "ProstT5_data" suffixes designate the type of embeddings, generated by either ESM2 [2] or ProstT5 [3].<br>The dictionnary contains the following keys: <ul> <li><strong>emb:</strong> The per-residue embedding.</li> <li><strong>data: </strong>A tuple containing "ID2" (the reference), the amino acid sequence, and the coverage of the positions in the original DANCE collection.</li> <li><strong>eigvect:</strong> The eigenvectors of the covariance matrix of the "ID1_ID2" collection, centered on reference conformaton "D2".</li> <li><strong>eigval: </strong>The associated eigenvalues.</li> <li><strong>ref:</strong> The coordinates of the C-alpha atoms of the reference conformaton "ID2".</li> </ul> </li> <li><strong>train_list.txt, train_list_5ref.txt, val_list.txt </strong>and<strong> test_list.txt</strong> contain the identifiers of the samples used for training and evaluating the SeaMoon models. In the "5ref" setting, we used up to 5 reference conformations per collection. </li> </ul> <p>For details on SeaMoon see:</p> <div> <div>SeaMoon: Prediction of molecular motions based on language models</div> </div> <div>Valentin Lombard, Dan Timsit, Sergei Grudinin, Elodie Laine</div> <div>bioRxiv 2024.09.23.614585; doi: https://doi.org/10.1101/2024.09.23.614585</div> <div> </div> <div>For more information on data usage and generation please see <a href="https://github.com/PhyloSofS-Team/seamoon">https://github.com/PhyloSofS-Team/seamoon</a>.</div> <div> </div> <div>Abstract:</div> <p>How protein move and deform determines their interactions with the environment and is thus of utmost importance for cellular functioning. Following the revolution in single protein 3D structure prediction, researchers have focused on repurposing or developing deep learning models for sampling alternative protein conformations. In this work, we explored whether continuous compact representations of protein motions could be predicted directly from protein sequences, without exploiting nor sampling protein structures. Our approach, called SeaMoon, leverages protein Language Model (pLM) embeddings as input to a lightweight (~1M trainable parameters) convolutional neural network. SeaMoon achieves a success rate of up to 40% when assessed against ~1,000 collections of experimental conformations exhibiting a wide range of motions. SeaMoon capture motions not accessible to the normal mode analysis, an unsupervised physics-based method relying solely on a protein structure's 3D geometry, and generalises to proteins that do not have any detectable sequence similarity to the training set. SeaMoon is easily retrainable with novel or updated pLMs. </p> <p> </p> <p>[1] Lombard, V.; Grudinin, S.; Laine, E. Explaining Conformational Diversity in Protein Families through Molecular Motions. Scientific Data 2024, 11, 752.</p> <p>[2] Lin, Z.; Akin, H.; Rao, R.; Hie, B.; Zhu, Z.; Lu, W.; Smetanin, N.; Verkuil, R.; Kabeli, O.; Shmueli, Y.; Dos Santos Costa, A.; Fazel-Zarandi, M.; Sercu, T.; Candido, S.; Rives, A. Evolutionary-scale prediction of atomic-level protein structure with a language model. Science 2023, 379, 1123–1130.</p> <p>[3] Heinzinger, M.; Weissenow, K.; Sanchez, J. G.; Henkel, A.; Steinegger, M.; Rost, B. ProstT5: Bilingual language model for protein sequence and structure. bioRxiv 2023, 2023–07.</p>
Embeddings from protein language models predict conservation and variant effects
