{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T20:51:02Z","timestamp":1791924662107,"version":"4.3.4"},"publisher-location":"New York, NY","reference-count":73,"publisher":"Springer US","isbn-type":[{"value":"9781071655702","type":"print"},{"value":"9781071655719","type":"electronic"}],"license":[{"start":{"date-parts":[[2026,10,12]],"date-time":"2026-10-12T00:00:00Z","timestamp":1791763200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2026,10,12]],"date-time":"2026-10-12T00:00:00Z","timestamp":1791763200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2027]]},"DOI":"10.1007\/978-1-0716-5571-9_1","type":"book-chapter","created":{"date-parts":[[2026,10,12]],"date-time":"2026-10-12T15:22:14Z","timestamp":1791818534000},"page":"1-17","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Key Points to Consider When Studying RNA Remodeling by Proteins"],"prefix":"10.1007","author":[{"given":"William Luke","family":"Ward","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4879-8563","authenticated-orcid":false,"given":"Rick","family":"Russell","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,10,12]]},"reference":[{"key":"1_CR1","doi-asserted-by":"publisher","first-page":"1514","DOI":"10.1126\/science.1111443","volume":"309","author":"MJ Moore","year":"2005","unstructured":"Moore MJ (2005) From birth to death: the complex lives of eukaryotic mRNAs. Science 309:1514\u20131518","journal-title":"Science"},{"key":"1_CR2","doi-asserted-by":"publisher","first-page":"879","DOI":"10.1038\/s41576-024-00749-3","volume":"25","author":"JS Xiang","year":"2024","unstructured":"Xiang JS, Schafer DM, Rothamel KL et al (2024) Decoding protein-RNA interactions using CLIP-based methodologies. Nat Rev Genet 25:879\u2013895","journal-title":"Nat Rev Genet"},{"key":"1_CR3","doi-asserted-by":"publisher","first-page":"3790","DOI":"10.1016\/j.molcel.2024.08.030","volume":"84","author":"LA Street","year":"2024","unstructured":"Street LA, Rothamel KL, Brannan KW et al (2024) Large-scale map of RNA-binding protein interactomes across the mRNA life cycle. Mol Cell 84:3790\u20133809.e8","journal-title":"Mol Cell"},{"key":"1_CR4","doi-asserted-by":"publisher","first-page":"118","DOI":"10.4161\/rna.4.3.5445","volume":"4","author":"L Rajkowitsch","year":"2007","unstructured":"Rajkowitsch L, Chen D, Stampfl S et al (2007) RNA chaperones, RNA annealers and RNA helicases. RNA Biol 4:118\u2013130","journal-title":"RNA Biol"},{"key":"1_CR5","doi-asserted-by":"publisher","first-page":"667","DOI":"10.4161\/rna.7.6.13571","volume":"7","author":"C Pan","year":"2010","unstructured":"Pan C, Russell R (2010) Roles of DEAD-box proteins in RNA and RNP folding. RNA Biol 7:667\u2013676","journal-title":"RNA Biol"},{"key":"1_CR6","doi-asserted-by":"publisher","first-page":"697","DOI":"10.1146\/annurev-biochem-060713-035546","volume":"83","author":"I Jarmoskaite","year":"2014","unstructured":"Jarmoskaite I, Russell R (2014) RNA helicase proteins as chaperones and remodelers. Annu Rev Biochem 83:697\u2013725","journal-title":"Annu Rev Biochem"},{"key":"1_CR7","doi-asserted-by":"crossref","unstructured":"Woodson SA, Panja S, Santiago-Frangos A (2018) Proteins that chaperone RNA regulation. Microbiol Spectr 