FI105103B - DNA-molekyyli ja sen käyttö - Google Patents

DNA-molekyyli ja sen käyttö Download PDF

Info

Publication number: FI105103B
Authority: FI; Finland
Prior art keywords: dna; rna; trna; ribozyme; gene
Prior art date: 1989-03-16

Application number

FI901296A

Other languages

English (en)

Finnish (fi)

Swedish (sv)

Other versions

FI901296A0 (fi

Inventor

Ernst Wagner

Max L Birnstiel

Hartmut Beug

Matthew Cotten

Harald Kandolf

Original Assignee

Boehringer Ingelheim Int

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1989-03-16

Filing date

1990-03-15

Publication date

2000-06-15

1990-03-15 Application filed by Boehringer Ingelheim Int filed Critical Boehringer Ingelheim Int

1990-03-15 Publication of FI901296A0 publication Critical patent/FI901296A0/fi

2000-06-15 Application granted granted Critical

2000-06-15 Publication of FI105103B publication Critical patent/FI105103B/fi

Links

108020004414 DNA Proteins 0.000 title claims description 63
102000053602 DNA Human genes 0.000 title claims description 22
108091032973 (ribonucleotides)n+m Proteins 0.000 claims abstract description 122
108090000994 Catalytic RNA Proteins 0.000 claims abstract description 116
102000053642 Catalytic RNA Human genes 0.000 claims abstract description 94
108091092562 ribozyme Proteins 0.000 claims abstract description 94
230000002401 inhibitory effect Effects 0.000 claims abstract description 37
238000013518 transcription Methods 0.000 claims abstract description 33
230000035897 transcription Effects 0.000 claims abstract description 33
238000000034 method Methods 0.000 claims abstract description 18
108020005544 Antisense RNA Proteins 0.000 claims abstract 2
108090000623 proteins and genes Proteins 0.000 claims description 99
210000004027 cell Anatomy 0.000 claims description 96
108020004566 Transfer RNA Proteins 0.000 claims description 92
108091028043 Nucleic acid sequence Proteins 0.000 claims description 18
238000000338 in vitro Methods 0.000 claims description 17
108020005098 Anticodon Proteins 0.000 claims description 12
108091034117 Oligonucleotide Proteins 0.000 claims description 12
230000002103 transcriptional effect Effects 0.000 claims description 8
238000004519 manufacturing process Methods 0.000 claims description 5
238000012546 transfer Methods 0.000 claims description 5
230000010261 cell growth Effects 0.000 claims description 4
239000002243 precursor Substances 0.000 claims description 4
241000251131 Sphyrna Species 0.000 claims description 3
230000024245 cell differentiation Effects 0.000 claims description 3
239000003184 complementary RNA Substances 0.000 claims description 3
230000009261 transgenic effect Effects 0.000 claims description 3
108020000999 Viral RNA Proteins 0.000 claims description 2
125000002091 cationic group Chemical group 0.000 claims description 2
230000000977 initiatory effect Effects 0.000 claims description 2
230000010837 receptor-mediated endocytosis Effects 0.000 claims description 2
108700020796 Oncogene Proteins 0.000 claims 1
210000003527 eukaryotic cell Anatomy 0.000 claims 1
230000001404 mediated effect Effects 0.000 claims 1
230000000694 effects Effects 0.000 abstract description 30
230000002068 genetic effect Effects 0.000 abstract description 22
230000005764 inhibitory process Effects 0.000 abstract description 10
230000008569 process Effects 0.000 abstract description 3
239000008194 pharmaceutical composition Substances 0.000 abstract 1
239000012581 transferrin Substances 0.000 description 31
102000004338 Transferrin Human genes 0.000 description 27
108090000901 Transferrin Proteins 0.000 description 27
238000003776 cleavage reaction Methods 0.000 description 26
239000013612 plasmid Substances 0.000 description 26
230000007017 scission Effects 0.000 description 26
210000004681 ovum Anatomy 0.000 description 22
239000002773 nucleotide Substances 0.000 description 20
125000003729 nucleotide group Chemical group 0.000 description 20
239000012634 fragment Substances 0.000 description 19
239000000203 mixture Substances 0.000 description 19
239000000243 solution Substances 0.000 description 19
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 18
108020004999 messenger RNA Proteins 0.000 description 18
229920000656 polylysine Polymers 0.000 description 18
238000002474 experimental method Methods 0.000 description 17
239000000047 product Substances 0.000 description 17
239000000499 gel Substances 0.000 description 15
241000287828 Gallus gallus Species 0.000 description 13
HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 12
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 12
ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 12
210000003743 erythrocyte Anatomy 0.000 description 12
238000011534 incubation Methods 0.000 description 12
239000013598 vector Substances 0.000 description 12
206010028980 Neoplasm Diseases 0.000 description 11
102000039446 nucleic acids Human genes 0.000 description 11
108020004707 nucleic acids Proteins 0.000 description 11
150000007523 nucleic acids Chemical class 0.000 description 11
XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 10
102000004169 proteins and genes Human genes 0.000 description 10
239000000523 sample Substances 0.000 description 10
DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 9
239000011780 sodium chloride Substances 0.000 description 9
XKRFYHLGVUSROY-UHFFFAOYSA-N Argon Chemical compound [Ar] XKRFYHLGVUSROY-UHFFFAOYSA-N 0.000 description 8
108010039918 Polylysine Proteins 0.000 description 8
238000010367 cloning Methods 0.000 description 8
238000012986 modification Methods 0.000 description 8
230000004048 modification Effects 0.000 description 8
KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 7
101000934338 Homo sapiens Myeloid cell surface antigen CD33 Proteins 0.000 description 7
102100025243 Myeloid cell surface antigen CD33 Human genes 0.000 description 7
241000269370 Xenopus <genus> Species 0.000 description 7
JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 7
238000003556 assay Methods 0.000 description 7
230000015572 biosynthetic process Effects 0.000 description 7
MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 7
238000001727 in vivo Methods 0.000 description 7
239000002609 medium Substances 0.000 description 7
