CA2298840A1 - Immune responses against hpv antigens elicited by compositions comprising an hpv antigen and a stress protein or an expression vector capable of expression of these proteins - Google Patents
Immune responses against hpv antigens elicited by compositions comprising an hpv antigen and a stress protein or an expression vector capable of expression of these proteins Download PDFInfo
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- CA2298840A1 CA2298840A1 CA 2298840 CA2298840A CA2298840A1 CA 2298840 A1 CA2298840 A1 CA 2298840A1 CA 2298840 CA2298840 CA 2298840 CA 2298840 A CA2298840 A CA 2298840A CA 2298840 A1 CA2298840 A1 CA 2298840A1
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- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
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- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
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Landscapes
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Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US5483597P | 1997-08-05 | 1997-08-05 | |
| US60/054,835 | 1997-08-05 | ||
| PCT/CA1998/000246 WO1999007860A1 (en) | 1997-08-05 | 1998-03-20 | Immune responses against hpv antigens elicited by compositions comprising an hpv antigen and a stress protein or an expression vector capable of expression of these proteins |
Publications (1)
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| CA2298840A1 true CA2298840A1 (en) | 1999-02-18 |
Family
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Family Applications (1)
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| CA 2298840 Abandoned CA2298840A1 (en) | 1997-08-05 | 1998-03-20 | Immune responses against hpv antigens elicited by compositions comprising an hpv antigen and a stress protein or an expression vector capable of expression of these proteins |
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| JP (2) | JP4198315B2 (enExample) |
| KR (2) | KR20060111731A (enExample) |
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| AT (2) | ATE327259T1 (enExample) |
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| BR (1) | BR9812272A (enExample) |
| CA (1) | CA2298840A1 (enExample) |
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| ES (2) | ES2266652T3 (enExample) |
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| IL (1) | IL134341A0 (enExample) |
| NZ (3) | NZ538399A (enExample) |
| PL (1) | PL196805B1 (enExample) |
| PT (2) | PT1336621E (enExample) |
| WO (1) | WO1999007860A1 (enExample) |
Families Citing this family (81)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE69429723T2 (de) | 1993-06-04 | 2002-09-26 | Whitehead Institute For Biomedical Research, Cambridge | Stressproteine und ihre verwendung |
| US7157089B1 (en) | 1996-11-26 | 2007-01-02 | Stressgen Biotechnologies Corporation | Immune responses using compositions containing stress proteins |
| PT1336621E (pt) * | 1997-08-05 | 2006-08-31 | Stressgen Biotechnologies Corp | Respostas imunitarias contra antigenios dos vph, suscitadas por composicoes que incorporam um antigenio de vph e uma proteina do stress ou um vector de expressao com aptidao para a expressao destas proteinas |
| EP1196772A2 (en) | 1999-07-08 | 2002-04-17 | Stressgen Biotechnologies Corporation | Induction of a th1-like response in vitro |
| US20050226890A1 (en) * | 1999-08-12 | 2005-10-13 | Cohen David I | Tat-based vaccine compositions and methods of making and using same |