6:10","DOI":"10.1128\/microbiolspec.RWR-0026-2018"},{"key":"1_CR8","doi-asserted-by":"publisher","first-page":"24","DOI":"10.1080\/15476286.2024.2415801","volume":"21","author":"N Lang","year":"2024","unstructured":"Lang N, Jagtap PKA, Hennig J (2024) Regulation and mechanisms of action of RNA helicases. RNA Biol 21:24\u201338","journal-title":"RNA Biol"},{"key":"1_CR9","doi-asserted-by":"publisher","first-page":"313","DOI":"10.1016\/j.sbi.2010.03.011","volume":"20","author":"ME Fairman-Williams","year":"2010","unstructured":"Fairman-Williams ME, Guenther UP, Jankowsky E (2010) SF1 and SF2 helicases: family matters. Curr Opin Struct Biol 20:313\u2013324","journal-title":"Curr Opin Struct Biol"},{"key":"1_CR10","doi-asserted-by":"publisher","first-page":"505","DOI":"10.1038\/nrm3154","volume":"12","author":"P Linder","year":"2011","unstructured":"Linder P, Jankowsky E (2011) From unwinding to clamping\u2014the DEAD box RNA helicase family. Nat Rev Mol Cell Biol 12:505\u2013516","journal-title":"Nat Rev Mol Cell Biol"},{"key":"1_CR11","doi-asserted-by":"publisher","first-page":"908","DOI":"10.1038\/nrm1497","volume":"5","author":"R Schroeder","year":"2004","unstructured":"Schroeder R, Barta A, Semrad K (2004) Strategies for RNA folding and assembly. Nat Rev Mol Cell Biol 5:908\u2013919","journal-title":"Nat Rev Mol Cell Biol"},{"key":"1_CR12","doi-asserted-by":"publisher","first-page":"130","DOI":"10.1016\/j.sbi.2017.08.001","volume":"46","author":"SH Scheres","year":"2017","unstructured":"Scheres SH, Nagai K (2017) CryoEM structures of spliceosomal complexes reveal the molecular mechanism of pre-mRNA splicing. Curr Opin Struct Biol 46:130\u2013139","journal-title":"Curr Opin Struct Biol"},{"key":"1_CR13","doi-asserted-by":"publisher","first-page":"e1519","DOI":"10.1002\/wrna.1519","volume":"10","author":"Z Xing","year":"2019","unstructured":"Xing Z, Ma WK, Tran EJ (2019) The DDX5\/Dbp2 subfamily of DEAD-box RNA helicases. Wiley Interdiscip Rev RNA 10:e1519","journal-title":"Wiley Interdiscip Rev RNA"},{"key":"1_CR14","doi-asserted-by":"publisher","first-page":"749","DOI":"10.1038\/s41580-023-00628-5","volume":"24","author":"KE Bohnsack","year":"2023","unstructured":"Bohnsack KE, Yi S, Venus S et al (2023) Cellular functions of eukaryotic RNA helicases and their links to human diseases. Nat Rev Mol Cell Biol 24:749\u2013769","journal-title":"Nat Rev Mol Cell Biol"},{"key":"1_CR15","doi-asserted-by":"publisher","first-page":"619","DOI":"10.4161\/rna.24044","volume":"10","author":"EG Wagner","year":"2013","unstructured":"Wagner EG (2013) Cycling of RNAs on Hfq. RNA Biol 10:619\u2013626","journal-title":"RNA Biol"},{"key":"1_CR16","doi-asserted-by":"publisher","first-page":"101384","DOI":"10.1016\/j.mam.2025.101384","volume":"104","author":"BR Sahoo","year":"2025","unstructured":"Sahoo BR, Bardwell JC (2025) Protein and RNA chaperones. Mol Aspects Med 104:101384","journal-title":"Mol Aspects Med"},{"key":"1_CR17","doi-asserted-by":"publisher","first-page":"474","DOI":"10.1038\/s41580-019-0136-0","volume":"20","author":"LR Ganser","year":"2019","unstructured":"Ganser LR, Kelly ML, Herschlag D et al (2019) The roles of structural dynamics in the cellular functions of RNAs. Nat Rev Mol Cell Biol 20:474\u2013489","journal-title":"Nat Rev Mol Cell