ES2202469T5 - Proteína relacionada con el vegf. - Google Patents
Proteína relacionada con el vegf. Download PDFInfo
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- ES2202469T5 ES2202469T5 ES96931450T ES96931450T ES2202469T5 ES 2202469 T5 ES2202469 T5 ES 2202469T5 ES 96931450 T ES96931450 T ES 96931450T ES 96931450 T ES96931450 T ES 96931450T ES 2202469 T5 ES2202469 T5 ES 2202469T5
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- vrp
- cells
- flt4
- protein
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- C—CHEMISTRY; METALLURGY
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- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/52—Cytokines; Lymphokines; Interferons
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
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- C07—ORGANIC CHEMISTRY
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- C07K2319/30—Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
Landscapes
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- Organic Chemistry (AREA)
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- Genetics & Genomics (AREA)
- Biochemistry (AREA)
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- Heart & Thoracic Surgery (AREA)
- Cardiology (AREA)
- Dermatology (AREA)
- Ophthalmology & Optometry (AREA)
- Hematology (AREA)
- Urology & Nephrology (AREA)
- Vascular Medicine (AREA)
- Cell Biology (AREA)
- Rheumatology (AREA)
- Endocrinology (AREA)
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Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US349195P | 1995-09-08 | 1995-09-08 | |
| US3491 | 1995-09-08 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| ES2202469T3 ES2202469T3 (es) | 2004-04-01 |
| ES2202469T5 true ES2202469T5 (es) | 2011-06-06 |
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| Application Number | Title | Priority Date | Filing Date |
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| ES96931450T Expired - Lifetime ES2202469T5 (es) | 1995-09-08 | 1996-08-30 | Proteína relacionada con el vegf. |
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| US (9) | US6451764B1 (enExample) |
| EP (2) | EP0848755B2 (enExample) |
| JP (3) | JPH11514976A (enExample) |
| AT (1) | ATE242809T1 (enExample) |
| AU (3) | AU710696C (enExample) |
| CA (1) | CA2231400A1 (enExample) |
| DE (1) | DE69628652T3 (enExample) |
| DK (1) | DK0848755T4 (enExample) |
| ES (1) | ES2202469T5 (enExample) |
| IL (2) | IL123332A (enExample) |
| PT (1) | PT848755E (enExample) |
| WO (1) | WO1997009427A1 (enExample) |
| ZA (1) | ZA967445B (enExample) |
Families Citing this family (103)
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| US6168778B1 (en) | 1990-06-11 | 2001-01-02 | Nexstar Pharmaceuticals, Inc. | Vascular endothelial growth factor (VEGF) Nucleic Acid Ligand Complexes |
| US6762290B1 (en) | 1999-07-29 | 2004-07-13 | Gilead Sciences, Inc. | High affinity vascular endothelial growth factor (VEGF) receptor nucleic acid ligands and inhibitors |
| US6824777B1 (en) | 1992-10-09 | 2004-11-30 | Licentia Ltd. | Flt4 (VEGFR-3) as a target for tumor imaging and anti-tumor therapy |
| US7153827B1 (en) | 1994-03-08 | 2006-12-26 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 and methods of use |
| US7109308B1 (en) | 1994-03-08 | 2006-09-19 | Human Genome Sciences, Inc. | Antibodies to human vascular endothelial growth factor 2 |