<p>For this work, we used protein language model representations (embeddings) to predict sequence conservation without multiple sequence alignments (MSAs). Embeddings alone predicted residue conservation almost as accurately from single sequences as ConSeq using MSAs (two-state Matthew Correlation Coefficient – MCC - for ProtT5 embeddings of 0.596±0.006 vs. 0.608±0.006 for ConSeq).</p> <p><strong><em>ConSurf10k</em>- Dataset for the development of ProtT5cons:</strong> The method (ProtT5cons) predicting residue conservation used <em>ConSurf-DB </em>(Ben Chorin et al. 2020). This resource provided sequences and conservation for 89,673 proteins. For all, experimental high-resolution three-dimensional (3D) structures were available in the Protein Data Bank (PDB) (Berman et al. 2000). As standard-of-truth for the conservation prediction, we used the values from ConSurf-DB generated using HMMER (Mistry et al. 2013), CD-HIT (Fu et al. 2012), and MAFFT-LINSi (Katoh and Standley 2013) to align proteins in the PDB (Burley et al. 2019). For proteins from families with over 50 proteins in the resulting MSA, an evolutionary rate at each residue position is computed and used along with the MSA to reconstruct a phylogenetic tree. The ConSurf-DB conservation scores ranged from 1 (most variable) to 9 (most conserved). The PISCES server (Wang and Dunbrack 2003) was used to redundancy reduce the data set such that no pair of proteins had more than 25% pairwise sequence identity. We removed proteins with resolutions >2.5Å, those shorter than 40 residues, and those longer than 10,000 residues. The resulting data set (ConSurf10k) with 10,507 proteins (or domains) was randomly partitioned into training (9,392 sequences), cross-training/validation (555) and test (519) sets.</p> <p>Uploaded data:</p> <ul> <li>ConSuf10k_PDBid_seq_cons.fasta: fasta file with PDBid, sequence and conservation annotation</li> <li>consurf10k_test_ids.txt: txt file with id's of test set</li> <li>consurf10k_train_ids.txt: txt file with id's of train set</li> <li>consurf10k_val_ids.txt: txt file with id's of cross-validation set</li> </ul>
Protein language model embeddings and predictions for the fly proteome (FlyBase)
<p>Residue and sequence embeddings of the fly (drosophila melanogaster) proteome (FlyBase for organism drosophila melanogaster, downloaded on 2022.03.01) computed using bio_embeddings (bioembeddings.com) using the ProtT5 embedder at full precision (https://www.biorxiv.org/content/10.1101/2020.07.12.199554v3). To open the embeddings file, please see <a href="https://github.com/sacdallago/bio_embeddings/blob/develop/notebooks/open_embedding_file.ipynb">this notebook</a>. The embeddings will be indexed by numbers according to the mapping file (mapping_file.csv) in this dataset. All following results will share the same mapping (for instance, to access the variation prediction results, by accessing index "0", you will query results for the sequence "FBpp0304622").</p> <p>Additionally:</p> <p>- Sequence-level predictions of subcellular localization in 10 classes using LA (https://www.biorxiv.org/content/10.1101/2021.04.25.441334v1)</p> <p>- Residue-level three state secondary structure prediction (alpha, sheet or other) using models reported in the ProtTrans paper (https://www.biorxiv.org/content/10.1101/2020.07.12.199554v3)</p> <p>- Residue-level prediction of conservation (in 9 states) and of variation effect (from 0 [no-effect] to 1 [effect]) using VESPAl (https://doi.org/10.1007/s00439-021-02411-y)</p> <p> </p> <p>Files included:</p> <p>- dmel-all-translation-r6.44.fasta --> FASTA-formatted sequences of drosophila melanogaster from FlyBase</p> <p>- mapping_file.csv --> A CSV file mapping the identifiers used in the following files (from 0 to 30737) to the identifiers in the FlyBase fasta file (dmel-all-translation-r6.44.fasta).</p> <p>- DSSP3_fly_ProtT5Sec.fasta --> Secondary structure predictions in three states for each residue of each protein in dmel-all-translation-r6.44.fasta. "H" stands for Helix; "E" stands for Sheet; "C" stands for Other.