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Journal articles on the topic 'DExH-box'

Author: Grafiati

Published: 5 June 2025

Last updated: 2 August 2025

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1

Marchat, Laurence A., Silvia I. Arzola-Rodríguez, Olga Hernandez-de la Cruz, Itzel Lopez-Rosas, and Cesar Lopez-Camarillo. "DEAD/DExH-Box RNA Helicases in Selected Human Parasites." Korean Journal of Parasitology 53, no. 5 (2015): 583–95. http://dx.doi.org/10.3347/kjp.2015.53.5.583.

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2

Ohlstein, B., C. A. Lavoie, O. Vef, E. Gateff, and D. M. McKearin. "The Drosophila Cystoblast Differentiation Factor, benign gonial cell neoplasm, Is Related to DExH-box Proteins and Interacts Genetically With bag-of-marbles." Genetics 155, no. 4 (2000): 1809–19. http://dx.doi.org/10.1093/genetics/155.4.1809.

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Abstract Selection of asymmetric cell fates can involve both intrinsic and extrinsic factors. Previously we have identified the bag-of-marbles (bam) gene as an intrinsic factor for cystoblast fate in Drosophila germline cells and shown that it requires active product from the benign gonial cell neoplasm (bgcn) gene. Here we present the cloning and characterization of bgcn. The predicted Bgcn protein is related to the DExH-box family of RNA-dependent helicases but lacks critical residues for ATPase and helicase functions. Expression of the bgcn gene is extremely limited in ovaries but, signific

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3

Poudevigne-Durance, Paul, Nele Hug, Ann Mukhortava, Javier Caceres, and David S. Rueda. "Single-molecule RNA remodelling by the DExH-Box 34 helicase." Biophysical Journal 121, no. 3 (2022): 481a. http://dx.doi.org/10.1016/j.bpj.2021.11.396.

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4

Lee, T., M. Paquet, O. Larsson, and J. Pelletier. "Tumor cell survival dependence on the DHX9 DExH-box helicase." Oncogene 35, no. 39 (2016): 5093–105. http://dx.doi.org/10.1038/onc.2016.52.

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5

Pietrzyk-Brzezinska, Agnieszka J., Eva Absmeier, Eberhard Klauck, Yanlin Wen, Haike Antelmann, and Markus C. Wahl. "Crystal Structure of the Escherichia coli DExH-Box NTPase HrpB." Structure 26, no. 11 (2018): 1462–73. http://dx.doi.org/10.1016/j.str.2018.07.013.

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6

Combs, D. Joshua, Roland J. Nagel, Manuel Ares, and Scott W. Stevens. "Prp43p Is a DEAH-Box Spliceosome Disassembly Factor Essential for Ribosome Biogenesis." Molecular and Cellular Biology 26, no. 2 (2006): 523–34. http://dx.doi.org/10.1128/mcb.26.2.523-534.2006.

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ABSTRACT The known function of the DEXH/D-box protein Prp43p is the removal of the U2, U5, and U6 snRNPs from the postsplicing lariat-intron ribonucleoprotein complex. We demonstrate that affinity-purified Prp43p-associated material includes the expected spliceosomal components; however, we also identify several preribosomal complexes that are specifically purified with Prp43p. Conditional prp43 mutant alleles confer a 35S pre-rRNA processing defect, with subsequent depletion of 27S and 20S precursors. Upon a shift to a nonpermissive temperature, both large and small-ribosomal-subunit proteins

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7

Martins, Alexandra, Christian H. Gross, and Stewart Shuman. "Mutational Analysis of Vaccinia Virus Nucleoside Triphosphate Phosphohydrolase I, a DNA-Dependent ATPase of the DExH Box Family." Journal of Virology 73, no. 2 (1999): 1302–8. http://dx.doi.org/10.1128/jvi.73.2.1302-1308.1999.

