JPH11513883A - ヒト血管内皮増殖因子２ - Google Patents
ヒト血管内皮増殖因子２Info
- Publication number
- JPH11513883A JPH11513883A JP9501427A JP50142797A JPH11513883A JP H11513883 A JPH11513883 A JP H11513883A JP 9501427 A JP9501427 A JP 9501427A JP 50142797 A JP50142797 A JP 50142797A JP H11513883 A JPH11513883 A JP H11513883A
- Authority
- JP
- Japan
- Prior art keywords
- polypeptide
- polynucleotide
- vegf2
- dna
- cells
- Prior art date
- Legal status (The legal status 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 status listed.)
- Withdrawn
Links
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Landscapes
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Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US08/465,968 | 1995-06-06 | ||
| US08/465,968 US6608182B1 (en) | 1994-03-08 | 1995-06-06 | Human vascular endothelial growth factor 2 |
| PCT/US1996/009001 WO1996039515A1 (en) | 1995-06-06 | 1996-06-06 | Human vascular endothelial growth factor 2 |
Related Child Applications (2)
| Application Number | Title | Priority Date | Filing Date |
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| JP11147333A Division JP2000069982A (ja) | 1995-06-06 | 1999-05-26 | ヒト血管内皮増殖因子２ |
| JP2007106593A Division JP2007244388A (ja) | 1995-06-06 | 2007-04-13 | ヒト血管内皮増殖因子２ |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH11513883A true JPH11513883A (ja) | 1999-11-30 |
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| Application Number | Title | Priority Date | Filing Date |
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| JP9501427A Withdrawn JPH11513883A (ja) | 1995-06-06 | 1996-06-06 | ヒト血管内皮増殖因子２ |
| JP11147333A Withdrawn JP2000069982A (ja) | 1995-06-06 | 1999-05-26 | ヒト血管内皮増殖因子２ |
| JP2007106593A Pending JP2007244388A (ja) | 1995-06-06 | 2007-04-13 | ヒト血管内皮増殖因子２ |
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| Application Number | Title | Priority Date | Filing Date |
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| JP11147333A Withdrawn JP2000069982A (ja) | 1995-06-06 | 1999-05-26 | ヒト血管内皮増殖因子２ |
| JP2007106593A Pending JP2007244388A (ja) | 1995-06-06 | 2007-04-13 | ヒト血管内皮増殖因子２ |
Country Status (10)
| Country | Link |
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| US (3) | US6608182B1 (enExample) |
| EP (1) | EP0837934B1 (enExample) |
| JP (3) | JPH11513883A (enExample) |
| KR (1) | KR100511692B1 (enExample) |
| CN (2) | CN1186518A (enExample) |
| AT (1) | ATE347595T1 (enExample) |
| AU (1) | AU714484B2 (enExample) |
| CA (1) | CA2224093C (enExample) |
| DE (1) | DE69636752T2 (enExample) |
| WO (1) | WO1996039515A1 (enExample) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2007244388A (ja) * | 1995-06-06 | 2007-09-27 | Human Genome Sciences Inc | ヒト血管内皮増殖因子２ |
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| US6824777B1 (en) | 1992-10-09 | 2004-11-30 | Licentia Ltd. | Flt4 (VEGFR-3) as a target for tumor imaging and anti-tumor therapy |
| US5932540A (en) | 1994-03-08 | 1999-08-03 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| JPH09510093A (ja) | 1994-03-08 | 1997-10-14 | 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 | 血管内皮細胞増殖因子２ |
| US7109308B1 (en) * | 1994-03-08 | 2006-09-19 | Human Genome Sciences, Inc. | Antibodies to human vascular endothelial growth factor 2 |
| US7153827B1 (en) | 1994-03-08 | 2006-12-26 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 and methods of use |
| 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 |
| 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 |
| US7597886B2 (en) | 1994-11-07 | 2009-10-06 | Human Genome Sciences, Inc. | Tumor necrosis factor-gamma |
| 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 |
| 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 |