| AUPQ233799A0 (en) * | 1999-08-19 | 1999-09-09 | Minister For Agriculture, Minister For Land And Water Conservation For And On Behalf Of The State Of New South Wales | Recombinant sub-unit vaccine |
| US20050100928A1 (en) * | 1999-09-16 | 2005-05-12 | Zycos Inc., A Delaware Corporation | Nucleic acids encoding polyepitope polypeptides |
| US6984384B1 (en) | 1999-09-30 | 2006-01-10 | Health Research, Inc. | Stress protein compositions and methods for prevention and treatment of cancer and infectious disease |
| US7378096B2 (en) | 1999-09-30 | 2008-05-27 | Health Research, Inc. | Stress protein compositions and methods for prevention and treatment of cancer and infectious disease |
| EP1222289B1 (en) * | 1999-10-20 | 2008-04-16 | The Johns Hopkins University School Of Medicine | Chimeric immunogenic compositions and nucleic acids encoding them |
| US8128922B2 (en) | 1999-10-20 | 2012-03-06 | Johns Hopkins University | Superior molecular vaccine linking the translocation domain of a bacterial toxin to an antigen |
| DE60042704D1 (de) * | 2000-01-14 | 2009-09-17 | Whitehead Biomedical Inst | Induktion zytotoxischer lymphozyten durch hitzeschockprotein-fusionsproteine hängt von der atp-bindungsdomäne in hsp ab und is cd4+ unabhängig |
| EP1282449A2 (en) * | 2000-05-12 | 2003-02-12 | The Regents Of The University Of California | Treatment of human papillomavirus (hpv)-infected cells |
| KR100919266B1 (ko) | 2000-06-26 | 2009-09-30 | 엔벤타 바이오파마슈티컬스 코포레이션 | 인간 파필로마 바이러스 치료법 |
| US7342002B2 (en) | 2000-08-03 | 2008-03-11 | The Johns Hopkins University | Molecular vaccine linking an endoplasmic chaperone polypeptide to an antigen |
| WO2005090392A1 (en) * | 2004-03-16 | 2005-09-29 | Inist Inc. | Tat-based tolerogen compositions and methods of making and using same |
| WO2006033665A1 (en) * | 2004-03-16 | 2006-03-30 | Inist Inc. | Tat-based vaccine compositions and methods of making and using same |
| CN100400099C (zh) * | 2001-01-04 | 2008-07-09 | 北京迪威华宇生物技术有限公司 | 预防和治疗人前列腺癌的重组蛋白疫苗 |
| EP1363660A4 (en) * | 2001-02-01 | 2006-06-21 | Univ Johns Hopkins | HIGHER MOLECULAR VACCINE BASED ON AUTOMPLICATIVE RNA, SUICIDE DNA OR UNDNA DNA VECTOR, WHICH LINKS ANTIGEN WITH A POLYPEPTIDE WHICH PROMOTES THE PRESENTATION OF THE ANTIGEN |
| PL373675A1 (en) * | 2001-02-05 | 2005-09-05 | Stressgen Biotechnologies Corporation | Hepatitis b virus treatment |
| AUPR446801A0 (en) | 2001-04-18 | 2001-05-17 | University Of Queensland, The | Novel compositions and uses therefor |
| KR100785397B1 (ko) * | 2001-06-28 | 2007-12-13 | 아피메즈 주식회사 | 인체 파필로마 바이러스 유사 입자를 생산하는 재조합아데노바이러스 벡터 및 자궁경부암 생백신 |
| KR100474114B1 (ko) * | 2001-12-24 | 2005-03-08 | 대한민국 | 소 타일레리아병에 대한 면역원성이 증진된 융합단백질, 및 그의 제조방법 및 용도 |
| RU2229307C1 (ru) * | 2002-10-22 | 2004-05-27 | ООО "Фирма"БиоМедИнвест" | Композиция рекомбинантных белков, способ получения такой композиции, фармацевтический набор реагентов для иммунотерапии и профилактической вакцинации опухолевых заболеваний аногенитальной сферы, способ иммунотерапии и профилактической вакцинации на его основе |
| US7763259B2 (en) * | 2003-01-10 | 2010-07-27 | The Regents Of The University Of Colorado | Therapeutic and prophylactic vaccine for the treatment and prevention of papillomavirus infection |
| US7211257B2 (en) * | 2003-02-10 | 2007-05-01 | Rosalind Franklin University Of Medicine And Science | Methods for inducing apoptosis in ovarian carcinoma cells using an anti-regeneration and tolerance factor antibody |
