IL300930A - שיטות והרכבים לטיפול במחלות אוטואימוניות וסרטן - Google Patents
שיטות והרכבים לטיפול במחלות אוטואימוניות וסרטןInfo
- Publication number
- IL300930A IL300930A IL300930A IL30093023A IL300930A IL 300930 A IL300930 A IL 300930A IL 300930 A IL300930 A IL 300930A IL 30093023 A IL30093023 A IL 30093023A IL 300930 A IL300930 A IL 300930A
- Authority
- IL
- Israel
- Prior art keywords
- construct
- seq
- tnfr2
- linker
- tnfr1
- Prior art date
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/569—Single domain, e.g. dAb, sdAb, VHH, VNAR or nanobody®
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/75—Agonist effect on antigen
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/94—Stability, e.g. half-life, pH, temperature or enzyme-resistance
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/30—Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/31—Fusion polypeptide fusions, other than Fc, for prolonged plasma life, e.g. albumin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/70—Fusion polypeptide containing domain for protein-protein interaction
- C07K2319/74—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Immunology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Epidemiology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oncology (AREA)
- Rheumatology (AREA)
- Neurosurgery (AREA)
- Biomedical Technology (AREA)
- Neurology (AREA)
- Pain & Pain Management (AREA)
- Hospice & Palliative Care (AREA)
- Psychiatry (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Physical Education & Sports Medicine (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Medicinal Preparation (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US202063071313P | 2020-08-27 | 2020-08-27 | |
| PCT/US2021/048074 WO2022047243A1 (en) | 2020-08-27 | 2021-08-27 | Methods and compositions to treat autoimmune diseases and cancer |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| IL300930A true IL300930A (he) | 2023-04-01 |
Family
ID=78078341
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| IL300930A IL300930A (he) | 2020-08-27 | 2021-08-27 | שיטות והרכבים לטיפול במחלות אוטואימוניות וסרטן |
Country Status (8)
| Country | Link |
|---|---|
| EP (1) | EP4204094A1 (he) |
| JP (1) | JP2023541816A (he) |
| KR (1) | KR20230078657A (he) |
| CN (1) | CN116847887A (he) |
| AU (1) | AU2021332460A1 (he) |
| CA (1) | CA3193273A1 (he) |
| IL (1) | IL300930A (he) |
| WO (1) | WO2022047243A1 (he) |
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| US12472266B2 (en) | 2019-02-21 | 2025-11-18 | Enosi Therapeutics Corporation | Antibodies and enonomers |
| WO2023168426A1 (en) | 2022-03-03 | 2023-09-07 | Enosi Therapeutics Corporation | Compositions and cells containing mixtures of oligo-trap fusion proteins (ofps) and uses thereof |
| EP4630451A2 (en) * | 2022-12-05 | 2025-10-15 | Fzata, Inc. | Oral treatments for pain comprising tnf-alpha binding proteins |
| WO2025049818A1 (en) | 2023-08-29 | 2025-03-06 | Enosi Therapeutics Corporation | Tnfr1 antagonists lacking agonist activity and uses thereof |
| CN118340891A (zh) * | 2024-04-03 | 2024-07-16 | 暨南大学附属第一医院(广州华侨医院) | Pdi抑制剂在制备抑制sting激活的产品中的应用 |
Family Cites Families (54)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| IL85035A0 (en) | 1987-01-08 | 1988-06-30 | Int Genetic Eng | Polynucleotide molecule,a chimeric antibody with specificity for human b cell surface antigen,a process for the preparation and methods utilizing the same |
| CA2055168A1 (en) | 1990-11-21 | 1992-05-22 | Walter Fiers | Tnf-muteins |
| WO1994004679A1 (en) | 1991-06-14 | 1994-03-03 | Genentech, Inc. | Method for making humanized antibodies |
| CA2103059C (en) | 1991-06-14 | 2005-03-22 | Paul J. Carter | Method for making humanized antibodies |
