AU756620B2 - Mutations in the myostation gene cause double-muscling in mammals - Google Patents
Mutations in the myostation gene cause double-muscling in mammals Download PDFInfo
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- AU756620B2 AU756620B2 AU84571/98A AU8457198A AU756620B2 AU 756620 B2 AU756620 B2 AU 756620B2 AU 84571/98 A AU84571/98 A AU 84571/98A AU 8457198 A AU8457198 A AU 8457198A AU 756620 B2 AU756620 B2 AU 756620B2
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- C12N15/85—Vectors or expression systems specially adapted for eukaryotic hosts for animal cells
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- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/475—Growth factors; Growth regulators
- C07K14/495—Transforming growth factor [TGF]
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- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/68—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving nucleic acids
- C12Q1/6876—Nucleic acid products used in the analysis of nucleic acids, e.g. primers or probes
- C12Q1/6883—Nucleic acid products used in the analysis of nucleic acids, e.g. primers or probes for diseases caused by alterations of genetic material
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- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2217/00—Genetically modified animals
- A01K2217/05—Animals comprising random inserted nucleic acids (transgenic)
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- A—HUMAN NECESSITIES
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- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2217/00—Genetically modified animals
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- A01K2217/075—Animals genetically altered by homologous recombination inducing loss of function, i.e. knock out
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- A—HUMAN NECESSITIES
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- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2217/00—Genetically modified animals
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- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
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- A01K2227/10—Mammal
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- A—HUMAN NECESSITIES
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- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
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- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
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- A—HUMAN NECESSITIES
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- A61K48/00—Medicinal preparations containing genetic material which is inserted into cells of the living body to treat genetic diseases; Gene therapy
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- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
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- General Chemical & Material Sciences (AREA)
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- Animal Behavior & Ethology (AREA)
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- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
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| US776198A | 1998-01-15 | 1998-01-15 | |
| US09/007761 | 1998-01-15 | ||
| PCT/IB1998/001197 WO1999002667A1 (en) | 1997-07-14 | 1998-07-14 | Mutations in the myostation gene cause double-muscling in mammals |
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| AU8457198A AU8457198A (en) | 1999-02-08 |
| AU756620B2 true AU756620B2 (en) | 2003-01-16 |
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| AU (1) | AU756620B2 (enExample) |
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| ES (1) | ES2547858T3 (enExample) |
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| PT (1) | PT2045322E (enExample) |
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Families Citing this family (43)
| Publication number | Priority date | Publication date | Assignee | Title |
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| ES2201076T3 (es) | 1993-03-19 | 2004-03-16 | The Johns Hopkins University School Of Medicine | Factor-8 de diferenciacion del crecimiento. |