</p> <p>- subcell_fly_LA_ProtT5.csv --> Subcellular location (10 states) and memrane-boundness (2 states) for each protein in dmel-all-translation-r6.44.fasta</p> <p>- embeddings_file.h5 --> per-residue embeddings of sequences in dmel-all-translation-r6.44.fasta. Each dataset in the .h5 file represents a protein sequence and contains a matrix of length Lx1024, with L being the length of the protein sequence. Datasets are indexed using integers. The original sequence identifier (from the FASTA header) can be accessed through the "original_id" attribute. See https://docs.bioembeddings.com/v0.2.0/notebooks/open_embedding_file.html for information on how to open the file.</p> <p>- reduced_embeddings_file.h5 --> per-sequence embeddings of sequences in dmel-all-translation-r6.44.fasta (obtained by mean-pooling the residue-embeddings along the length dimension of the protein sequence). Each dataset in the .h5 file represents a protein sequence and contains a vector of size 1024 (meaning, each sequence has the same dimension).</p> <p>- conspred_probs.h5 --> per-sequence conservation probability (softmax) prediction of sequences in dmel-all-translation-r6.44.fasta in 9 classes. Each dataset in the .h5 file represents a protein sequence and contains a matrix of length 9xL, with L being the length of the protein sequence, and 9 being the predicted conservation class (index 0 = very variable; index 8 = very conserved)</p> <p>- vespal_SAVeffect_fly.zip --> zipped .h5 file of per-sequence variation predictions of sequences in dmel-all-translation-r6.44.fasta on a scale from 0 (neutral) to 1 (effect). -1 indicates WT substitution. Each dataset in the .h5 file represents a protein sequence and contains a matrix of length 20xL, with L being the length of the protein sequence, and 20 being the predicted variation score for each residue substitution (AAs in the following order: "<strong>ALGVSREDTIPKFQNYMHWC</strong>" . Meaning that index 0 = substitution of the residue to "A", index = 1 substitution to residue "L", aso.)</p>
Prediction and Visualization of Human Transmembrane Proteins using AlphaFold and Protein Language Models
<p><strong>Description:</strong> <strong>TMvis</strong> ("TMvis496.tar.gz") is a dataset containing 496 3D-structures of predicted human transmembrane proteins (TMP) and their predicted membrane embedding. The method TMbed [1], based on the protein language model ProtT5 [2] predicted 4.967 TMP for the human proteome (20,375 proteins, UniProt [3] version April 2022; excluding TITIN_HUMAN due to length). For these proteins, we obtained AlphaFold [4] structures from AlphaFoldDB [5] with an average per-residue confidence score (pLDDT) of more than 90%. This resulted in the 496 proteins of TMvis, as can be found in "TMvis496.fasta". The membrane embedding was predicted using the methods ANVIL [6], PPM3 [7], and per-residue TMbed predictions. As the three methods are based on different approaches, we decided to publish results for all. The figure “TMvis_project_overview.png” provides a graphical overview for each step described above.</p> <p><strong>TMvis Folder Structure:</strong> TMvis is separated into “alpha” containing predicted alpha-helical TMPs, and “beta” containing predicted beta-barrel TMPs. Within these folders, each protein is assigned one folder, identifiable by the respective unique UniProt ID. Each protein folder consists of:<br> - “UniprotID.fasta” with UniProt ID, sequence, TMbed per-residue prediction<br> - “AF-UniprotID-F1-model_v2.pdb” with the AlphaFold structure<br> - “AF-UniprotID-F1-model_v2.cif” with the AlphaFold structure<br> - “AF-UniprotID-F1-model_v2_ANVIL.pdb” with predicted ANVIL membrane embedding<br> - “AF-UniprotID-F1-model_v2_ppm.pdb” predicted