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ABSTRACT Vaccinia virus nucleoside triphosphate phosphohydrolase I (NPH-I) is a DNA-dependent ATPase that serves as a transcription termination factor during viral mRNA synthesis. NPH-I is a member of the DExH box family of nucleic acid-dependent nucleoside triphosphatases (NTPases), which is defined by the presence of several conserved sequence motifs. We have assessed the contributions of individual amino acids (underlined) in motifs I (GxGKT), II (DExHN), III (SAT), and VI (QxxGRxxR) to ATP hydrolysis by performing alanine scanning mutagenesis. Significant decrements in ATPase activity resu

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8

Lee, Teresa, and Jerry Pelletier. "Dependence of p53-deficient cells on the DHX9 DExH-box helicase." Oncotarget 8, no. 19 (2017): 30908–21. http://dx.doi.org/10.18632/oncotarget.15889.

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9

Marchat, Laurence A., Esther Orozco, Nancy Guillen, Christian Weber, and César López-Camarillo. "Putative DEAD and DExH-box RNA helicases families in Entamoeba histolytica." Gene 424, no. 1-2 (2008): 1–10. http://dx.doi.org/10.1016/j.gene.2008.07.042.

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10

Shi, Rui-Zhu, Yuan-Qing Pan, and Li Xing. "RNA Helicase A Regulates the Replication of RNA Viruses." Viruses 13, no. 3 (2021): 361. http://dx.doi.org/10.3390/v13030361.

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The RNA helicase A (RHA) is a member of DExH-box helicases and characterized by two double-stranded RNA binding domains at the N-terminus. RHA unwinds double-stranded RNA in vitro and is involved in RNA metabolisms in the cell. RHA is also hijacked by a variety of RNA viruses to facilitate virus replication. Herein, this review will provide an overview of the role of RHA in the replication of RNA viruses.

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11

Capitanio, Juliana S., Ben Montpetit, and Richard W. Wozniak. "Nucleoplasmic Nup98 controls gene expression by regulating a DExH/D-box protein." Nucleus 9, no. 1 (2017): 1–8. http://dx.doi.org/10.1080/19491034.2017.1364826.

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12

da Silva, Rahisa Helena, Manassés Daniel da Silva, José Ribamar Costa Ferreira-Neto, et al. "DEAD-Box RNA Helicase Family in Physic Nut (Jatropha curcas L.): Structural Characterization and Response to Salinity." Plants 13, no. 6 (2024): 905. http://dx.doi.org/10.3390/plants13060905.

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Helicases, motor proteins present in both prokaryotes and eukaryotes, play a direct role in various steps of RNA metabolism. Specifically, SF2 RNA helicases, a subset of the DEAD-box family, are essential players in plant developmental processes and responses to biotic and abiotic stresses. Despite this, information on this family in the physic nut (Jatropha curcas L.) remains limited, spanning from structural patterns to stress responses. We identified 79 genes encoding DEAD-box RNA helicases (JcDHX) in the J. curcas genome. These genes were further categorized into three subfamilies: DEAD (4

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13

Hausmann, Stéphane, Johan Geiser, Oscar Vadas, Verena Ducret, Karl Perron, and Martina Valentini. "Auxiliary domains of the HrpB bacterial DExH-box helicase shape its RNA preferences." RNA Biology 17, no. 5 (2020): 637–50. http://dx.doi.org/10.1080/15476286.2020.1720376.

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14

Gross, C. H., and S. Shuman. "Mutational analysis of vaccinia virus nucleoside triphosphate phosphohydrolase II, a DExH box RNA helicase." Journal of virology 69, no. 8 (1995): 4727–36. http://dx.doi.org/10.1128/jvi.69.8.4727-4736.1995.

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15

Xie, Qingyun, Jing Liu, Yanke Shan, Shouyu Wang, and Fei Liu. "Substrate Determinants for Unwinding Activity of the DExH/D-Box Protein RNA Helicase A." Biochemistry 57, no. 48 (2018): 6662–68. http://dx.doi.org/10.1021/acs.biochem.8b01025.

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16

Laggerbauer, B., T. Achsel, and R. Luhrmann. "The human U5-200kD DEXH-box protein unwinds U4/U6 RNA duplices in vitro." Proceedings of the National Academy of Sciences 95, no. 8 (1998): 4188–92. http://dx.doi.org/10.1073/pnas.95.8.4188.

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17

Pisareva, Vera P., Andrey V. Pisarev, Anton A. Komar, Christopher U. T. Hellen, and Tatyana V. Pestova. "Translation Initiation on Mammalian mRNAs with Structured 5′UTRs Requires DExH-Box Protein DHX29." Cell 135, no. 7 (2008): 1237–50. http://dx.doi.org/10.1016/j.cell.2008.10.037.