Biol"},{"key":"1_CR18","doi-asserted-by":"publisher","first-page":"835","DOI":"10.1038\/s41586-023-06080-x","volume":"617","author":"ML Ken","year":"2023","unstructured":"Ken ML, Roy R, Geng A et al (2023) RNA conformational propensities determine cellular activity. Nature 617:835\u2013841","journal-title":"Nature"},{"key":"1_CR19","doi-asserted-by":"publisher","first-page":"477","DOI":"10.1146\/annurev.bb.04.060175.002401","volume":"4","author":"PB Sigler","year":"1975","unstructured":"Sigler PB (1975) An analysis of the structure of tRNA. Annu Rev Biophys Bioeng 4:477\u2013527","journal-title":"Annu Rev Biophys Bioeng"},{"key":"1_CR20","doi-asserted-by":"publisher","first-page":"20871","DOI":"10.1074\/jbc.270.36.20871","volume":"270","author":"D Herschlag","year":"1995","unstructured":"Herschlag D (1995) RNA chaperones and the RNA folding problem. J Biol Chem 270:20871\u201320874","journal-title":"J Biol Chem"},{"key":"1_CR21","doi-asserted-by":"publisher","first-page":"1","DOI":"10.2741\/2557","volume":"13","author":"R Russell","year":"2008","unstructured":"Russell R (2008) RNA misfolding and the action of chaperones. Front Biosci 13:1\u201320","journal-title":"Front Biosci"},{"key":"1_CR22","doi-asserted-by":"publisher","first-page":"223","DOI":"10.1017\/S0033583513000048","volume":"46","author":"JL Fiore","year":"2013","unstructured":"Fiore JL, Nesbitt DJ (2013) An RNA folding motif: GNRA tetraloop-receptor interactions. Q Rev Biophys 46:223\u2013264","journal-title":"Q Rev Biophys"},{"key":"1_CR23","doi-asserted-by":"publisher","first-page":"E7688","DOI":"10.1073\/pnas.1703507114","volume":"114","author":"N Bisaria","year":"2017","unstructured":"Bisaria N, Greenfeld M, Limouse C et al (2017) Quantitative tests of a reconstitution model for RNA folding thermodynamics and kinetics. Proc Natl Acad Sci U S A 114:E7688\u2013E7696","journal-title":"Proc Natl Acad Sci U S A"},{"key":"1_CR24","doi-asserted-by":"crossref","unstructured":"Bonilla SL, Denny SK, Shin JH et al (2021) High-throughput dissection of the thermodynamic and conformational properties of a ubiquitous class of RNA tertiary contact motifs. Proc Natl Acad Sci U S A 118:e2109085118","DOI":"10.1073\/pnas.2109085118"},{"key":"1_CR25","doi-asserted-by":"publisher","first-page":"E2928","DOI":"10.1073\/pnas.1404307111","volume":"111","author":"I Jarmoskaite","year":"2014","unstructured":"Jarmoskaite I, Bhaskaran H, Seifert S et al (2014) DEAD-box protein CYT-19 is activated by exposed helices in a group I intron RNA. Proc Natl Acad Sci U S A 111:E2928\u2013E2936","journal-title":"Proc Natl Acad Sci U S A"},{"key":"1_CR26","doi-asserted-by":"publisher","first-page":"287","DOI":"10.1016\/j.cell.2006.01.054","volume":"125","author":"T Sengoku","year":"2006","unstructured":"Sengoku T, Nureki O, Nakamura A et al (2006) Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa. Cell 125:287\u2013300","journal-title":"Cell"},{"key":"1_CR27","doi-asserted-by":"publisher","first-page":"713","DOI":"10.1016\/j.cell.2006.08.006","volume":"126","author":"F Bono","year":"2006","unstructured":"Bono F, Ebert J, Lorentzen E et al (2006) The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA. Cell 126:713\u2013725","journal-title":"Cell"},{"key":"1_CR28","doi-asserted-by":"publisher","first-page":"19292","DOI":"10.1073\/pnas.0908744106","volume":"106","author":"TM