PPM3 membrane embedding</p> <p>TMvis <br> | <br> ├── alpha <br> │ │ <br> │ ├── A0A087X1C5 <br> │ │ ├── A0A087X1C5.fasta <br> │ │ ├── AF-A0A087X1C5-F1-model_v2.pdb <br> │ │ ├── AF-A0A087X1C5-F1-model_v2.cif <br> │ │ ├── AF-A0A087X1C5-F1-model_v2_ANVIL.pdb <br> │ │ └── AF-A0A087X1C5-F1-model_v2_ppm.PDB <br> │ └── ... <br> └── beta <br> └── P45880</p> <p><strong>TMvis visualization:</strong> The 3D-visualization of every protein in the dataset TMvis can be easily accessed using the Jupyter Notebook “TMvis.ipynb”. It contains detailed descriptions the different membrane prediction tools ANVIL, PPM3, and TMbed as well as the respective code. Additionally, it allows to visualize the per-residue confidence scores (pLDDT) of AlphaFold.</p> <p>——————————————————————————————————————————————————————————————————————————</p> <p><strong>References:</strong></p> <p>[1] TMbed - TMbed Bernhofer, Michael, and Burkhard Rost. 2022. “TMbed – Transmembrane Proteins Predicted through Language Model Embeddings.” bioRxiv.</p> <p>[2] ProtT5 - A. Elnaggar et al., "ProtTrans: Towards Cracking the Language of Lifes Code Through Self-Supervised Deep Learning and High Performance Computing," in IEEE Transactions on Pattern Analysis and Machine Intelligence, doi: 10.1109/TPAMI.2021.3095381.</p> <p>[3] UniProt - UniProt Consortium (2021). UniProt: the universal protein knowledgebase in 2021. Nucleic acids research, 49(D1), D480–D489.</p> <p>[4] AlphaFold - AlphaFold Jumper, John, Richard Evans, Alexander Pritzel, Tim Green, Michael Figurnov, Olaf Ronneberger, Kathryn Tunyasuvunakool, et al. 2021. “Highly Accurate Protein Structure Prediction with AlphaFold.” Nature 596 (7873): 583–89.</p> <p>[5] Alphafold DB - Varadi, Mihaly, Stephen Anyango, Mandar Deshpande, Sreenath Nair, Cindy Natassia, Galabina Yordanova, David Yuan, et al. 2022. “AlphaFold Protein Structure Database: Massively Expanding the Structural Coverage of Protein-Sequence Space with High-Accuracy Models.” Nucleic Acids Research 50 (D1): D439–44.</p> <p>[6] ANVIL - ANVIL Postic, Guillaume, Yassine Ghouzam, Vincent Guiraud, and Jean-Christophe Gelly. 2016. “Membrane Positioning for High- and Low-Resolution Protein Structures through a Binary Classification Approach.” Protein Engineering, Design & Selection: PEDS 29 (3): 87–91.</p> <p>[7] PPM3 - PPM3 Lomize, Mikhail A., Irina D. Pogozheva, Hyeon Joo, Henry I. Mosberg, and Andrei L. Lomize. 2012. “OPM Database and PPM Web Server: Resources for Positioning of Proteins in Membranes.” Nucleic Acids Research 40 (Database issue): D370–76.</p> <p>——————————————————————————————————————————————————————————————————————————</p> <p><strong>License:</strong></p> <p>This work is licensed under a Creative Commons Attribution 4.0 International License (CC-BY 4.0).</p> <p> </p>
Data for 'VespaG: Expert-guided protein language models enable accurate and blazingly fast fitness prediction'
<div>Datasets used for development of VespaG and VespaG predictions generated with <a href="https://github.com/JSchlensok/VespaG">https://github.com/JSchlensok/VespaG</a>. </div> <div> </div> <div>Uploads contain:</div> <div> <ol> <li><strong>Performance</strong> summaries for ProteinGym [1]:<br>- Spearman and Pearson correlation for VespaG: <em>proteingym_performance_vespag.csv </em>(columns: 'DMS_id', 'Spearman', 'Pearson')<br>- Spearman correlation for evaluated methods VespaG, GEMME [2], VESPA [3], TranceptEVE [4], AlphaMissense [5], PoET [6]: <em>proteingym_spearman_allmethods.csv </em>(columns: 'DMS_id', 'Trancept EVE-L', 'VESPA', 'VespaG', 'GEMME', 'AlphaMissense', 'PoET', 'UniProt_ID', 'coarse_selection_type' (function), 'taxon')</li> <li><strong>Fasta</strong> files with sequences for all