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18

Gross, Christian H., and Stewart Shuman. "The Nucleoside Triphosphatase and Helicase Activities of Vaccinia Virus NPH-II Are Essential for Virus Replication." Journal of Virology 72, no. 6 (1998): 4729–36. http://dx.doi.org/10.1128/jvi.72.6.4729-4736.1998.

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ABSTRACT Vaccinia virus NPH-II is the prototypal RNA helicase of the DExH box protein family, which is defined by six shared sequence motifs. The contributions of conserved amino acids in motifs I (TGVGKTSQ), Ia (PRI), II (DExHE), and III (TAT) to enzyme activity were assessed by alanine scanning. NPH-II-Ala proteins were expressed in baculovirus-infected Sf9 cells, purified, and characterized with respect to their RNA helicase, nucleic acid-dependent ATPase, and RNA binding functions. Alanine substitutions at Lys-191 and Thr-192 (motif I), Arg-229 (motif Ia), and Glu-300 (motif II) caused sev

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19

Xing, Jun, Xiaoxi Feng, Rutong Zhang, and Kaiguang Zhang. "Targeting Hepatocellular Carcinoma Growth: Haprolid’s Inhibition of AKT Signaling Through DExH-Box Helicase 9 Downregulation." Cancers 17, no. 3 (2025): 443. https://doi.org/10.3390/cancers17030443.

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Objective: Haprolid, a novel compound extracted from Myxobacterium, has been proven to possess selective toxicity towards various tumor cells, effectively inhibiting the growth of hepatocellular carcinoma (HCC). However, the underlying molecular mechanism remains unclear. Methods: To identify differentially expressed proteins (DEPs), isobaric tags for relative and absolute quantitation (iTRAQ) were employed. The clinical significance of DExH-Box Helicase 9 (DHX9) was determined using tissue microarrays in HCC patients. Changes in protein expression were detected using Western blotting, qPCR, a

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20

Zhou, Lei, Shiwei Sun, Liang Xu, Yueming Yu, Tieqi Zhang та Minghai Wang. "DExH-Box helicase 58 enhances osteoblast differentiation of osteoblastic cells via Wnt/β-Catenin signaling". Biochemical and Biophysical Research Communications 511, № 2 (2019): 307–11. http://dx.doi.org/10.1016/j.bbrc.2019.02.039.

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21

Gatfield, David, Hervé Le Hir, Christel Schmitt, et al. "The DExH/D box protein HEL/UAP56 is essential for mRNA nuclear export in Drosophila." Current Biology 11, no. 21 (2001): 1716–21. http://dx.doi.org/10.1016/s0960-9822(01)00532-2.

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22

Schwer, Beate, and Christian H. Gross. "Prp22, a DExH-box RNA helicase, plays two distinct roles in yeast pre-mRNA splicing." EMBO Journal 17, no. 7 (1998): 2086–94. http://dx.doi.org/10.1093/emboj/17.7.2086.

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23

Ye, Peiying, Shufeng Liu, Yiping Zhu, Guifang Chen, and Guangxia Gao. "DEXH-Box protein DHX30 is required for optimal function of the zinc-finger antiviral protein." Protein & Cell 1, no. 10 (2010): 956–64. http://dx.doi.org/10.1007/s13238-010-0117-8.

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24

Gulliver, Chloe, Ralf Hoffmann, and George S. Baillie. "The enigmatic helicase DHX9 and its association with the hallmarks of cancer." Future Science OA 7, no. 2 (2021): FSO650. http://dx.doi.org/10.2144/fsoa-2020-0140.

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Much interest has been expended lately in characterizing the association between DExH-Box helicase 9 (DHX9) dysregulation and malignant development, however, the enigmatic nature of DHX9 has caused conflict as to whether it regularly functions as an oncogene or tumor suppressor. The impact of DHX9 on malignancy appears to be cell-type specific, dependent upon the availability of binding partners and activation of inter-connected signaling pathways. Realization of DHX9’s pivotal role in the development of several hallmarks of cancer has boosted the enzyme's potential as a cancer biomarker and t

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25

Western, Tamara L., Yulan Cheng, Jun Liu, and Xuemei Chen. "HUA ENHANCER2, a putative DExH-box RNA helicase, maintains homeotic B and C gene expression inArabidopsis." Development 129, no. 7 (2002): 1569–81. http://dx.doi.org/10.1242/dev.129.7.1569.