| US7393682B1 (en) | 1993-03-19 | 2008-07-01 | The Johns Hopkins University School Of Medicine | Polynucleotides encoding promyostatin polypeptides |
| US5994618A (en) | 1997-02-05 | 1999-11-30 | Johns Hopkins University School Of Medicine | Growth differentiation factor-8 transgenic mice |
| US7566768B1 (en) | 1995-10-26 | 2009-07-28 | The Johns Hopkins University School Of Medicine | Promyostatin peptides and methods of using same |
| US7332575B2 (en) | 1994-03-18 | 2008-02-19 | The Johns Hopkins University School Of Medicine | Growth differentiation factor-8 nucleic acid and polypeptide from aquatic species, and transgenic aquatic species |
| US6008434A (en) | 1994-07-08 | 1999-12-28 | Johns Hopkins University School Of Medicine | Growth differentiation factor-11 transgenic mice |
| GB2333706A (en) * | 1998-02-02 | 1999-08-04 | Merck & Co Inc | Method for increasing muscle mass in animals |
| US6369201B1 (en) * | 1998-02-19 | 2002-04-09 | Metamorphix International, Inc. | Myostatin multimers |
| AU5483599A (en) * | 1998-08-14 | 2000-03-06 | Board Of Regents, The University Of Texas System | Calcineurin-dependent control of skeletal muscle fiber type |
| ATE322681T1 (de) * | 1999-01-21 | 2006-04-15 | Metamorphix Inc | Inhibitoren für wachstumdifferenzierungsfaktor und ihre anwendungen |
| MXPA01013232A (es) | 1999-07-20 | 2005-05-24 | Pharmexa As | Metodo para identificar la actividad de gdf-8. |
| ZA200003786B (en) * | 1999-07-30 | 2002-01-21 | Pfizer Prod Inc | Myostatin regulatory region, nucleotide sequence determination and methods for its use. |
| EP1322784B1 (en) * | 2000-09-06 | 2008-08-13 | Timothy A. Hodge | Method for screening of genomic DNA, in particular in relation to transgenic and targeted mutagenesis |
| US7011943B2 (en) | 2000-09-06 | 2006-03-14 | Transnetyx, Inc. | Method for detecting a designated genetic sequence in murine genomic DNA |
| US7494817B2 (en) | 2000-09-06 | 2009-02-24 | Transnet Yx, Inc. | Methods for genotype screening using magnetic particles |
| US7037501B2 (en) | 2001-01-04 | 2006-05-02 | Regents Of The University Of Minnesota | Myostatin immnoconjugate |
| TW200526779A (en) | 2001-02-08 | 2005-08-16 | Wyeth Corp | Modified and stabilized GDF propeptides and uses thereof |
| US7320789B2 (en) | 2001-09-26 | 2008-01-22 | Wyeth | Antibody inhibitors of GDF-8 and uses thereof |
| US7261893B2 (en) | 2002-10-22 | 2007-08-28 | Wyeth | Neutralizing antibodies against GDF-8 and uses therefor |
| EA009056B1 (ru) | 2002-12-20 | 2007-10-26 | Амген, Инк. | Связывающие агенты, ингибирующие миостатин |
| CN101405404A (zh) | 2002-12-31 | 2009-04-08 | 迈特默菲公司 | 用于推断牛的性状的组合物、方法和系统 |
| JP5110877B2 (ja) | 2003-06-02 | 2012-12-26 | ワイス・エルエルシー | 神経筋障害を処置するための、コルチコステロイドと組み合わせたミオスタチン（ｇｄｆ８）インヒビターの使用 |
| EP1855694B1 (en) | 2005-02-09 | 2020-12-02 | Sarepta Therapeutics, Inc. | Antisense composition for treating muscle atrophy |
| WO2008005002A1 (en) * | 2006-06-30 | 2008-01-10 | Oligos Ets. Inc. | Compositions and methods for the treatment of muscle wasting |
| EP3327033A1 (en) | 2005-08-19 | 2018-05-30 | Wyeth LLC | Antagonist antibodies against gdf-8 and uses in treatment of als and other gdf-8-associated disorders |
| KR100872042B1 (ko) * | 2005-09-14 | 2008-12-05 | 주식회사 바이오리더스 | 마이오스타틴을 발현하는 세포표면 발현벡터 및 상기벡터에 의해 형질전환된 미생물 |
| GB2433320B (en) * | 2005-12-16 | 2009-10-07 | Norwegian University Of Life S | Diagnostic method |
| KR100857861B1 (ko) * | 2007-10-15 | 2008-09-11 | 주식회사 바이오리더스 | Ｍｙｏ－２ 펩타이드 중합체와 마이오스타틴의 융합단백질표면발현용 벡터 및 상기 벡터로 형질전환된 미생물 |
| CA2828239C (en) * | 2011-02-25 | 2020-10-06 | Recombinetics, Inc. | Genetically modified animals and methods for making the same |
| US9528124B2 (en) | 2013-08-27 | 2016-12-27 | Recombinetics, Inc. | Efficient non-meiotic allele introgression |
| US10920242B2 (en) | 2011-02-25 | 2021-02-16 | Recombinetics, Inc. | Non-meiotic allele introgression |
| US20130085139A1 (en) | 2011-10-04 | 2013-04-04 | Royal Holloway And Bedford New College | Oligomers |
| MY177331A (en) | 2012-06-15 | 2020-09-12 | Pfizer | Improved antagonist antibodies against gdf-8 and uses therefor |