| US6734285B2 (en) | 1994-03-08 | 2004-05-11 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 proteins and compositions |
| US6040157A (en) | 1994-03-08 | 2000-03-21 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| US6608182B1 (en) | 1994-03-08 | 2003-08-19 | Human Genome Sciences, Inc. | Human vascular endothelial growth factor 2 |
| US5932540A (en) * | 1994-03-08 | 1999-08-03 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| US7186688B1 (en) * | 1994-03-08 | 2007-03-06 | Human Genome Sciences, Inc. | Methods of stimulating angiogenesis in a patient by administering vascular endothelial growth factor 2 |
| CN1267550C (zh) * | 1994-03-08 | 2006-08-02 | 人体基因组科学有限公司 | 血管内皮生长因子2 |
| WO1998033917A1 (en) * | 1994-11-14 | 1998-08-06 | The Ludwig Institute For Cancer Research | Vascular endothelial growth factor c (vegf-c) protein and gene, mutants thereof, and uses thereof |
| US6818220B1 (en) | 1994-11-14 | 2004-11-16 | Licentia Ltd. | Vascular endothelial growth factor C (VEGF-C) protein and gene mutants thereof, and uses thereof |
| US6645933B1 (en) | 1995-08-01 | 2003-11-11 | Helsinki University Licensing Ltd. Oy | Receptor ligand VEGF-C |
| US6221839B1 (en) | 1994-11-14 | 2001-04-24 | Helsinki University Licensing Ltd. Oy | FIt4 ligand and methods of use |
| US6403088B1 (en) | 1995-08-01 | 2002-06-11 | Helsinki University Licensing, Ltd. | Antibodies reactive with VEGF-C, a ligand for the Flt4 receptor tyrosine kinase (VEGFR-3) |
| US6245530B1 (en) | 1995-08-01 | 2001-06-12 | Ludwig Institute For Cancer Research | Receptor ligand |
| US6130071A (en) * | 1997-02-05 | 2000-10-10 | Helsinki University Licensing, Ltd. | Vascular endothelial growth factor C (VEGF-C) ΔCys156 protein and gene, and uses thereof |
| US6361946B1 (en) | 1997-02-05 | 2002-03-26 | Licentia Ltd | Vascular endothelial growth factor C (VEGF-C) protein and gene, mutants thereof, and uses thereof |
| US7423125B2 (en) | 1995-08-01 | 2008-09-09 | Vegenics Limited | Antibodies to VEGF-C |
| ES2202469T5 (es) * | 1995-09-08 | 2011-06-06 | Genentech, Inc. | Proteína relacionada con el vegf. |
| AU1116297A (en) | 1995-11-08 | 1997-05-29 | Immunex Corporation | Flk-1 binding protein |
| US6994989B1 (en) * | 1995-11-08 | 2006-02-07 | Immunex Corp. | FLK-1 binding proteins |
| AU733322B2 (en) | 1996-07-15 | 2001-05-10 | Chugai Seiyaku Kabushiki Kaisha | Novel VEGF-like factor |
| DE69734359T2 (de) * | 1996-08-23 | 2006-07-06 | Ludwig Institute For Cancer Research | Rekombinanter vaskulärer endothelzellen wachstumsfaktor d (vegf-d) |
| US6426335B1 (en) | 1997-10-17 | 2002-07-30 | Gilead Sciences, Inc. | Vascular endothelial growth factor (VEGF) nucleic acid ligand complexes |
| US6051698A (en) * | 1997-06-06 | 2000-04-18 | Janjic; Nebojsa | Vascular endothelial growth factor (VEGF) nucleic acid ligand complexes |
| US20050163818A1 (en) * | 1996-11-05 | 2005-07-28 | Hsing-Wen Sung | Drug-eluting device chemically treated with genipin |
| US7351421B2 (en) * | 1996-11-05 | 2008-04-01 | Hsing-Wen Sung | Drug-eluting stent having collagen drug carrier chemically treated with genipin |
| US7125714B2 (en) * | 1997-02-05 | 2006-10-24 | Licentia Ltd. | Progenitor cell materials and methods |
| JP2002505873A (ja) * | 1998-03-13 | 2002-02-26 | ヒューマン ジノーム サイエンシーズ， インコーポレイテッド | 血管内皮増殖因子２ |
| US6887674B1 (en) | 1998-04-13 | 2005-05-03 | California Institute Of Technology | Artery- and vein-specific proteins and uses therefor |