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Reproductive organ identity in Arabidopsis is controlled by the B, C and SEPALLATA classes of floral homeotic genes. We have identified a recessive mutation in a novel gene, HUA ENHANCER2, which, when combined with mutations in two weak class C genes, HUA1 and HUA2, leads to the production of third whorl sepal-petal-stamens and fourth whorl sepal-carpels. Quadruple mutant analysis and in situ localization of A, B, C and SEPALLATA floral homeotic RNAs suggest that HUA ENHANCER2 is required for the maintenance of B and C gene expression in the reproductive whorls. In addition to its role in flor

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26

Deng, L., and S. Shuman. "Vaccinia NPH-I, a DExH-box ATPase, is the energy coupling factor for mRNA transcription termination." Genes & Development 12, no. 4 (1998): 538–46. http://dx.doi.org/10.1101/gad.12.4.538.

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27

Bifano, Abby L., and Mark G. Caprara. "A DExH/D-box Protein Coordinates the Two Steps of Splicing in a Group I Intron." Journal of Molecular Biology 383, no. 3 (2008): 667–82. http://dx.doi.org/10.1016/j.jmb.2008.08.070.

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28

Cencic, Regina, and Jerry Pelletier. "Throwing a monkey wrench in the motor: Targeting DExH/D box proteins with small molecule inhibitors." Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms 1829, no. 8 (2013): 894–903. http://dx.doi.org/10.1016/j.bbagrm.2013.01.008.

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29

Shen, Leo, and Jerry Pelletier. "General and Target-Specific DExD/H RNA Helicases in Eukaryotic Translation Initiation." International Journal of Molecular Sciences 21, no. 12 (2020): 4402. http://dx.doi.org/10.3390/ijms21124402.

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DExD (DDX)- and DExH (DHX)-box RNA helicases, named after their Asp-Glu-x-Asp/His motifs, are integral to almost all RNA metabolic processes in eukaryotic cells. They play myriad roles in processes ranging from transcription and mRNA-protein complex remodeling, to RNA decay and translation. This last facet, translation, is an intricate process that involves DDX/DHX helicases and presents a regulatory node that is highly targetable. Studies aimed at better understanding this family of conserved proteins have revealed insights into their structures, catalytic mechanisms, and biological roles. Th

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30

Ott, Kristen M., Tram Nguyen, and Caryn Navarro. "The DExH Box Helicase Domain of Spindle-E Is Necessary for Retrotransposon Silencing and Axial Patterning DuringDrosophilaOogenesis." G3: Genes|Genomes|Genetics 4, no. 11 (2014): 2247–57. http://dx.doi.org/10.1534/g3.114.014332.

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31

Lopez, Joaquin, Pablo Cruz Nunez, Camila Benavides, et al. "DExH-Box helicase 9 (DHX9) is a novel SARAF interactor and store-operated calcium entry (SOCE) regulator." Biophysical Journal 123, no. 3 (2024): 257a—258a. http://dx.doi.org/10.1016/j.bpj.2023.11.1618.

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32

Cui, Xue-Fan, Tadaatsu Imaizumi, Hidemi Yoshida, Ernest C. Borden та Kei Satoh. "Retinoic acid-inducible gene-I is induced by interferon-γ and regulates the expression of interferon-γ stimulated gene 15 in MCF-7 cells". Biochemistry and Cell Biology 82, № 3 (2004): 401–5. http://dx.doi.org/10.1139/o04-041.