239000000758 substrate Substances 0.000 description 7
230000032258 transport Effects 0.000 description 7
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 7
HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 6
241000588724 Escherichia coli Species 0.000 description 6
ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 6
XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 6
241000700605 Viruses Species 0.000 description 6
239000000872 buffer Substances 0.000 description 6
239000004202 carbamide Substances 0.000 description 6
230000004069 differentiation Effects 0.000 description 6
230000037431 insertion Effects 0.000 description 6
239000002244 precipitate Substances 0.000 description 6
230000002829 reductive effect Effects 0.000 description 6
238000010186 staining Methods 0.000 description 6
238000003786 synthesis reaction Methods 0.000 description 6
102000001554 Hemoglobins Human genes 0.000 description 5
108010054147 Hemoglobins Proteins 0.000 description 5
101000917826 Homo sapiens Low affinity immunoglobulin gamma Fc region receptor II-a Proteins 0.000 description 5
101000917824 Homo sapiens Low affinity immunoglobulin gamma Fc region receptor II-b Proteins 0.000 description 5
108091092195 Intron Proteins 0.000 description 5
102100029204 Low affinity immunoglobulin gamma Fc region receptor II-a Human genes 0.000 description 5
230000001580 bacterial effect Effects 0.000 description 5
HFACYLZERDEVSX-UHFFFAOYSA-N benzidine Chemical compound C1=CC(N)=CC=C1C1=CC=C(N)C=C1 HFACYLZERDEVSX-UHFFFAOYSA-N 0.000 description 5
238000006243 chemical reaction Methods 0.000 description 5
238000010276 construction Methods 0.000 description 5
238000003780 insertion Methods 0.000 description 5
238000002360 preparation method Methods 0.000 description 5
238000012545 processing Methods 0.000 description 5
238000010561 standard procedure Methods 0.000 description 5
238000012360 testing method Methods 0.000 description 5
241001430294 unidentified retrovirus Species 0.000 description 5
CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 4
108091026890 Coding region Proteins 0.000 description 4
TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 4
239000007983 Tris buffer Substances 0.000 description 4
229910052786 argon Inorganic materials 0.000 description 4
230000029087 digestion Effects 0.000 description 4
238000001502 gel electrophoresis Methods 0.000 description 4
239000003112 inhibitor Substances 0.000 description 4
210000000287 oocyte Anatomy 0.000 description 4
108091008146 restriction endonucleases Proteins 0.000 description 4
239000007974 sodium acetate buffer Substances 0.000 description 4
239000012064 sodium phosphate buffer Substances 0.000 description 4
241000894007 species Species 0.000 description 4
210000001519 tissue Anatomy 0.000 description 4
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 4
QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 3
102000001301 EGF receptor Human genes 0.000 description 3
108060006698 EGF receptor Proteins 0.000 description 3
241000196324 Embryophyta Species 0.000 description 3
108010067770 Endopeptidase K Proteins 0.000 description 3
108090000790 Enzymes Proteins 0.000 description 3
WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 3
FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 3
108010065868 RNA polymerase SP6 Proteins 0.000 description 3
230000007022 RNA scission Effects 0.000 description 3
241000269368 Xenopus laevis Species 0.000 description 3
230000008901 benefit Effects 0.000 description 3
230000001413 cellular effect Effects 0.000 description 3
230000006378 damage Effects 0.000 description 3
238000012869 ethanol precipitation Methods 0.000 description 3
208000015181 infectious disease Diseases 0.000 description 3
238000002347 injection Methods 0.000 description 3
239000007924 injection Substances 0.000 description 3
230000003834 intracellular effect Effects 0.000 description 3
229910052742 iron Inorganic materials 0.000 description 3
230000007246 mechanism Effects 0.000 description 3
229930182817 methionine Natural products 0.000 description 3
238000000520 microinjection Methods 0.000 description 3
239000007858 starting material Substances 0.000 description 3
238000003756 stirring Methods 0.000 description 3
-1 succinimidyl pyridyl Chemical group 0.000 description 3
239000006228 supernatant Substances 0.000 description 3
108091029536 tRNA precursor Proteins 0.000 description 3
108700008272 transferrin-polylysine conjugate Proteins 0.000 description 3
230000001131 transforming effect Effects 0.000 description 3
238000011144 upstream manufacturing Methods 0.000 description 3
230000003612 virological effect Effects 0.000 description 3
JWDFQMWEFLOOED-UHFFFAOYSA-N (2,5-dioxopyrrolidin-1-yl) 3-(pyridin-2-yldisulfanyl)propanoate Chemical compound O=C1CCC(=O)N1OC(=O)CCSSC1=CC=CC=N1 JWDFQMWEFLOOED-UHFFFAOYSA-N 0.000 description 2
102000040650 (ribonucleotides)n+m Human genes 0.000 description 2
JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 2
KIUMMUBSPKGMOY-UHFFFAOYSA-N 3,3'-Dithiobis(6-nitrobenzoic acid) Chemical compound C1=C([N+]([O-])=O)C(C(=O)O)=CC(SSC=2C=C(C(=CC=2)[N+]([O-])=O)C(O)=O)=C1 KIUMMUBSPKGMOY-UHFFFAOYSA-N 0.000 description 2
108020005029 5' Flanking Region Proteins 0.000 description 2
229920000936 Agarose Polymers 0.000 description 2
108020004394 Complementary RNA Proteins 0.000 description 2
102000016928 DNA-directed DNA polymerase Human genes 0.000 description 2
108010014303 DNA-directed DNA polymerase Proteins 0.000 description 2
108010000912 Egg Proteins Proteins 0.000 description 2
102000002322 Egg Proteins Human genes 0.000 description 2
102000004190 Enzymes Human genes 0.000 description 2
102000003951 Erythropoietin Human genes 0.000 description 2
108090000394 Erythropoietin Proteins 0.000 description 2
108060002716 Exonuclease Proteins 0.000 description 2
239000007995 HEPES buffer Substances 0.000 description 2
101150098499 III gene Proteins 0.000 description 2
102000003960 Ligases Human genes 0.000 description 2
108090000364 Ligases Proteins 0.000 description 2
241001465754 Metazoa Species 0.000 description 2
108010083644 Ribonucleases Proteins 0.000 description 2
102000006382 Ribonucleases Human genes 0.000 description 2
238000012300 Sequence Analysis Methods 0.000 description 2