| US6864227B1 (en) | 1998-04-13 | 2005-03-08 | California Institute Of Technology | Artery-and vein-specific proteins and uses therefor |
| NZ511408A (en) * | 1998-10-09 | 2004-04-30 | Licentia Ltd | Flt4 (VEGFR-3) as a target for tumor imaging and anti-tumor therapy |
| US6958147B1 (en) | 1998-10-26 | 2005-10-25 | Licentia Ltd | Use of VEGF-C to prevent restenosis |
| AU2486300A (en) * | 1998-12-30 | 2000-07-31 | Millennium Pharmaceuticals, Inc. | Secreted proteins and nucleic acids encoding them |
| US7223724B1 (en) | 1999-02-08 | 2007-05-29 | Human Genome Sciences, Inc. | Use of vascular endothelial growth factor to treat photoreceptor cells |
| US6764820B2 (en) * | 1999-03-26 | 2004-07-20 | Ludwig Institute For Cancer Research | Screening for lymphatic disorders involving the FLT4 receptor tyrosine kinase (VEGFR-3) |
| WO2000058511A1 (en) * | 1999-03-26 | 2000-10-05 | Ludwig Institute For Cancer Research | Screening and therapy for lymphatic disorders involving the flt4 receptor tyrosine kinase (vegfr-3) |
| GB9918057D0 (en) * | 1999-07-30 | 1999-10-06 | Univ Bristol | Therapeutic agents |
| US6965010B2 (en) | 2000-02-25 | 2005-11-15 | Licentia, Ltd. | Materials and methods involving hybrid vascular endothelial growth factor DNAs and proteins |
| AUPQ592100A0 (en) * | 2000-02-29 | 2000-03-23 | Council Of The Queensland Institute Of Medical Research, The | A method of treatment and prophylaxis |
| NZ518077A (en) * | 2000-08-04 | 2003-11-28 | Human Genome Sciences Inc | Biologically active fragments, analogues and derivatives of VEGF-2 for the treatment of peripheral artery diseases such as critical limb ischemia and coronary disease |
| AU2002228841C1 (en) | 2000-12-07 | 2006-11-23 | Sangamo Biosciences, Inc | Regulation of angiogenesis with zinc finger proteins |
| US7067317B2 (en) | 2000-12-07 | 2006-06-27 | Sangamo Biosciences, Inc. | Regulation of angiogenesis with zinc finger proteins |
| US7611711B2 (en) * | 2001-01-17 | 2009-11-03 | Vegenics Limited | VEGFR-3 inhibitor materials and methods |
| DE60219419T2 (de) * | 2001-01-19 | 2007-08-16 | Ludwig Institute For Cancer Research | Flt4 (vegfr-3) als ein ziel für krebsdarstellung und anti-krebs-behandlung |
| WO2002083704A1 (en) | 2001-04-13 | 2002-10-24 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| US20050232921A1 (en) * | 2001-04-13 | 2005-10-20 | Rosen Craig A | Vascular endothelial growth factor 2 |
| WO2002083849A2 (en) * | 2001-04-13 | 2002-10-24 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| US7402312B2 (en) | 2001-04-13 | 2008-07-22 | Human Genome Sciences, Inc. | Antibodies to vascular endothelial growth factor 2 (VEGF-2) |
| JP2005500045A (ja) * | 2001-07-12 | 2005-01-06 | ルードビッヒ、インスティテュート、フォー、キャンサー、リサーチ | リンパ管内皮細胞材料および方法 |
| US20030113324A1 (en) * | 2001-10-01 | 2003-06-19 | Kari Alitalo | Neuropilin/VEGF-C/VEGFR-3 materials and methods |
| US20040214766A1 (en) * | 2001-10-01 | 2004-10-28 | Kari Alitalo | VEGF-C or VEGF-D materials and methods for treatment of neuropathologies |
| US8623822B2 (en) | 2002-03-01 | 2014-01-07 | Bracco Suisse Sa | KDR and VEGF/KDR binding peptides and their use in diagnosis and therapy |
| AU2003278807A1 (en) | 2002-03-01 | 2004-08-13 | Bracco International B.V. | Kdr and vegf/kdr binding peptides and their use in diagnosis and therapy |
| US7985402B2 (en) * | 2002-03-01 | 2011-07-26 | Bracco Suisse Sa | Targeting vector-phospholipid conjugates |