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Retinoic acid-inducible gene-І (RIG-І) is a member of the DExH box family proteins, which have diverse roles in regulation of gene expression and cellular functions. We found RIG-I mRNA and protein were expressed in MCF-7 human breast cancer cells stimulated with interferon-γ (IFN-γ). This effect of IFN-γ was observed in concentration- and time-dependent manners, and IFN-γ also induced promoter activity of RIG-I. Transfection of GFP-RIG-I cDNA into MCF-7 cells resulted in the expression of RIG-I protein in cytoplasm. Overexpression of RIG-I induced the upregulation of IFN-γ stimulated gene 15,

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33

van Nues, Rob W., and Jean D. Beggs. "Functional Contacts With a Range of Splicing Proteins Suggest a Central Role for Brr2p in the Dynamic Control of the Order of Events in Spliceosomes ofSaccharomyces cerevisiae." Genetics 157, no. 4 (2001): 1451–67. http://dx.doi.org/10.1093/genetics/157.4.1451.

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AbstractMapping of functional protein interactions will help in understanding conformational rearrangements that occur within large complexes like spliceosomes. Because the U5 snRNP plays a central role in pre-mRNA splicing, we undertook exhaustive two-hybrid screening with Brr2p, Prp8p, and other U5 snRNP-associated proteins. DExH-box protein Brr2p interacted specifically with five splicing factors: Prp8p, DEAH-box protein Prp16p, U1 snRNP protein Snp1p, second-step factor Slu7p, and U4/U6.U5 tri-snRNP protein Snu66p, which is required for splicing at low temperatures. Co-immunoprecipitation

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34

Li, Chao, Peng Dou, Xin Lu, et al. "Identification and Validation of TRIM25 as a Glucose Metabolism Regulator in Prostate Cancer." International Journal of Molecular Sciences 23, no. 16 (2022): 9325. http://dx.doi.org/10.3390/ijms23169325.

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Prostate cancer (PCa) malignant progression is accompanied with the reprogramming of glucose metabolism. However, the genes involved in the regulation of glucose metabolism in PCa are not fully understood. Here, we propose a new method, DMRG, which constructs a weighted differential network (W-K-DN) to define the important metabolism-related genes. Based on biological knowledge and prostate cancer transcriptome data, a tripartite motif-containing 25 (TRIM25) was defined using DMRG; TRIM25 was involved in the regulation of glucose metabolism, which was verified by overexpressing or knocking dow

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35

Sofos, Nicholas, Mikael B. L. Winkler, and Ditlev E. Brodersen. "RRM domain of human RBM7: purification, crystallization and structure determination." Acta Crystallographica Section F Structural Biology Communications 72, no. 5 (2016): 397–402. http://dx.doi.org/10.1107/s2053230x16006129.

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RNA decay is an important process that is essential for controlling the abundance, quality and maturation of transcripts. In eukaryotes, RNA decay in the 3′–5′ direction is carried out by the exosome, an RNA-degradation machine that is conserved from yeast to humans. A range of cofactors stimulate the enzymatic activity of the exosome and serve as adapters for the many RNA substrates. In human cells, the exosome associates with the heterotrimeric nuclear exosome targeting (NEXT) complex consisting of the DExH-box helicase hMTR4, the zinc-finger protein hZCCHC8 and the RRM-type protein hRBM7. H

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36

Perutka, Jiri, Wenjun Wang, David Goerlitz, and Alan M. Lambowitz. "Use of Computer-designed Group II Introns to Disrupt Escherichia coli DExH/D-box Protein and DNA Helicase Genes." Journal of Molecular Biology 336, no. 2 (2004): 421–39. http://dx.doi.org/10.1016/j.jmb.2003.12.009.

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37

Apostolidou, Sofia, Theresa Harbauer, Peter Lasch, et al. "Fatal COVID-19 in a Child with Persistence of SARS-CoV-2 Despite Extensive Multidisciplinary Treatment: A Case Report." Children 8, no. 7 (2021): 564. http://dx.doi.org/10.3390/children8070564.

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Critical Coronavirus disease 2019 (COVID-19) developed in a 7-year-old girl with a history of dystrophy, microcephaly, and central hypothyroidism. Starting with gastrointestinal symptoms, the patient developed severe myocarditis followed by progressive multiple organ failure complicated by Pseudomonas aeruginosa bloodstream infection. Intensive care treatment consisting of invasive ventilation, drainage of pleural effusion, and high catecholamine therapy could not prevent the progression of heart failure, leading to the implantation of venoarterial extracorporeal life support (VA-ECLS) and add

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38

Nakagawa, Takuro, and Richard D. Kolodner. "Saccharomyces cerevisiae Mer3 Is a DNA Helicase Involved in Meiotic Crossing Over." Molecular and Cellular Biology 22, no. 10 (2002): 3281–91. http://dx.doi.org/10.1128/mcb.22.10.3281-3291.2002.