102000004598 Small Nuclear Ribonucleoproteins Human genes 0.000 description 2
108010003165 Small Nuclear Ribonucleoproteins Proteins 0.000 description 2
UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 2
108091081024 Start codon Proteins 0.000 description 2
108700005078 Synthetic Genes Proteins 0.000 description 2
101710137500 T7 RNA polymerase Proteins 0.000 description 2
108010033576 Transferrin Receptors Proteins 0.000 description 2
239000007984 Tris EDTA buffer Substances 0.000 description 2
241000726445 Viroids Species 0.000 description 2
230000004913 activation Effects 0.000 description 2
230000002411 adverse Effects 0.000 description 2
230000004888 barrier function Effects 0.000 description 2
230000000903 blocking effect Effects 0.000 description 2
239000001569 carbon dioxide Substances 0.000 description 2
229910002092 carbon dioxide Inorganic materials 0.000 description 2
230000015556 catabolic process Effects 0.000 description 2
230000011748 cell maturation Effects 0.000 description 2
HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 2
238000000975 co-precipitation Methods 0.000 description 2
238000006731 degradation reaction Methods 0.000 description 2
230000001419 dependent effect Effects 0.000 description 2
208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 2
229940105423 erythropoietin Drugs 0.000 description 2
102000013165 exonuclease Human genes 0.000 description 2
238000000605 extraction Methods 0.000 description 2
238000003682 fluorination reaction Methods 0.000 description 2
239000012737 fresh medium Substances 0.000 description 2
239000007789 gas Substances 0.000 description 2
239000001963 growth medium Substances 0.000 description 2
NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
230000010354 integration Effects 0.000 description 2
230000002427 irreversible effect Effects 0.000 description 2
230000000670 limiting effect Effects 0.000 description 2
229910001629 magnesium chloride Inorganic materials 0.000 description 2
239000003550 marker Substances 0.000 description 2
238000005259 measurement Methods 0.000 description 2
210000004400 mucous membrane Anatomy 0.000 description 2
FEMOMIGRRWSMCU-UHFFFAOYSA-N ninhydrin Chemical compound C1=CC=C2C(=O)C(O)(O)C(=O)C2=C1 FEMOMIGRRWSMCU-UHFFFAOYSA-N 0.000 description 2
239000002245 particle Substances 0.000 description 2
239000008188 pellet Substances 0.000 description 2
229920002401 polyacrylamide Polymers 0.000 description 2
OXCMYAYHXIHQOA-UHFFFAOYSA-N potassium;[2-butyl-5-chloro-3-[[4-[2-(1,2,4-triaza-3-azanidacyclopenta-1,4-dien-5-yl)phenyl]phenyl]methyl]imidazol-4-yl]methanol Chemical compound [K+].CCCCC1=NC(Cl)=C(CO)N1CC1=CC=C(C=2C(=CC=CC=2)C2=N[N-]N=N2)C=C1 OXCMYAYHXIHQOA-UHFFFAOYSA-N 0.000 description 2
108090000765 processed proteins & peptides Proteins 0.000 description 2
FFISLTWEISOMFC-UHFFFAOYSA-N pyridin-2-yl propanedithioate Chemical compound CCC(=S)SC1=CC=CC=N1 FFISLTWEISOMFC-UHFFFAOYSA-N 0.000 description 2
230000002441 reversible effect Effects 0.000 description 2
238000000926 separation method Methods 0.000 description 2
125000003396 thiol group Chemical group [H]S* 0.000 description 2
230000005030 transcription termination Effects 0.000 description 2
238000013519 translation Methods 0.000 description 2
LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 2
210000004881 tumor cell Anatomy 0.000 description 2
DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
IQFYYKKMVGJFEH-OFKYTIFKSA-N 1-[(2r,4s,5r)-4-hydroxy-5-(tritiooxymethyl)oxolan-2-yl]-5-methylpyrimidine-2,4-dione Chemical compound C1[C@H](O)[C@@H](CO[3H])O[C@H]1N1C(=O)NC(=O)C(C)=C1 IQFYYKKMVGJFEH-OFKYTIFKSA-N 0.000 description 1
IHPYMWDTONKSCO-UHFFFAOYSA-N 2,2'-piperazine-1,4-diylbisethanesulfonic acid Chemical compound OS(=O)(=O)CCN1CCN(CCS(O)(=O)=O)CC1 IHPYMWDTONKSCO-UHFFFAOYSA-N 0.000 description 1
LDGWQMRUWMSZIU-LQDDAWAPSA-M 2,3-bis[(z)-octadec-9-enoxy]propyl-trimethylazanium;chloride Chemical compound [Cl-].CCCCCCCC\C=C/CCCCCCCCOCC(C[N+](C)(C)C)OCCCCCCCC\C=C/CCCCCCCC LDGWQMRUWMSZIU-LQDDAWAPSA-M 0.000 description 1
OSBLTNPMIGYQGY-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;2-[2-[bis(carboxymethyl)amino]ethyl-(carboxymethyl)amino]acetic acid;boric acid Chemical compound OB(O)O.OCC(N)(CO)CO.OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O OSBLTNPMIGYQGY-UHFFFAOYSA-N 0.000 description 1
108020005065 3' Flanking Region Proteins 0.000 description 1
208000024827 Alzheimer disease Diseases 0.000 description 1
USFZMSVCRYTOJT-UHFFFAOYSA-N Ammonium acetate Chemical compound N.CC(O)=O USFZMSVCRYTOJT-UHFFFAOYSA-N 0.000 description 1
239000005695 Ammonium acetate Substances 0.000 description 1
241001244729 Apalis Species 0.000 description 1
208000023275 Autoimmune disease Diseases 0.000 description 1
241000271566 Aves Species 0.000 description 1
241000711404 Avian avulavirus 1 Species 0.000 description 1
241000894006 Bacteria Species 0.000 description 1
BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
108091003079 Bovine Serum Albumin Proteins 0.000 description 1
241000701822 Bovine papillomavirus Species 0.000 description 1
102000011022 Chorionic Gonadotropin Human genes 0.000 description 1
108010062540 Chorionic Gonadotropin Proteins 0.000 description 1
KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
108020004705 Codon Proteins 0.000 description 1
108010026206 Conalbumin Proteins 0.000 description 1
102000008130 Cyclic AMP-Dependent Protein Kinases Human genes 0.000 description 1
108010049894 Cyclic AMP-Dependent Protein Kinases Proteins 0.000 description 1
102000004594 DNA Polymerase I Human genes 0.000 description 1
108010017826 DNA Polymerase I Proteins 0.000 description 1
238000001712 DNA sequencing Methods 0.000 description 1
229920002307 Dextran Polymers 0.000 description 1
BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
108020004437 Endogenous Retroviruses Proteins 0.000 description 1
IMROMDMJAWUWLK-UHFFFAOYSA-N Ethenol Chemical compound OC=C IMROMDMJAWUWLK-UHFFFAOYSA-N 0.000 description 1
101150066718 FMOD gene Proteins 0.000 description 1
PXGOKWXKJXAPGV-UHFFFAOYSA-N Fluorine Chemical compound FF PXGOKWXKJXAPGV-UHFFFAOYSA-N 0.000 description 1
241000710198 Foot-and-mouth disease virus Species 0.000 description 1
SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
241000724709 Hepatitis delta virus Species 0.000 description 1