| 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 |
| 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 |
| US7429646B1 (en) | 1995-06-05 | 2008-09-30 | Human Genome Sciences, Inc. | Antibodies to human tumor necrosis factor receptor-like 2 |
| 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 |
| AU2003201371B2 (en) * | 1995-08-01 | 2007-03-01 | Helsinki University Licensing Ltd. Oy | Receptor Ligand VEGF-C |
| US7727761B2 (en) | 1995-08-01 | 2010-06-01 | Vegenics Limited | Vascular endothelial growth factor C (VEGF-C) protein and gene, mutants thereof, and uses thereof |
| AU755708B2 (en) * | 1995-08-01 | 2002-12-19 | Vegenics Limited | Receptor ligand VEGF-C |
| US6451764B1 (en) * | 1995-09-08 | 2002-09-17 | Genentech, Inc. | VEGF-related protein |
| US6994989B1 (en) | 1995-11-08 | 2006-02-07 | Immunex Corp. | FLK-1 binding proteins |
| WO1997017442A1 (en) | 1995-11-08 | 1997-05-15 | Immunex Corporation | Flk-1 binding protein |
| WO1997033904A1 (en) | 1996-03-12 | 1997-09-18 | Human Genome Sciences, Inc. | Death domain containing receptors |
| US6713061B1 (en) | 1996-03-12 | 2004-03-30 | Human Genome Sciences, Inc. | Death domain containing receptors |
| US7357927B2 (en) | 1996-03-12 | 2008-04-15 | Human Genome Sciences, Inc. | Death domain containing receptors |
| US6635743B1 (en) | 1996-03-22 | 2003-10-21 | Human Genome Sciences, Inc. | Apoptosis inducing molecule II and methods of use |
| US7964190B2 (en) | 1996-03-22 | 2011-06-21 | Human Genome Sciences, Inc. | Methods and compositions for decreasing T-cell activity |
| US20060171907A1 (en) * | 1996-11-21 | 2006-08-03 | The Procter & Gamble Company | Oral care compositions providing enhanced whitening and stain prevention |
| US7125714B2 (en) | 1997-02-05 | 2006-10-24 | Licentia Ltd. | Progenitor cell materials and methods |
| AU6691098A (en) * | 1997-03-07 | 1998-09-22 | Wistar Institute Of Anatomy & Biology, The | Method and compositions for healing tissue defects and inducing hypervascularityin mammalian tissue |
| US6676937B1 (en) | 1998-03-09 | 2004-01-13 | Caritas St. Elizabeth's Medical Center Of Boston Inc. | Compositions and methods for modulating vascularization |
| WO1999046364A1 (en) * | 1998-03-13 | 1999-09-16 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| CN100340291C (zh) | 1998-10-09 | 2007-10-03 | 路德维格癌症研究院 | F1t4(VEGFR－3)作为肿瘤显像和抗肿瘤治疗的靶 |
| US6958147B1 (en) | 1998-10-26 | 2005-10-25 | Licentia Ltd | Use of VEGF-C to prevent restenosis |
| US6783953B1 (en) | 1998-12-22 | 2004-08-31 | Janssen Pharmaceutica N.V. | Vascular endothelial growth factor-X |
| US7223724B1 (en) * | 1999-02-08 | 2007-05-29 | Human Genome Sciences, Inc. | Use of vascular endothelial growth factor to treat photoreceptor cells |
| JP2002537769A (ja) | 1999-02-26 | 2002-11-12 | 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 | ヒトエンドカインαおよび使用方法 |
| 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) |
| ATE377081T1 (de) * | 2000-02-25 | 2007-11-15 | Ludwig Inst Cancer Res | Material und verfahren die hybridvaskularendothelwachstumfaktoren dns und proteine enthalten und screeningverfahren für modulatoren |
| US7288521B2 (en) * | 2000-04-06 | 2007-10-30 | Franco Wayne P | Growth factor therapy mobilization of stem cells into the peripheral blood |
| US7291597B2 (en) * | 2000-04-06 | 2007-11-06 | Franco Wayne P | Growth factor therapy mobilization of stem cells into the peripheral blood |
| AU2001264563A1 (en) | 2000-04-12 | 2001-10-30 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| CN1211126C (zh) * | 2000-08-04 | 2005-07-20 | 人体基因组科学有限公司 | 血管内皮生长因子2 |
| AU2884102A (en) | 2000-12-07 | 2002-06-18 | 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 |
