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Artykuły w czasopismach na temat „Morpholino Oligomers”

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Data publikacji: 7 września 2023

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1

Aung-Htut, May T., Craig S. McIntosh, Kristin A. West, Sue Fletcher i Steve D. Wilton. "In Vitro Validation of Phosphorodiamidate Morpholino Oligomers". Molecules 24, nr 16 (12.08.2019): 2922. http://dx.doi.org/10.3390/molecules24162922.

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One of the crucial aspects of screening antisense oligonucleotides destined for therapeutic application is confidence that the antisense oligomer is delivered efficiently into cultured cells. Efficient delivery is particularly vital for antisense phosphorodiamidate morpholino oligomers, which have a neutral backbone, and are known to show poor gymnotic uptake. Here, we report several methods to deliver these oligomers into cultured cells. Although 4D-Nucleofector™ or Neon™ electroporation systems provide efficient delivery and use lower amounts of phosphorodiamidate morpholino oligomer, both systems are costly. We show that some readily available transfection reagents can be used to deliver phosphorodiamidate morpholino oligomers as efficiently as the electroporation systems. Among the transfection reagents tested, we recommend Lipofectamine 3000™ for delivering phosphorodiamidate morpholino oligomers into fibroblasts and Lipofectamine 3000™ or Lipofectamine 2000™ for myoblasts/myotubes. We also provide optimal programs for nucleofection into various cell lines using the P3 Primary Cell 4D-Nucleofector™ X Kit (Lonza), as well as antisense oligomers that redirect expression of ubiquitously expressed genes that may be used as positive treatments for human and murine cell transfections.
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2

Neuman, Benjamin W., David A. Stein, Andrew D. Kroeker, Amy D. Paulino, Hong M. Moulton, Patrick L. Iversen i Michael J. Buchmeier. "Antisense Morpholino-Oligomers Directed against the 5′ End of the Genome Inhibit Coronavirus Proliferation and Growth†". Journal of Virology 78, nr 11 (1.06.2004): 5891–99. http://dx.doi.org/10.1128/jvi.78.11.5891-5899.2004.

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ABSTRACT Conjugation of a peptide related to the human immunodeficiency virus type 1 Tat represents a novel method for delivery of antisense morpholino-oligomers. Conjugated and unconjugated oligomers were tested to determine sequence-specific antiviral efficacy against a member of the Coronaviridae, Mouse hepatitis virus (MHV). Specific antisense activity designed to block translation of the viral replicase polyprotein was first confirmed by reduction of luciferase expression from a target sequence-containing reporter construct in both cell-free and transfected cell culture assays. Peptide-conjugated morpholino-oligomers exhibited low toxicity in DBT astrocytoma cells used for culturing MHV. Oligomer administered at micromolar concentrations was delivered to >80% of cells and inhibited virus titers 10- to 100-fold in a sequence-specific and dose-responsive manner. In addition, targeted viral protein synthesis, plaque diameter, and cytopathic effect were significantly reduced. Inhibition of virus infectivity by peptide-conjugated morpholino was comparable to the antiviral activity of the aminoglycoside hygromycin B used at a concentration fivefold higher than the oligomer. These results suggest that this composition of antisense compound has therapeutic potential for control of coronavirus infection.
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3

McIntosh, Craig S., May Thandar Aung-Htut, Sue Fletcher i Steve D. Wilton. "Removal of the Polyglutamine Repeat of Ataxin-3 by Redirecting pre-mRNA Processing". International Journal of Molecular Sciences 20, nr 21 (31.10.2019): 5434. http://dx.doi.org/10.3390/ijms20215434.

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Spinocerebellar ataxia type 3 (SCA3) is a devastating neurodegenerative disease for which there is currently no cure, nor effective treatment strategy. One of nine polyglutamine disorders known to date, SCA3 is clinically heterogeneous and the main feature is progressive ataxia, which in turn affects speech, balance and gait of the affected individual. SCA3 is caused by an expanded polyglutamine tract in the ataxin-3 protein, resulting in conformational changes that lead to toxic gain of function. The expanded glutamine tract is located at the 5′ end of the penultimate exon (exon 10) of ATXN3 gene transcript. Other studies reported removal of the expanded glutamine tract using splice switching antisense oligonucleotides. Here, we describe improved efficiency in the removal of the toxic polyglutamine tract of ataxin-3 in vitro using phosphorodiamidate morpholino oligomers, when compared to antisense oligonucleotides composed of 2′-O-methyl modified bases on a phosphorothioate backbone. Significant downregulation of both the expanded and non-expanded protein was induced by the morpholino antisense oligomer, with a greater proportion of ataxin-3 protein missing the polyglutamine tract. With growing concerns over toxicity associated with long-term administration of phosphorothioate oligonucleotides, the use of a phosphorodiamidate morpholino oligomer may be preferable for clinical application. These results suggest that morpholino oligomers may provide greater therapeutic benefit for the treatment of spinocerebellar ataxia type 3, without toxic effects.
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4

Burgess, Darren J. "Targeting huntingtin through morpholino oligomers". Nature Reviews Genetics 15, nr 9 (12.08.2014): 572. http://dx.doi.org/10.1038/nrg3804.