108010033040 Histones Proteins 0.000 description 1
206010061218 Inflammation Diseases 0.000 description 1
102000004877 Insulin Human genes 0.000 description 1
108090001061 Insulin Proteins 0.000 description 1
102100034343 Integrase Human genes 0.000 description 1
101710203526 Integrase Proteins 0.000 description 1
OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
241001529936 Murinae Species 0.000 description 1
244000061176 Nicotiana tabacum Species 0.000 description 1
235000002637 Nicotiana tabacum Nutrition 0.000 description 1
108010074118 Oncogene Proteins v-erbB Proteins 0.000 description 1
241000283973 Oryctolagus cuniculus Species 0.000 description 1
239000007990 PIPES buffer Substances 0.000 description 1
108020002230 Pancreatic Ribonuclease Proteins 0.000 description 1
102000005891 Pancreatic ribonuclease Human genes 0.000 description 1
241001631646 Papillomaviridae Species 0.000 description 1
239000005662 Paraffin oil Substances 0.000 description 1
108010029485 Protein Isoforms Proteins 0.000 description 1
102000001708 Protein Isoforms Human genes 0.000 description 1
239000013614 RNA sample Substances 0.000 description 1
108090000621 Ribonuclease P Proteins 0.000 description 1
102000004167 Ribonuclease P Human genes 0.000 description 1
108010046983 Ribonuclease T1 Proteins 0.000 description 1
108020005543 Satellite RNA Proteins 0.000 description 1
229920005654 Sephadex Polymers 0.000 description 1
239000012507 Sephadex™ Substances 0.000 description 1
102000039471 Small Nuclear RNA Human genes 0.000 description 1
108020004688 Small Nuclear RNA Proteins 0.000 description 1
244000061456 Solanum tuberosum Species 0.000 description 1
235000002595 Solanum tuberosum Nutrition 0.000 description 1
239000008051 TBE buffer Substances 0.000 description 1
IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 1
108700009124 Transcription Initiation Site Proteins 0.000 description 1
108091023040 Transcription factor Proteins 0.000 description 1
102000040945 Transcription factor Human genes 0.000 description 1
102000007238 Transferrin Receptors Human genes 0.000 description 1
102100026144 Transferrin receptor protein 1 Human genes 0.000 description 1
108091026823 U7 small nuclear RNA Proteins 0.000 description 1
241001672648 Vieira Species 0.000 description 1
108700005077 Viral Genes Proteins 0.000 description 1
238000010521 absorption reaction Methods 0.000 description 1
238000009825 accumulation Methods 0.000 description 1
239000002253 acid Substances 0.000 description 1
NIXOWILDQLNWCW-UHFFFAOYSA-N acrylic acid group Chemical group C(C=C)(=O)O NIXOWILDQLNWCW-UHFFFAOYSA-N 0.000 description 1
239000004480 active ingredient Substances 0.000 description 1
239000011543 agarose gel Substances 0.000 description 1
125000000266 alpha-aminoacyl group Chemical group 0.000 description 1
230000004075 alteration Effects 0.000 description 1
150000001408 amides Chemical class 0.000 description 1
229940043376 ammonium acetate Drugs 0.000 description 1
235000019257 ammonium acetate Nutrition 0.000 description 1
AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
229960000723 ampicillin Drugs 0.000 description 1
210000003423 ankle Anatomy 0.000 description 1
230000000840 anti-viral effect Effects 0.000 description 1
239000000427 antigen Substances 0.000 description 1
108091007433 antigens Proteins 0.000 description 1
102000036639 antigens Human genes 0.000 description 1
238000013475 authorization Methods 0.000 description 1
230000004071 biological effect Effects 0.000 description 1
230000031018 biological processes and functions Effects 0.000 description 1
230000033228 biological regulation Effects 0.000 description 1
210000000601 blood cell Anatomy 0.000 description 1
229940098773 bovine serum albumin Drugs 0.000 description 1
238000004364 calculation method Methods 0.000 description 1
230000030833 cell death Effects 0.000 description 1
210000000170 cell membrane Anatomy 0.000 description 1
239000006285 cell suspension Substances 0.000 description 1
230000004700 cellular uptake Effects 0.000 description 1
239000002801 charged material Substances 0.000 description 1
239000007795 chemical reaction product Substances 0.000 description 1
239000003153 chemical reaction reagent Substances 0.000 description 1
235000012000 cholesterol Nutrition 0.000 description 1
208000030499 combat disease Diseases 0.000 description 1
230000000295 complement effect Effects 0.000 description 1
230000021615 conjugation Effects 0.000 description 1
108091036078 conserved sequence Proteins 0.000 description 1
239000000470 constituent Substances 0.000 description 1
238000007796 conventional method Methods 0.000 description 1
230000008878 coupling Effects 0.000 description 1
238000010168 coupling process Methods 0.000 description 1
238000005859 coupling reaction Methods 0.000 description 1
210000000805 cytoplasm Anatomy 0.000 description 1
238000004925 denaturation Methods 0.000 description 1
230000036425 denaturation Effects 0.000 description 1
238000001514 detection method Methods 0.000 description 1
238000011161 development Methods 0.000 description 1
230000018109 developmental process Effects 0.000 description 1
238000009792 diffusion process Methods 0.000 description 1
LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
201000010099 disease Diseases 0.000 description 1
230000005684 electric field Effects 0.000 description 1
238000001962 electrophoresis Methods 0.000 description 1
238000004520 electroporation Methods 0.000 description 1
239000003480 eluent Substances 0.000 description 1
238000010828 elution Methods 0.000 description 1
238000001976 enzyme digestion Methods 0.000 description 1
230000007457 establishment of nucleus localization Effects 0.000 description 1
ZMMJGEGLRURXTF-UHFFFAOYSA-N ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 0.000 description 1
229960005542 ethidium bromide Drugs 0.000 description 1
230000005284 excitation Effects 0.000 description 1
239000000284 extract Substances 0.000 description 1
239000011536 extraction buffer Substances 0.000 description 1
238000000799 fluorescence microscopy Methods 0.000 description 1
239000011737 fluorine Substances 0.000 description 1
229910052731 fluorine Inorganic materials 0.000 description 1
230000002496 gastric effect Effects 0.000 description 1