| JP4669984B2 (ja) * | 2001-01-19 | 2011-04-13 | ベジェニクス リミテッド | 腫瘍画像化のターゲットとしてのＦ１ｔ４（ＶＥＧＦＲ−３）および抗腫瘍療法 |
| KR20030093316A (ko) | 2001-04-13 | 2003-12-06 | 휴먼 게놈 사이언시즈, 인코포레이티드 | 혈관 내피 성장 인자 ２ |
| US7402312B2 (en) | 2001-04-13 | 2008-07-22 | Human Genome Sciences, Inc. | Antibodies to vascular endothelial growth factor 2 (VEGF-2) |
| CA2444624A1 (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 |
| EP1425580A4 (en) * | 2001-07-12 | 2006-03-29 | Ludwig Inst Cancer Res | LYMPHATIC ENDOTHELIAL CELLS AND METHODS THEREOF |
| US7217570B2 (en) | 2001-08-23 | 2007-05-15 | The Wistar Institute Of Anatomy And Biology | Organotypic intestinal culture and methods of use thereof |
| US20040214766A1 (en) * | 2001-10-01 | 2004-10-28 | Kari Alitalo | VEGF-C or VEGF-D materials and methods for treatment of neuropathologies |
| US20030113324A1 (en) * | 2001-10-01 | 2003-06-19 | Kari Alitalo | Neuropilin/VEGF-C/VEGFR-3 materials and methods |
| ES2545090T3 (es) | 2001-12-21 | 2015-09-08 | Human Genome Sciences, Inc. | Proteínas de fusión de albúmina y GCSF |
| JP4643255B2 (ja) | 2002-06-10 | 2011-03-02 | バクシネックス インコーポレーティッド | 乳癌および膀胱癌において差次的に発現される遺伝子ならびにコードされるポリペプチド |
| US20040120950A1 (en) * | 2002-12-20 | 2004-06-24 | Kari Alitalo | Modulation of VEGF-C/VEGFR-3 interactions in the treatment of rheumatoid arthritis |
| JP2006517586A (ja) * | 2003-02-04 | 2006-07-27 | ラドウィグ インスティテュート フォー キャンサー リサーチ | 幹細胞のｖｅｇｆ−ｂ及びｐｄｇｆ調節 |
| US20050032697A1 (en) * | 2003-06-12 | 2005-02-10 | Kari Alitalo | Heparin binding VEGFR-3 ligands |
| EP1635860A2 (en) * | 2003-06-12 | 2006-03-22 | Ludwig Institute For Cancer Research | Use of vegf-c or vegf-d in reconstructive surgery |
| US7597884B2 (en) | 2004-08-09 | 2009-10-06 | Alios Biopharma, Inc. | Hyperglycosylated polypeptide variants and methods of use |
| US7358085B2 (en) | 2005-02-28 | 2008-04-15 | Sangamo Biosciences, Inc. | Anti-angiogenic methods and compositions |
| SG161258A1 (en) * | 2005-06-21 | 2010-05-27 | Pervasis Therapeutics Inc | Methods and compositions for enhancing vascular access |
| US8637026B2 (en) | 2007-12-26 | 2014-01-28 | Vaccinex, Inc. | Anti-C35 antibody combination therapies and methods |
| EP2310507A4 (en) | 2008-07-08 | 2013-03-20 | David Gladstone Inst | METHOD AND COMPOSITIONS FOR ANGIOGENIC MODULATION |
| CA2901226C (en) | 2013-02-18 | 2020-11-17 | Vegenics Pty Limited | Vascular endothelial growth factor binding proteins |
| CN108339154A (zh) * | 2017-01-25 | 2018-07-31 | 中国科学院遗传与发育生物学研究所 | 一种诱导颅脑损伤组织再生的功能生物材料及其应用 |
| CN111303271B (zh) * | 2020-02-19 | 2022-02-01 | 西安交通大学医学院第一附属医院 | 一种用于治疗肺纤维化的血小板源性生长因子重组疫苗及其应用 |
Family Cites Families (66)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0186084B1 (en) | 1984-12-24 | 1991-09-04 | Merck & Co. Inc. | Brain-derived growth factor |
| US5073492A (en) | 1987-01-09 | 1991-12-17 | The Johns Hopkins University | Synergistic composition for endothelial cell growth |
| JPS6438100A (en) | 1987-07-31 | 1989-02-08 | Toray Industries | Vascular endothelial cell growth factor |
| JPH02117698A (ja) | 1988-10-27 | 1990-05-02 | Toray Ind Inc | 血管内皮細胞成長因子 |
| US5240848A (en) | 1988-11-21 | 1993-08-31 | Monsanto Company | Dna sequences encoding human vascular permeability factor having 189 amino acids |
| US5693622A (en) | 1989-03-21 | 1997-12-02 | Vical Incorporated | Expression of exogenous polynucleotide sequences cardiac muscle of a mammal |
| EP0399816B1 (en) | 1989-05-24 | 1995-12-20 | Merck & Co. Inc. | Purification and characterization of a glioma-derived growth factor |
| 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 |
| DE69132040T2 (de) | 1990-09-21 | 2000-11-02 | Merck & Co., Inc. | Wachstumsfaktor II für vaskuläre Endothelzellen |
| WO1992014748A1 (en) | 1991-02-22 | 1992-09-03 | American Cyanamid Company | Identification of a novel human receptor tyrosine kinase gene |