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5

Summerton, James, i Dwight Weller. "Antisense Properties of Morpholino Oligomers". Nucleosides and Nucleotides 16, nr 7-9 (lipiec 1997): 889–98. http://dx.doi.org/10.1080/07328319708006105.

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6

Iversen, Patrick, Katherine Aird, Rebecca Wu, Michael Morse i Gayathri Devi. "Cellular Uptake of Neutral Phosphorodiamidate Morpholino Oligomers". Current Pharmaceutical Biotechnology 10, nr 6 (1.09.2009): 579–88. http://dx.doi.org/10.2174/138920109789069279.

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7

SUMMERTON, JAMES, i DWIGHT WELLER. "Morpholino Antisense Oligomers: Design, Preparation, and Properties". Antisense and Nucleic Acid Drug Development 7, nr 3 (czerwiec 1997): 187–95. http://dx.doi.org/10.1089/oli.1.1997.7.187.

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8

Puckett, Susan E., Kaleb A. Reese, Georgi M. Mitev, Valerie Mullen, Rudd C. Johnson, Kyle R. Pomraning, Brett L. Mellbye i in. "Bacterial Resistance to Antisense Peptide Phosphorodiamidate Morpholino Oligomers". Antimicrobial Agents and Chemotherapy 56, nr 12 (17.09.2012): 6147–53. http://dx.doi.org/10.1128/aac.00850-12.

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ABSTRACTPeptide phosphorodiamidate morpholino oligomers (PPMOs) are synthetic DNA mimics that bind cRNA and inhibit bacterial gene expression. The PPMO (RFF)3RXB-AcpP (where R is arginine, F, phenylalanine, X is 6-aminohexanoic acid, B is β-alanine, and AcpP is acyl carrier protein) is complementary to 11 bases of the essential geneacpP(which encodes acyl carrier protein). The MIC of (RFF)3RXB-AcpP was 2.5 μM (14 μg/ml) inEscherichia coliW3110. The rate of spontaneous resistance ofE. colito (RFF)3RXB-AcpP was 4 × 10−7mutations/cell division. A spontaneous (RFF)3RXB-AcpP-resistant mutant (PR200.1) was isolated. The MIC of (RFF)3RXB-AcpP was 40 μM (224 μg/ml) for PR200.1. The MICs of standard antibiotics for PR200.1 and W3110 were identical. The sequence ofacpPwas identical in PR200.1 and W3110. PR200.1 was also resistant to other PPMOs conjugated to (RFF)3RXB or peptides with a similar composition or pattern of cationic and nonpolar residues. Genomic sequencing of PR200.1 identified a mutation insbmA, which encodes an active transport protein. In separate experiments, a (RFF)3RXB-AcpP-resistant isolate (RR3) was selected from a transposome library, and the insertion was mapped tosbmA. Genetic complementation of PR200.1 or RR3 withsbmArestored susceptibility to (RFF)3RXB-AcpP. Deletion ofsbmAcaused resistance to (RFF)3RXB-AcpP. We conclude that resistance to (RFF)3RXB-AcpP was linked to the peptide and not the phosphorodiamidate morpholino oligomer, dependent on the composition or repeating pattern of amino acids, and caused by mutations insbmA. The data further suggest that (RFF)3R-XB PPMOs may be transported across the plasma membrane by SbmA.
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9

Ham, Kristin A., May Thandar Aung-Htut, Sue Fletcher i Steve D. Wilton. "Nonsequential Splicing Events Alter Antisense-Mediated Exon Skipping Outcome in COL7A1". International Journal of Molecular Sciences 21, nr 20 (18.10.2020): 7705. http://dx.doi.org/10.3390/ijms21207705.