train sets (<em>vespag_fasta_training_datasets.zip</em> with seq_all9k.fasta, seq_human5k.fasta, seq_droso4k.fasta, seq_ecoli2k.fasta, seq_virus1k.fasta) and test set (<em>proteingym_217.fasta</em>)</li> <li><strong>VespaG</strong> <strong>Predictions</strong> for test set: <em>vespag_proteingym_rawpreds_by_training_dataset.zip</em> with raw_preds_ecoli.csv, raw_preds_human.csv, raw_preds_virus.csv, raw_preds_all.csv, raw_preds_droso.csv (columns: 'DMS_id', 'mutation', 'DMS_score', 'VespaG'). Predictions are based on different training data, the final model VespaG was trained on a subset of the human proteome and <strong>raw VespaG predictions</strong> <strong>for</strong> <strong>the</strong> <strong>ProteinGym benchmark are in raw_preds_human.csv </strong>(used to calculate the performances above).</li> <li><strong>GEMME predictions</strong> for train sets: <em>vespag_proteingym_rawpreds_by_training_dataset.zip </em>with folders 'human', 'droso', 'ecoli', 'virus', 'all' for respective fasta file (each containing GEMME mutational landscape output files named '<em>ID' + '</em>_normPred_evolCombi.txt')</li> <li><strong>ESM-2</strong> <strong>embeddings</strong> [7] for test set (<em>proteingym_217_esm2.h5</em>)</li> </ol> </div> <div>For details on VespaG see:</div> <div> <div> <div>VespaG: Expert-guided protein Language Models enable accurate and blazingly fast fitness prediction</div> </div> <div>Celine Marquet, Julius Schlensok, Marina Abakarova, Burkhard Rost, Elodie Laine</div> <div>bioRxiv 2024.04.24.590982; doi: https://doi.org/10.1101/2024.04.24.590982</div> <div> </div> <div>For more information on data usage and generation please see <a href="https://github.com/JSchlensok/VespaG">https://github.com/JSchlensok/VespaG</a>.</div> <div> </div> <div>Abstract:</div> <div>Exhaustive experimental annotation of the effect of all known protein variants remains daunting and expensive, stressing the need for scalable effect predictions. We introduce VespaG, a blazingly fast single amino acid variant effect predictor, leveraging embeddings of protein Language Models as input to a minimal deep learning model. To overcome the sparsity of experimental training data, we created a dataset of 39 million single amino acid variants from the human proteome applying the multiple sequence alignment-based effect predictor GEMME as a pseudo standard-of-truth. Assessed against the ProteinGym Substitution Benchmark (217 multiplex assays of variant effect with 2.5 million variants), VespaG achieved a mean Spearman correlation of 0.48 +/- 0.01, matching state-of-the-art methods such as GEMME, TranceptEVE, PoET, AlphaMissense, and VESPA. VespaG reached its top-level performance several orders of magnitude faster, predicting all mutational landscapes of the human proteome in 30 minutes on a consumer laptop (12-core CPU, 16 GB RAM).</div> <div> </div> <div>[1] Notin, Pascal, et al. "ProteinGym: large-scale benchmarks for protein fitness prediction and design." <em>Advances in Neural Information Processing Systems</em> 36 (2024).<br>[2] Laine, Elodie, Yasaman Karami, and Alessandra Carbone. "GEMME: a simple and fast global epistatic model predicting mutational effects." <em>Molecular biology and evolution</em> 36.11 (2019): 2604-2619.</div> <div>[3] Marquet, Céline, et al. "Embeddings from protein language models predict conservation and variant effects." <em>Human genetics</em> 141.10 (2022): 1629-1647.</div> <div>[4] Notin, Pascal, et al. "TranceptEVE: Combining family-specific and family-agnostic models of protein sequences for improved fitness prediction." <em>bioRxiv</em> (2022): 2022-12.</div> <div>[5] Cheng, Jun, et al. "Accurate proteome-wide missense variant effect prediction with AlphaMissense." <em>Science</em> 381.6664 (2023): eadg7492.</div> <div>[6] Truong Jr, Timothy, and Tristan Bepler. "PoET: A generative model of protein families as sequences-of-sequences." <em>Advances in Neural Information Processing Systems</em> 36 (2024).</div> <div>[7] Lin, Zeming, et al. "Evolutionary-scale prediction of atomic-level protein structure with a language model." <em>Science</em>379.6637 (2023): 1123-1130.</div> </div>