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ABSTRACT Crossing over is regulated to occur at least once per each pair of homologous chromosomes during meiotic prophase to ensure proper segregation of chromosomes at the first meiotic division. In a mer3 deletion mutant of Saccharomyces cerevisiae, crossing over is decreased, and the distribution of the crossovers that occur is random. The predicted Mer3 protein contains seven motifs characteristic of the DExH box type of DNA/RNA helicases. The mer3G166D and the mer3K167A mutation, amino acid substitutions of conserved residues in a putative nucleotide-binding domain of the helicase motifs

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39

He, Junna, Ying Duan, Deping Hua, et al. "DEXH Box RNA Helicase–Mediated Mitochondrial Reactive Oxygen Species Production in Arabidopsis Mediates Crosstalk between Abscisic Acid and Auxin Signaling." Plant Cell 24, no. 5 (2012): 1815–33. http://dx.doi.org/10.1105/tpc.112.098707.

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40

Liang, W. Q., J. A. Clark, and M. J. Fournier. "The rRNA-processing function of the yeast U14 small nucleolar RNA can be rescued by a conserved RNA helicase-like protein." Molecular and Cellular Biology 17, no. 7 (1997): 4124–32. http://dx.doi.org/10.1128/mcb.17.7.4124.

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The phylogenetically conserved U14 small nucleolar RNA is required for processing of rRNA, and this function involves base pairing with conserved complementary sequences in 18S RNA. With a view to identifying other important U14 interactions, a stem-loop domain required for activity of Saccharomyces cerevisiae U14 RNAs (the Y domain) was first subjected to detailed mutational analysis. The mapping results showed that most nucleotides of the Y domain can be replaced without affecting function, except for loop nucleotides conserved among five different yeast species. Defective variants were then

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41

Beran, Rudolf K. F., Brett D. Lindenbach, and Anna Marie Pyle. "The NS4A Protein of Hepatitis C Virus Promotes RNA-Coupled ATP Hydrolysis by the NS3 Helicase." Journal of Virology 83, no. 7 (2009): 3268–75. http://dx.doi.org/10.1128/jvi.01849-08.

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ABSTRACT Nonstructural protein 3 (NS3) is an essential replicative component of the hepatitis C virus (HCV) and a member of the DExH/D-box family of proteins. The C-terminal region of NS3 (NS3hel) exhibits RNA-stimulated NTPase and helicase activity, while the N-terminal serine protease domain of NS3 enhances RNA binding and unwinding by NS3hel. The nonstructural protein 4A (NS4A) binds to the NS3 protease domain and serves as an obligate cofactor for NS3 serine protease activity. Given its role in stimulating protease activity, we sought to determine whether NS4A also influences the activity

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42

Morra, Rosa, Edwin R. Smith, Ruth Yokoyama, and John C. Lucchesi. "The MLE Subunit of the Drosophila MSL Complex Uses Its ATPase Activity for Dosage Compensation and Its Helicase Activity for Targeting." Molecular and Cellular Biology 28, no. 3 (2007): 958–66. http://dx.doi.org/10.1128/mcb.00995-07.

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ABSTRACT In Drosophila, dosage compensation—the equalization of most X-linked gene products between XY males and XX females—is mediated by the MSL complex that preferentially associates with numerous sites on the X chromosome in somatic cells of males, but not of females. The complex consists of a noncoding RNA and a core of five protein subunits that includes a histone acetyltransferase (MOF) and an ATP-dependent DEXH box RNA/DNA helicase (MLE). Both of these enzymatic activities are necessary for the spreading of the complex to its sites of action along the X chromosome. MLE is related to th

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43

Zheng, Hua-Jun, Masatoshi Tsukahara, Enuo Liu, et al. "The Novel HelicasehelG(DHX30) Is Expressed During Gastrulation in Mice and Has a Structure Similar to a Human DExH Box Helicase." Stem Cells and Development 24, no. 3 (2015): 372–83. http://dx.doi.org/10.1089/scd.2014.0077.

