JP2001510683A - Ｐｓｅｕｄｏｍｏｎａｓ体外毒素Ａ様キメラ免疫原 - Google Patents
Ｐｓｅｕｄｏｍｏｎａｓ体外毒素Ａ様キメラ免疫原Info
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- JP2001510683A JP2001510683A JP2000502207A JP2000502207A JP2001510683A JP 2001510683 A JP2001510683 A JP 2001510683A JP 2000502207 A JP2000502207 A JP 2000502207A JP 2000502207 A JP2000502207 A JP 2000502207A JP 2001510683 A JP2001510683 A JP 2001510683A
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Classifications
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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
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/21—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Pseudomonadaceae (F)
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/08—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses
- C07K16/10—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses from RNA viruses
- C07K16/1036—Retroviridae, e.g. leukemia viruses
- C07K16/1045—Lentiviridae, e.g. HIV, FIV, SIV
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- C07K2319/00—Fusion polypeptide
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
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- C12N2740/16111—Human Immunodeficiency Virus, HIV concerning HIV env
- C12N2740/16122—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
Landscapes
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- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
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| PCT/US1998/014341 WO1999002713A1 (en) | 1997-07-11 | 1998-07-10 | Pseudomonas exotoxin a-like chimeric immunogens |
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| EP (1) | EP1000163B1 (enExample) |
| JP (2) | JP2001510683A (enExample) |
| AT (1) | ATE307208T1 (enExample) |
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Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2006025782A (ja) * | 2004-07-21 | 2006-02-02 | Healthbanks Biotech Co Ltd | スーパー抗原融合蛋白及びその応用方法 |
| JP2011510988A (ja) * | 2008-01-31 | 2011-04-07 | ヘルスバンクス ユーエスエー インコーポレイテッド | ワクチンとしてのキメラｈｉｖ融合タンパク質 |
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| EP1078988A1 (en) * | 1999-08-27 | 2001-02-28 | Academia Sinica | Pseudomonas fusion protein vaccines |
| US6838553B1 (en) * | 1999-10-05 | 2005-01-04 | Academia Sinica | Peptide repeat immunogens |
| ATE444081T1 (de) * | 1999-10-22 | 2009-10-15 | Us Gov Health & Human Serv | Proteine-abgabe durch polare epithelzellen schichte |
| AU2006247188A1 (en) | 2005-05-18 | 2006-11-23 | Children's Hospital & Research Center At Oakland | Methods and compositions for immunizing against chlamydia infection |
| US11246915B2 (en) | 2010-09-15 | 2022-02-15 | Applied Molecular Transport Inc. | Cholix toxin-derived fusion molecules for oral delivery of biologically active cargo |
| US8932586B2 (en) | 2011-09-06 | 2015-01-13 | Intrexon Corporation | Modified forms of Pseudomonas exotoxin A |
| BR112015013183A2 (pt) * | 2012-12-05 | 2017-09-26 | Thevax Genetics Vaccine Co Ltd | proteínas de fusão para uso como aperfeiçoadores imunogênicos para indução de respostas de células t específicas para antígenos |
| WO2014172309A2 (en) | 2013-04-18 | 2014-10-23 | The United States Of America As Represented By The Secretary Of The Army, On Behalf Of The United | Therapeutic compositions for neutralizing type i interferons, and methods of use |
| DK3302543T3 (da) * | 2015-06-01 | 2020-05-18 | Reber Genetics Co Ltd | Vaccinesammensætninger mod porcint reproduktions- og respirationssyndrom og porcint circovirus-associerede sygdomme |
| EP4316586A3 (en) | 2018-03-08 | 2024-05-08 | Applied Molecular Transport Inc. | Toxin-derived delivery constructs for oral delivery |
| JP7487193B2 (ja) | 2018-11-07 | 2024-05-20 | アプライド モレキュラー トランスポート インコーポレイテッド | 異種ペイロードの経口送達のためのコリックス由来担体 |
Family Cites Families (46)
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| US4545985A (en) | 1984-01-26 | 1985-10-08 | The United States Of America As Represented By The Secretary, Dept. Of Health And Human Services | Pseudomonas exotoxin conjugate immunotoxins |
| US6022950A (en) | 1984-06-07 | 2000-02-08 | Seragen, Inc. | Hybrid molecules having translocation region and cell-binding region |
| US5668255A (en) | 1984-06-07 | 1997-09-16 | Seragen, Inc. | Hybrid molecules having translocation region and cell-binding region |
| CA1289880C (en) | 1985-12-06 | 1991-10-01 | Jeffrey L. Winkelhake | Anti-human ovarian cancer immunotoxins and methods of use thereof |