238000002523 gelfiltration Methods 0.000 description 1
238000001415 gene therapy Methods 0.000 description 1
102000034356 gene-regulatory proteins Human genes 0.000 description 1
108091006104 gene-regulatory proteins Proteins 0.000 description 1
230000012010 growth Effects 0.000 description 1
238000010438 heat treatment Methods 0.000 description 1
230000001744 histochemical effect Effects 0.000 description 1
230000006872 improvement Effects 0.000 description 1
238000010348 incorporation Methods 0.000 description 1
230000006698 induction Effects 0.000 description 1
230000002458 infectious effect Effects 0.000 description 1
230000004054 inflammatory process Effects 0.000 description 1
229940125396 insulin Drugs 0.000 description 1
230000000968 intestinal effect Effects 0.000 description 1
238000004255 ion exchange chromatography Methods 0.000 description 1
150000004698 iron complex Chemical class 0.000 description 1
229940043355 kinase inhibitor Drugs 0.000 description 1
208000032839 leukemia Diseases 0.000 description 1
239000002502 liposome Substances 0.000 description 1
UEGPKNKPLBYCNK-UHFFFAOYSA-L magnesium acetate Chemical compound [Mg+2].CC([O-])=O.CC([O-])=O UEGPKNKPLBYCNK-UHFFFAOYSA-L 0.000 description 1
235000011285 magnesium acetate Nutrition 0.000 description 1
239000011654 magnesium acetate Substances 0.000 description 1
229940069446 magnesium acetate Drugs 0.000 description 1
210000001161 mammalian embryo Anatomy 0.000 description 1
230000035800 maturation Effects 0.000 description 1
210000004379 membrane Anatomy 0.000 description 1
239000012528 membrane Substances 0.000 description 1
238000013508 migration Methods 0.000 description 1
230000005012 migration Effects 0.000 description 1
238000012544 monitoring process Methods 0.000 description 1
210000004877 mucosa Anatomy 0.000 description 1
230000007935 neutral effect Effects 0.000 description 1
108091027963 non-coding RNA Proteins 0.000 description 1
102000042567 non-coding RNA Human genes 0.000 description 1
231100000252 nontoxic Toxicity 0.000 description 1
230000003000 nontoxic effect Effects 0.000 description 1
229940124276 oligodeoxyribonucleotide Drugs 0.000 description 1
230000008520 organization Effects 0.000 description 1
239000000825 pharmaceutical preparation Substances 0.000 description 1
239000002953 phosphate buffered saline Substances 0.000 description 1
238000005375 photometry Methods 0.000 description 1
229920000729 poly(L-lysine) polymer Polymers 0.000 description 1
229920000642 polymer Polymers 0.000 description 1
238000003752 polymerase chain reaction Methods 0.000 description 1
238000006116 polymerization reaction Methods 0.000 description 1
229920002451 polyvinyl alcohol Polymers 0.000 description 1
239000011148 porous material Substances 0.000 description 1
229910000160 potassium phosphate Inorganic materials 0.000 description 1
235000011009 potassium phosphates Nutrition 0.000 description 1
230000003389 potentiating effect Effects 0.000 description 1
238000002203 pretreatment Methods 0.000 description 1
102000004196 processed proteins & peptides Human genes 0.000 description 1
230000000644 propagated effect Effects 0.000 description 1
239000003909 protein kinase inhibitor Substances 0.000 description 1
208000009305 pseudorabies Diseases 0.000 description 1
WHMDPDGBKYUEMW-UHFFFAOYSA-N pyridine-2-thiol Chemical compound SC1=CC=CC=N1 WHMDPDGBKYUEMW-UHFFFAOYSA-N 0.000 description 1
239000011541 reaction mixture Substances 0.000 description 1
238000011084 recovery Methods 0.000 description 1
238000004064 recycling Methods 0.000 description 1
230000001105 regulatory effect Effects 0.000 description 1
230000010076 replication Effects 0.000 description 1
239000011347 resin Substances 0.000 description 1
229920005989 resin Polymers 0.000 description 1
230000000717 retained effect Effects 0.000 description 1
210000001995 reticulocyte Anatomy 0.000 description 1
230000001177 retroviral effect Effects 0.000 description 1
210000003705 ribosome Anatomy 0.000 description 1
229920006395 saturated elastomer Polymers 0.000 description 1
238000012216 screening Methods 0.000 description 1
230000035945 sensitivity Effects 0.000 description 1
235000017557 sodium bicarbonate Nutrition 0.000 description 1
229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
210000001082 somatic cell Anatomy 0.000 description 1
230000006641 stabilisation Effects 0.000 description 1
238000011105 stabilization Methods 0.000 description 1
239000008223 sterile water Substances 0.000 description 1
230000008685 targeting Effects 0.000 description 1
238000010998 test method Methods 0.000 description 1
JGVWCANSWKRBCS-UHFFFAOYSA-N tetramethylrhodamine thiocyanate Chemical compound [Cl-].C=12C=CC(N(C)C)=CC2=[O+]C2=CC(N(C)C)=CC=C2C=1C1=CC=C(SC#N)C=C1C(O)=O JGVWCANSWKRBCS-UHFFFAOYSA-N 0.000 description 1
230000001225 therapeutic effect Effects 0.000 description 1
230000009772 tissue formation Effects 0.000 description 1
231100000331 toxic Toxicity 0.000 description 1
230000002588 toxic effect Effects 0.000 description 1
239000003053 toxin Substances 0.000 description 1
231100000765 toxin Toxicity 0.000 description 1
108700012359 toxins Proteins 0.000 description 1
230000005026 transcription initiation Effects 0.000 description 1
238000001890 transfection Methods 0.000 description 1
230000007723 transport mechanism Effects 0.000 description 1
230000001960 triggered effect Effects 0.000 description 1
OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
239000013603 viral vector Substances 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/113—Non-coding nucleic acids modulating the expression of genes, e.g. antisense oligonucleotides; Antisense DNA or RNA; Triplex- forming oligonucleotides; Catalytic nucleic acids, e.g. ribozymes; Nucleic acids used in co-suppression or gene silencing
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2310/00—Structure or type of the nucleic acid
- C12N2310/10—Type of nucleic acid
- C12N2310/11—Antisense
- C12N2310/111—Antisense spanning the whole gene, or a large part of it
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2310/00—Structure or type of the nucleic acid
- C12N2310/10—Type of nucleic acid
- C12N2310/12—Type of nucleic acid catalytic nucleic acids, e.g. ribozymes
- C12N2310/121—Hammerhead