| EP0506477B1 (en) | 1991-03-28 | 1999-06-23 | Merck & Co. Inc. | 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 |
| US5234908A (en) | 1991-04-12 | 1993-08-10 | Creative Biomolecules, Inc. | Method of treating gastrointestinal ulcers with platelet derived growth factor |
| US5661133B1 (en) | 1991-11-12 | 1999-06-01 | Univ Michigan | Collateral blood vessel formation in cardiac muscle by injecting a dna sequence encoding an angiogenic protein |
| US5861301A (en) | 1992-02-20 | 1999-01-19 | American Cayanamid Company | Recombinant kinase insert domain containing receptor and gene encoding same |
| US5326695A (en) * | 1992-05-15 | 1994-07-05 | Ludwig Institute For Cancer Research | Platelet derived growth factor agonists |
| US5776755A (en) * | 1992-10-09 | 1998-07-07 | Helsinki University Licensing, Ltd. | FLT4, a receptor tyrosine kinase |
| WO1994011506A1 (en) | 1992-11-18 | 1994-05-26 | Arch Development Corporation | Adenovirus-mediated gene transfer to cardiac and vascular smooth muscle |
| US5922572A (en) | 1994-01-25 | 1999-07-13 | Human Genome Sciences, Inc. | Polynucleotides encoding haemopoietic maturation factor |
| US6608182B1 (en) | 1994-03-08 | 2003-08-19 | Human Genome Sciences, Inc. | Human vascular endothelial growth factor 2 |
| US5633147A (en) | 1994-03-08 | 1997-05-27 | Human Genome Sciences, Inc. | Transforming growth factor αH1 |
| JPH09510093A (ja) | 1994-03-08 | 1997-10-14 | 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 | 血管内皮細胞増殖因子２ |
| US5932540A (en) | 1994-03-08 | 1999-08-03 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| US5817485A (en) | 1994-03-08 | 1998-10-06 | Human Genome Sciences, Inc. | Nucleic acids and cells for recombinant production of fibroblast growth factor-10 |
| US6040157A (en) | 1994-03-08 | 2000-03-21 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| ATE262345T1 (de) | 1994-08-23 | 2004-04-15 | Human Genome Sciences Inc | Menschliche chemokin-polypeptide |
| US5652225A (en) | 1994-10-04 | 1997-07-29 | St. Elizabeth's Medical Center Of Boston, Inc. | Methods and products for nucleic acid delivery |
| 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 |
| 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 |
| 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) |
| US6645933B1 (en) * | 1995-08-01 | 2003-11-11 | Helsinki University Licensing Ltd. Oy | Receptor ligand VEGF-C |
| US5792453A (en) | 1995-02-28 | 1998-08-11 | The Regents Of The University Of California | Gene transfer-mediated angiogenesis therapy |
| 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 |
| EP2258726A1 (en) | 1995-06-14 | 2010-12-08 | The Regents of the University of California | High affinity human antibodies to c-erbB-2 |
| 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 |
| DE69621940T2 (de) | 1995-08-18 | 2003-01-16 | Morphosys Ag | Protein-/(poly)peptidbibliotheken |
| US6451764B1 (en) | 1995-09-08 | 2002-09-17 | Genentech, Inc. | VEGF-related protein |
| US6121246A (en) | 1995-10-20 | 2000-09-19 | St. Elizabeth's Medical Center Of Boston, Inc. | Method for treating ischemic tissue |
| WO1997017442A1 (en) | 1995-11-08 | 1997-05-15 | Immunex Corporation | Flk-1 binding protein |
| US5641750A (en) | 1995-11-29 | 1997-06-24 | Amgen Inc. | Methods for treating photoreceptors using glial cell line-derived neurotrophic factor (GDNF) protein product |
| ES2212121T3 (es) | 1996-08-13 | 2004-07-16 | Human Genome Sciences, Inc. | Mutantes de factor-2 de crecimiento queranocitico (kgf-2 o factor -12 de crecimiento fibroblastico, fgf-12). |
| EP2107109B1 (en) | 1996-08-23 | 2012-06-20 | Vegenics Pty Ltd | Recombinant vascular endothelial cell growth factor D (VEGF-D) |
