{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,12,11]],"date-time":"2025-12-11T12:58:56Z","timestamp":1765457936801,"version":"3.46.0"},"reference-count":60,"publisher":"Oxford University Press (OUP)","issue":"6","license":[{"start":{"date-parts":[[2025,12,11]],"date-time":"2025-12-11T00:00:00Z","timestamp":1765411200000},"content-version":"vor","delay-in-days":40,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2025,11,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>A ubiquitous and reversible phosphorylation is important for molecular signaling cascades, regulated by the transient interaction of protein kinases. The coupled folding and phosphorylation determining substrate specificity re-calibrates the interactive environment of intrinsically disordered regions (IDRs). There are over 50 computational methods for predicting IDRs in the proteome, yet achieving an accurate depiction remains an ongoing challenge. In this study, we present a standardized and kinase-centric approach for IDR prediction within the human kinome, employing a long short-term memory deep learning framework that achieves a high predictive performance (AUC\u2009=\u20090.97). The web server is now publicly accessible at: https:\/\/ciods.in\/kindisorder. Our workflow begins with proteome-wide IDR prediction and proceeds with the categorization of short and long IDR segments, followed by an in-depth analysis of their distribution relative to the kinase domain regulatory core. We evaluated the conservation of these IDRs across all 137 human kinase families, computing a trend-setting conservation index to identify both conserved and variable disorder patterns. Through this framework, we uncovered 1039 functional disorder region hotspots that correlate with dynamic conformational shifts, phosphorylation sites, functional motif enrichment, and mutation impact embedded within IDRs. To further validate their regulatory significance, we conducted biophysical profiling of conserved and variable IDRs. Finally, we developed a structural integrity framework to link these IDRs to their influence on intrinsic signaling cascades and substrate specificity. This study offers a comprehensive functional characterization of IDRs in the human kinome, providing a valuable resource for exploring kinase regulation and opportunities in drug repurposing.<\/jats:p>","DOI":"10.1093\/bib\/bbaf662","type":"journal-article","created":{"date-parts":[[2025,11,27]],"date-time":"2025-11-27T13:13:00Z","timestamp":1764249180000},"source":"Crossref","is-referenced-by-count":0,"title":["Impact of intrinsically disordered regions and functional disorder hotspots in the human kinome"],"prefix":"10.1093","volume":"26","author":[{"given":"Sonet Daniel","family":"Thomas","sequence":"first","affiliation":[{"name":"Centre for Integrative Omics Data Science (CIODS), Centre for Systems Biology and Molecular Medicine, Yenepoya (Deemed to be University) , Deralakatte, Manglore 575018, Karnataka ,","place":["India"]}]},{"given":"Aparna","family":"Rajan","sequence":"additional","affiliation":[{"name":"Centre for Integrative Omics Data Science (CIODS), Centre for Systems Biology and Molecular Medicine, Yenepoya (Deemed to be University) , Deralakatte, Manglore 575018, Karnataka ,","place":["India"]}]},{"given":"Althaf","family":"Mahin","sequence":"additional","affiliation":[{"name":"Centre for Integrative Omics Data Science (CIODS), Centre for Systems Biology and Molecular Medicine, Yenepoya (Deemed to be University) , Deralakatte, Manglore 575018, Karnataka ,","place":["India"]}]},{"given":"Mukthar","family":"Ahmed","sequence":"additional","affiliation":[{"name":"Department of Zoology, College of Science, King Saud University , P. O. Box 