Link","year":"2009","unstructured":"Link TM, Valentin-Hansen P, Brennan RG (2009) Structure of Escherichia coli Hfq bound to polyriboadenylate RNA. Proc Natl Acad Sci U S A 106:19292\u201319297","journal-title":"Proc Natl Acad Sci U S A"},{"key":"1_CR29","doi-asserted-by":"publisher","first-page":"578","DOI":"10.1038\/nrmicro2615","volume":"9","author":"J Vogel","year":"2011","unstructured":"Vogel J, Luisi BF (2011) Hfq and its constellation of RNA. Nat Rev Microbiol 9:578\u2013589","journal-title":"Nat Rev Microbiol"},{"key":"1_CR30","doi-asserted-by":"publisher","first-page":"487","DOI":"10.1016\/j.molcel.2015.10.011","volume":"60","author":"JR Prabu","year":"2015","unstructured":"Prabu JR, Muller M, Thomae AW et al (2015) Structure of the RNA helicase MLE reveals the molecular mechanisms for uridine specificity and RNA-ATP coupling. Mol Cell 60:487\u2013499","journal-title":"Mol Cell"},{"key":"1_CR31","doi-asserted-by":"publisher","first-page":"247","DOI":"10.1146\/annurev-biophys-050511-102243","volume":"41","author":"A Henn","year":"2012","unstructured":"Henn A, Bradley MJ, De La Cruz EM (2012) ATP utilization and RNA conformational rearrangement by DEAD-box proteins. Annu Rev Biophys 41:247\u2013267","journal-title":"Annu Rev Biophys"},{"key":"1_CR32","doi-asserted-by":"publisher","first-page":"10644","DOI":"10.1093\/nar\/gku747","volume":"42","author":"B Samatanga","year":"2014","unstructured":"Samatanga B, Klostermeier D (2014) DEAD-box RNA helicase domains exhibit a continuum between complete functional independence and high thermodynamic coupling in nucleotide and RNA duplex recognition. Nucleic Acids Res 42:10644\u201310654","journal-title":"Nucleic Acids Res"},{"key":"1_CR33","doi-asserted-by":"publisher","first-page":"701","DOI":"10.1038\/nature12894","volume":"505","author":"S Rouskin","year":"2014","unstructured":"Rouskin S, Zubradt M, Washietl S et al (2014) Genome-wide probing of RNA structure reveals active unfolding of mRNA structures in vivo. Nature 505:701\u2013705","journal-title":"Nature"},{"key":"1_CR34","doi-asserted-by":"publisher","first-page":"322","DOI":"10.1038\/s41594-019-0200-7","volume":"26","author":"L Sun","year":"2019","unstructured":"Sun L, Fazal FM, Li P et al (2019) RNA structure maps across mammalian cellular compartments. Nat Struct Mol Biol 26:322\u2013330","journal-title":"Nat Struct Mol Biol"},{"key":"1_CR35","doi-asserted-by":"publisher","first-page":"1014","DOI":"10.1038\/nature06235","volume":"449","author":"H Bhaskaran","year":"2007","unstructured":"Bhaskaran H, Russell R (2007) Kinetic redistribution of native and misfolded RNAs by a DEAD-box chaperone. Nature 449:1014\u20131018","journal-title":"Nature"},{"key":"1_CR36","doi-asserted-by":"publisher","first-page":"1427","DOI":"10.1093\/nar\/30.7.1427","volume":"30","author":"V Anantharaman","year":"2002","unstructured":"Anantharaman V, Koonin EV, Aravind L (2002) Comparative genomics and evolution of proteins involved in RNA metabolism. Nucleic Acids Res 30:1427\u20131464","journal-title":"Nucleic Acids Res"},{"key":"1_CR37","doi-asserted-by":"publisher","first-page":"4","DOI":"10.4161\/rna.21879","volume":"10","author":"R Martin","year":"2013","unstructured":"Martin R, Straub AU, Doebele C et al (2013) DExD\/H-box RNA helicases