| WO2004098526A2 (en) | 2003-05-05 | 2004-11-18 | Johns Hopkins University | Anti-cancer dna vaccine employing plasmids encoding signal sequence, mutant oncoprotein antigen, and heat shock protein |
| CA2526720C (en) | 2003-05-22 | 2013-10-22 | Fraunhofer Usa, Inc. | Recombinant carrier molecule for expression, delivery and purification of target polypeptides |
| AU2004274430A1 (en) | 2003-09-12 | 2005-03-31 | Antigenics, Inc. | Vaccine for treatment and prevention of herpes simplex virus infection |
| US7304139B2 (en) * | 2003-10-28 | 2007-12-04 | University Of Florida Research Foundation, Inc. | Polynucleotides and polypeptides of Anaplasma phagocytophilum and methods of using the same |
| FR2868781B1 (fr) * | 2004-04-13 | 2008-02-22 | Immutep | Composition de vaccin comprenant un ligand cmh de classe ii couple a un antigene, procede de preparation et utilisations |
| CN1727362B (zh) * | 2004-07-30 | 2010-12-01 | 中国人民解放军第二军医大学 | 癌胚抗原阳性肿瘤治疗性疫苗的制备及应用 |
| CN1769298B (zh) * | 2004-11-05 | 2010-04-07 | 中国人民解放军军事医学科学院生物工程研究所 | 一种具有抗肿瘤作用的融合蛋白及其编码基因与应用 |
| CA2594040A1 (en) | 2005-01-06 | 2006-07-13 | The Johns Hopkins University | Rna interference that blocks expression of pro-apoptotic proteins potentiates immunity induced by dna and transfected dendritic cell vaccines |
| CN1299769C (zh) * | 2005-01-31 | 2007-02-14 | 中国医学科学院肿瘤医院肿瘤研究所 | 人乳头瘤病毒和热休克蛋白重组蛋白疫苗及其用途 |
| RU2285537C1 (ru) * | 2005-04-05 | 2006-10-20 | Автономная некоммерческая организация "Институт молекулярной диагностики (АНО "ИнМоДи") | Противоопухолевый пептидный препарат на основе фрагмента альфа-фетопротеина, его конъюгат, фармацевтическая композиция и способ лечения гормонзависимых опухолей |
| RU2283128C1 (ru) * | 2005-04-05 | 2006-09-10 | Сергей Викторович Луценко | Способ получения препарата белка из семейства стрессовых и препарат белка hsp70, полученный этим способом |
| ES2363247T3 (es) * | 2005-04-27 | 2011-07-28 | Leiden University Medical Center | Tratamiento para neoplasias intraepiteliales anogenitales inducidas por vph. |
| RU2290204C1 (ru) * | 2005-07-27 | 2006-12-27 | Общество с ограниченной ответственностью "Аванген" | Рекомбинантный гибридный белок, препарат для иммунотерапии на его основе и способ иммунотерапии рецидивирующего папилломатоза гортани |
| CA2616859C (en) | 2005-08-03 | 2015-04-14 | Fraunhofer Usa, Inc. | Compositions and methods for production of immunoglobulins |
| US7951384B2 (en) * | 2005-08-05 | 2011-05-31 | University Of Massachusetts | Virus-like particles as vaccines for paramyxovirus |
| US9216212B2 (en) * | 2005-08-05 | 2015-12-22 | University Of Massachusetts | Virus-like particles as vaccines for paramyxovirus |
| US7622121B2 (en) * | 2005-09-21 | 2009-11-24 | New York University | Heat shock proteins from Mycobacterium leprae and uses thereof |
| US7972776B2 (en) * | 2005-11-15 | 2011-07-05 | Oncohealth Corporation | Protein chips for HPV detection |
| US7732166B2 (en) * | 2005-11-15 | 2010-06-08 | Oncohealth Corporation | Detection method for human pappilomavirus (HPV) and its application in cervical cancer |
| BRPI0707779B8 (pt) * | 2006-02-13 | 2021-05-25 | Fraunhofer Usa Inc | antígeno isolado, composição de vacina e método para produção de uma proteína antígeno |
| AU2007215080A1 (en) | 2006-02-13 | 2007-08-23 | Fraunhofer Usa, Inc. | Influenza antigens, vaccine compositions, and related methods |
| WO2008048344A2 (en) * | 2006-02-13 | 2008-04-24 | Fraunhofer Usa, Inc. | Bacillus anthracis antigens, vaccine compositions, and related methods |