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The COL7A1 gene encodes homotrimer fibrils essential for anchoring dermal and epidermal layers, and pathogenic mutations in COL7A1 can cause recessive or dominant dystrophic epidermolysis bullosa. As a monogenic disease gene, COL7A1 constitutes a potential target for antisense oligomer-mediated exon skipping, a therapy applicable to a growing number of other genetic disorders. However, certain characteristics of COL7A1: many exons, low average intron size, and repetitive and guanine-cytosine rich coding sequence, present challenges to the design of specific and effective antisense oligomers. While targeting COL7A1 exons 10 and 73 for excision from the mature mRNA, we discovered that antisense oligomers comprised of 2′-O-methyl modified bases on a phosphorothioate backbone and phosphorodiamidate morpholino oligomers produced similar, but distinctive, splicing patterns including excision of adjacent nontargeted exons and/or retention of nearby introns in some transcripts. We found that the nonsequential splicing of certain introns may alter pre-mRNA processing during antisense oligomer-mediated exon skipping and, therefore, additional studies are required to determine if the order of intron removal influences multiexon skipping and/or intron retention in processing of the COL7A1 pre-mRNA.
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10

HUDZIAK, ROBERT M., ELISABETH BAROFSKY, DOUGLAS F. BAROFSKY, DOREEN L. WELLER, SUNG-BEN HUANG i DWIGHT D. WELLER. "Resistance of Morpholino Phosphorodiamidate Oligomers to Enzymatic Degradation". Antisense and Nucleic Acid Drug Development 6, nr 4 (styczeń 1996): 267–72. http://dx.doi.org/10.1089/oli.1.1996.6.267.

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11

Ghosh, Chandramallika, i Patrick L. Iversen. "Intracellular Delivery Strategies for Antisense Phosphorodiamidate Morpholino Oligomers". Antisense and Nucleic Acid Drug Development 10, nr 4 (sierpień 2000): 263–74. http://dx.doi.org/10.1089/108729000421448.

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12

AMANTANA, A., i P. IVERSEN. "Pharmacokinetics and biodistribution of phosphorodiamidate morpholino antisense oligomers". Current Opinion in Pharmacology 5, nr 5 (październik 2005): 550–55. http://dx.doi.org/10.1016/j.coph.2005.07.001.

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13

Contini, Alessandro, Emanuela Erba, Valeria Bondavalli, Alberto Barbiroli, Maria Luisa Gelmi i Alessandra Romanelli. "Morpholino-based peptide oligomers: Synthesis and DNA binding properties". Biochemical and Biophysical Research Communications 549 (kwiecień 2021): 8–13. http://dx.doi.org/10.1016/j.bbrc.2021.02.087.

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14

Warren, Travis K., Amy C. Shurtleff i Sina Bavari. "Advanced morpholino oligomers: A novel approach to antiviral therapy". Antiviral Research 94, nr 1 (kwiecień 2012): 80–88. http://dx.doi.org/10.1016/j.antiviral.2012.02.004.

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15

Arora, Vikram, Gayathri Devi i Patrick Iversen. "Neutrally Charged Phosphorodiamidate Morpholino Antisense Oligomers: Uptake, Efficacy and Pharmacokinetics". Current Pharmaceutical Biotechnology 5, nr 5 (1.10.2004): 431–39. http://dx.doi.org/10.2174/1389201043376706.

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16

Neuman, Benjamin W., Lydia H. Bederka, David A. Stein, Joey P. C. Ting, Hong M. Moulton i Michael J. Buchmeier. "Development of Peptide-Conjugated Morpholino Oligomers as Pan-Arenavirus Inhibitors". Antimicrobial Agents and Chemotherapy 55, nr 10 (8.08.2011): 4631–38. http://dx.doi.org/10.1128/aac.00650-11.

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ABSTRACTMembers of theArenaviridaefamily are a threat to public health and can cause meningitis and hemorrhagic fever, and yet treatment options remain limited by a lack of effective antivirals. In this study, we found that peptide-conjugated phosphorodiamidate morpholino oligomers (PPMO) complementary to viral genomic RNA were effective in reducing arenavirus replication in cell cultures andin vivo. PPMO complementary to the Junín virus genome were designed to interfere with viral RNA synthesis or translation or both. However, only PPMO designed to potentially interfere with translation were effective in reducing virus replication. PPMO complementary to sequences that are highly conserved across the arenaviruses and located at the 5′ termini of both genomic segments were effective against Junín virus, Tacaribe virus, Pichinde virus, and lymphocytic choriomeningitis virus (LCMV)-infected cell cultures and suppressed viral titers in the livers of LCMV-infected mice. These results suggest that arenavirus 5′ genomic termini represent promising targets for pan-arenavirus antiviral therapeutic development.
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17

Sun, Xin, Leonard O. Marque, Zachary Cordner, Jennifer L. Pruitt, Manik Bhat, Pan P. Li, Geetha Kannan i in. "Phosphorodiamidate morpholino oligomers suppress mutant huntingtin expression and attenuate neurotoxicity". Human Molecular Genetics 23, nr 23 (4.07.2014): 6302–17. http://dx.doi.org/10.1093/hmg/ddu349.