in ribosome biogenesis. RNA Biol 10:4\u201318","journal-title":"RNA Biol"},{"key":"1_CR38","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-018-07783-w","volume":"9","author":"L Bruning","year":"2018","unstructured":"Bruning L, Hackert P, Martin R et al (2018) RNA helicases mediate structural transitions and compositional changes in pre-ribosomal complexes. Nat Commun 9: 5383","journal-title":"Nat Commun"},{"key":"1_CR39","doi-asserted-by":"publisher","first-page":"781","DOI":"10.1080\/15476286.2022.2079890","volume":"19","author":"V Mitterer","year":"2022","unstructured":"Mitterer V, Pertschy B (2022) RNA folding and functions of RNA helicases in ribosome biogenesis. RNA Biol 19:781\u2013810","journal-title":"RNA Biol"},{"key":"1_CR40","doi-asserted-by":"publisher","first-page":"2083","DOI":"10.1261\/rna.1792109","volume":"15","author":"BS Strunk","year":"2009","unstructured":"Strunk BS, Karbstein K (2009) Powering through ribosome assembly. RNA 15:2083\u20132104","journal-title":"RNA"},{"key":"1_CR41","doi-asserted-by":"publisher","first-page":"e1002480","DOI":"10.1371\/journal.pbio.1002480","volume":"14","author":"S Khoshnevis","year":"2016","unstructured":"Khoshnevis S, Askenasy I, Johnson MC et al (2016) The DEAD-box protein Rok1 orchestrates 40S and 60S ribosome assembly by promoting the release of Rrp5 from Pre-40S ribosomes to allow for 60S maturation. PLoS Biol 14:e1002480","journal-title":"PLoS Biol"},{"key":"1_CR42","doi-asserted-by":"publisher","first-page":"e56910","DOI":"10.15252\/embr.202356910","volume":"24","author":"B Lau","year":"2023","unstructured":"Lau B, Huang Z, Kellner N et al (2023) Mechanism of 5S RNP recruitment and helicase-surveilled rRNA maturation during pre-60S biogenesis. EMBO Rep 24:e56910","journal-title":"EMBO Rep"},{"key":"1_CR43","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-024-47616-7","volume":"15","author":"VE Cruz","year":"2024","unstructured":"Cruz VE, Weirich CS, Peddada N et al (2024) The DEAD-box ATPase Dbp10\/DDX54 initiates peptidyl transferase center formation during 60S ribosome biogenesis. Nat Commun 15: 3296","journal-title":"Nat Commun"},{"key":"1_CR44","doi-asserted-by":"publisher","first-page":"431","DOI":"10.1016\/j.ceb.2012.03.004","volume":"24","author":"O Cordin","year":"2012","unstructured":"Cordin O, Hahn D, Beggs JD (2012) Structure, function and regulation of spliceosomal RNA helicases. Curr Opin Cell Biol 24:431\u2013438","journal-title":"Curr Opin Cell Biol"},{"key":"1_CR45","doi-asserted-by":"publisher","first-page":"263","DOI":"10.1016\/j.tibs.2012.04.001","volume":"37","author":"DR Semlow","year":"2012","unstructured":"Semlow DR, Staley JP (2012) Staying on message: ensuring fidelity in pre-mRNA splicing. Trends Biochem Sci 37:263\u2013273","journal-title":"Trends Biochem Sci"},{"key":"1_CR46","doi-asserted-by":"publisher","first-page":"197","DOI":"10.1038\/nature19316","volume":"537","author":"WP Galej","year":"2016","unstructured":"Galej WP, Wilkinson ME, Fica SM et al (2016) Cryo-EM structure of the spliceosome immediately after branching. Nature 537:197\u2013201","journal-title":"Nature"},{"key":"1_CR47","doi-asserted-by":"publisher","first-page":"1283","DOI":"10.1126\/science.aar3729","volume":"358","author":"ME Wilkinson","year":"2017","unstructured":"Wilkinson