2455, Riyadh Province, Riyadh 11451 ,","place":["Kingdom of Saudi Arabia"]}]},{"given":"S","family":"Pavithra","sequence":"additional","affiliation":[{"name":"School of Computer Science and Engineering, Vellore Institute of Technology , Chennai 600127, Tamil Nadu ,","place":["India"]}]},{"given":"U","family":"Vignesh","sequence":"additional","affiliation":[{"name":"School of Computer Science and Engineering, Vellore Institute of Technology , Chennai 600127, Tamil Nadu ,","place":["India"]}]},{"given":"Naveen","family":"Joy","sequence":"additional","affiliation":[{"name":"Centre for Integrative Omics Data Science (CIODS), Centre for Systems Biology and Molecular Medicine, Yenepoya (Deemed to be University) , Deralakatte, Manglore 575018, Karnataka ,","place":["India"]}]},{"given":"Levin","family":"John","sequence":"additional","affiliation":[{"name":"Centre for Integrative Omics Data Science (CIODS), Centre for Systems Biology and Molecular Medicine, Yenepoya (Deemed to be University) , Deralakatte, Manglore 575018, Karnataka ,","place":["India"]},{"name":"Institute for Regeneration and Repair, University of Edinburgh , Edinburgh EH16 4UU ,","place":["Scotland"]}]},{"given":"Lijin","family":"Varghese","sequence":"additional","affiliation":[{"name":"Centre for Integrative Omics Data Science (CIODS), Centre for Systems Biology and Molecular Medicine, Yenepoya (Deemed to be University) , Deralakatte, Manglore 575018, Karnataka ,","place":["India"]}]},{"given":"Alimath","family":"Sambreena","sequence":"additional","affiliation":[{"name":"Centre for Integrative Omics Data Science (CIODS), Centre for Systems Biology and Molecular Medicine, Yenepoya (Deemed to be University) , Deralakatte, Manglore 575018, Karnataka ,","place":["India"]}]},{"given":"Jalaluddin Akbar Kandel","family":"Codi","sequence":"additional","affiliation":[{"name":"Centre for Integrative Omics Data Science (CIODS), Centre for Systems Biology and Molecular Medicine, Yenepoya (Deemed to be University) , Deralakatte, Manglore 575018, Karnataka ,","place":["India"]}]},{"given":"Thottethodi Subrahmanya Keshava","family":"Prasad","sequence":"additional","affiliation":[{"name":"Centre for Integrative Omics Data Science (CIODS), Centre for Systems Biology and Molecular Medicine, Yenepoya (Deemed to be University) , Deralakatte, Manglore 575018, Karnataka ,","place":["India"]}]},{"given":"Manavalan","family":"Vijayakumar","sequence":"additional","affiliation":[{"name":"Centre for Integrative Omics Data Science (CIODS), Centre for Systems Biology and Molecular Medicine, Yenepoya (Deemed to be University) , Deralakatte, Manglore 575018, Karnataka ,","place":["India"]}]},{"given":"S","family":"Geetha","sequence":"additional","affiliation":[{"name":"School of Computer Science and Engineering, Vellore Institute of Technology , Chennai 600127, Tamil Nadu ,","place":["India"]}]},{"given":"R","family":"Parvathi","sequence":"additional","affiliation":[{"name":"School of Computer Science and Engineering, Vellore Institute of Technology , Chennai 600127, Tamil Nadu ,","place":["India"]}]},{"given":"R","family":"Ganesan","sequence":"additional","affiliation":[{"name":"School of Computer Science and Engineering, Vellore Institute of Technology , Chennai 600127, Tamil Nadu ,","place":["India"]}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2319-121X","authenticated-orcid":false,"given":"Rajesh","family":"Raju","sequence":"additional","affiliation":[{"name":"Centre for Integrative Omics Data Science (CIODS), Centre for Systems Biology and Molecular Medicine, Yenepoya (Deemed to be University) , Deralakatte, Manglore 575018, Karnataka ,","place":["India"]}]}],"member":"286","published-online":{"date-parts":[[2025,12,11]]},"reference":[{"key":"2025121107551566500_ref1","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.phrs.2015.07.010","article-title":"A historical overview of protein kinases and their targeted small molecule inhibitors","volume":"100","author":"Roskoski","year":"2015","journal-title":"Pharmacol Res"},{"key":"2025121107551566500_ref2","doi-asserted-by":"publisher","first-page":"42","DOI":"10.1126\/science.3291115","article-title":"The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains","volume":"241","author":"Hanks","year":"1988","journal-title":"Science"},{"key":"2025121107551566500_ref3","doi-asserted-by":"publisher","first-page":"149","DOI":"10.1016\/S0092-8674(00)81092-2","article-title":"Active and inactive protein kinases: Structural basis for regulation","volume":"85","author":"Johnson","year":"1996","journal-title":"Cell"},{"key":"2025121107551566500_ref4","doi-asserted-by":"publisher","DOI":"10.1126\/scisignal.aau8645","article-title":"Illuminating the dark phosphoproteome","volume":"12","author":"Needham","year":"2019","journal-title":"Sci Signal"},{"key":"2025121107551566500_ref5","doi-asserted-by":"publisher","first-page":"103881","DOI":"10.1016\/j.drudis.2024.103881","article-title":"Illuminating function of the understudied druggable kinome","volume":"29","author":"Gomez","year":"2024","journal-title":"Drug Discov Today"},{"key":"2025121107551566500_ref6","doi-asserted-by":"publisher","first-page":"D529","DOI":"10.1093\/nar\/gkaa853","article-title":"The dark kinase knowledgebase: An online compendium of knowledge and experimental results of understudied kinases","volume":"49","author":"Berginski","year":"2021","journal-title":"Nucleic Acids Res"},{"key":"2025121107551566500_ref7","doi-asserted-by":"publisher","first-page":"102247","DOI":"10.1016\/j.jbc.2022.102247","article-title":"Structural features of the protein kinase domain and targeted binding by small-molecule inhibitors","volume":"298","author":"Arter","year":"2022","journal-title":"J Biol Chem"},{"key":"2025121107551566500_ref8","doi-asserted-by":"publisher","first-page":"759","DOI":"10.1038\/s41586-022-05575-3","article-title":"An atlas of substrate specificities for the human serine\/threonine kinome","volume":"613","author":"Johnson","year":"2023","journal-title":"Nature"},{"key":"2025121107551566500_ref9","doi-asserted-by":"publisher","first-page":"637","DOI":"10.1038\/d41586-022-04583-7","article-title":"Targets mapped for almost all human kinase enzymes","volume":"613","author":"Humphrey","year":"2023","journal-title":"Nature"},{"key":"2025121107551566500_ref10","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1007\/978-1-0716-3922-1_2","article-title":"Systematic identification of kinase-substrate relationship by integrated Phosphoproteome and Interactome analysis","volume":"2823","author":"Muraoka","year":"2024","journal-title":"Methods Mol Biol"},{"key":"2025121107551566500_ref11","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1038\/s41421-023-00523-5","article-title":"Structure and dynamics of the EGFR\/HER2 heterodimer","volume":"9","author":"Bai","year":"2023","journal-title":"Cell Discov"},{"key":"2025121107551566500_ref12","doi-asserted-by":"publisher","first-page":"190","DOI":"10.1021\/cb500870a","article-title":"Targeting conformational plasticity of protein kinases","volume":"10","author":"Tong","year":"2015","journal-title":"ACS Chem Biol"},{"key":"2025121107551566500_ref13","doi-asserted-by":"publisher","first-page":"3541","DOI":"10.1038\/s41467-022-31215-5","article-title":"Mapping the conformational energy landscape of Abl kinase using ClyA nanopore tweezers","volume":"13","author":"Li","year":"2022","journal-title":"Nat