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18

Liu, Guozheng, Surong Zhang, Jiang He, Zhihong Zhu, Mary Rusckowski i Donald J. Hnatowich. "Improving the Labeling ofS-Acetyl NHS−MAG3-Conjugated Morpholino Oligomers". Bioconjugate Chemistry 13, nr 4 (lipiec 2002): 893–97. http://dx.doi.org/10.1021/bc0255384.

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19

Phumesin, Patta, Mutita Junking, Aussara Panya, Petlada Yongpitakwattana, Sansanee Noisakran, Thawornchai Limjindaporn i Pa-thai Yenchitsomanus. "Vivo-morpholino oligomers strongly inhibit dengue virus replication and production". Archives of Virology 163, nr 4 (19.12.2017): 867–76. http://dx.doi.org/10.1007/s00705-017-3666-9.

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Liu, Guozheng, Jiang He, Surong Zhang, Changbin Liu, Mary Rusckowski i Donald J. Hnatowich. "Cytosine Residues Influence Kidney Accumulations of 99mTc-Labeled Morpholino Oligomers". Antisense and Nucleic Acid Drug Development 12, nr 6 (grudzień 2002): 393–98. http://dx.doi.org/10.1089/108729002321082465.

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21

Moulton, Hong M., Michelle C. Hase, Kristen M. Smith i Patrick L. Iversen. "HIV Tat Peptide Enhances Cellular Delivery of Antisense Morpholino Oligomers". Antisense and Nucleic Acid Drug Development 13, nr 1 (luty 2003): 31–43. http://dx.doi.org/10.1089/108729003764097322.

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Stein, David. "Inhibition of RNA Virus Infections with Peptide-Conjugated Morpholino Oligomers". Current Pharmaceutical Design 14, nr 25 (1.09.2008): 2619–34. http://dx.doi.org/10.2174/138161208786071290.

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Pannier, Angela K., Vikram Arora, Patrick L. Iversen i Rhonda M. Brand. "Transdermal delivery of phosphorodiamidate Morpholino oligomers across hairless mouse skin". International Journal of Pharmaceutics 275, nr 1-2 (maj 2004): 217–26. http://dx.doi.org/10.1016/j.ijpharm.2004.02.001.

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Enterlein, Sven, Kelly L. Warfield, Dana L. Swenson, David A. Stein, Jeffery L. Smith, C. Scott Gamble, Andrew D. Kroeker, Patrick L. Iversen, Sina Bavari i Elke Mühlberger. "VP35 Knockdown Inhibits Ebola Virus Amplification and Protects against Lethal Infection in Mice". Antimicrobial Agents and Chemotherapy 50, nr 3 (marzec 2006): 984–93. http://dx.doi.org/10.1128/aac.50.3.984-993.2006.

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ABSTRACT Phosphorodiamidate morpholino oligomers (PMO) are a class of uncharged single-stranded DNA analogs modified such that each subunit includes a phosphorodiamidate linkage and morpholine ring. PMO antisense agents have been reported to effectively interfere with the replication of several positive-strand RNA viruses in cell culture. The filoviruses, Marburg virus and Ebola virus (EBOV), are negative-strand RNA viruses that cause up to 90% lethality in human outbreaks. There is currently no commercially available vaccine or efficacious therapeutic for any filovirus. In this study, PMO conjugated to arginine-rich cell-penetrating peptide (P-PMO) and nonconjugated PMO were assayed for the ability to inhibit EBOV infection in cell culture and in a mouse model of lethal EBOV infection. A 22-mer P-PMO designed to base pair with the translation start site region of EBOV VP35 positive-sense RNA generated sequence-specific and time- and dose-dependent inhibition of EBOV amplification in cell culture. The same oligomer provided complete protection to mice when administered before or after an otherwise lethal infection of EBOV. A corresponding nonconjugated PMO, as well as nonconjugated truncated versions of 16 and 19 base residues, provided length-dependent protection to mice when administered prophylactically. Together, these data suggest that antisense PMO and P-PMO have the potential to control EBOV infection and are promising therapeutic candidates.
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Greer, Kane, Russell Johnsen, Yoram Nevo, Yakov Fellig, Susan Fletcher i Steve D. Wilton. "Single Exon Skipping Can Address a Multi-Exon Duplication in the Dystrophin Gene". International Journal of Molecular Sciences 21, nr 12 (25.06.2020): 4511. http://dx.doi.org/10.3390/ijms21124511.