Landscapes

Genetics & Genomics (AREA)
Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Engineering & Computer Science (AREA)
Biomedical Technology (AREA)
Organic Chemistry (AREA)
Wood Science & Technology (AREA)
General Engineering & Computer Science (AREA)
Biotechnology (AREA)
Chemical & Material Sciences (AREA)
Bioinformatics & Cheminformatics (AREA)
Zoology (AREA)
Molecular Biology (AREA)
Biochemistry (AREA)
Microbiology (AREA)
Plant Pathology (AREA)
Biophysics (AREA)
General Health & Medical Sciences (AREA)
Physics & Mathematics (AREA)
Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Saccharide Compounds (AREA)
Nitrogen Condensed Heterocyclic Rings (AREA)
Enzymes And Modification Thereof (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Medicines Containing Material From Animals Or Micro-Organisms (AREA)

FI901296A 1989-03-16 1990-03-15 DNA-molekyyli ja sen käyttö FI105103B (fi)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
AT60989		1989-03-16
AT60989		1989-03-16

Publications (2)

Publication Number	Publication Date
FI901296A0 FI901296A0 (fi)	1990-03-15
FI105103B true FI105103B (fi)	2000-06-15

Family

ID=3495118

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
FI901296A FI105103B (fi)	1989-03-16	1990-03-15	DNA-molekyyli ja sen käyttö

Country Status (20)

Country	Link
EP (1)	EP0387775B1 (he)
JP (1)	JP3330930B2 (he)
KR (1)	KR900014591A (he)
AT (1)	ATE140961T1 (he)
AU (1)	AU637354B2 (he)
CA (1)	CA2012312C (he)
DD (1)	DD297838A5 (he)
DE (1)	DE59010432D1 (he)
DK (1)	DK0387775T3 (he)
ES (1)	ES2090049T3 (he)
FI (1)	FI105103B (he)
GR (1)	GR3020935T3 (he)
HU (2)	HU215187B (he)
IE (1)	IE74850B1 (he)
IL (1)	IL93754A (he)
NO (1)	NO306623B1 (he)
NZ (1)	NZ232917A (he)
PT (1)	PT93440B (he)
RU (1)	RU2136751C1 (he)
ZA (1)	ZA901973B (he)