Commun"},{"key":"2025121107551566500_ref14","doi-asserted-by":"publisher","first-page":"1036","DOI":"10.3390\/biom12081036","article-title":"Protein phosphorylation in cancer: Unraveling the Signaling pathways","volume":"12","author":"Coopman","year":"2022","journal-title":"Biomolecules"},{"key":"2025121107551566500_ref15","doi-asserted-by":"publisher","first-page":"1097","DOI":"10.3390\/biom10081097","article-title":"Protein-protein interactions mediated by intrinsically disordered protein regions are enriched in missense mutations","volume":"10","author":"Wong","year":"2020","journal-title":"Biomolecules"},{"key":"2025121107551566500_ref16","doi-asserted-by":"publisher","first-page":"161","DOI":"10.1016\/j.molcel.2014.05.032","article-title":"A million peptide motifs for the molecular biologist","volume":"55","author":"Tompa","year":"2014","journal-title":"Mol Cell"},{"key":"2025121107551566500_ref17","doi-asserted-by":"publisher","first-page":"e1012028","DOI":"10.1371\/journal.pcbi.1012028","article-title":"Evolutionary analyses of intrinsically disordered regions reveal widespread signals of conservation","volume":"20","author":"Singleton","year":"2024","journal-title":"PLoS Comput Biol"},{"key":"2025121107551566500_ref18","doi-asserted-by":"publisher","DOI":"10.3390\/ijms23031589","article-title":"The inherent coupling of intrinsically disordered regions in the multidomain receptor tyrosine kinase KIT","volume":"23","author":"Ledoux","year":"2022","journal-title":"Int J Mol Sci"},{"key":"2025121107551566500_ref19","doi-asserted-by":"publisher","first-page":"1021","DOI":"10.1038\/nature05858","article-title":"Mechanism of coupled folding and binding of an intrinsically disordered protein","volume":"447","author":"Sugase","year":"2007","journal-title":"Nature"},{"key":"2025121107551566500_ref20","doi-asserted-by":"publisher","first-page":"e1002709","DOI":"10.1371\/journal.pcbi.1002709","article-title":"Disease-associated mutations disrupt functionally important regions of intrinsic protein disorder","volume":"8","author":"Vacic","year":"2012","journal-title":"PLoS Comput Biol"},{"key":"2025121107551566500_ref21","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1039\/C1MB05251A","article-title":"Disease mutations in disordered regions--exception to the rule?","volume":"8","author":"Vacic","year":"2012","journal-title":"Mol BioSyst"},{"key":"2025121107551566500_ref22","doi-asserted-by":"publisher","first-page":"573","DOI":"10.1016\/S0022-2836(02)00969-5","article-title":"Intrinsic disorder in cell-signaling and cancer-associated proteins","volume":"323","author":"Iakoucheva","year":"2002","journal-title":"J Mol Biol"},{"key":"2025121107551566500_ref23","doi-asserted-by":"publisher","first-page":"10448","DOI":"10.1021\/bi060981d","article-title":"Abundance of intrinsic disorder in protein associated with cardiovascular disease","volume":"45","author":"Cheng","year":"2006","journal-title":"Biochemistry"},{"key":"2025121107551566500_ref24","doi-asserted-by":"publisher","first-page":"300","DOI":"10.1016\/j.tibs.2018.12.002","article-title":"Disordered protein kinase regions in regulation of kinase domain cores","volume":"44","author":"Gogl","year":"2019","journal-title":"Trends Biochem Sci"},{"key":"2025121107551566500_ref25","doi-asserted-by":"publisher","first-page":"20","DOI":"10.1186\/s12964-022-00821-7","article-title":"Intrinsically disordered proteins play diverse roles in cell signaling","volume":"20","author":"Bondos","year":"2022","journal-title":"Cell Commun Signal"},{"key":"2025121107551566500_ref26","doi-asserted-by":"publisher","first-page":"1272","DOI":"10.1073\/pnas.0610251104","article-title":"The hallmark of AGC kinase functional divergence is its C-terminal tail, a cis-acting regulatory