| US5082927A (en) | 1986-09-24 | 1992-01-21 | The United States Of America As Represented By The Department Of Health And Human Services | Selectively cytotoxic IL-4-PE40 fusion protein |
| US6051405A (en) | 1986-09-24 | 2000-04-18 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Constructs encoding recombinant antibody-toxin fusion proteins |
| US4892827A (en) | 1986-09-24 | 1990-01-09 | The United States Of America As Represented By The Department Of Health And Human Services | Recombinant pseudomonas exotoxins: construction of an active immunotoxin with low side effects |
| US5206353A (en) | 1988-07-23 | 1993-04-27 | The United States Of America As Represented By The Department Of Health And Human Services | CD-4/cytotoxic gene fusions |
| CA1340530C (en) | 1989-04-28 | 1999-05-04 | Kok Kheong Lee | Synthetic pseudomonas aeruginosa pilin peptide and related vaccines and diagnostics |
| US5980896A (en) | 1989-06-30 | 1999-11-09 | Bristol-Myers Squibb Company | Antibodies reactive with human carcinomas |
| US6020145A (en) | 1989-06-30 | 2000-02-01 | Bristol-Myers Squibb Company | Methods for determining the presence of carcinoma using the antigen binding region of monoclonal antibody BR96 |
| AU657087B2 (en) * | 1989-12-22 | 1995-03-02 | Seragen Incorporated | Hybrid molecules having translocation region and cell-binding region |
| US5458878A (en) | 1990-01-02 | 1995-10-17 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | P. exotoxin fusio proteins have COOHG220101al alterations which increase cytotoxicity |
| AU646673B2 (en) | 1990-05-11 | 1994-03-03 | United States of America, as represented by the Secretary, U.S. Department of Commerce, The | Improved pseudomonas exotoxins of low animal toxicity and high cytocidal activity |
| US5608039A (en) | 1990-10-12 | 1997-03-04 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Single chain B3 antibody fusion proteins and their uses |
| US6099842A (en) | 1990-12-03 | 2000-08-08 | The United States Of America As Represented By The Department Of Health And Human Services | Recombinant immunotoxin composed of a single chain antibody reacting with the human transferrin receptor and diptheria toxin |
| US5328984A (en) * | 1991-03-04 | 1994-07-12 | The United States As Represented By The Department Of Health & Human Services | Recombinant chimeric proteins deliverable across cellular membranes into cytosol of target cells |
| US5190873A (en) | 1991-06-21 | 1993-03-02 | California Institute Of Biological Research | Hybrid tryptophan aporepressor containing ligand binding sites |
| US5621083A (en) | 1991-11-04 | 1997-04-15 | Xoma Corporation | Immunotoxins comprising ribosome-inactivating proteins |
| US5935580A (en) | 1992-04-21 | 1999-08-10 | Institut Pasteur | Recombinant mutants for inducing specific immune responses |
| ATE314475T1 (de) | 1992-06-18 | 2006-01-15 | Us Gov Health & Human Serv | Rekombinantes pseudomonas exotoxin mit gesteigerter aktivität |
| US6303120B1 (en) | 1994-03-15 | 2001-10-16 | Memorial Sloan-Kettering Institute For Cancer Research | Synthesis of glycoconjugates of the lewis y epitope and uses thereof |
| US5635599A (en) * | 1994-04-08 | 1997-06-03 | The United States Of America As Represented By The Department Of Health And Human Services | Fusion proteins comprising circularly permuted ligands |
| ATE204300T1 (de) | 1994-05-13 | 2001-09-15 | Biovation Ltd | Zielzellen-bindende chimäre peptide |
| US5573916A (en) | 1994-05-19 | 1996-11-12 | Coretech, Inc. | Immunogenic constructs comprising b-cell and t-cell epitopes on common carrier |
| EP0789776B1 (en) | 1994-11-01 | 2001-06-13 | Winfried Wels | Nucleic acid transfer system |
| US5843882A (en) | 1995-04-27 | 1998-12-01 | The United States Of America As Represented By The Department Of Health And Human Services | Antiviral proteins and peptides |
| US5980895A (en) | 1995-10-13 | 1999-11-09 | The United States Of America As Represented By The Department Of Health And Human Services | Immunotoxin containing a disulfide-stabilized antibody fragment joined to a Pseudomonas exotoxin that does not require proteolytic activation |
| IL116559A (en) | 1995-11-17 | 2005-11-20 | Yissum Res Dev Co | Chimeric protein consisting of a bacterial toxin and a myelin basic protein sequence |
| CA2241604C (en) | 1996-01-05 | 2010-03-30 | Ira Pastan | Mesothelium antigen and methods and kits for targeting it |