| WO1998024811A2 (en) | 1996-12-06 | 1998-06-11 | Zymogenetics, Inc. | Vascular endothelial growth factor |
| AU6691098A (en) | 1997-03-07 | 1998-09-22 | Wistar Institute Of Anatomy & Biology, The | Method and compositions for healing tissue defects and inducing hypervascularityin mammalian tissue |
| NZ500530A (en) | 1997-04-25 | 2001-12-21 | Collateral Therapeutics | Truncated VEGF-B, VEGF-C, VEGF-3, PlGF, VRF-2, poxvirus ORF-1 and ORF-2 proteins |
| WO1998055619A1 (de) | 1997-06-06 | 1998-12-10 | Asat Ag Applied Science & Technology | Anti-gpiib/iiia rekombinante antikörper |
| EP0990042A1 (en) | 1997-06-10 | 2000-04-05 | Max-Planck-Gesellschaft zur Förderung der Wissenschaften e.V. | Regulatory sequences involved in hypoxia regulated gene expression and uses thereof |
| AU7927398A (en) | 1997-07-08 | 1999-02-08 | Viventia Biotech Inc. | Antigen binding fragments, designated 4b5, that specifically detect cancer cells, nucleotides encoding the fragments, and use thereof for the prophylaxis and detection of cancers |
| CA2300964A1 (en) | 1997-08-15 | 1999-02-25 | Ludwig Institute For Cancer Research | Stimulation, modulation and/or inhibition of endothelial proteolytic activity and/or angiogenic activity |
| GB9722131D0 (en) | 1997-10-20 | 1997-12-17 | Medical Res Council | Method |
| CA2307953A1 (en) | 1997-10-27 | 1999-05-06 | Merck & Co., Inc. | Gene therapy for stimulation of angiogenesis |
| WO1999046364A1 (en) | 1998-03-13 | 1999-09-16 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| KR20010101981A (ko) | 1999-02-08 | 2001-11-15 | 벤슨 로버트 에이치. | 혈관 내피 성장 인자-2 |
| CA2375033A1 (en) | 1999-05-27 | 2000-12-07 | Max-Delbruck-Centrum Fur Molekulare Medizin | Vaccines against conformation-dependent antigens and against antigens that are not or are not only proteins or peptides |
| JP2003509011A (ja) | 1999-06-03 | 2003-03-11 | 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 | 脈管形成タンパク質およびそれらの使用 |
| EP1255844B1 (en) | 2000-02-03 | 2007-09-19 | Millennium Pharmaceuticals, Inc. | Humanized anti-ccr2 antibodies and methods of use therefor |
| EP2332579A3 (en) | 2000-02-10 | 2011-09-21 | Abbott Laboratories | Antibodies that bind human interleukin-18 and methods of making and using |
| CN1211126C (zh) | 2000-08-04 | 2005-07-20 | 人体基因组科学有限公司 | 血管内皮生长因子2 |
| CA2444624A1 (en) | 2001-04-13 | 2002-10-24 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| AU2002256172A1 (en) | 2001-04-13 | 2002-10-28 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| KR20030093316A (ko) | 2001-04-13 | 2003-12-06 | 휴먼 게놈 사이언시즈, 인코포레이티드 | 혈관 내피 성장 인자 ２ |
| WO2003097660A1 (en) | 2002-04-12 | 2003-11-27 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
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1996
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2007244388A (ja) * | 1995-06-06 | 2007-09-27 | Human Genome Sciences Inc | ヒト血管内皮増殖因子２ |
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| US6608182B1 (en) | 2003-08-19 |
| EP0837934B1 (en) | 2006-12-06 |
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| EP0837934A4 (en) | 2000-11-02 |
| KR100511692B1 (ko) | 2005-12-27 |
| US7115392B2 (en) | 2006-10-03 |
| US20100143360A1 (en) | 2010-06-10 |
| MX9709243A (es) | 1998-03-31 |
| CN1186518A (zh) | 1998-07-01 |
| EP0837934A1 (en) | 1998-04-29 |
| ATE347595T1 (de) | 2006-12-15 |
| AU714484B2 (en) | 2000-01-06 |
| WO1996039515A1 (en) | 1996-12-12 |
| CA2224093A1 (en) | 1996-12-12 |
| JP2007244388A (ja) | 2007-09-27 |
| JP2000069982A (ja) | 2000-03-07 |
| DE69636752T2 (de) | 2007-10-11 |
| CA2224093C (en) | 2003-03-25 |
| AU6046796A (en) | 1996-12-24 |
| KR19990022522A (ko) | 1999-03-25 |
| DE69636752D1 (de) | 2007-01-18 |
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