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Duchenne muscular dystrophy (DMD) is a severe muscle wasting disease typically caused by protein-truncating mutations that preclude synthesis of a functional dystrophin. Exonic deletions are the most common type of DMD lesion, however, whole exon duplications account for between 10–15% of all reported mutations. Here, we describe in vitro evaluation of antisense oligonucleotide-induced splice switching strategies to re-frame the transcript disrupted by a multi-exon duplication within the DMD gene. Phosphorodiamidate morpholino oligomers and phosphorodiamidate morpholino oligomers coupled to a cell penetrating peptide were evaluated in a Duchenne muscular dystrophy patient cell strain carrying an exon 14–17 duplication. Two strategies were employed; the conventional approach was to remove both copies of exon 17 in addition to exon 18, and the second strategy was to remove only the first copy of exon 17. Both approaches result in a larger than normal but in-frame DMD transcript, but surprisingly, the removal of only the first exon 17 appeared to be more efficient in restoring dystrophin, as determined using western blotting. The emergence of a normal sized DMD mRNA transcript that was not apparent in untreated samples may have arisen from back splicing and could also account for some of the dystrophin protein being produced.
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Wang, Yuan, Li Wu, Peng Wang, Cong Lv, Zhenjun Yang i Xinjing Tang. "Manipulation of gene expression in zebrafish using caged circular morpholino oligomers". Nucleic Acids Research 40, nr 21 (21.09.2012): 11155–62. http://dx.doi.org/10.1093/nar/gks840.

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Greenberg, David E., Kimberly R. Marshall‐Batty, Lauren R. Brinster, Kol A. Zarember, Pamela A. Shaw, Brett L. Mellbye, Patrick L. Iversen, Steven M. Holland i Bruce L. Geller. "Antisense Phosphorodiamidate Morpholino Oligomers Targeted to an Essential Gene InhibitBurkholderia cepaciaComplex". Journal of Infectious Diseases 201, nr 12 (15.06.2010): 1822–30. http://dx.doi.org/10.1086/652807.

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Moulton, Hong M., Michelle H. Nelson, Susie A. Hatlevig, Muralimohan T. Reddy i Patrick L. Iversen. "Cellular Uptake of Antisense Morpholino Oligomers Conjugated to Arginine-Rich Peptides". Bioconjugate Chemistry 15, nr 2 (marzec 2004): 290–99. http://dx.doi.org/10.1021/bc034221g.

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He, Jiang, Guozheng Liu, Shuping Dou, Suresh Gupta, Mary Rusckowski i Donald Hnatowich. "An Improved Method for Covalently Conjugating Morpholino Oligomers to Antitumor Antibodies". Bioconjugate Chemistry 18, nr 3 (maj 2007): 983–88. http://dx.doi.org/10.1021/bc060208v.

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Nan, Yuchen, Zexu Ma, Harilakshmi Kannan, David A. Stein, Patrick I. Iversen, Xiang-Jin Meng i Yan-Jin Zhang. "Inhibition of hepatitis E virus replication by peptide-conjugated morpholino oligomers". Antiviral Research 120 (sierpień 2015): 134–39. http://dx.doi.org/10.1016/j.antiviral.2015.06.006.

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Burrer, Renaud, Benjamin W. Neuman, Joey P. C. Ting, David A. Stein, Hong M. Moulton, Patrick L. Iversen, Peter Kuhn i Michael J. Buchmeier. "Antiviral Effects of Antisense Morpholino Oligomers in Murine Coronavirus Infection Models". Journal of Virology 81, nr 11 (7.03.2007): 5637–48. http://dx.doi.org/10.1128/jvi.02360-06.