| US7794693B2 (en) * | 2002-03-01 | 2010-09-14 | Bracco International B.V. | Targeting vector-phospholipid conjugates |
| US7666979B2 (en) | 2002-03-01 | 2010-02-23 | Bracco International B.V. | Methods for preparing multivalent constructs for therapeutic and diagnostic applications and methods of preparing the same |
| US20050250700A1 (en) * | 2002-03-01 | 2005-11-10 | Sato Aaron K | KDR and VEGF/KDR binding peptides |
| US7261876B2 (en) | 2002-03-01 | 2007-08-28 | Bracco International Bv | Multivalent constructs for therapeutic and diagnostic applications |
| US7211240B2 (en) | 2002-03-01 | 2007-05-01 | Bracco International B.V. | Multivalent constructs for therapeutic and diagnostic applications |
| AU2003251397B2 (en) * | 2002-06-05 | 2009-10-01 | Genentech, Inc. | Compositions and methods for liver growth and liver protection |
| US7696320B2 (en) | 2004-08-24 | 2010-04-13 | Domantis Limited | Ligands that have binding specificity for VEGF and/or EGFR and methods of use therefor |
| US20050163821A1 (en) * | 2002-08-02 | 2005-07-28 | Hsing-Wen Sung | Drug-eluting Biodegradable Stent and Delivery Means |
| US20050019404A1 (en) * | 2003-06-30 | 2005-01-27 | Hsing-Wen Sung | Drug-eluting biodegradable stent |
| US20040120950A1 (en) * | 2002-12-20 | 2004-06-24 | Kari Alitalo | Modulation of VEGF-C/VEGFR-3 interactions in the treatment of rheumatoid arthritis |
| EP1594527A2 (en) * | 2003-02-04 | 2005-11-16 | Ludwig Institute For Cancer Research | Vegf-b and pdgf modulation of stem cells |
| EP1603935A4 (en) | 2003-03-03 | 2007-03-21 | Dyax Corp | SPECIFIC TO HGF RECEPTOR (cMET) BINDING PEPTIDES AND THEIR USE |
| CA2518912A1 (en) | 2003-03-12 | 2004-09-23 | Vasgene Therapeutics, Inc. | Polypeptide compounds for inhibiting angiogenesis and tumor growth |
| US7381410B2 (en) | 2003-03-12 | 2008-06-03 | Vasgene Therapeutics, Inc. | Polypeptide compounds for inhibiting angiogenesis and tumor growth |
| TWI353991B (en) | 2003-05-06 | 2011-12-11 | Syntonix Pharmaceuticals Inc | Immunoglobulin chimeric monomer-dimer hybrids |
| WO2005016963A2 (en) * | 2003-06-12 | 2005-02-24 | Ludwig Institute For Cancer Research | Heparin binding veger-3 ligands |
| US20050043235A1 (en) * | 2003-06-12 | 2005-02-24 | Kari Alitalo | Use of VEGF-C or VEGF-D in reconstructive surgery |
| NZ617083A (en) | 2003-08-27 | 2015-04-24 | Ophthotech Corp | Combination therapy for the treatment of ocular neovascular disorders |
| AU2004290070A1 (en) | 2003-11-12 | 2005-05-26 | Biogen Idec Ma Inc. | Neonatal Fc receptor (FcRn)-binding polypeptide variants, dimeric Fc binding proteins and methods related thereto |
| EP1730196B1 (en) | 2004-03-12 | 2010-12-22 | Vasgene Therapeutics, Inc. | Antibodies binding to ephb4 for inhibiting angiogenesis and tumor growth |
| ATE492564T1 (de) | 2004-03-12 | 2011-01-15 | Vasgene Therapeutics Inc | Ephb4-bindende antikörper zur inhibierung von angiogenese und tumorwachstum |
| US8415315B2 (en) | 2004-05-06 | 2013-04-09 | University Of Central Florida Research Foundation, Inc. | Methods and compositions for inhibiting the proliferation of cancer cells |
| WO2006017447A1 (en) | 2004-08-02 | 2006-02-16 | University Of Iowa Research Foundation | Methods of inhibiting vegf-c |
| EP1799713B1 (en) | 2004-09-23 | 2014-11-05 | VasGene Therapeutics, Inc. | Polypeptide compounds for inhibiting angiogenesis and tumor growth |
| CA2593212A1 (en) | 2005-01-05 | 2006-07-13 | Biogen Idec Ma Inc. | Cripto binding molecules |