ME, Fica SM, Galej WP et al (2017) Postcatalytic spliceosome structure reveals mechanism of 3\u2019-splice site selection. Science 358:1283\u20131288","journal-title":"Science"},{"key":"1_CR48","doi-asserted-by":"publisher","first-page":"1278","DOI":"10.1126\/science.aar3462","volume":"358","author":"S Liu","year":"2017","unstructured":"Liu S, Li X, Zhang L et al (2017) Structure of the yeast spliceosomal postcatalytic P complex. Science 358:1278\u20131283","journal-title":"Science"},{"key":"1_CR49","doi-asserted-by":"publisher","first-page":"791","DOI":"10.1038\/nsmb.3463","volume":"24","author":"SM Fica","year":"2017","unstructured":"Fica SM, Nagai K (2017) Cryo-electron microscopy snapshots of the spliceosome: structural insights into a dynamic ribonucleoprotein machine. Nat Struct Mol Biol 24:791\u2013799","journal-title":"Nat Struct Mol Biol"},{"key":"1_CR50","doi-asserted-by":"publisher","first-page":"318","DOI":"10.1038\/nature21079","volume":"542","author":"K Bertram","year":"2017","unstructured":"Bertram K, Agafonov DE, Liu WT et al (2017) Cryo-EM structure of a human spliceosome activated for step 2 of splicing. Nature 542:318\u2013323","journal-title":"Nature"},{"key":"1_CR51","doi-asserted-by":"publisher","first-page":"362","DOI":"10.1126\/science.aax3289","volume":"364","author":"C Charenton","year":"2019","unstructured":"Charenton C, Wilkinson ME, Nagai K (2019) Mechanism of 5\u2032 splice site transfer for human spliceosome activation. Science 364:362\u2013367","journal-title":"Science"},{"key":"1_CR52","doi-asserted-by":"publisher","first-page":"359","DOI":"10.1146\/annurev-biochem-091719-064225","volume":"89","author":"ME Wilkinson","year":"2020","unstructured":"Wilkinson ME, Charenton C, Nagai K (2020) RNA splicing by the spliceosome. Annu Rev Biochem 89:359\u2013388","journal-title":"Annu Rev Biochem"},{"key":"1_CR53","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-024-50785-0","volume":"15","author":"X Zhan","year":"2024","unstructured":"Zhan X, Lu Y, Shi Y (2024) Molecular basis for the activation of human spliceosome. Nat Commun 15: 6348","journal-title":"Nat Commun"},{"key":"1_CR54","doi-asserted-by":"publisher","first-page":"6921","DOI":"10.1073\/pnas.88.16.6921","volume":"88","author":"D Herschlag","year":"1991","unstructured":"Herschlag D (1991) Implications of ribozyme kinetics for targeting the cleavage of specific RNA molecules in vivo: more isn\u2019t always better. Proc Natl Acad Sci U S A 88:6921\u20136925","journal-title":"Proc Natl Acad Sci U S A"},{"key":"1_CR55","doi-asserted-by":"publisher","first-page":"985","DOI":"10.1016\/j.cell.2016.01.025","volume":"164","author":"DR Semlow","year":"2016","unstructured":"Semlow DR, Blanco MR, Walter NG et al (2016) Spliceosomal DEAH-box ATPases remodel pre-mRNA to activate alternative splice sites. Cell 164:985\u2013998","journal-title":"Cell"},{"key":"1_CR56","doi-asserted-by":"publisher","first-page":"225","DOI":"10.1016\/j.tibs.2020.10.006","volume":"46","author":"F De Bortoli","year":"2021","unstructured":"De Bortoli F, Espinosa S, Zhao R (2021) DEAH-Box RNA helicases in pre-mRNA splicing. Trends Biochem Sci 46:225\u2013238","journal-title":"Trends Biochem Sci"},{"key":"1_CR57","doi-asserted-by":"publisher","first-page":"133","DOI":"10.4161\/rna.23507","volume":"10","author":"SL