Protein language model embeddings and predictions of the human proteome
<p>Residue and sequence embeddings of the human proteome (SwissProt for organism Human, downloaded on 2021.06.09) computed using bio_embeddings (bioembeddings.com) using the ProtT5 embedder at full precision (https://www.biorxiv.org/content/10.1101/2020.07.12.199554v3).</p> <p>Additionally:</p> <p>- Sequence-level predictions of subcellular localization in 10 classes using LA (https://www.biorxiv.org/content/10.1101/2021.04.25.441334v1)</p> <p>- Residue-level three state secondary structure prediction (alpha, sheet or other) using models reported in the ProtTrans paper (https://www.biorxiv.org/content/10.1101/2020.07.12.199554v3)</p> <p> </p> <p>Files included:</p> <p>- human.fasta --> FASTA-formatted sequences of human from SwissProt</p> <p>- DSSP3_human_ProtT5Sec.fasta --> Secondary structure predictions in three states for each residue of each protein in human.fasta. "H" stands for Helix; "E" stands for Sheet; "C" stands for Other.</p> <p>- subcell_human_LA_ProtT5.csv --> Subcellular location (10 states) and memrane-boundness (2 states) for each protein in human.fasta</p> <p>- embeddings_file.h5 --> per-residue embeddings of sequences in human.fasta. Each dataset in the .h5 file represents a protein sequence and contains a matrix of length Lx1024, with L being the length of the protein sequence. Datasets are indexed using integers. The original sequence identifier (from the FASTA header) can be accessed through the "original_id" attribute. See https://docs.bioembeddings.com/v0.2.0/notebooks/open_embedding_file.html for information on how to open the file</p> <p>- reduced_embeddings_file.h5 --> per-sequence embeddings of sequences in human.fasta (obtained by mean-pooling the residue-embeddings along the length dimension of the protein sequence). Each dataset in the .h5 file represents a protein sequence and contains a vector of size 1024 (meaning, each sequence has the same dimension).</p>
Data from: Protein Set Transformer: A protein-based genome language model to power high diversity viromics
Open the record for dataset details and reuse information.
pLMMoRF: A web server that accurately predicts membrane-interacting molecular recognition features by employing a protein language model
<p>pLMMMoRF predictor scrips and MemMoRF prediction of the human proteome.</p>
Data from: Genome-scale annotation of protein binding sites via language model and geometric deep learning
<p>The dataset contains the training and test sets of protein binding sites with DNA, RNA, peptide, protein, ATP, HEM, Zn2+, Ca2+, Mg2+ and Mn2+. Each protein is associated with 3 lines indicating the protein name (PDB accession code and chain), sequence and residue labels (0 for non-binding and 1 for binding), respectively. The ESMFold-predicted structures are also provided.</p>
Training datasets for "Multi-purpose controllable protein generation via prompted language models"
<div> <p>The datasets used to tune modular prompts of PROPEND fall into three main categories based on their design objectives: tertiary structure, secondary structure, and functional annotation.</p> </div>
Data from: Investigating the human and non-obese diabetic mouse MHC class II immunopeptidome using protein language modelling.