| EP2314614B1 (en) | 2005-02-28 | 2015-11-25 | Sangamo BioSciences, Inc. | Anti-angiogenic methods and compositions |
| US9073997B2 (en) * | 2007-02-02 | 2015-07-07 | Vegenics Pty Limited | Growth factor antagonists for organ transplant alloimmunity and arteriosclerosis |
| CN102083861B (zh) | 2007-08-13 | 2016-04-13 | 瓦斯基因治疗公司 | 使用结合EphB4的人源化抗体的癌症治疗 |
| US20100029491A1 (en) * | 2008-07-11 | 2010-02-04 | Maike Schmidt | Methods and compositions for diagnostic use for tumor treatment |
| EP2446027A1 (en) * | 2009-06-25 | 2012-05-02 | Danisco A/S | Protein |
| BR112012000735A2 (pt) | 2009-07-13 | 2016-11-16 | Genentech Inc | "métodos, kits e conjuntos de compostos" |
| SG179070A1 (en) | 2009-09-11 | 2012-04-27 | Genentech Inc | Method to identify a patient with an increased likelihood of responding to an anti-cancer agent |
| WO2011056494A1 (en) | 2009-10-26 | 2011-05-12 | Genentech, Inc. | Activin receptor-like kinase-1 antagonist and vegfr3 antagonist combinations |
| WO2011071577A1 (en) | 2009-12-11 | 2011-06-16 | Genentech, Inc. | Anti-vegf-c antibodies and methods using same |
| DK2591099T3 (da) | 2010-07-09 | 2021-02-15 | Bioverativ Therapeutics Inc | Kimære koagulationsfaktorer |
| US8472271B2 (en) | 2011-02-18 | 2013-06-25 | International Business Machines Corporation | Systems and methods for memory device precharging |
| WO2013012733A1 (en) | 2011-07-15 | 2013-01-24 | Biogen Idec Ma Inc. | Heterodimeric fc regions, binding molecules comprising same, and methods relating thereto |
| HRP20180937T1 (hr) | 2012-01-10 | 2018-08-10 | Biogen Ma Inc. | Poboljšavanje transporta terapijskih molekula kroz krvno-moždanu barijeru |
| MX368730B (es) | 2013-02-18 | 2019-10-14 | Vegenics Pty Ltd | Moleculas que unen ligando y usos de las mismas. |
| TWI788044B (zh) | 2013-03-15 | 2022-12-21 | 美商百歐維拉提夫治療公司 | 因子ｉｘ多肽調配物 |
| EP2994758B1 (en) | 2013-05-08 | 2017-12-20 | Opthea Limited | Biomarkers for age-related macular degeneration (amd) |
| KR20220061248A (ko) | 2013-07-12 | 2022-05-12 | 이베릭 바이오, 인크. | 안과적 질환을 치료하거나 예방하기 위한 방법 |
| KR102131370B1 (ko) | 2013-10-18 | 2020-07-08 | 삼성전자주식회사 | Vegf-c에 특이적으로 결합하는 폴리펩타이드 및 그의 용도 |
| MA41586A (fr) | 2015-02-04 | 2017-12-13 | Hoffmann La Roche | Oligomères antisens de la protéine tau et leurs utilisations |
| EP3254104B1 (en) | 2015-02-04 | 2021-08-25 | Bristol-Myers Squibb Company | Methods of selecting therapeutic molecules |
| CA3089279A1 (en) | 2018-02-07 | 2019-08-15 | Dana-Farber Cancer Institute, Inc. | Cell-permeable stapled peptide modules for cellular delivery |
Family Cites Families (77)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4399216A (en) | 1980-02-25 | 1983-08-16 | The Trustees Of Columbia University | Processes for inserting DNA into eucaryotic cells and for producing proteinaceous materials |
| US4943529A (en) | 1982-05-19 | 1990-07-24 | Gist-Brocades Nv | Kluyveromyces as a host strain |
| AU2353384A (en) | 1983-01-19 | 1984-07-26 | Genentech Inc. | Amplification in eukaryotic host cells |
| US4713339A (en) | 1983-01-19 | 1987-12-15 | Genentech, Inc. | Polycistronic expression vector construction |
| DD266710A3 (de) | 1983-06-06 | 1989-04-12 | Ve Forschungszentrum Biotechnologie | Verfahren zur biotechnischen Herstellung van alkalischer Phosphatase |
| AU3145184A (en) | 1983-08-16 | 1985-02-21 | Zymogenetics Inc. | High expression of foreign genes in schizosaccharomyces pombe |