| RU2316342C1 (ru) * | 2006-03-31 | 2008-02-10 | Автономная некоммерческая организация "Институт молекулярной диагностики" (АНО "ИнМоДи") | Вакцинная композиция для профилактики и лечения онкологических заболеваний, рекомбинантная плазмидная днк, обеспечивающая синтез гибридного белка, способ его получения |
| WO2007137427A1 (en) * | 2006-05-31 | 2007-12-06 | Nventa Biopharmaceuticals Corporation | Bioactive purified hspe7 compositions |
| CN100410382C (zh) * | 2006-08-18 | 2008-08-13 | 上海交通大学医学院 | 一种可诱生细胞免疫应答的共表达载体和真核表达载体 |
| US8968995B2 (en) * | 2008-11-12 | 2015-03-03 | Oncohealth Corp. | Detection, screening, and diagnosis of HPV-associated cancers |
| US8859218B2 (en) * | 2008-06-13 | 2014-10-14 | Oncohealth Corp. | In situ detection of early stages and late stages HPV infection |
| WO2008143713A2 (en) * | 2006-12-22 | 2008-11-27 | Dow Agrosciences Llc | Plant-made west nile virus (wnv) vaccines, vectors and plant codon optimized sequences |
| US9085638B2 (en) | 2007-03-07 | 2015-07-21 | The Johns Hopkins University | DNA vaccine enhancement with MHC class II activators |
| US20080311145A1 (en) * | 2007-04-04 | 2008-12-18 | Specigen, Inc. | Protein cage immunotherapeutics |
| BRPI0810865A2 (pt) * | 2007-04-28 | 2017-05-09 | Fraunhofer Usa Inc | antígenos de tripanossoma, composições vacinais, e métodos relacionados |
| JP5545209B2 (ja) * | 2007-06-18 | 2014-07-09 | 上海▲沢▼▲潤▼安珂生物▲製▼▲薬▼有限公司 | 免疫原性を有する物質 |
| US8088392B2 (en) * | 2007-06-18 | 2012-01-03 | Yunxu Cao | Capsid proteins and uses therefore |
| US8404252B2 (en) | 2007-07-11 | 2013-03-26 | Fraunhofer Usa, Inc. | Yersinia pestis antigens, vaccine compositions, and related methods |
| CU23674A1 (es) | 2007-07-31 | 2011-05-27 | Ct Ingenieria Genetica Biotech | Péptidos penetradores a células fusionados a una biomolécula con acción terapéutica |
| CA2696764A1 (en) * | 2007-08-20 | 2009-02-26 | Fraunhofer Usa, Inc. | Prophylactic and therapeutic influenza vaccines, antigens, compositions, and methods |
| WO2009127988A1 (en) * | 2008-04-16 | 2009-10-22 | Universite De Lausanne | Method and vaccine for optimizing the specific immune responses |
| ES2922534T3 (es) | 2008-04-18 | 2022-09-16 | Massachusetts Gen Hospital | Inmunoterapias que emplean vacunas autoensamblantes |
| WO2010037046A1 (en) | 2008-09-28 | 2010-04-01 | Fraunhofer Usa, Inc. | Humanized neuraminidase antibody and methods of use thereof |
| WO2010039224A2 (en) | 2008-09-30 | 2010-04-08 | University Of Massachusetts Medical School | Respiratory syncytial virus (rsv) sequences for protein expression and vaccines |
| WO2010111292A1 (en) | 2009-03-23 | 2010-09-30 | Nanirx, Inc. | Treatment of cancer with immunostimulatory hiv tat derivative polypeptides |
| EP2427763A4 (en) | 2009-05-07 | 2013-08-21 | Oncohealth Corp | IDENTIFICATION OF HIGH GRADE OR CIN2 FOR DETECTION, MONITORING AND DIAGNOSIS, AT EARLY STAGES AND ADVANCED STAGES, OF HUMAN PAPILLOMAVIRUS (HPV) AND HPV ASSOCIATED CANCERS |
| US8784819B2 (en) | 2009-09-29 | 2014-07-22 | Ibio Inc. | Influenza hemagglutinin antibodies, compositions and related methods |
| EP2521914A4 (en) | 2010-01-08 | 2013-07-10 | Oncohealth Corp | CELL-BASED HPV IMMUNOTESTS HAVE A HIGH PERFORMANCE FOR DIAGNOSIS AND SCANNING OF HPV ASSOCIATED CANCER |
| US8853149B2 (en) | 2010-03-19 | 2014-10-07 | H. Lee Moffitt Cancer Center And Research Institute, Inc. | Integrin interaction inhibitors for the treatment of cancer |
| WO2012145509A2 (en) | 2011-04-19 | 2012-10-26 | The Research Foundation Of State University Of New York | Adeno-associated-virus rep sequences, vectors, and viruses |