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44

Pollpeter, Darja, Akihiko Komuro, Glen N. Barber, and Curt M. Horvath. "PS3-13 A role for the DEXH box protein LGP2 in innate immune responses induced by cytosolic DNA and Listeria monocytogenes." Cytokine 52, no. 1-2 (2010): 84–85. http://dx.doi.org/10.1016/j.cyto.2010.07.352.

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45

Margossian, Steven P., Huilin Li, Hans Peter Zassenhaus, and Ronald A. Butow. "The DExH Box Protein Suv3p Is a Component of a Yeast Mitochondrial 3′-to-5′ Exoribonuclease That Suppresses Group I Intron Toxicity." Cell 84, no. 2 (1996): 199–209. http://dx.doi.org/10.1016/s0092-8674(00)80975-7.

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46

McPheeters, D. S. "Interaction of the yeast DExH-box RNA helicase Prp22p with the 3' splice site during the second step of nuclear pre-mRNA splicing." Nucleic Acids Research 28, no. 6 (2000): 1313–21. http://dx.doi.org/10.1093/nar/28.6.1313.

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47

Tabara, Hiroaki, Erbay Yigit, Haruhiko Siomi, and Craig C. Mello. "The dsRNA Binding Protein RDE-4 Interacts with RDE-1, DCR-1, and a DExH-Box Helicase to Direct RNAi in C. elegans." Cell 109, no. 7 (2002): 861–71. http://dx.doi.org/10.1016/s0092-8674(02)00793-6.

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Mishra, Aastha, Shankar Chanchal, and Mohammad Z. Ashraf. "Host–Viral Interactions Revealed among Shared Transcriptomics Signatures of ARDS and Thrombosis: A Clue into COVID-19 Pathogenesis." TH Open 04, no. 04 (2020): e403-e412. http://dx.doi.org/10.1055/s-0040-1721706.

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AbstractSevere novel corona virus disease 2019 (COVID-19) infection is associated with a considerable activation of coagulation pathways, endothelial damage, and subsequent thrombotic microvascular injuries. These consistent observations may have serious implications for the treatment and management of this highly pathogenic disease. As a consequence, the anticoagulant therapeutic strategies, such as low molecular weight heparin, have shown some encouraging results. Cytokine burst leading to sepsis which is one of the primary reasons for acute respiratory distress syndrome (ARDS) drive that co

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Faridoon, Faridoon, Jiapeng Li, Jiyue Zheng, Xiang Wang, and Guiping Zhang. "Abstract 4247: Discovery of GH3595: a novel allosteric DHX9 inhibitor for cancer therapy." Cancer Research 85, no. 8_Supplement_1 (2025): 4247. https://doi.org/10.1158/1538-7445.am2025-4247.

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Abstract DExH-Box helicase 9 (DHX9), also known as RNA helicase A (RHA), belongs to the DExD/H-Box superfamily II of helicases. Due to its fundamental roles in processes such as transcription and maintenance of genomic stability, DHX9 has emerged as a key regulator in various cancer types. Specifically, microsatellite instable (MSI) cancers, such as MSI-high (MSI-H) colorectal cancer, and tumors with defective homologous recombination exhibit a strong dependency on DHX9, suggesting that targeting DHX9 could offer a significant therapeutic opportunity. Employing fragment-based drug design, we h

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Jacobsen, S. E., M. P. Running, and E. M. Meyerowitz. "Disruption of an RNA helicase/RNAse III gene in Arabidopsis causes unregulated cell division in floral meristems." Development 126, no. 23 (1999): 5231–43. http://dx.doi.org/10.1242/dev.126.23.5231.

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Arabidopsis thaliana floral meristems are determinate structures that produce a defined number of organs, after which cell division ceases. A new recessive mutant, carpel factory (caf), converts the floral meristems to an indeterminate state. They produce extra whorls of stamens, and an indefinite number of carpels. Thus, CAF appears to suppress cell division in floral meristems. The function of CAF is partially redundant with the function of the CLAVATA (CLV) and SUPERMAN (SUP) genes, as caf clv and caf sup double mutants show dramatically enhanced floral meristem over-proliferation. caf muta

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