| US4879231A (en) | 1984-10-30 | 1989-11-07 | Phillips Petroleum Company | Transformation of yeasts of the genus pichia |
| GB8610600D0 (en) | 1986-04-30 | 1986-06-04 | Novo Industri As | Transformation of trichoderma |
| US4946783A (en) | 1987-01-30 | 1990-08-07 | President And Fellows Of Harvard College | Periplasmic protease mutants of Escherichia coli |
| IL87737A (en) | 1987-09-11 | 1993-08-18 | Genentech Inc | Method for culturing polypeptide factor dependent vertebrate recombinant cells |
| EP0321196A3 (en) | 1987-12-18 | 1990-07-18 | Mycogen Plant Science, Inc. | 780 t-dna gene transcription activator |
| US5169770A (en) | 1987-12-21 | 1992-12-08 | The University Of Toledo | Agrobacterium mediated transformation of germinating plant seeds |
| US5530101A (en) * | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| US5147638A (en) | 1988-12-30 | 1992-09-15 | Oklahoma Medical Research Foundation | Inhibition of tumor growth by blockade of the protein C system |
| ES2038579T3 (es) | 1989-04-28 | 1997-02-16 | Rhein Biotech Proz & Prod Gmbh | Celulas de levadura del genero schwanniomyces. |
| US5332671A (en) | 1989-05-12 | 1994-07-26 | Genetech, Inc. | Production of vascular endothelial cell growth factor and DNA encoding same |
| EP0402226A1 (en) | 1989-06-06 | 1990-12-12 | Institut National De La Recherche Agronomique | Transformation vectors for yeast yarrowia |
| DK168302B1 (da) | 1989-06-29 | 1994-03-07 | Danisco | Fremgangsmåde til indføring af molekyler, især genetisk materiale i planteceller |
| FR2649120B1 (fr) | 1989-06-30 | 1994-01-28 | Cayla | Nouvelle souche et ses mutants de champignons filamenteux, procede de production de proteines recombinantes a l'aide de ladite souche et souches et proteines obtenues selon ce procede |
| US5219739A (en) | 1989-07-27 | 1993-06-15 | Scios Nova Inc. | DNA sequences encoding bVEGF120 and hVEGF121 and methods for the production of bovine and human vascular endothelial cell growth factors, bVEGF120 and hVEGF121 |
| US5194596A (en) | 1989-07-27 | 1993-03-16 | California Biotechnology Inc. | Production of vascular endothelial cell growth factor |
| DK0502036T3 (da) | 1989-11-22 | 1996-05-06 | Genentech Inc | Latens-associeret peptid og anvendelser herfor |
| US5206161A (en) | 1991-02-01 | 1993-04-27 | Genentech, Inc. | Human plasma carboxypeptidase B |
| WO1992014748A1 (en) | 1991-02-22 | 1992-09-03 | American Cyanamid Company | Identification of a novel human receptor tyrosine kinase gene |
| CA2064331C (en) | 1991-03-28 | 2003-02-18 | Marvin L. Bayne | Vascular endothelial cell growth factor c subunit |
| US5185438A (en) * | 1991-04-02 | 1993-02-09 | The Trustees Of Princeton University | Nucleic acids encoding hencatoporetic stem cell receptor flk-2 |
| JPH07504813A (ja) | 1992-01-22 | 1995-06-01 | ニユー・イングランド・デイーコネス・ホスピタル | 新規蛋白質チロシンキナーゼ類 |
| US5326695A (en) | 1992-05-15 | 1994-07-05 | Ludwig Institute For Cancer Research | Platelet derived growth factor agonists |
| US6228609B1 (en) | 1992-07-09 | 2001-05-08 | Systemix, Inc. | Soluble Flk-2 sequence |
| US6824777B1 (en) * | 1992-10-09 | 2004-11-30 | Licentia Ltd. | Flt4 (VEGFR-3) as a target for tumor imaging and anti-tumor therapy |
| US5776755A (en) * | 1992-10-09 | 1998-07-07 | Helsinki University Licensing, Ltd. | FLT4, a receptor tyrosine kinase |
| US6107046A (en) | 1992-10-09 | 2000-08-22 | Orion Corporation | Antibodies to Flt4, a receptor tyrosine kinase and uses thereof |