Families Citing this family (34)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
EP0471796A4 (en) *	1989-05-10	1993-05-05	Sloan Kettering Institute For Cancer Research	Stably transformed eucaryotic cells comprising a foreign transcribable dna under the control of a pol iii promoter
DE4091533T (he) *	1989-08-31	1992-01-30
JP2507895B2 (ja) *	1989-12-19	1996-06-19	工業技術院長	リボザイムの新規合成系
ATE150789T1 (de) *	1990-06-19	1997-04-15	Gene Shears Pty Ltd	Endonukleasen
US6008343A (en) *	1990-06-19	1999-12-28	Gene Shears Pty. Ltd.	Nucleotide based endonucleases
WO1992007065A1 (en)	1990-10-12	1992-04-30	MAX-PLANCK-Gesellschaft zur Förderung der Wissenschaften e.V.	Modified ribozymes
DE4104186A1 (de) *	1991-02-12	1992-08-13	Genentech Inc	Neue, ueber endozytose in hoehere eukaryotische zellen aufnehmbare, nukleinsaeure enthaltende komplexe
FR2687411A1 (fr) *	1992-02-13	1993-08-20	Nice Sophia Antipolis Universi	Vecteur comportant un gene viral transcrit par l'arn polymerase iii, et procede de production intracellulaire d'arn.
AU4259193A (en) *	1992-04-28	1993-11-29	Frank Andreas Harald Meyer	Medicament for the gene-therapeutic treatment of human beings, animals and plants, especially to block virus multiplication and carcinogenes and process for producing the medicament
EP0641212A4 (en) *	1992-05-14	1997-05-21	Ribozyme Pharm Inc	PROCESS AND REAGENT FOR PREVENTING THE DEVELOPMENT OF CANCER.
US5989906A (en) *	1992-05-14	1999-11-23	Ribozyme Pharmaceuticals, Inc.	Method and reagent for inhibiting P-glycoprotein (mdr-1-gene)
US5610052A (en) *	1992-08-26	1997-03-11	Ribozyme Pharmaceuticals Inc.	Enzymatic RNA with activity to ras
US5827935A (en) *	1992-05-27	1998-10-27	City Of Hope	Chimeric tRNAlys -ribozyme molecules
CA2114312A1 (en) *	1992-05-27	1993-12-09	John J. Rossi	Chimeric trnalys-ribozyme molecules
ATE312510T1 (de) *	1992-06-29	2005-12-15	Gene Shears Pty Ltd	Nukleinsäuren und sie verwendende verfahren zur bekämpfung viraler pathogene
WO1994013798A1 (en) *	1992-12-16	1994-06-23	Bergmann Johanna E	Agents for the prevention and treatment of human alzheimer's disease
EP0647716B1 (fr) *	1993-07-06	2003-09-24	Universite De Nice-Sophia Antipolis	Vecteur comportant un gène viral transcrit par l'ARN polymérase III
US5837503A (en) *	1993-07-07	1998-11-17	Universite De Nice-Sophia-Antipolis	Vector containing viral gene transcribed by RNA polymerase III and methods for use
US5817635A (en) *	1993-08-09	1998-10-06	Max-Planck-Gesellschaft Zur Forderung Der Wissenschaften E.V.	Modified ribozymes
EP0707493A4 (en) *	1994-01-24	1999-03-31	Hope City	COLOLIZATION OF TARGET MOLECULE AND ITS INHIBITOR
DE4424761C1 (de) *	1994-07-04	1995-06-08	Max Planck Gesellschaft	Expressionskassette für die Antisense- und die Ribozym-Expression
EP0837933A4 (en)	1995-06-07	2003-05-21	Commw Scient Ind Res Org	OPTIMIZED MINIZYMS AND MINIRIBOZYMS AND THEIR APPLICATIONS
FR2755976B1 (fr) *	1996-11-15	1999-01-15	Idm Immuno Designed Molecules	Nouveaux complexes d'acides nucleiques et de polymere substitue par des residus entrainant la destabilisation des membranes cellulaires
US6057156A (en)	1997-01-31	2000-05-02	Robozyme Pharmaceuticals, Inc.	Enzymatic nucleic acid treatment of diseases or conditions related to levels of epidermal growth factor receptors
WO1999020753A2 (en) *	1997-10-21	1999-04-29	Ribozyme Pharmaceuticals, Inc.	Peptide bond formation using nucleic acid catalysts
US6506559B1 (en)	1997-12-23	2003-01-14	Carnegie Institute Of Washington	Genetic inhibition by double-stranded RNA
BRPI9908967B1 (pt)	1998-03-20	2017-05-30	Benitec Australia Ltd	processos para reprimir, retardar ou de outro modo reduzir a expressão de um gene alvo em uma célula de planta
AUPP249298A0 (en)	1998-03-20	1998-04-23	Ag-Gene Australia Limited	Synthetic genes and genetic constructs comprising same I
WO2000044914A1 (en)	1999-01-28	2000-08-03	Medical College Of Georgia Research Institute, Inc.	Composition and method for in vivo and in vitro attenuation of gene expression using double stranded rna
US6423885B1 (en)	1999-08-13	2002-07-23	Commonwealth Scientific And Industrial Research Organization (Csiro)	Methods for obtaining modified phenotypes in plant cells
CA2369944A1 (en)	2001-01-31	2002-07-31	Nucleonics Inc.	Use of post-transcriptional gene silencing for identifying nucleic acid sequences that modulate the function of a cell
AUPR621501A0 (en)	2001-07-06	2001-08-02	Commonwealth Scientific And Industrial Research Organisation	Delivery of ds rna
MX2020002872A (es)	2017-09-15	2020-10-05	Commw Scient Ind Res Org	Moléculas de arn.
WO2025111506A1 (en) *	2023-11-22	2025-05-30	Tevard Biosciences, Inc.	Modified transfer rnas and methods of use

Family Cites Families (2)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US4987071A (en) *	1986-12-03	1991-01-22	University Patents, Inc.	RNA ribozyme polymerases, dephosphorylases, restriction endoribonucleases and methods
SU1759873A1 (ru) *	1990-08-14	1992-09-07	Новосибирский государственный университет им.Ленинского комсомола	Фрагмент дезоксирибонуклиновой кислоты, кодирующий промотор SP6 РНК-полимеразы