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ABSTRACT The recent emergence of novel pathogenic human and animal coronaviruses has highlighted the need for antiviral therapies that are effective against a spectrum of these viruses. We have used several strains of murine hepatitis virus (MHV) in cell culture and in vivo in mouse models to investigate the antiviral characteristics of peptide-conjugated antisense phosphorodiamidate morpholino oligomers (P-PMOs). Ten P-PMOs directed against various target sites in the viral genome were tested in cell culture, and one of these (5TERM), which was complementary to the 5′ terminus of the genomic RNA, was effective against six strains of MHV. Further studies were carried out with various arginine-rich peptides conjugated to the 5TERM PMO sequence in order to evaluate efficacy and toxicity and thereby select candidates for in vivo testing. In uninfected mice, prolonged P-PMO treatment did not result in weight loss or detectable histopathologic changes. 5TERM P-PMO treatment reduced viral titers in target organs and protected mice against virus-induced tissue damage. Prophylactic 5TERM P-PMO treatment decreased the amount of weight loss associated with infection under most experimental conditions. Treatment also prolonged survival in two lethal challenge models. In some cases of high-dose viral inoculation followed by delayed treatment, 5TERM P-PMO treatment was not protective and increased morbidity in the treated group, suggesting that P-PMO may cause toxic effects in diseased mice that were not apparent in the uninfected animals. However, the strong antiviral effect observed suggests that with further development, P-PMO may provide an effective therapeutic approach against a broad range of coronavirus infections.
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Kate, Maresh, Tiet May, Guglieri Michela, Domingos Joana, Straub Volker, Voit Thomas i Muntoni Francesco. "WED 237 Phosphorodiamidate morpholino oligomers for treatment of duchenne muscular dystrophy". Journal of Neurology, Neurosurgery & Psychiatry 89, nr 10 (13.09.2018): A34.2—A34. http://dx.doi.org/10.1136/jnnp-2018-abn.118.

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Exon skipping is a novel, mutation-specific approach to treating patients with Duchenne muscular dystrophy (DMD). Phosphorodiamidate morpholino oligomers are nucleic acid analogues that selectively redirect pre-mRNA splicing to enable production of internally truncated dystrophin.In exon 51 skipping (eteplirsen; n=36) and exon 53 skipping (golodirsen; n=25) clinical studies, internally shortened dystrophin mRNA was observed in all treated patients (per reverse transcription polymerase chain reaction). Eteplirsen increased dystrophin expression 15.5-fold, 11.6-fold, and 2.4-fold vs untreated controls (percent dystrophin-positive fibres, Western blot, and immunohistochemistry intensity, respectively; all, p≤0.007) in a 180 week study, and 2.8-fold (Western blot; p=0.008) in a 48 week study. Golodirsen increased dystrophin expression 10.7-fold (Western blot) over baseline following 48 weeks of treatment. Over 4 years, versus comparable external controls, eteplirsen slowed ambulatory decline (6 min walk test difference, 165 m; p=0.001) and cumulative risk of losing ambulation (83% vs 17%). In 2 clinical studies that included non-ambulatory patients, eteplirsen slowed pulmonary decline versus natural history data (assessed by spirometry).Eteplirsen and golodirsen demonstrated clinical and biochemical effects in patients with DMD; ongoing studies of these compounds are further characterising their effects in various patient populations.
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Geller, Bruce L., i David E. Greenberg. "Peptide-conjugated phosphorodiamidate morpholino oligomers: a new strategy for tackling antibiotic resistance". Therapeutic Delivery 5, nr 3 (marzec 2014): 243–45. http://dx.doi.org/10.4155/tde.13.145.

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KO, YOO-JOUNG, GAYATHRI R. DEVI, CARLA A. LONDON, ANTHONY KAYAS, MURALIMOHAN T. REDDY, PATRICK L. IVERSEN, GLENN J. BUBLEY i STEVEN P. BALK. "ANDROGEN RECEPTOR DOWN-REGULATION IN PROSTATE CANCER WITH PHOSPHORODIAMIDATE MORPHOLINO ANTISENSE OLIGOMERS". Journal of Urology 172, nr 3 (wrzesień 2004): 1140–44. http://dx.doi.org/10.1097/01.ju.0000134698.87862.e6.

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Geller, B. L., J. D. Deere, D. A. Stein, A. D. Kroeker, H. M. Moulton i P. L. Iversen. "Inhibition of Gene Expression in Escherichia coli by Antisense Phosphorodiamidate Morpholino Oligomers". Antimicrobial Agents and Chemotherapy 47, nr 10 (październik 2003): 3233–39. http://dx.doi.org/10.1128/aac.47.10.3233-3239.2003.