| CZ291047B6 (cs) | 1992-10-28 | 2002-12-11 | Genentech, Inc. | Farmaceutický prostředek obsahující antagonisty faktoru růstu vaskulárních endoteliálních buněk |
| US6177401B1 (en) | 1992-11-13 | 2001-01-23 | Max-Planck-Gesellschaft Zur Forderung Der Wissenschaften | Use of organic compounds for the inhibition of Flk-1 mediated vasculogenesis and angiogenesis |
| CN1173991C (zh) | 1992-11-13 | 2004-11-03 | 马克斯普朗克科学促进协会 | 作为血管内皮生长因子受体的f1k-1 |
| AU7847494A (en) * | 1993-10-01 | 1995-05-01 | New York University | Novel receptor-type phosphotyrosine phosphatase-sigma |
| AUPM379394A0 (en) | 1994-02-10 | 1994-03-03 | Ludwig Institute For Cancer Research | Immunointeractive molecules - i |
| US5840301A (en) | 1994-02-10 | 1998-11-24 | Imclone Systems Incorporated | Methods of use of chimerized, humanized, and single chain antibodies specific to VEGF receptors |
| US7153827B1 (en) | 1994-03-08 | 2006-12-26 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 and methods of use |
| CN1267550C (zh) * | 1994-03-08 | 2006-08-02 | 人体基因组科学有限公司 | 血管内皮生长因子2 |
| US6608182B1 (en) * | 1994-03-08 | 2003-08-19 | Human Genome Sciences, Inc. | Human vascular endothelial growth factor 2 |
| US6040157A (en) * | 1994-03-08 | 2000-03-21 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| US7186688B1 (en) * | 1994-03-08 | 2007-03-06 | Human Genome Sciences, Inc. | Methods of stimulating angiogenesis in a patient by administering vascular endothelial growth factor 2 |
| US6734285B2 (en) * | 1994-03-08 | 2004-05-11 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 proteins and compositions |
| US5932540A (en) | 1994-03-08 | 1999-08-03 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| US7109308B1 (en) * | 1994-03-08 | 2006-09-19 | Human Genome Sciences, Inc. | Antibodies to human vascular endothelial growth factor 2 |
| ES2263152T3 (es) | 1994-06-09 | 2006-12-01 | Licentia Oy | Anticuerpo monoclonal contra el receptor flt4 tirosina quinasa y su uso en diagnostico y terapia. |
| US6818220B1 (en) * | 1994-11-14 | 2004-11-16 | Licentia Ltd. | Vascular endothelial growth factor C (VEGF-C) protein and gene mutants thereof, and uses thereof |
| US6130071A (en) * | 1997-02-05 | 2000-10-10 | Helsinki University Licensing, Ltd. | Vascular endothelial growth factor C (VEGF-C) ΔCys156 protein and gene, and uses thereof |
| US6245530B1 (en) * | 1995-08-01 | 2001-06-12 | Ludwig Institute For Cancer Research | Receptor ligand |
| US6403088B1 (en) * | 1995-08-01 | 2002-06-11 | Helsinki University Licensing, Ltd. | Antibodies reactive with VEGF-C, a ligand for the Flt4 receptor tyrosine kinase (VEGFR-3) |
| US6221839B1 (en) * | 1994-11-14 | 2001-04-24 | Helsinki University Licensing Ltd. Oy | FIt4 ligand and methods of use |
| US6645933B1 (en) * | 1995-08-01 | 2003-11-11 | Helsinki University Licensing Ltd. Oy | Receptor ligand VEGF-C |
| WO1998033917A1 (en) | 1994-11-14 | 1998-08-06 | The Ludwig Institute For Cancer Research | Vascular endothelial growth factor c (vegf-c) protein and gene, mutants thereof, and uses thereof |
| US5928939A (en) | 1995-03-01 | 1999-07-27 | Ludwig Institute For Cancer Research | Vascular endothelial growth factor-b and dna coding therefor |
| US5607918A (en) * | 1995-03-01 | 1997-03-04 | Ludwig Institute For Cancer Research | Vascular endothelial growth factor-B and DNA coding therefor |