Konig","year":"2013","unstructured":"Konig SL, Liyanage PS, Sigel RK et al (2013) Helicase-mediated changes in RNA structure at the single-molecule level. RNA Biol 10:133\u2013148","journal-title":"RNA Biol"},{"key":"1_CR58","doi-asserted-by":"publisher","first-page":"924","DOI":"10.1063\/1.1672157","volume":"51","author":"GS Manning","year":"1969","unstructured":"Manning GS (1969) Limiting laws and counterion condensation in polyelectrolyte solutions I. Colligative properties. J Chem Phys 51:924\u2013933","journal-title":"J Chem Phys"},{"key":"1_CR59","doi-asserted-by":"publisher","first-page":"335","DOI":"10.1261\/rna.5205404","volume":"10","author":"DE Draper","year":"2004","unstructured":"Draper DE (2004) A guide to ions and RNA structure. RNA 10:335\u2013343","journal-title":"RNA"},{"key":"1_CR60","doi-asserted-by":"publisher","first-page":"619","DOI":"10.1016\/j.cbpa.2008.10.010","volume":"12","author":"VB Chu","year":"2008","unstructured":"Chu VB, Bai Y, Lipfert J et al (2008) A repulsive field: advances in the electrostatics of the ion atmosphere. Curr Opin Chem Biol 12:619\u2013625","journal-title":"Curr Opin Chem Biol"},{"key":"1_CR61","doi-asserted-by":"publisher","first-page":"1087","DOI":"10.1016\/j.jmb.2007.02.071","volume":"368","author":"Q Yang","year":"2007","unstructured":"Yang Q, Fairman ME, Jankowsky E (2007) DEAD-box-protein-assisted RNA structure conversion towards and against thermodynamic equilibrium values. J Mol Biol 368:1087\u20131100","journal-title":"J Mol Biol"},{"key":"1_CR62","doi-asserted-by":"publisher","first-page":"5163","DOI":"10.1016\/S0021-9258(19)42342-9","volume":"249","author":"IA Rose","year":"1974","unstructured":"Rose IA, O\u2019Connell EL, Litwin S (1974) Determination of the rate of hexokinase-glucose dissociation by the isotope-trapping method. J Biol Chem 249:5163\u20135168","journal-title":"J Biol Chem"},{"key":"1_CR63","doi-asserted-by":"publisher","first-page":"8960","DOI":"10.1021\/bi00028a004","volume":"34","author":"AJ Fisher","year":"1995","unstructured":"Fisher AJ, Smith CA, Thoden JB et al (1995) X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4. Biochemistry 34:8960\u20138972","journal-title":"Biochemistry"},{"key":"1_CR64","first-page":"272","volume":"57","author":"M Golicnik","year":"2010","unstructured":"Golicnik M (2010) Metallic fluoride complexes as phosphate analogues for structural and mechanistic studies of phosphoryl group transfer enzymes. Acta Chim Slov 57:272\u2013287","journal-title":"Acta Chim Slov"},{"key":"1_CR65","doi-asserted-by":"publisher","first-page":"367","DOI":"10.1146\/annurev.bi.54.070185.002055","volume":"54","author":"F Eckstein","year":"1985","unstructured":"Eckstein F (1985) Nucleoside phosphorothioates. Annu Rev Biochem 54:367\u2013402","journal-title":"Annu Rev Biochem"},{"key":"1_CR66","doi-asserted-by":"publisher","first-page":"1180","DOI":"10.1261\/rna.2103703","volume":"9","author":"ML Peck","year":"2003","unstructured":"Peck ML, Herschlag D (2003) Adenosine 5\u2032-O-(3-thio)triphosphate (ATPgammaS) is a substrate for the nucleotide hydrolysis and RNA unwinding activities of eukaryotic translation initiation factor eIF4A. RNA 