JP2010500880A5 - - Google Patents
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- JP2010500880A5 JP2010500880A5 JP2009524682A JP2009524682A JP2010500880A5 JP 2010500880 A5 JP2010500880 A5 JP 2010500880A5 JP 2009524682 A JP2009524682 A JP 2009524682A JP 2009524682 A JP2009524682 A JP 2009524682A JP 2010500880 A5 JP2010500880 A5 JP 2010500880A5
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- JP
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- Prior art keywords
- glycans
- polypeptide
- glycan
- binding
- neu5acα2
- 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.)
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| KR (1) | KR20090050056A (cg-RX-API-DMAC7.html) |
| AU (2) | AU2007332987B2 (cg-RX-API-DMAC7.html) |
| CA (2) | CA2660038A1 (cg-RX-API-DMAC7.html) |
| IL (1) | IL196738A0 (cg-RX-API-DMAC7.html) |
| WO (2) | WO2008073161A2 (cg-RX-API-DMAC7.html) |
Families Citing this family (35)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP5174014B2 (ja) * | 2006-05-30 | 2013-04-03 | ボゴーク，サミュエル | レプリキンペプチドおよびその使用 |
| EP2092059A4 (en) * | 2006-10-24 | 2012-03-28 | Bogoch Samuel | METHOD FOR FORECASTING INFLUENZA EXCESSIONS BY CORRELATION OF AN INCREASED REPLICINE MIRROR IN WHITE SPOT AND / OR TAURA VIRUSES IN CRABES |
| US20090017052A1 (en) * | 2007-01-18 | 2009-01-15 | Samuel Bogoch | Methods of determining lethality of pathogens and malignancies involving replikin peak genes |
| NZ581332A (en) * | 2007-05-30 | 2012-06-29 | Samuel Bogoch | Synthetic replikin peptides against pathogenic infection of invertebrates in aquaculture |
| WO2009089119A2 (en) * | 2008-01-03 | 2009-07-16 | Massachusetts Institute Of Technology | Decoy influenza therapies |
| CA2711334A1 (en) * | 2008-01-03 | 2009-07-16 | Massachusetts Institute Of Technology | Hemagglutinin polypeptides, and reagents and methods relating thereto |
| US20090269367A1 (en) * | 2008-04-23 | 2009-10-29 | Samuel Bogoch | Methods and compounds for mitigating pathogenic outbreaks using replikin count cycles |
| US20100144589A1 (en) * | 2008-08-08 | 2010-06-10 | Samuel Bogoch | Methods of predicting cancer lethality using replikin counts |
| US9233148B2 (en) * | 2009-01-09 | 2016-01-12 | Samuel Bogoch | Replikin-based compounds for prevention and treatment of influenza and methods of differentiating infectivity and lethality in influenza |
| JP5396111B2 (ja) * | 2009-03-12 | 2014-01-22 | 学校法人慶應義塾 | インフルエンザ治療／予防薬 |
| CN103200961B (zh) * | 2009-03-27 | 2017-10-27 | 中央研究院 | 抗病毒免疫的方法和组合物 |
| WO2010123519A1 (en) * | 2009-04-23 | 2010-10-28 | Samuel Bogoch | Replikin-sequences for preventing/treating influenza and determining infectivity/lethality |
| EP2448596B1 (en) * | 2009-07-02 | 2016-01-06 | Massachusetts Institute of Technology | Compositions and methods for diagnosing and/or treating influenza infection |
| CN103977394B (zh) * | 2009-07-17 | 2016-03-09 | 翰林大学校产学协力团 | 包含脂质体包胶的寡核苷酸和表位的免疫刺激性组合物 |
| US9320784B2 (en) | 2009-08-07 | 2016-04-26 | Samuel Bogoch | Peptides shared among lethal cancers and therapeutic compositions comprising said peptides |
| US20110091493A1 (en) * | 2009-10-16 | 2011-04-21 | Northwestern University | Vaccine compositions and uses thereof |
| WO2011094445A1 (en) | 2010-01-27 | 2011-08-04 | Massachusetts Institute Of Technology | Engineered polypeptide agents for targeted broad spectrum influenza neutralization |
| EP2640405A4 (en) | 2010-09-21 | 2015-04-15 | Massachusetts Inst Technology | HA-POLYPEPTIDES ADAPTED TO HUMANS, VACCINES THEREOF AND INFLUENZA TREATMENT THEREWITH |
| SG10201709806VA (en) * | 2010-10-04 | 2017-12-28 | Massachusetts Inst Technology | Hemagglutinin polypeptides, and reagents and methods relating thereto |
| TWI537385B (zh) | 2010-11-04 | 2016-06-11 | 中央研究院 | 產生具簡單醣基化之表面蛋白質之病毒顆粒的方法 |
| WO2012082634A1 (en) | 2010-12-13 | 2012-06-21 | University Of Utah Research Foundation | Vaccine antigens that direct immunity to conserved epitopes |