module","volume":"104","author":"Kannan","year":"2007","journal-title":"Proc Natl Acad Sci USA"},{"key":"2025121107551566500_ref27","doi-asserted-by":"publisher","first-page":"1037","DOI":"10.1093\/nar\/gkh253","article-title":"The importance of intrinsic disorder for protein phosphorylation","volume":"32","author":"Iakoucheva","year":"2004","journal-title":"Nucleic Acids Res"},{"key":"2025121107551566500_ref28","doi-asserted-by":"publisher","first-page":"3433","DOI":"10.1093\/bioinformatics\/bti541","article-title":"IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content","volume":"21","author":"Dosztanyi","year":"2005","journal-title":"Bioinformatics"},{"key":"2025121107551566500_ref29","doi-asserted-by":"publisher","first-page":"996","DOI":"10.1016\/j.bbapap.2010.01.011","article-title":"PONDR-FIT: A meta-predictor of intrinsically disordered amino acids","volume":"1804","author":"Xue","year":"2010","journal-title":"Biochim Biophys Acta"},{"key":"2025121107551566500_ref30","doi-asserted-by":"publisher","first-page":"3369","DOI":"10.1093\/bioinformatics\/bti534","article-title":"RONN: The bio-basis function neural network technique applied to the detection of natively disordered regions in proteins","volume":"21","author":"Yang","year":"2005","journal-title":"Bioinformatics"},{"key":"2025121107551566500_ref31","doi-asserted-by":"publisher","first-page":"S9","DOI":"10.1186\/1471-2164-9-S1-S9","article-title":"Protein disorder prediction at multiple levels of sensitivity and specificity","volume":"9","author":"Hecker","year":"2008","journal-title":"BMC Genomics"},{"key":"2025121107551566500_ref32","doi-asserted-by":"publisher","first-page":"2138","DOI":"10.1093\/bioinformatics\/bth195","article-title":"The DISOPRED server for the prediction of protein disorder","volume":"20","author":"Ward","year":"2004","journal-title":"Bioinformatics"},{"key":"2025121107551566500_ref33","doi-asserted-by":"publisher","first-page":"1316","DOI":"10.1016\/j.str.2003.10.009","article-title":"Order, disorder, and flexibility: Prediction from protein sequence","volume":"11","author":"Iakoucheva","year":"2003","journal-title":"Structure"},{"key":"2025121107551566500_ref34","doi-asserted-by":"publisher","first-page":"141801","DOI":"10.1016\/j.ijbiomac.2025.141801","article-title":"PredIDR2: Improving accuracy of protein intrinsic disorder prediction by updating deep convolutional neural network and supplementing DisProt data","volume":"306","author":"Han","year":"2025","journal-title":"Int J Biol Macromol"},{"key":"2025121107551566500_ref35","doi-asserted-by":"publisher","first-page":"4438","DOI":"10.1038\/s41467-021-24773-7","article-title":"flDPnn: Accurate intrinsic disorder prediction with putative propensities of disorder functions","volume":"12","author":"Hu","year":"2021","journal-title":"Nat Commun"},{"key":"2025121107551566500_ref36","doi-asserted-by":"publisher","first-page":"17315","DOI":"10.3390\/ijms160817315","article-title":"DeepCNF-D: Predicting protein order\/disorder regions by weighted deep convolutional neural fields","volume":"16","author":"Wang","year":"2015","journal-title":"Int J Mol Sci"},{"key":"2025121107551566500_ref37","doi-asserted-by":"publisher","first-page":"1123","DOI":"10.1126\/science.ade2574","article-title":"Evolutionary-scale prediction of atomic-level protein structure with a language model","volume":"379","author":"Lin","year":"2023","journal-title":"Science"},{"key":"2025121107551566500_ref38","doi-asserted-by":"publisher","first-page":"2102","DOI":"10.1093\/bioinformatics\/btac020","article-title":"ProteinBERT: a universal deep-learning model of protein sequence and function","volume":"38","author":"Brandes","year":"2022","journal-title":"Bioinformatics"},{"key":"2025121107551566500_ref39","doi-asserted-by":"publisher","first-page":"472","DOI":"10.1038\/s41592-021-01117-3","article-title":"Critical