| AR091482A1 (es) * | 2012-06-21 | 2015-02-04 | Recombinetics Inc | Celulas modificadas geneticamente y metodos par su obtencion |
| AU2014262843B2 (en) | 2013-05-06 | 2017-06-22 | Scholar Rock, Inc. | Compositions and methods for growth factor modulation |
| EP2960653A1 (en) * | 2014-06-24 | 2015-12-30 | Stichting Kwaliteitsgarantie Vleeskalversector | Diagnostic kit and method for the identification of the manipulation of muscle mass in a domestic animal |
| MA41795A (fr) | 2015-03-18 | 2018-01-23 | Sarepta Therapeutics Inc | Exclusion d'un exon induite par des composés antisens dans la myostatine |
| EP3359668A4 (en) * | 2015-10-09 | 2019-06-05 | Sarepta Therapeutics, Inc. | COMPOSITIONS AND METHODS OF TREATING DUCHENNE MUSCLE DYSTROPHY AND ASSOCIATED ILLNESSES THEREOF |
| CN106472430A (zh) * | 2016-10-21 | 2017-03-08 | 延边朝鲜族自治州农业科学院（延边特产研究所） | 一种寒冷地区烟蚜茧蜂冬季保种方法 |
| EP3766529A4 (en) * | 2018-03-14 | 2022-03-23 | Beacon Medcare (HK) Limited | Composition for purification of biofluids |
| CN110157818B (zh) * | 2019-07-08 | 2023-04-25 | 云南东恒经贸集团猪育种有限公司 | 一种与猪眼肌高产性状相关的分子标记及其应用 |
| KR20230130639A (ko) * | 2020-12-03 | 2023-09-12 | (주)라트바이오 | 마이오스타틴 유전자가 변형된 형질전환 동물 |
| CN120192396A (zh) * | 2023-12-21 | 2025-06-24 | 江苏省农业科学院 | 一种肌肉生长抑制素mstn蛋白突变体及其制备方法和应用 |
Family Cites Families (17)
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| US4870009A (en) | 1982-11-22 | 1989-09-26 | The Salk Institute For Biological Studies | Method of obtaining gene product through the generation of transgenic animals |
| GB8308235D0 (en) | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US4736866A (en) | 1984-06-22 | 1988-04-12 | President And Fellows Of Harvard College | Transgenic non-human mammals |
| JPS6147500A (ja) | 1984-08-15 | 1986-03-07 | Res Dev Corp Of Japan | キメラモノクロ−ナル抗体及びその製造法 |
| EP0173494A3 (en) | 1984-08-27 | 1987-11-25 | The Board Of Trustees Of The Leland Stanford Junior University | Chimeric receptors by dna splicing and expression |
| GB8422238D0 (en) | 1984-09-03 | 1984-10-10 | Neuberger M S | Chimeric proteins |
| GB8607679D0 (en) | 1986-03-27 | 1986-04-30 | Winter G P | Recombinant dna product |
| US5264558A (en) | 1987-06-19 | 1993-11-23 | The Regents Of The University Of California | Single-chain monellin analog as a low calorie protein sweetner |
| AU617739B2 (en) | 1987-12-23 | 1991-12-05 | Pharmacia & Upjohn Company | Chimeric glycoproteins containing immunogenic segments of the glycoproteins of human respiratory syncytial virus |
| US5633076A (en) | 1989-12-01 | 1997-05-27 | Pharming Bv | Method of producing a transgenic bovine or transgenic bovine embryo |
| GB9021679D0 (en) | 1990-10-05 | 1990-11-21 | Gorman Scott David | Antibody preparation |
| US5162209A (en) * | 1991-01-18 | 1992-11-10 | Beth Israel Hospital Association | Synthesis of full-length, double-stranded dna from a single-stranded linear dna template |
| US5962316A (en) * | 1992-10-16 | 1999-10-05 | Cold Spring Harbor Laboratory | Cell-cycle regulatory proteins, and uses related thereto |
| ES2201076T3 (es) * | 1993-03-19 | 2004-03-16 | The Johns Hopkins University School Of Medicine | Factor-8 de diferenciacion del crecimiento. |
| ES2233936T3 (es) * | 1994-02-04 | 2005-06-16 | Bio Merieux | Virus msrv1 asociado a la esclerosis en placas, sus constituyentes nucleicos y sus aplicaciones. |
| WO1998033887A1 (en) * | 1997-02-05 | 1998-08-06 | The Johns Hopkins University School Of Medicine | Growth differentiation factor-8 |
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- 1998-07-14 WO PCT/IB1998/001197 patent/WO1999002667A1/en not_active Ceased
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2015
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Non-Patent Citations (1)
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| MCPHERRON AC NATURE 1997 387:83-90 * |
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| CA2296434C (en) | 2013-10-15 |
| JP4368522B2 (ja) | 2009-11-18 |
| AU8457198A (en) | 1999-02-08 |
| DE69841139D1 (de) | 2009-10-22 |
| PT2045322E (pt) | 2015-10-16 |
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