| CN104144941B (zh) | 2012-02-13 | 2017-06-09 | 高等教育联邦系统-匹兹堡大学 | 以计算方式优化的人和禽h5n1流感的广泛反应性抗原 |
| SG11201405317QA (en) * | 2012-02-29 | 2014-09-26 | Agency Science Tech & Res | Modulating the interaction between zo-2/tjp2 and a snail zinc finger transcription factor family member |
| CA2871160C (en) | 2012-05-10 | 2023-03-14 | Massachusetts Institute Of Technology | Agents for influenza neutralization |
| US9969794B2 (en) | 2012-05-10 | 2018-05-15 | Visterra, Inc. | HA binding agents |
| MX358772B (es) | 2012-07-19 | 2018-09-04 | Toray Industries | Metodo para detectar cancer. |
| US20140286981A1 (en) | 2013-03-14 | 2014-09-25 | Wisconsin Alumni Research Foundation | Broadly reactive mosaic peptide for influenza vaccine |
| WO2014197723A2 (en) | 2013-06-05 | 2014-12-11 | Massachusetts Institute Of Technology | Human adaptation of h7 ha |
| EP3916390A1 (en) * | 2014-06-04 | 2021-12-01 | Indevr, Inc. | Universal capture array for multiplexed subtype-specific quantification and stability determination of influenza proteins |
| JP6964581B2 (ja) * | 2015-08-20 | 2021-11-10 | シーラス ロジック インターナショナル セミコンダクター リミテッド | 固定応答フィルタによって部分的に提供されるフィードバック応答を有するフィードバック適応雑音消去（ａｎｃ）コントローラおよび方法 |
| US10513553B2 (en) | 2015-11-13 | 2019-12-24 | Visterra, Inc. | Compositions and methods for treating and preventing influenza |
| AU2017222564A1 (en) | 2016-02-24 | 2018-09-06 | Visterra, Inc. | Formulations of antibody molecules to influenza virus |
| ES2991988T3 (es) | 2017-10-30 | 2024-12-05 | Takeda Pharmaceuticals Co | Detergentes compatibles con el medio ambiente para la inactivación de virus con envoltura lipídica |
| EP3946613A1 (en) | 2019-03-25 | 2022-02-09 | Visterra, Inc. | Compositions and methods for treating and preventing influenza |
| US20230257449A1 (en) | 2019-12-11 | 2023-08-17 | Visterra, Inc. | Compositions and methods for treating and preventing influenza |
Family Cites Families (38)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4166452A (en) * | 1976-05-03 | 1979-09-04 | Generales Constantine D J Jr | Apparatus for testing human responses to stimuli |
| US4270537A (en) * | 1979-11-19 | 1981-06-02 | Romaine Richard A | Automatic hypodermic syringe |
| US4816567A (en) * | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US4596556A (en) * | 1985-03-25 | 1986-06-24 | Bioject, Inc. | Hypodermic injection apparatus |
| US4886499A (en) * | 1986-12-18 | 1989-12-12 | Hoffmann-La Roche Inc. | Portable injection appliance |
| GB8704027D0 (en) * | 1987-02-20 | 1987-03-25 | Owen Mumford Ltd | Syringe needle combination |
| US4790824A (en) * | 1987-06-19 | 1988-12-13 | Bioject, Inc. | Non-invasive hypodermic injection device |
| US4941880A (en) * | 1987-06-19 | 1990-07-17 | Bioject, Inc. | Pre-filled ampule and non-invasive hypodermic injection device assembly |
| US4940460A (en) * | 1987-06-19 | 1990-07-10 | Bioject, Inc. | Patient-fillable and non-invasive hypodermic injection device assembly |
| US5339163A (en) * | 1988-03-16 | 1994-08-16 | Canon Kabushiki Kaisha | Automatic exposure control device using plural image plane detection areas |
| FR2638359A1 (fr) * | 1988-11-03 | 1990-05-04 | Tino Dalto | Guide de seringue avec reglage de la profondeur de penetration de l'aiguille dans la peau |
| US5064413A (en) * | 1989-11-09 | 1991-11-12 | Bioject, Inc. | Needleless hypodermic injection device |
| US5312335A (en) * | 1989-11-09 | 1994-05-17 | Bioject Inc. | Needleless hypodermic injection device |
| US5190521A (en) * | 1990-08-22 | 1993-03-02 | Tecnol Medical Products, Inc. | Apparatus and method for raising a skin wheal and anesthetizing skin |
| US5527288A (en) * | 1990-12-13 | 1996-06-18 | Elan Medical Technologies Limited | Intradermal drug delivery device and method for intradermal delivery of drugs |
| JPH06247995A (ja) * | 1991-06-24 | 1994-09-06 | Asahi Chem Ind Co Ltd | 新規なシアリル（α２−６）ラクトテトラオシルセラミド |
| GB9118204D0 (en) * | 1991-08-23 | 1991-10-09 | Weston Terence E | Needle-less injector |