| ES2206558T3 (es) | 1995-03-02 | 2004-05-16 | Amrad Operations Pty.,Ltd. | Nuevo factor de crecimiento y secuencia genetica que lo codifica. |
| EP0873348A4 (en) | 1995-06-06 | 2000-11-08 | Human Genome Sciences Inc | GROWTH FACTOR 3 OF THE HUMAN VASCULAR ENDOTHELIUM |
| US7423125B2 (en) * | 1995-08-01 | 2008-09-09 | Vegenics Limited | Antibodies to VEGF-C |
| US6361946B1 (en) * | 1997-02-05 | 2002-03-26 | Licentia Ltd | Vascular endothelial growth factor C (VEGF-C) protein and gene, mutants thereof, and uses thereof |
| ES2202469T5 (es) * | 1995-09-08 | 2011-06-06 | Genentech, Inc. | Proteína relacionada con el vegf. |
| ES2239338T5 (es) | 1995-09-29 | 2013-05-31 | Vegenics Pty Ltd | Genes regulados y sus usos |
| US6994989B1 (en) * | 1995-11-08 | 2006-02-07 | Immunex Corp. | FLK-1 binding proteins |
| AU1116297A (en) | 1995-11-08 | 1997-05-29 | Immunex Corporation | Flk-1 binding protein |
| AU733322B2 (en) * | 1996-07-15 | 2001-05-10 | Chugai Seiyaku Kabushiki Kaisha | Novel VEGF-like factor |
| DE69734359T2 (de) | 1996-08-23 | 2006-07-06 | Ludwig Institute For Cancer Research | Rekombinanter vaskulärer endothelzellen wachstumsfaktor d (vegf-d) |
| WO1998024811A2 (en) | 1996-12-06 | 1998-06-11 | Zymogenetics, Inc. | Vascular endothelial growth factor |
| KR100244853B1 (ko) * | 1996-12-31 | 2000-02-15 | 구자홍 | 가변형 광원과 그를 이용한 이종 광디스크용광픽업 장치 |
| US7125714B2 (en) * | 1997-02-05 | 2006-10-24 | Licentia Ltd. | Progenitor cell materials and methods |
| WO1998049300A2 (en) | 1997-04-25 | 1998-11-05 | Collateral Therapeutics | Truncated vegf-related proteins |
| DE19748734A1 (de) | 1997-11-05 | 1999-05-06 | Biotechnolog Forschung Gmbh | Verfahren zur Gewinnung von biologisch aktiven Dimeren von rekombinanten humanen Wachstumsfaktoren aus der Cystein-Knoten-Familie sowie Verwendung der gewonnenen Dimere |
| JP2002505873A (ja) | 1998-03-13 | 2002-02-26 | ヒューマン ジノーム サイエンシーズ， インコーポレイテッド | 血管内皮増殖因子２ |
| FR2777904B1 (fr) * | 1998-04-24 | 2000-12-15 | Millipore Sa | Cassette ainsi que procede et appareil d'analyse de l'air l'utilisant |
| NZ511408A (en) | 1998-10-09 | 2004-04-30 | Licentia Ltd | Flt4 (VEGFR-3) as a target for tumor imaging and anti-tumor therapy |
| DE60219419T2 (de) | 2001-01-19 | 2007-08-16 | Ludwig Institute For Cancer Research | Flt4 (vegfr-3) als ein ziel für krebsdarstellung und anti-krebs-behandlung |
| US7142876B2 (en) * | 2003-03-03 | 2006-11-28 | Nokia Corporation | Location dependent services |
| TW200829215A (en) | 2007-01-03 | 2008-07-16 | Univ Nat Chiao Tung | Micro probe array and manufacturing method of the trans-print mold thereof |
-
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- 1996-08-30 DK DK96931450.9T patent/DK0848755T4/da active
- 1996-08-30 JP JP9511317A patent/JPH11514976A/ja not_active Withdrawn
- 1996-08-30 AT AT96931450T patent/ATE242809T1/de not_active IP Right Cessation
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- 1996-08-30 US US08/706,054 patent/US6451764B1/en not_active Expired - Fee Related
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- 2003-01-17 US US10/346,802 patent/US20030166873A1/en not_active Abandoned
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- 2008-03-03 JP JP2008052407A patent/JP2008228730A/ja not_active Withdrawn
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- 2008-08-21 AU AU2008207460A patent/AU2008207460B2/en not_active Ceased
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