| CN103687616A (zh) * | 2011-07-21 | 2014-03-26 | 生物技术工具公司 | Dnak制剂 |
| WO2014164727A1 (en) * | 2013-03-12 | 2014-10-09 | Wisconsin Alumni Research Foundation | A method of treating fungal infection |
| RU2537233C2 (ru) * | 2013-03-26 | 2014-12-27 | Федеральное государственное бюджетное образовательное учреждение высшего профессионального образования "Кабардино-Балкарский государственный университет им. Х.М. Бербекова" (КБГУ) | Применение комплекса антиоксидантных витаминов и аминокислот в качестве дополнения к стандартным методам терапии и способ лечения папилломавирус-ассоциированных предраковых заболеваний шейки матки и профилактики канцерогенеза при папилломавирусной инфекции |
| WO2015051245A1 (en) | 2013-10-04 | 2015-04-09 | Pin Pharma, Inc. | Immunostimulatory hiv tat derivative polypeptides for use in cancer treatment |
| FR3011850B1 (fr) * | 2013-10-15 | 2018-04-06 | Cfl Biotech | Vaccin therapeutique contre le cancer a base de proteines de stress rendues immunogenes |
| WO2016149643A2 (en) * | 2015-03-18 | 2016-09-22 | Omnicyte | Fusion proteins comprising modified alpha virus surface glycoproteins and tumor associated antigen and methods thereof |
| WO2017015504A1 (en) | 2015-07-21 | 2017-01-26 | Scheibel Steven Frederick | Treatment and prevention of anal conditions |
| CN108484776B (zh) * | 2018-03-19 | 2019-11-05 | 首都医科大学附属北京朝阳医院 | 一种融合蛋白、制备方法及其应用 |
| CN120607593A (zh) * | 2024-03-06 | 2025-09-09 | 诺未生物技术(无锡)有限公司 | 治疗hpv感染相关疾病的药物 |
Family Cites Families (50)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US550405A (en) * | 1895-11-26 | Island | ||
| GB8404280D0 (en) | 1984-02-17 | 1984-03-21 | Stanford J L | Biological preparations |
| IL71683A0 (en) | 1984-04-27 | 1984-09-30 | Yeda Res & Dev | Pharmaceutical compositions for treating arthritis type diseases comprising fractions obtained from mycobacteria |
| US4906742A (en) | 1986-07-31 | 1990-03-06 | Whitehead Institute For Biomedical Research | Encoding antigens of M. Leprae |
| US6007806A (en) | 1986-08-13 | 1999-12-28 | Transgene S.A. | Expression of a tumor-specific antigen by a recombinant vector virus and use thereof in preventive or curative treatment of the corresponding tumor |
| NL8701163A (nl) | 1986-09-09 | 1988-04-05 | Nederlanden Staat | Gebruik van een peptide voor de bereiding van preparaten voor het verlichten, het behandelen en de diagnose van autoimmuunziekten, in het bijzonder arthritische toestanden, verbindingen die met dit peptide verwant zijn, alsmede farmaceutische en diagnostische preparaten en testkits. |
| AU1548388A (en) | 1987-02-02 | 1988-08-24 | Whitehead Institute For Biomedical Research | Mycobacterium tuberculosis genes and encoding protein antigens |
| US4952395A (en) | 1987-02-26 | 1990-08-28 | Scripps Clinic And Research Foundation | Mycobacterial recombinants and peptides |
| US5504005A (en) | 1987-03-02 | 1996-04-02 | Albert Einstein College Of Medicine Of Yeshiva University | Recombinant mycobacterial vaccine |
| US4918166A (en) | 1987-04-10 | 1990-04-17 | Oxford Gene Systems Limited | Particulate hybrid HIV antigens |
| NL8703107A (nl) | 1987-12-22 | 1989-07-17 | Nederlanden Staat | Polypeptiden en derivaten daarvan, alsmede de toepassing daarvan in farmaceutische en diagnostische preparaten. |
| CA1338778C (en) | 1988-06-15 | 1996-12-10 | Richard A. Young | Stress proteins and uses therefor |
| US5114844A (en) | 1989-03-14 | 1992-05-19 | Yeda Research And Development Co., Ltd. | Diagnosis and treatment of insulin dependent diabetes mellitus |