| SE9102652D0 (sv) * | 1991-09-13 | 1991-09-13 | Kabi Pharmacia Ab | Injection needle arrangement |
| US5328483A (en) * | 1992-02-27 | 1994-07-12 | Jacoby Richard M | Intradermal injection device with medication and needle guard |
| US5383851A (en) * | 1992-07-24 | 1995-01-24 | Bioject Inc. | Needleless hypodermic injection device |
| US5569189A (en) * | 1992-09-28 | 1996-10-29 | Equidyne Systems, Inc. | hypodermic jet injector |
| US5334144A (en) * | 1992-10-30 | 1994-08-02 | Becton, Dickinson And Company | Single use disposable needleless injector |
| WO1995024176A1 (en) * | 1994-03-07 | 1995-09-14 | Bioject, Inc. | Ampule filling device |
| US5466220A (en) * | 1994-03-08 | 1995-11-14 | Bioject, Inc. | Drug vial mixing and transfer device |
| US5599302A (en) * | 1995-01-09 | 1997-02-04 | Medi-Ject Corporation | Medical injection system and method, gas spring thereof and launching device using gas spring |
| US5893397A (en) * | 1996-01-12 | 1999-04-13 | Bioject Inc. | Medication vial/syringe liquid-transfer apparatus |
| US5993412A (en) * | 1997-05-19 | 1999-11-30 | Bioject, Inc. | Injection apparatus |
| CA2365575A1 (en) * | 1999-03-31 | 2000-10-12 | Otsuka Pharmaceutical Co., Ltd. | Influenza virus hemagglutinin-binding peptides |
| WO2003074570A1 (fr) * | 2002-03-04 | 2003-09-12 | Japan Science And Technology Agency | Nouvelles molecules de sialo-sucre ramifiees et agents antiviraux les utilisant |
| WO2004018698A2 (en) * | 2002-08-20 | 2004-03-04 | Genitrix, Llc | Lectin compositions and methods for modulating an immune response to an antigen |
| US20050221337A1 (en) * | 2003-10-02 | 2005-10-06 | Massachusetts Institute Of Technology | Microarrays and microspheres comprising oligosaccharides, complex carbohydrates or glycoproteins |
| EP1723422A2 (en) * | 2004-03-05 | 2006-11-22 | The Scripps Research Institute | High throughput glycan microarrays |
| EP2272950A3 (en) * | 2004-11-11 | 2011-07-20 | Abbott Biologicals B.V. | Defective influenza virus particles |
| US7959929B2 (en) * | 2005-04-21 | 2011-06-14 | University Of Florida Research Foundation, Inc. | Materials and methods for respiratory disease control in canines |
| US7871626B2 (en) * | 2005-08-04 | 2011-01-18 | St. Jude Children's Research Hospital | Modified influenza virus for monitoring and improving vaccine efficiency |
| US20090099036A1 (en) * | 2006-04-18 | 2009-04-16 | The Regents Of The University Of Michigan | Methods and compositions for screening glycan structures |
| US20080220988A1 (en) * | 2007-03-07 | 2008-09-11 | Ada Technologies, Inc. | Preparing carbohydrate microarrays and conjugated nanoparticles |
| WO2011130575A1 (en) * | 2010-04-16 | 2011-10-20 | Massachusetts Institute Of Technology | Modular glycan arrays |
-
2007
- 2007-08-14 AU AU2007332987A patent/AU2007332987B2/en not_active Ceased
- 2007-08-14 EP EP07870741A patent/EP2049569A4/en not_active Withdrawn
- 2007-08-14 KR KR1020097003179A patent/KR20090050056A/ko not_active Ceased
- 2007-08-14 US US12/301,126 patent/US20100061990A1/en not_active Abandoned
- 2007-08-14 US US11/893,171 patent/US20080241918A1/en not_active Abandoned
- 2007-08-14 CA CA002660038A patent/CA2660038A1/en not_active Abandoned
- 2007-08-14 JP JP2009524675A patent/JP2010501074A/ja active Pending
- 2007-08-14 EP EP07836884A patent/EP2052340A4/en not_active Withdrawn
- 2007-08-14 WO PCT/US2007/018160 patent/WO2008073161A2/en not_active Ceased
- 2007-08-14 CA CA002660128A patent/CA2660128A1/en not_active Abandoned
- 2007-08-14 AU AU2007284496A patent/AU2007284496A1/en not_active Abandoned
- 2007-08-14 US US11/915,194 patent/US20100125043A1/en not_active Abandoned
- 2007-08-14 WO PCT/US2007/018103 patent/WO2008021415A2/en not_active Ceased
- 2007-08-14 JP JP2009524682A patent/JP2010500880A/ja active Pending
-
2009
- 2009-01-27 IL IL196738A patent/IL196738A0/en unknown
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