CN1314806C - 小型化抗eb病毒肿瘤多肽及其应用与制备方法 - Google Patents
小型化抗eb病毒肿瘤多肽及其应用与制备方法 Download PDFInfo
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- CN1314806C CN1314806C CNB200510020168XA CN200510020168A CN1314806C CN 1314806 C CN1314806 C CN 1314806C CN B200510020168X A CNB200510020168X A CN B200510020168XA CN 200510020168 A CN200510020168 A CN 200510020168A CN 1314806 C CN1314806 C CN 1314806C
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Images
Classifications
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- C07K16/081—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses from DNA viruses
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- A61K47/68—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment
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- C—CHEMISTRY; METALLURGY
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- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
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Abstract
Description
Claims (21)
Priority Applications (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CNB200510020168XA CN1314806C (zh) | 2005-01-14 | 2005-01-14 | 小型化抗eb病毒肿瘤多肽及其应用与制备方法 |
US11/333,487 US20060193867A1 (en) | 2004-12-10 | 2006-01-17 | Antiviral bifunctional molecules, methods of construction and methods of treating virus-induced cancer therewith |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CNB200510020168XA CN1314806C (zh) | 2005-01-14 | 2005-01-14 | 小型化抗eb病毒肿瘤多肽及其应用与制备方法 |
Publications (2)
Publication Number | Publication Date |
---|---|
CN1661012A CN1661012A (zh) | 2005-08-31 |
CN1314806C true CN1314806C (zh) | 2007-05-09 |
Family
ID=35010564
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
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CNB200510020168XA Expired - Fee Related CN1314806C (zh) | 2004-12-10 | 2005-01-14 | 小型化抗eb病毒肿瘤多肽及其应用与制备方法 |
Country Status (2)
Country | Link |
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US (1) | US20060193867A1 (zh) |
CN (1) | CN1314806C (zh) |
Families Citing this family (9)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN1274829C (zh) * | 2004-12-10 | 2006-09-13 | 四川大学华西医院 | 抗eb病毒所致肿瘤多肽及其应用与制备方法 |
WO2007083175A1 (en) * | 2006-01-17 | 2007-07-26 | West China Hospital, Sichuan University | Antiviral bifunctional molecules, methods of construction and methods of treating virus-induced cancer therewith |
WO2009014835A2 (en) * | 2007-06-21 | 2009-01-29 | Angelica Therapeutics, Inc. | Modified toxins |
EP2268297A4 (en) * | 2008-02-29 | 2011-11-16 | Angelica Therapeutics Inc | MODIFIED TOXINS |
CN102101888B (zh) * | 2009-12-17 | 2013-03-20 | 畿晋庆三联(北京)生物技术有限公司 | 一种新型抗eb病毒所致肿瘤多肽及其应用与制备方法 |
US9200251B1 (en) | 2011-03-31 | 2015-12-01 | David Gordon Bermudes | Bacterial methionine analogue and methionine synthesis inhibitor anticancer, antiinfective and coronary heart disease protective microcins and methods of treatment therewith |
JP2016519651A (ja) | 2013-03-15 | 2016-07-07 | アンジェリカ セラピューティックス,インク. | 改質された毒素 |
CN106532101A (zh) * | 2016-12-03 | 2017-03-22 | 合肥国轩高科动力能源有限公司 | 一种去除轧辊表面粘滞物料的溶液及其制备方法 |
CN110172513A (zh) * | 2019-05-30 | 2019-08-27 | 浙江自贸区锐赛生物医药科技有限公司 | 突变型免疫多肽临床入组的筛选方法 |
Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
EP0247873A2 (en) * | 1986-05-28 | 1987-12-02 | The University Of Toronto Innovations Foundation | Bacteriocins and compositions thereof in anti-viral treatment |
CN1396178A (zh) * | 2002-06-17 | 2003-02-12 | 成都阳辉生物科技有限责任公司 | 抗乙肝病毒等包膜病毒感染的工程多肽及其制备方法 |
CN1482242A (zh) * | 2002-06-17 | 2004-03-17 | 成都阳辉生物科技有限责任公司 | 一种重组抗包膜病毒多肽及其制备方法 |
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2005
- 2005-01-14 CN CNB200510020168XA patent/CN1314806C/zh not_active Expired - Fee Related
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2006
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Patent Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
EP0247873A2 (en) * | 1986-05-28 | 1987-12-02 | The University Of Toronto Innovations Foundation | Bacteriocins and compositions thereof in anti-viral treatment |
CN1396178A (zh) * | 2002-06-17 | 2003-02-12 | 成都阳辉生物科技有限责任公司 | 抗乙肝病毒等包膜病毒感染的工程多肽及其制备方法 |
CN1482242A (zh) * | 2002-06-17 | 2004-03-17 | 成都阳辉生物科技有限责任公司 | 一种重组抗包膜病毒多肽及其制备方法 |
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