<p><strong>Background</strong>: Identifying peptides associated with the major histocompability complex class II (MHCII) is a central task in the evaluation of the immunoregulatory function of therapeutics and drug prototypes. MHCII-peptide presentation prediction has multiple biopharmaceutical applications, including the safety assessment of biologics and engineered derivatives in silico, or the fast progression of antigen-specific immunomodulatory drug discovery programs in immune disease and cancer. This has resulted in the collection of large–scale data sets on adaptive immune receptor antigenic responses and MHC-associated peptide proteomics. In parallel, recent deep learning algorithmic advances in natural language processing (NLP) and protein language modelling (PLM) have shown potential in leveraging large collections of sequence data and improve MHC presentation prediction. <strong>Methodology</strong>: We trained a compact transformer model (AEGIS) on human and mouse MHCII immunopeptidome data, including a preclinical murine model, and evaluated its performance on the peptide presentation prediction task. <strong>Data</strong>: The data and models used in AEGIS are contained in the uploaded tar files. <strong>Results</strong>: The transformer performs on par with existing deep learning algorithms and that combining datasets from multiple organisms increases model performance (see preprint). We trained variants of the model with and without MHCII information. In both alternatives, the inclusion of peptides presented by the I-Ag7 MHC class II molecule expressed by the non-obese diabetic (NOD) mice enabled the in silico prediction of presented peptides in a preclinical type 1 diabetes model organism, which has promising therapeutic applications.</p>
Integration of protein and coding sequences enables mutual augmentation of the language model
<p><strong>The file structure is as follows:</strong></p> <p>Project Root<br>├── TE_MRL<br>│ ├── MRL_dataset.zip<br>│ └── TE_dataset.zip<br>│<br>├── finetuned_model<br>│ ├── FoldP<br>│ ├── LocP<br>│ ├── SSP<br>│ └── SolP<br>│<br>├── tax_tsne<br>│ └── emb_3models.zip<br>│<br>└── training_data<br> ├── FoldP.csv<br> ├── LocP.csv<br> ├── SolP.csv<br> ├── SSP.pkl<br> └── pretrain_source_GCF.txt</p>
Enhancing Protein Sequence Annotation in Viral Genomics Using Large Language Models and Soft Alignments.
<p>List of 200 most abundant VOG descriptions.</p>
HiPHD: Hierarchical Classification for Protein Remote Homology Detection using Graph Neural Networks and Language Models
Open the record for dataset details and reuse information.
Feature Reuse and Scaling: Understanding Transfer Learning with Protein Language Models
<p>Data and checkpoints for 'Feature Reuse and Scaling: Understanding Transfer Learning with Protein Language Models'</p>
Genomic language model predicts protein co-regulation and function
<p>Model for "Genomic language model predicts protein co-regulation and function" </p>
Protein language models-assisted optimization of a Uracil-N glycosylase variant enables programmable T-to-S base editing
GEO Series GSE253655. Homo sapiens. 9 samples. Type: Expression profiling by high throughput sequencing.
ScienceDex guides
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These curated guides explain access requirements, typical timelines, costs, and reuse considerations for widely used research datasets.
Allen Brain Atlas
Allen Brain Atlas is an Allen Institute collection of brain map atlases, datasets, APIs, and analysis tools covering mouse, human, and non-human primate brain resources.
Annotated Behaviour and Observability Dataset (ABODe)
ABODe is a University of Edinburgh DataShare dataset for behavior classification in group-housed mice using home-cage video, identities, bounding boxes, ground-plate positions, and annotator labels.
DANDI Archive for NWB datasets
DANDI is a BRAIN Initiative archive for publishing and sharing neurophysiology data, including electrophysiology, optophysiology, and behavioral data packaged as NWB and related standards.
International Brain Laboratory public data
The International Brain Laboratory public data releases expose standardized mouse decision-making experiments, including Neuropixels recordings, widefield calcium imaging, behavior, and session metadata accessed through the ONE API.
OpenNeuro
OpenNeuro is a free, open platform for sharing neuroimaging datasets, with public search, dataset pages, and download paths for web, S3, DataLad, and the OpenNeuro CLI.