| AU5848090A (en) | 1989-06-19 | 1991-01-08 | Whitehead Institute For Biomedical Research | Vector-mediated genomic insertion and expression of dna in bcg |
| GB8919321D0 (en) | 1989-08-25 | 1989-10-11 | Univ London | Treatment of chronic inflammatory conditions |
| GB9007194D0 (en) | 1990-03-30 | 1990-05-30 | Wellcome Found | Live vaccines |
| US5348945A (en) | 1990-04-06 | 1994-09-20 | Wake Forest University | Method of treatment with hsp70 |
| JPH06501479A (ja) | 1990-11-08 | 1994-02-17 | スタンフオード・ルツク・リミテツド | 抗原担体 |
| GB9024320D0 (en) | 1990-11-08 | 1990-12-19 | Univ London | Treatment of uveitis |
| GB2251186A (en) | 1990-12-04 | 1992-07-01 | Randall Neal Gatz | Polypeptide for use in treatment of autoimmune disease |
| IT1262896B (it) | 1992-03-06 | 1996-07-22 | Composti coniugati formati da proteine heat shock (hsp) e oligo-poli- saccaridi, loro uso per la produzione di vaccini. | |
| US5580563A (en) | 1992-05-01 | 1996-12-03 | Tam; James P. | Multiple antigen peptide system having adjuvant properties, vaccines prepared therefrom and methods of use thereof |
| GB9211736D0 (en) | 1992-06-03 | 1992-07-15 | Univ Cardiff | Allergic treatment |
| IL102687A (en) | 1992-07-30 | 1997-06-10 | Yeda Res & Dev | Conjugates of poorly immunogenic antigens and synthetic pepide carriers and vaccines comprising them |
| US5736146A (en) | 1992-07-30 | 1998-04-07 | Yeda Research And Development Co. Ltd. | Conjugates of poorly immunogenic antigens and synthetic peptide carriers and vaccines comprising them |
| JP2541081B2 (ja) * | 1992-08-28 | 1996-10-09 | 日本電気株式会社 | バイオセンサ及びバイオセンサの製造・使用方法 |
| DE69429723T2 (de) | 1993-06-04 | 2002-09-26 | Whitehead Institute For Biomedical Research, Cambridge | Stressproteine und ihre verwendung |
| US5762939A (en) | 1993-09-13 | 1998-06-09 | Mg-Pmc, Llc | Method for producing influenza hemagglutinin multivalent vaccines using baculovirus |
| US5997873A (en) | 1994-01-13 | 1999-12-07 | Mount Sinai School Of Medicine Of The City University Of New York | Method of preparation of heat shock protein 70-peptide complexes |
| US5750119A (en) | 1994-01-13 | 1998-05-12 | Mount Sinai School Of Medicine Of The City University Of New York | Immunotherapeutic stress protein-peptide complexes against cancer |
| US5961979A (en) | 1994-03-16 | 1999-10-05 | Mount Sinai School Of Medicine Of The City University Of New York | Stress protein-peptide complexes as prophylactic and therapeutic vaccines against intracellular pathogens |
| IL109790A0 (en) * | 1994-05-25 | 1994-08-26 | Yeda Res & Dev | Peptides used as carriers in immunogenic constructs suitable for development of synthetic vaccines |
| GB9419979D0 (en) | 1994-10-04 | 1994-11-16 | Medeva Holdings Bv | Vaccine compositions |
| AUPN015794A0 (en) * | 1994-12-20 | 1995-01-19 | Csl Limited | Variants of human papilloma virus antigens |
| CA2211995A1 (en) * | 1995-02-24 | 1996-08-29 | Cantab Pharmaceuticals Research Limited | Polypeptides useful as immunotherapeutic agents and methods of polypeptide preparation |
| IL123219A0 (en) * | 1995-08-18 | 1998-09-24 | Sloan Kettering Inst Cancer | Method for treatment of cancer and infectious diseases and compositions useful in same |
| US5985270A (en) | 1995-09-13 | 1999-11-16 | Fordham University | Adoptive immunotherapy using macrophages sensitized with heat shock protein-epitope complexes |