| US6214345B1 (en) | 1993-05-14 | 2001-04-10 | Bristol-Myers Squibb Co. | Lysosomal enzyme-cleavable antitumor drug conjugates |
| US5753230A (en) | 1994-03-18 | 1998-05-19 | The Scripps Research Institute | Methods and compositions useful for inhibition of angiogenesis |
| US5804396A (en) | 1994-10-12 | 1998-09-08 | Sugen, Inc. | Assay for agents active in proliferative disorders |
| EP0817775B1 (en) | 1995-03-30 | 2001-09-12 | Pfizer Inc. | Quinazoline derivatives |
| GB9508565D0 (en) | 1995-04-27 | 1995-06-14 | Zeneca Ltd | Quiazoline derivative |
| GB9508537D0 (en) | 1995-04-27 | 1995-06-14 | Zeneca Ltd | Quinazoline derivatives |
| GB9508538D0 (en) | 1995-04-27 | 1995-06-14 | Zeneca Ltd | Quinazoline derivatives |
| EP0892789B2 (en) | 1996-04-12 | 2009-11-18 | Warner-Lambert Company LLC | Irreversible inhibitors of tyrosine kinases |
| UA73073C2 (uk) | 1997-04-03 | 2005-06-15 | Уайт Холдінгз Корпорейшн | Заміщені 3-ціанохіноліни, спосіб їх одержання та фармацевтична композиція |
| ZA986732B (en) | 1997-07-29 | 1999-02-02 | Warner Lambert Co | Irreversible inhibitiors of tyrosine kinases |
| ZA986729B (en) | 1997-07-29 | 1999-02-02 | Warner Lambert Co | Irreversible inhibitors of tyrosine kinases |
| TW436485B (en) | 1997-08-01 | 2001-05-28 | American Cyanamid Co | Substituted quinazoline derivatives |
| US7229619B1 (en) | 2000-11-28 | 2007-06-12 | Medimmune, Inc. | Methods of administering/dosing anti-RSV antibodies for prophylaxis and treatment |
| US6884869B2 (en) | 2001-04-30 | 2005-04-26 | Seattle Genetics, Inc. | Pentapeptide compounds and uses related thereto |
| CN1671416B (zh) | 2001-07-12 | 2013-01-02 | 杰斐逊·富特 | 超人源化抗体 |
| WO2003026577A2 (en) | 2001-09-24 | 2003-04-03 | Seattle Genetics, Inc. | P-amidobenzylethers in drug delivery agents |
| US7091186B2 (en) | 2001-09-24 | 2006-08-15 | Seattle Genetics, Inc. | p-Amidobenzylethers in drug delivery agents |
| WO2003043583A2 (en) | 2001-11-20 | 2003-05-30 | Seattle Genetics, Inc. | Treatment of immunological disorders using anti-cd30 antibodies |
| DE60315145T2 (de) | 2002-03-13 | 2008-04-30 | Beijing Jiankai Technology Co., Ltd. | Hydrophiles polymerderivat mit y-verzweigung und herstellungsverfahren dafür; obige verbindung enthaltender medizinischer verbundwerkstoff |
| AU2003243651B2 (en) | 2002-06-17 | 2008-10-16 | The Government Of The United States Of America, As Represented By The Secretary Of The Department Of Health And Human Services | Specificity grafting of a murine antibody onto a human framework |
| US9028822B2 (en) | 2002-06-28 | 2015-05-12 | Domantis Limited | Antagonists against TNFR1 and methods of use therefor |
| US20060002935A1 (en) | 2002-06-28 | 2006-01-05 | Domantis Limited | Tumor Necrosis Factor Receptor 1 antagonists and methods of use therefor |
| WO2004032828A2 (en) | 2002-07-31 | 2004-04-22 | Seattle Genetics, Inc. | Anti-cd20 antibody-drug conjugates for the treatment of cancer and immune disorders |
| GB0230203D0 (en) | 2002-12-27 | 2003-02-05 | Domantis Ltd | Fc fusion |
| DK1639011T3 (da) | 2003-06-30 | 2009-02-16 | Domantis Ltd | Pegylerede enkelt-domæne antistoffer (dAb) |
| BRPI0510883B8 (pt) | 2004-06-01 | 2021-05-25 | Genentech Inc | composto conjugado de droga e anticorpo, composição farmacêutica, método de fabricação de composto conjugado de droga e anticorpo e usos de uma formulação, de um conjugado de droga e anticorpo e um agente quimioterapêutico e de uma combinação |
| GB0521621D0 (en) | 2005-10-24 | 2005-11-30 | Domantis Ltd | Tumor necrosis factor receptor 1 antagonists for treating respiratory diseases |
| WO2006109044A2 (en) | 2005-04-11 | 2006-10-19 | Yale University | Selective modulation of tumour necrosis factor receptors in therapy |