| AU716564B2 (en) * | 1996-11-06 | 2000-03-02 | Government Of The United States Of America, As Represented By The Secretary Of The Department Of Health And Human Services, The | Protease-activatable pseudomonas exotoxin A-like proproteins |
| WO1998042876A1 (en) | 1997-03-26 | 1998-10-01 | Board Of Regents, The University Of Texas System | Methods and compositions for using membrane-penetrating proteins to carry materials across cell membranes |
| US20030054012A1 (en) | 2000-05-12 | 2003-03-20 | Fitzgerald David J. | Pseudomonas exotoxin a-like chimeric immunogens for eliciting a secretory iga-mediated immune response |
| US6140066A (en) | 1998-03-24 | 2000-10-31 | Lorberboum-Galski; Haya | Methods of cancer diagnosis using a chimeric toxin |
| US6090388A (en) | 1998-06-20 | 2000-07-18 | United Biomedical Inc. | Peptide composition for prevention and treatment of HIV infection and immune disorders |
| EP1224290B1 (en) | 1999-10-22 | 2006-06-28 | THE GOVERNMENT OF THE UNITED STATES OF AMERICA, as represented by THE SECRETARY, DEPARTMENT OF HEALTH AND HUMAN SERVICES | Disulfide conjugated cell toxins and methods of making and using them |
| ATE444081T1 (de) * | 1999-10-22 | 2009-10-15 | Us Gov Health & Human Serv | Proteine-abgabe durch polare epithelzellen schichte |
| US6783761B2 (en) | 2000-05-05 | 2004-08-31 | Aphton Corporation | Chimeric peptide immunogens |
| WO2002060935A2 (en) * | 2000-12-21 | 2002-08-08 | The Government Of The United States As Represented By The Secretary Of The Department Of Health And Human Services | A chimeric protein comprising non-toxic pseudomonas exotoxin a and type iv pilin sequences |
| CA2501235A1 (en) * | 2002-10-04 | 2004-04-22 | The Regents Of The University Of California | Methods for treating cancer by inhibiting wnt signaling |
| JP2006516091A (ja) * | 2002-10-07 | 2006-06-22 | アンティジェニクス インコーポレーテッド | 熱ショックタンパク質結合性のｃｄ９１断片およびその使用 |
| US7335361B2 (en) | 2003-06-09 | 2008-02-26 | Animal Technology Institute Taiwan | Fusion antigen used as vaccine |
| AU2005294436A1 (en) * | 2004-10-04 | 2006-04-20 | Trinity Biosystems, Inc. | Methods and compositions for immunizing against Pseudomonas infection |
| US8877714B2 (en) * | 2005-06-14 | 2014-11-04 | Raptor Pharmaceutical Inc. | Compositions comprising receptor-associated protein (RAP) variants specific for LRP2 and uses thereof |
| DK2308514T3 (da) * | 2007-03-23 | 2013-09-02 | To Bbb Holding B V | Konjugater til målrettet lægemiddeltransport gennem blod-hjerne barrieren |
| WO2008124010A1 (en) * | 2007-04-06 | 2008-10-16 | The Trustees Of The University Of Pennsylvania | Surfactant protein d is a biomarker for steroid responsiveness in asthma and chronic obstructive pulmonary disease |
-
1998
- 1998-07-10 AT AT98935604T patent/ATE307208T1/de active
- 1998-07-10 WO PCT/US1998/014341 patent/WO1999002713A1/en not_active Ceased
- 1998-07-10 ES ES98935604T patent/ES2249838T3/es not_active Expired - Lifetime
- 1998-07-10 DE DE69831951T patent/DE69831951T2/de not_active Expired - Lifetime
- 1998-07-10 AU AU84813/98A patent/AU731703B2/en not_active Ceased
- 1998-07-10 DK DK98935604T patent/DK1000163T3/da active
- 1998-07-10 CA CA2295971A patent/CA2295971C/en not_active Expired - Fee Related
- 1998-07-10 JP JP2000502207A patent/JP2001510683A/ja active Pending
- 1998-07-10 EP EP98935604A patent/EP1000163B1/en not_active Expired - Lifetime
-
2007
- 2007-12-20 US US11/962,007 patent/US8092809B2/en not_active Expired - Fee Related
-
2008
- 2008-12-11 JP JP2008316284A patent/JP2009079068A/ja active Pending
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2006025782A (ja) * | 2004-07-21 | 2006-02-02 | Healthbanks Biotech Co Ltd | スーパー抗原融合蛋白及びその応用方法 |
| JP2011510988A (ja) * | 2008-01-31 | 2011-04-07 | ヘルスバンクス ユーエスエー インコーポレイテッド | ワクチンとしてのキメラｈｉｖ融合タンパク質 |
Also Published As
| Publication number | Publication date |
|---|---|
| DE69831951T2 (de) | 2006-07-27 |
| JP2009079068A (ja) | 2009-04-16 |
| ATE307208T1 (de) | 2005-11-15 |
| AU8481398A (en) | 1999-02-08 |
| US20090269368A1 (en) | 2009-10-29 |
| DK1000163T3 (da) | 2006-02-06 |
| EP1000163B1 (en) | 2005-10-19 |
| CA2295971A1 (en) | 1999-01-21 |
| US8092809B2 (en) | 2012-01-10 |
| DE69831951D1 (de) | 2006-03-02 |
| AU731703B2 (en) | 2001-04-05 |
| CA2295971C (en) | 2011-02-08 |
| WO1999002713A1 (en) | 1999-01-21 |
| ES2249838T3 (es) | 2006-04-01 |
| EP1000163A1 (en) | 2000-05-17 |
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