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ABSTRACT Antisense phosphorodiamidate morpholino oligomers (PMOs) were tested for the ability to inhibit gene expression in Escherichia coli. PMOs targeted to either a myc-luciferase reporter gene product or 16S rRNA did not inhibit luciferase expression or growth. However, in a strain with defective lipopolysaccharide (lpxA mutant), which has a leaky outer membrane, PMOs targeted to the myc-luciferase or acyl carrier protein (acpP) mRNA significantly inhibited their targets in a dose-dependent response. A significant improvement was made by covalently joining the peptide (KFF)3KC to the end of PMOs. In strains with an intact outer membrane, (KFF)3KC-myc PMO inhibited luciferase expression by 63%. A second (KFF)3KC-PMO conjugate targeted to lacI mRNA induced β-galactosidase in a dose-dependent response. The end of the PMO to which (KFF)3KC is attached affected the efficiency of target inhibition but in various ways depending on the PMO. Another peptide-lacI PMO conjugate was synthesized with the cationic peptide CRRRQRRKKR and was found not to induce β-galactosidase. We conclude that the outer membrane of E. coli inhibits entry of PMOs and that (KFF)3KC-PMO conjugates are transported across both membranes and specifically inhibit expression of their genetic targets.
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36

Tan, Chee Wah, Yoke Fun Chan, Yi Wan Quah i Chit Laa Poh. "Inhibition of enterovirus 71 infection by antisense octaguanidinium dendrimer-conjugated morpholino oligomers". Antiviral Research 107 (lipiec 2014): 35–41. http://dx.doi.org/10.1016/j.antiviral.2014.04.004.

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37

Summerton, James. "Morpholino antisense oligomers: the case for an RNase H-independent structural type". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1489, nr 1 (grudzień 1999): 141–58. http://dx.doi.org/10.1016/s0167-4781(99)00150-5.

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38

Patel, Deendayal, Tanja Opriessnig, David A. Stein, Patrick G. Halbur, Xiang-Jin Meng, Patrick L. Iversen i Yan-Jin Zhang. "Peptide-conjugated morpholino oligomers inhibit porcine reproductive and respiratory syndrome virus replication". Antiviral Research 77, nr 2 (luty 2008): 95–107. http://dx.doi.org/10.1016/j.antiviral.2007.09.002.

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39

Lupfer, Christopher, David A. Stein, Dan V. Mourich, Samuel E. Tepper, Patrick L. Iversen i Manoj Pastey. "Inhibition of influenza A H3N8 virus infections in mice by morpholino oligomers". Archives of Virology 153, nr 5 (28.03.2008): 929–37. http://dx.doi.org/10.1007/s00705-008-0067-0.

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Stein, David A., Douglas E. Skilling, Patrick L. Iversen i Alvin W. Smith. "Inhibition of Vesivirus Infections in Mammalian Tissue Culture with Antisense Morpholino Oligomers". Antisense and Nucleic Acid Drug Development 11, nr 5 (październik 2001): 317–25. http://dx.doi.org/10.1089/108729001753231696.

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41

Warfield, Kelly L., Dana L. Swenson, Gene G. Olinger, Donald K. Nichols, William D. Pratt, Robert Blouch, David A. Stein, M. Javad Aman, Patrick L. Iversen i Sina Bavari. "Gene-Specific Countermeasures against Ebola Virus Based on Antisense Phosphorodiamidate Morpholino Oligomers". PLoS Pathogens 2, nr 1 (13.01.2006): e1. http://dx.doi.org/10.1371/journal.ppat.0020001.

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42

Johnstone, V., H. Viola, A. Adams, S. Wilton, S. Fletcher i L. Hool. "Treatment of mdx Mice with Morpholino Oligomers Improves Metabolic Function and Contractility". Heart, Lung and Circulation 25 (sierpień 2016): S83—S84. http://dx.doi.org/10.1016/j.hlc.2016.06.194.

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43

Crumley, Stacy, Dan Mourich i Patrick Iversen. "A bioanalytical method for detection of phosphorodiamidate morpholino oligomers in cells. (65.44)". Journal of Immunology 186, nr 1_Supplement (1.04.2011): 65.44. http://dx.doi.org/10.4049/jimmunol.186.supp.65.44.

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Abstract Phosphorodiamidate morpholino oligomers (PMOs) are neutrally charged antisense agents that interfere with target gene expression by inhibition of translation or by altering splicing of pre-mRNA. PMOs have been shown to be highly specific and potent therapies after cellular uptake, yet a method to detect PMO inside the cell has not been developed. We offer in this report a novel method for the detection of cellular resident PMO using flow cytometry-fluorescence in situ hybridization (flow FISH) which takes advantage of locked nucleic acid (LNA) oligonucleotides as probes. A biotinylated LNA probe complementary to an Influenza A specific PMO (IA-PMO) was used to specifically detect and quantify intracellular IA-PMO after in vitro or in vivo administration with or without Influenza A infection. While IA-PMO was detected in non-hematopoietic and hematopoietic cells of the lung regardless of influenza virus infection, it was detected at higher levels in influenza infected hematopoietic lung cells as compared to uninfected cells. Coincident measurement of target knock down to intracellular IA-PMO concentration allowed for the calculation of an EC50. Furthermore, it was observed that an increase in IA-PMO uptake occurs in infected hematopoietic cells.
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Carver, Michael P., Jay S. Charleston, Courtney Shanks, Jianbo Zhang, Mark Mense, Alok K. Sharma, Harjeet Kaur i Peter Sazani. "Toxicological Characterization of Exon Skipping Phosphorodiamidate Morpholino Oligomers (PMOs) in Non-human Primates". Journal of Neuromuscular Diseases 3, nr 3 (30.08.2016): 381–93. http://dx.doi.org/10.3233/jnd-160157.