| US5837251A (en) | 1995-09-13 | 1998-11-17 | Fordham University | Compositions and methods using complexes of heat shock proteins and antigenic molecules for the treatment and prevention of neoplastic diseases |
| US5935576A (en) | 1995-09-13 | 1999-08-10 | Fordham University | Compositions and methods for the treatment and prevention of neoplastic diseases using heat shock proteins complexed with exogenous antigens |
| EP0851765A4 (en) | 1995-09-13 | 2000-01-19 | Univ Fordham | THERAPEUTIC AND PROPHYLACTIC PROCESSES THAT USE HEAT SHOCK PROTEINS |
| WO1997026910A2 (de) | 1996-01-27 | 1997-07-31 | Max-Delbrück-Centrum für Molekulare Medizin | Tumorimpfstoff für die immuntherapie von malignen tumoren |
| US6130087A (en) | 1996-10-07 | 2000-10-10 | Fordham University | Methods for generating cytotoxic T cells in vitro |
| DK0941315T3 (da) | 1996-11-26 | 2006-05-15 | Stressgen Biotechnologies Corp | Fusionsproteiner indeholdende stressproteiner til induktion af immunreaktioner |
| US6017540A (en) | 1997-02-07 | 2000-01-25 | Fordham University | Prevention and treatment of primary and metastatic neoplastic diseases and infectious diseases with heat shock/stress protein-peptide complexes |
| US5830464A (en) | 1997-02-07 | 1998-11-03 | Fordham University | Compositions and methods for the treatment and growth inhibition of cancer using heat shock/stress protein-peptide complexes in combination with adoptive immunotherapy |
| WO1998035705A1 (en) | 1997-02-18 | 1998-08-20 | Whitehead Institute For Biomedical Research | Use of heat shock proteins to deliver moieties into cells |
| PT1336621E (pt) * | 1997-08-05 | 2006-08-31 | Stressgen Biotechnologies Corp | Respostas imunitarias contra antigenios dos vph, suscitadas por composicoes que incorporam um antigenio de vph e uma proteina do stress ou um vector de expressao com aptidao para a expressao destas proteinas |
| US6007821A (en) | 1997-10-16 | 1999-12-28 | Fordham University | Method and compositions for the treatment of autoimmune disease using heat shock proteins |
| US5948646A (en) | 1997-12-11 | 1999-09-07 | Fordham University | Methods for preparation of vaccines against cancer comprising heat shock protein-peptide complexes |
| EP1196772A2 (en) * | 1999-07-08 | 2002-04-17 | Stressgen Biotechnologies Corporation | Induction of a th1-like response in vitro |
-
1998
- 1998-03-20 PT PT03001726T patent/PT1336621E/pt unknown
- 1998-03-20 BR BR9812272A patent/BR9812272A/pt not_active Application Discontinuation
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- 1998-03-20 WO PCT/CA1998/000246 patent/WO1999007860A1/en not_active Ceased
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- 1998-03-20 KR KR1020067019653A patent/KR20060111731A/ko not_active Ceased
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- 1998-03-20 CA CA 2298840 patent/CA2298840A1/en not_active Abandoned
-
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- 2000-02-04 US US09/498,918 patent/US6524825B1/en not_active Expired - Fee Related
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- 2002-11-07 US US10/289,760 patent/US6900035B2/en not_active Expired - Fee Related
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- 2004-09-10 US US10/938,695 patent/US7262014B2/en not_active Expired - Fee Related
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- 2005-07-21 JP JP2005211965A patent/JP2006001939A/ja not_active Withdrawn
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- 2007-07-26 US US11/828,900 patent/US20080050399A1/en not_active Abandoned
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