assessment of protein intrinsic disorder prediction","volume":"18","author":"Necci","year":"2021","journal-title":"Nat Methods"},{"key":"2025121107551566500_ref40","doi-asserted-by":"publisher","first-page":"137","DOI":"10.1093\/bioinformatics\/bth476","article-title":"DisProt: A database of protein disorder","volume":"21","author":"Vucetic","year":"2005","journal-title":"Bioinformatics"},{"key":"2025121107551566500_ref41","doi-asserted-by":"publisher","first-page":"D438","DOI":"10.1093\/nar\/gkac1065","article-title":"MobiDB: 10 years of intrinsically disordered proteins","volume":"51","author":"Piovesan","year":"2023","journal-title":"Nucleic Acids Res"},{"key":"2025121107551566500_ref42","doi-asserted-by":"publisher","first-page":"D434","DOI":"10.1093\/nar\/gkad928","article-title":"DisProt in 2024: Improving function annotation of intrinsically disordered proteins","volume":"52","author":"Aspromonte","year":"2024","journal-title":"Nucleic Acids Res"},{"key":"2025121107551566500_ref43","doi-asserted-by":"publisher","first-page":"168605","DOI":"10.1016\/j.jmb.2024.168605","article-title":"flDPnn2: Accurate and fast predictor of intrinsic disorder in proteins","volume":"436","author":"Wang","year":"2024","journal-title":"J Mol Biol"},{"key":"2025121107551566500_ref44","doi-asserted-by":"publisher","first-page":"lqad041","DOI":"10.1093\/nargab\/lqad041","article-title":"ADOPT: intrinsic protein disorder prediction through deep bidirectional transformers","volume":"5","author":"Redl","year":"2023","journal-title":"NAR Genom Bioinform"},{"key":"2025121107551566500_ref45","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1186\/s12915-023-01803-y","article-title":"DisoFLAG: Accurate prediction of protein intrinsic disorder and its functions using graph-based interaction protein language model","volume":"22","author":"Pang","year":"2024","journal-title":"BMC Biol"},{"key":"2025121107551566500_ref46","doi-asserted-by":"publisher","first-page":"W176","DOI":"10.1093\/nar\/gkae385","article-title":"AIUPred: Combining energy estimation with deep learning for the enhanced prediction of protein disorder","volume":"52","author":"Erdos","year":"2024","journal-title":"Nucleic Acids Res"},{"key":"2025121107551566500_ref47","doi-asserted-by":"publisher","first-page":"269","DOI":"10.1021\/cb500696t","article-title":"DFGmodel: Predicting protein kinase structures in inactive states for structure-based discovery of type-II inhibitors","volume":"10","author":"Ung","year":"2015","journal-title":"ACS Chem Biol"},{"key":"2025121107551566500_ref48","doi-asserted-by":"publisher","first-page":"65","DOI":"10.1016\/j.tibs.2010.09.006","article-title":"Protein kinases: evolution of dynamic regulatory proteins","volume":"36","author":"Taylor","year":"2011","journal-title":"Trends Biochem Sci"},{"key":"2025121107551566500_ref49","doi-asserted-by":"publisher","first-page":"6545","DOI":"10.1038\/s41467-024-50812-0","article-title":"Evolutionary sequence and structural basis for the distinct conformational landscapes of Tyr and Ser\/Thr kinases","volume":"15","author":"Gizzio","year":"2024","journal-title":"Nat Commun"},{"key":"2025121107551566500_ref50","doi-asserted-by":"publisher","first-page":"D512","DOI":"10.1093\/nar\/gku1267","article-title":"PhosphoSitePlus, 2014: Mutations, PTMs and recalibrations","volume":"43","author":"Hornbeck","year":"2015","journal-title":"Nucleic Acids Res"},{"key":"2025121107551566500_ref51","doi-asserted-by":"publisher","first-page":"D552","DOI":"10.1093\/nar\/gkaa945","article-title":"KinaseMD: Kinase mutations and drug response