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Oliver, Ryan A., Meghan E. Ahern, Annika B. Malmberg i Kevin J. Kim. "Peptide-conjugated phosphorodiamidate morpholino oligomers for the treatment of late-onset Pompe disease". Molecular Genetics and Metabolism 135, nr 2 (luty 2022): S92. http://dx.doi.org/10.1016/j.ymgme.2021.11.239.

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46

Swenson, Dana L., Kelly L. Warfield, Travis K. Warren, Candace Lovejoy, Jed N. Hassinger, Gordon Ruthel, Robert E. Blouch i in. "Chemical Modifications of Antisense Morpholino Oligomers Enhance Their Efficacy against Ebola Virus Infection". Antimicrobial Agents and Chemotherapy 53, nr 5 (17.02.2009): 2089–99. http://dx.doi.org/10.1128/aac.00936-08.

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ABSTRACT Phosphorodiamidate morpholino oligomers (PMOs) are uncharged nucleic acid-like molecules designed to inactivate the expression of specific genes via the antisense-based steric hindrance of mRNA translation. PMOs have been successful at knocking out viral gene expression and replication in the case of acute viral infections in animal models and have been well tolerated in human clinical trials. We propose that antisense PMOs represent a promising class of therapeutic agents that may be useful for combating filoviral infections. We have previously shown that mice treated with a PMO whose sequence is complementary to a region spanning the start codon of VP24 mRNA were protected against lethal Ebola virus challenge. In the present study, we report on the abilities of two additional VP24-specific PMOs to reduce the cell-free translation of a VP24 reporter, to inhibit the in vitro replication of Ebola virus, and to protect mice against lethal challenge when the PMOs are delivered prior to infection. Additionally, structure-activity relationship evaluations were conducted to assess the enhancement of antiviral efficacy associated with PMO chemical modifications that included conjugation with peptides of various lengths and compositions, positioning of conjugated peptides to either the 5′ or the 3′ terminus, and the conferring of charge modifications by the addition of piperazine moieties. Conjugation with arginine-rich peptides greatly enhanced the antiviral efficacy of VP24-specific PMOs in infected cells and mice during lethal Ebola virus challenge.
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Deiters, Alexander, R. Aaron Garner, Hrvoje Lusic, Jeane M. Govan, Mike Dush, Nanette M. Nascone-Yoder i Jeffrey A. Yoder. "Photocaged Morpholino Oligomers for the Light-Regulation of Gene Function in Zebrafish andXenopusEmbryos". Journal of the American Chemical Society 132, nr 44 (10.11.2010): 15644–50. http://dx.doi.org/10.1021/ja1053863.

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Nazmi, Arshed, Kallol Dutta i Anirban Basu. "Antiviral and Neuroprotective Role of Octaguanidinium Dendrimer-Conjugated Morpholino Oligomers in Japanese Encephalitis". PLoS Neglected Tropical Diseases 4, nr 11 (23.11.2010): e892. http://dx.doi.org/10.1371/journal.pntd.0000892.

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Panchal, Rekha G., Bruce L. Geller, Brett Mellbye, Douglas Lane, Patrick L. Iversen i Sina Bavari. "Peptide Conjugated Phosphorodiamidate Morpholino Oligomers Increase Survival of Mice Challenged with AmesBacillus anthracis". Nucleic Acid Therapeutics 22, nr 5 (październik 2012): 316–22. http://dx.doi.org/10.1089/nat.2012.0362.

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Jearawiriyapaisarn, Natee, Hong M. Moulton, Peter Sazani, Ryszard Kole i Monte S. Willis. "Long-term improvement in mdx cardiomyopathy after therapy with peptide-conjugated morpholino oligomers†". Cardiovascular Research 85, nr 3 (8.10.2009): 444–53. http://dx.doi.org/10.1093/cvr/cvp335.

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