Vural O, Jololian L
Front Bioinform. 2025; 5:1520382.
PMID: 39963299
PMC: 11830693.
DOI: 10.3389/fbinf.2025.1520382.
Gulotta M, Perricone U, Rubino P, Bonura A, Feo S, Giallongo A
ACS Omega. 2025; 10(5):5036-5046.
PMID: 39959117
PMC: 11822713.
DOI: 10.1021/acsomega.4c10808.
Zhang F, Kurgan L
Comput Struct Biotechnol J. 2025; 27():78-88.
PMID: 39811792
PMC: 11732247.
DOI: 10.1016/j.csbj.2024.12.009.
Kyriukha Y, Watkins M, Redington J, Chintalapati N, Ganti A, Dastvan R
iScience. 2024; 27(12):111259.
PMID: 39584160
PMC: 11582789.
DOI: 10.1016/j.isci.2024.111259.
Zhang J, Zhou F, Liang X, Kurgan L
Methods Mol Biol. 2024; 2867:247-260.
PMID: 39576586
DOI: 10.1007/978-1-0716-4196-5_15.
Computational Prediction of Linear Interacting Peptides.
Malhis N, Gsponer J
Methods Mol Biol. 2024; 2867:233-245.
PMID: 39576585
DOI: 10.1007/978-1-0716-4196-5_14.
Landscape of intrinsically disordered proteins in mental disorder diseases.
Zhang X, Song X, Hu G, Yang Y, Liu R, Zhou N
Comput Struct Biotechnol J. 2024; 23:3839-3849.
PMID: 39534590
PMC: 11554586.
DOI: 10.1016/j.csbj.2024.10.043.
iDLB-Pred: identification of disordered lipid binding residues in protein sequences using convolutional neural network.
Malebary S, Alromema N
Sci Rep. 2024; 14(1):24724.
PMID: 39433833
PMC: 11494137.
DOI: 10.1038/s41598-024-75700-x.
Structural study of the intrinsically disordered tardigrade damage suppressor protein (Dsup) and its complex with DNA.
Zarubin M, Murugova T, Ryzhykau Y, Ivankov O, Uversky V, Kravchenko E
Sci Rep. 2024; 14(1):22910.
PMID: 39358423
PMC: 11447161.
DOI: 10.1038/s41598-024-74335-2.
Investigating the Interactions of the Cucumber Mosaic Virus 2b Protein with the Viral 1a Replicase Component and the Cellular RNA Silencing Factor Argonaute 1.
Crawshaw S, Murphy A, Rowling P, Nietlispach D, Itzhaki L, Carr J
Viruses. 2024; 16(5).
PMID: 38793558
PMC: 11125589.
DOI: 10.3390/v16050676.
Experimental methods to study the structure and dynamics of intrinsically disordered regions in proteins.
Maiti S, Singh A, Maji T, Saibo N, De S
Curr Res Struct Biol. 2024; 7:100138.
PMID: 38707546
PMC: 11068507.
DOI: 10.1016/j.crstbi.2024.100138.
Advanced computational approaches to understand protein aggregation.
Ghosh D, Biswas A, Radhakrishna M
Biophys Rev (Melville). 2024; 5(2):021302.
PMID: 38681860
PMC: 11045254.
DOI: 10.1063/5.0180691.
Pathological mutations reveal the key role of the cytosolic iRhom2 N-terminus for phosphorylation-independent 14-3-3 interaction and ADAM17 binding, stability, and activity.
Blasius K, Ludwig L, Knapp S, Flasshove C, Sonnabend F, Keller D
Cell Mol Life Sci. 2024; 81(1):102.
PMID: 38409522
PMC: 10896983.
DOI: 10.1007/s00018-024-05132-3.
Comparative evaluation of AlphaFold2 and disorder predictors for prediction of intrinsic disorder, disorder content and fully disordered proteins.
Zhao B, Ghadermarzi S, Kurgan L
Comput Struct Biotechnol J. 2024; 21:3248-3258.
PMID: 38213902
PMC: 10782001.
DOI: 10.1016/j.csbj.2023.06.001.
A cyclin D1 intrinsically disordered domain accesses modified histone motifs to govern gene transcription.
Jiao X, Di Sante G, Casimiro M, Tantos A, Ashton A, Li Z
Oncogenesis. 2024; 13(1):4.
PMID: 38191593
PMC: 10774418.
DOI: 10.1038/s41389-023-00502-1.
DisoFLAG: accurate prediction of protein intrinsic disorder and its functions using graph-based interaction protein language model.
Pang Y, Liu B
BMC Biol. 2024; 22(1):3.
PMID: 38166858
PMC: 10762911.
DOI: 10.1186/s12915-023-01803-y.
MMPatho: Leveraging Multilevel Consensus and Evolutionary Information for Enhanced Missense Mutation Pathogenic Prediction.
Ge F, Arif M, Yan Z, Alahmadi H, Worachartcheewan A, Yu D
J Chem Inf Model. 2023; 63(22):7239-7257.
PMID: 37947586
PMC: 10685454.
DOI: 10.1021/acs.jcim.3c00950.
Diversity and Complexity of Internally Deleted Viral Genomes in Influenza A Virus Subpopulations with Enhanced Interferon-Inducing Phenotypes.
Ghorbani A, Ngunjiri J, Rendon G, Brooke C, Kenney S, Lee C
Viruses. 2023; 15(10).
PMID: 37896883
PMC: 10612045.
DOI: 10.3390/v15102107.
The Intrinsically Disordered N Terminus in Atg12 from Yeast Is Necessary for the Functional Structure of the Protein.
Popelka H, Lahiri V, Hawkins W, Veiga Leprevost F, Nesvizhskii A, Klionsky D
Int J Mol Sci. 2023; 24(20).
PMID: 37894717
PMC: 10606595.
DOI: 10.3390/ijms242015036.
HMGA2 directly mediates chromatin condensation in association with neuronal fate regulation.
Kuwayama N, Kujirai T, Kishi Y, Hirano R, Echigoya K, Fang L
Nat Commun. 2023; 14(1):6420.
PMID: 37828010
PMC: 10570362.
DOI: 10.1038/s41467-023-42094-9.