database","volume":"49","author":"Hu","year":"2021","journal-title":"Nucleic Acids Res"},{"key":"2025121107551566500_ref52","doi-asserted-by":"publisher","first-page":"1185","DOI":"10.1042\/BST20160172","article-title":"The contribution of intrinsically disordered regions to protein function, cellular complexity, and human disease","volume":"44","author":"Babu","year":"2016","journal-title":"Biochem Soc Trans"},{"key":"2025121107551566500_ref53","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1038\/nrm3920","article-title":"Intrinsically disordered proteins in cellular signalling and regulation","volume":"16","author":"Wright","year":"2015","journal-title":"Nat Rev Mol Cell Biol"},{"key":"2025121107551566500_ref54","doi-asserted-by":"publisher","first-page":"e0217889","DOI":"10.1371\/journal.pone.0217889","article-title":"Intrinsically disordered proteins and structured proteins with intrinsically disordered regions have different functional roles in the cell","volume":"14","author":"Deiana","year":"2019","journal-title":"PLoS One"},{"key":"2025121107551566500_ref55","doi-asserted-by":"publisher","first-page":"268","DOI":"10.1107\/S0907444910000314","article-title":"Rapid model building of alpha-helices in electron-density maps","volume":"66","author":"Terwilliger","year":"2010","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"2025121107551566500_ref56","doi-asserted-by":"publisher","first-page":"2967","DOI":"10.3390\/molecules29132967","article-title":"The effect of beta-sheet secondary structure on all-beta proteins by molecular dynamics simulations","volume":"29","author":"Feng","year":"2024","journal-title":"Molecules"},{"key":"2025121107551566500_ref57","doi-asserted-by":"publisher","first-page":"16","DOI":"10.1186\/s12859-016-1433-7","article-title":"KinMap: A web-based tool for interactive navigation through human kinome data","volume":"18","author":"Eid","year":"2017","journal-title":"BMC Bioinformatics"},{"key":"2025121107551566500_ref58","doi-asserted-by":"publisher","first-page":"D508","DOI":"10.1093\/nar\/gks1226","article-title":"D(2)P(2): Database of disordered protein predictions","volume":"41","author":"Oates","year":"2013","journal-title":"Nucleic Acids Res"},{"key":"2025121107551566500_ref59","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.88210","article-title":"A critical evaluation of protein kinase regulation by activation loop autophosphorylation","volume":"12","author":"Reinhardt","year":"2023","journal-title":"elife"},{"key":"2025121107551566500_ref60","doi-asserted-by":"publisher","first-page":"2068","DOI":"10.1038\/s41598-020-58868-w","article-title":"The order-disorder continuum: Linking predictions of protein structure and disorder through molecular simulation","volume":"10","author":"Hsu","year":"2020","journal-title":"Sci Rep"}],"container-title":["Briefings in Bioinformatics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/academic.oup.com\/bib\/article-pdf\/26\/6\/bbaf662\/65837578\/bbaf662.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/bib\/article-pdf\/26\/6\/bbaf662\/65837578\/bbaf662.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,12,11]],"date-time":"2025-12-11T12:55:24Z","timestamp":1765457724000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/bib\/article\/doi\/10.1093\/bib\/bbaf662\/8377154"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,11,1]]},"references-count":60,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2025,11,1]]}},"URL":"https:\/\/doi.org\/10.1093\/bib\/bbaf662","relation":{},"ISSN":["1467-5463","1477-4054"],"issn-type":[{"value":"1467-5463","type":"print"},{"value":"1477-4054","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2025,11]]},"published":{"date-parts":[[2025,11,1]]},"article-number":"bbaf662"}}