1990
- 1990-03-13 AT AT90104701T patent/ATE140961T1/de not_active IP Right Cessation
- 1990-03-13 ES ES90104701T patent/ES2090049T3/es not_active Expired - Lifetime
- 1990-03-13 DE DE59010432T patent/DE59010432D1/de not_active Expired - Lifetime
- 1990-03-13 EP EP90104701A patent/EP0387775B1/de not_active Expired - Lifetime
- 1990-03-13 DK DK90104701.9T patent/DK0387775T3/da active
- 1990-03-14 HU HU901584A patent/HU215187B/hu unknown
- 1990-03-14 NZ NZ232917A patent/NZ232917A/en unknown
- 1990-03-14 DD DD90338709A patent/DD297838A5/de not_active IP Right Cessation
- 1990-03-15 IL IL9375490A patent/IL93754A/he not_active IP Right Cessation
- 1990-03-15 FI FI901296A patent/FI105103B/fi active IP Right Grant
- 1990-03-15 AU AU51301/90A patent/AU637354B2/en not_active Expired
- 1990-03-15 PT PT93440A patent/PT93440B/pt not_active IP Right Cessation
- 1990-03-15 IE IE93190A patent/IE74850B1/en not_active IP Right Cessation
- 1990-03-15 NO NO901213A patent/NO306623B1/no not_active IP Right Cessation
- 1990-03-15 CA CA002012312A patent/CA2012312C/en not_active Expired - Lifetime
- 1990-03-15 JP JP06549390A patent/JP3330930B2/ja not_active Expired - Lifetime
- 1990-03-15 ZA ZA901973A patent/ZA901973B/xx unknown
- 1990-03-15 KR KR1019900003438A patent/KR900014591A/ko not_active Ceased
- 1990-03-16 RU SU5010032A patent/RU2136751C1/ru active
1995
- 1995-06-30 HU HU95P/P00692P patent/HU211868A9/hu unknown
1996
- 1996-09-03 GR GR960402292T patent/GR3020935T3/el unknown

Also Published As

Publication number	Publication date
GR3020935T3 (en)	1996-12-31
NO901213L (no)	1990-09-17
CA2012312C (en)	2001-08-14
ZA901973B (en)	1991-11-27
ES2090049T3 (es)	1996-10-16
FI901296A0 (fi)	1990-03-15
HUT54206A (en)	1991-01-28
CA2012312A1 (en)	1990-09-16
IE900931L (en)	1990-09-16
ATE140961T1 (de)	1996-08-15
IL93754A0 (en)	1990-12-23
KR900014591A (ko)	1990-10-24
IE74850B1 (en)	1997-08-13
AU637354B2 (en)	1993-05-27
NO306623B1 (no)	1999-11-29
EP0387775A1 (de)	1990-09-19
DD297838A5 (de)	1992-01-23
JPH03130080A (ja)	1991-06-03
HU901584D0 (en)	1990-06-28
IL93754A (he)	1995-12-31
NZ232917A (en)	1997-07-27
AU5130190A (en)	1990-11-01
PT93440B (pt)	2001-07-31
JP3330930B2 (ja)	2002-10-07
NO901213D0 (no)	1990-03-15
DK0387775T3 (da)	1996-11-04
HU215187B (hu)	1998-10-28
EP0387775B1 (de)	1996-07-31
PT93440A (pt)	1990-11-07
RU2136751C1 (ru)	1999-09-10
DE59010432D1 (de)	1996-09-05
HU211868A9 (en)	1995-12-28

Legal Events

Date	Code	Title	Description
2004-08-31	FG	Patent granted	Owner name: BOEHRINGER INGELHEIM INTERNATIONAL GMBH

Publication	Publication Date	Title
CA2012312C (en)	2001-08-14	Genetic units for inhibiting the function of rna
JP3316216B2 (ja)	2002-08-19	安定化外部ガイド配列
AU687001B2 (en)	1998-02-19	Method and reagent for inhibiting cancer development
US5989906A (en)	1999-11-23	Method and reagent for inhibiting P-glycoprotein (mdr-1-gene)
US20030105051A1 (en)	2003-06-05	Nucleic acid treatment of diseases or conditions related to levels of HER2
JP2009000105A (ja)	2009-01-08	短干渉核酸（ｓｉＮＡ）を用いた血管内皮成長因子および血管内皮成長因子レセプター遺伝子発現のＲＮＡ干渉媒介阻害
JP2009060893A (ja)	2009-03-26	短干渉核酸（ｓｉＮＡ）を用いる遺伝子発現のＲＮＡ干渉媒介性阻害
JP2005517452A (ja)	2005-06-16	短干渉核酸（ｓｉＮＡ）を用いるＢＣＬ２遺伝子発現のＲＮＡ干渉媒介性阻害
JPH1052264A (ja)	1998-02-24	Ｎ‐ｒａｓ発現阻害剤およびその方法
US5599704A (en)	1997-02-04	ErbB2/neu targeted ribozymes
JP2003511025A (ja)	2003-03-25	インビボで製造されたｓｓＤＮＡによる遺伝子発現の改変
Levi et al.	1988	Constitutive expression of c-fos antisense RNA blocks c-fos gene induction by interferon and by phorbol ester and reduces c-myc expression in F9 embryonal carcinoma cells.
Zhang et al.	2000	Generation of ribozyme-adenoviral vector against K-ras mutant human lung cancer cells
US20040072783A1 (en)	2004-04-15	Nucleozymes with endonuclease activity
US6830923B1 (en)	2004-12-14	Genetics units for inhibiting the function of RNA
JP2010538661A (ja)	2010-12-16	ＳＴＡＴ５ｓｉＲＮＡ含有組成物及びそれらの使用法
AU2006219666B2 (en)	2011-01-27	Inhibition of SPAG9 expression with siRNAs
WO2001062911A2 (en)	2001-08-30	Antisense and catalytically acting nucleic acid molecules targeted to grb2- related with insert domain (grid) proteins and their uses
Kessler et al.	1991	A 21-base pair DNA fragment directs transcription attenuation within the simian virus 40 late leader
JP2007505605A (ja)	2007-03-15	低分子干渉核酸（ｓｉＮＡ）を使用したＲＮＡ干渉により媒介される血管内皮増殖因子遺伝子発現および血管内皮増殖因子遺伝子受容体遺伝子発現のＲＮＡ干渉媒介性抑制
JP2007505605A6 (ja)	2007-07-12	低分子干渉核酸（ｓｉＮＡ）を使用したＲＮＡ干渉により媒介される血管内皮増殖因子遺伝子発現および血管内皮増殖因子遺伝子受容体遺伝子発現のＲＮＡ干渉媒介性抑制
AU730506B2 (en)	2001-03-08	Method and reagent for inhibiting cancer development
CA2578402A1 (en)	1995-11-23	Human papilloma virus inhibition by a hairpin ribozyme
JPH09501318A (ja)	1997-02-10	ヒト免疫不全ウイルスの複製を阻害するための方法および試薬