9:1180\u20131187","journal-title":"RNA"},{"key":"1_CR67","doi-asserted-by":"publisher","first-page":"7307","DOI":"10.1021\/bi0357208","volume":"43","author":"JJ Fak","year":"2004","unstructured":"Fak JJ, Itkin A, Ciobanu DD et al (2004) Nucleotide exchange from the high-affinity ATP-binding site in SecA is the rate-limiting step in the ATPase cycle of the soluble enzyme and occurs through a specialized conformational state. Biochemistry 43:7307\u20137327","journal-title":"Biochemistry"},{"key":"1_CR68","doi-asserted-by":"publisher","first-page":"20203","DOI":"10.1073\/pnas.0811075106","volume":"105","author":"Y Chen","year":"2008","unstructured":"Chen Y, Potratz JP, Tijerina P et al (2008) DEAD-box proteins can completely separate an RNA duplex using a single ATP. Proc Natl Acad Sci U S A 105:20203\u201320208","journal-title":"Proc Natl Acad Sci U S A"},{"key":"1_CR69","doi-asserted-by":"publisher","first-page":"20209","DOI":"10.1073\/pnas.0811115106","volume":"105","author":"F Liu","year":"2008","unstructured":"Liu F, Putnam A, Jankowsky E (2008) ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding. Proc Natl Acad Sci U S A 105:20209\u201320214","journal-title":"Proc Natl Acad Sci U S A"},{"key":"1_CR70","doi-asserted-by":"publisher","first-page":"423","DOI":"10.1021\/bi401540q","volume":"53","author":"F Liu","year":"2014","unstructured":"Liu F, Putnam AA, Jankowsky E (2014) DEAD-box helicases form nucleotide-dependent, long-lived complexes with RNA. Biochemistry 53:423\u2013433","journal-title":"Biochemistry"},{"key":"1_CR71","doi-asserted-by":"publisher","first-page":"1","DOI":"10.7554\/eLife.21510","volume":"6","author":"MJ Tauchert","year":"2017","unstructured":"Tauchert MJ, Fourmann JB, Luhrmann R et al (2017) Structural insights into the mechanism of the DEAH-box RNA helicase Prp43. Elife 6:1\u201325","journal-title":"Elife"},{"key":"1_CR72","doi-asserted-by":"publisher","first-page":"598","DOI":"10.1016\/j.molcel.2009.07.032","volume":"35","author":"M Del Campo","year":"2009","unstructured":"Del Campo M, Lambowitz AM (2009) Structure of the yeast DEAD box protein Mss116p reveals two wedges that crimp RNA. Mol Cell 35:598\u2013609","journal-title":"Mol Cell"},{"key":"1_CR73","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1007\/978-1-0716-0935-4_2","volume":"2209","author":"M Valentini","year":"2021","unstructured":"Valentini M, Linder P (2021) Happy birthday: 30 years of RNA helicases. Methods Mol Biol 2209:17\u201334","journal-title":"Methods Mol Biol"}],"container-title":["Methods in Molecular Biology","RNA Remodeling Proteins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/978-1-0716-5571-9_1","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T20:29:54Z","timestamp":1791923394000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/978-1-0716-5571-9_1"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,10,12]]},"ISBN":["9781071655702","9781071655719"],"references-count":73,"URL":"https:\/\/doi.org\/10.1007\/978-1-0716-5571-9_1","relation":{},"ISSN":["1064-3745","1940-6029"],"issn-type":[{"value":"1064-3745","type":"print"},{"value":"1940-6029","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,10,12]]},"assertion":[{"value":"12 October 2026","order":1,"name":"first_online","label":"First Online","group":{"name":"ChapterHistory","label":"Chapter History"}}]}}