| SG172692A1 (en) | 2006-06-12 | 2011-07-28 | Symphogen As | Pan-cell surface receptor- specific therapeutics |
| US8093068B2 (en) | 2006-10-26 | 2012-01-10 | Centocor, Inc. | Methods for use in human-adapting monoclonal antibodies |
| CA2683791A1 (en) * | 2007-06-06 | 2008-12-11 | Domantis Limited | Polypeptides, antibody variable domains & antagonists |
| GB0724331D0 (en) | 2007-12-13 | 2008-01-23 | Domantis Ltd | Compositions for pulmonary delivery |
| CN102321155A (zh) * | 2008-12-19 | 2012-01-18 | 华中科技大学 | Tnf结合肽和tnfr1封闭肽及其在治疗溃疡性结肠炎中的应用 |
| JP2012517818A (ja) | 2009-02-19 | 2012-08-09 | グラクソ グループ リミテッド | 改善された抗tnfr1ポリペプチド、抗体可変ドメインおよびアンタゴニスト |
| WO2011008814A2 (en) | 2009-07-14 | 2011-01-20 | Immune Tolerance Institute, Inc., A California Not-For-Profit Corporation | Multiplexed measurement of exogenous and endogenous dna |
| WO2011006914A2 (en) | 2009-07-16 | 2011-01-20 | Glaxo Group Limited | Antagonists, uses & methods for partially inhibiting tnfr1 |
| NZ599114A (en) | 2009-10-27 | 2014-09-26 | Glaxo Group Ltd | Stable anti-tnfr1 polypeptides, antibody variable domains & antagonists |
| SE1150065A1 (sv) | 2011-01-31 | 2012-07-17 | Fairchild Semiconductor | Bipolär transistor i kiselkarbid med övervuxen emitter |
| US20140112929A1 (en) | 2011-06-17 | 2014-04-24 | Glaxo Group Limited | Tumour necrosis factor receptor 1 antagonists |
| KR102162413B1 (ko) * | 2011-08-17 | 2020-10-07 | 글락소 그룹 리미티드 | 변형된 단백질 및 펩티드 |
| WO2014040076A1 (en) | 2012-09-10 | 2014-03-13 | Xencor | Methods of treating neurological diseases |
| JP6367836B2 (ja) | 2013-02-07 | 2018-08-01 | ザ ジェネラル ホスピタル コーポレイション | T制御性細胞の増殖または枯渇方法 |
| WO2015104322A1 (en) | 2014-01-09 | 2015-07-16 | Glaxosmithkline Intellectual Property Development Limited | Treatment of inflammatory diseases with non-competitive tnfr1 antagonists |
| WO2016081643A1 (en) * | 2014-11-19 | 2016-05-26 | Genentech, Inc. | Anti-transferrin receptor antibodies and methods of use |
| US20190135929A1 (en) | 2015-08-28 | 2019-05-09 | The General Hospital Corporation | Agonistic anti-tumor necrosis factor receptor 2 antibodies |
| UA120981C2 (uk) * | 2015-09-18 | 2020-03-10 | Чугаі Сейяку Кабусікі Кайся | Антитіло, що зв'язується з il-8, та його застосування |
| AU2017263833B2 (en) | 2016-05-13 | 2023-08-03 | The General Hospital Corporation | Antagonistic anti-tumor necrosis factor receptor superfamily antibodies |
| WO2018185247A1 (en) | 2017-04-06 | 2018-10-11 | Universität Stuttgart | Tumor necrosis factor receptor (tnfr) binding protein complex with improved binding and bioactivity |
| WO2019226750A1 (en) | 2018-05-23 | 2019-11-28 | Kantum Diagnostics, Inc. | Methods of treating and preventing renal inflammation by inhibiting udp-hexose signaling |
| US12472266B2 (en) | 2019-02-21 | 2025-11-18 | Enosi Therapeutics Corporation | Antibodies and enonomers |
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2021
- 2021-08-27 IL IL300930A patent/IL300930A/he unknown
- 2021-08-27 KR KR1020237009895A patent/KR20230078657A/ko active Pending
- 2021-08-27 CN CN202180072889.2A patent/CN116847887A/zh active Pending
- 2021-08-27 CA CA3193273A patent/CA3193273A1/en active Pending
- 2021-08-27 EP EP21786626.8A patent/EP4204094A1/en active Pending
- 2021-08-27 WO PCT/US2021/048074 patent/WO2022047243A1/en not_active Ceased
- 2021-08-27 JP JP2023514071A patent/JP2023541816A/ja active Pending
- 2021-08-27 AU AU2021332460A patent/AU2021332460A1/en active Pending
Also Published As
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|---|---|
| WO2022047243A1 (en) | 2022-03-03 |
| CA3193273A1 (en) | 2022-03-03 |
| JP2023541816A (ja) | 2023-10-04 |
| KR20230078657A (ko) | 2023-06-02 |
| EP4204094A1 (en) | 2023-07-05 |
| AU2021332460A1 (en) | 2023-04-06 |
| CN116847887A (zh) | 2023-10-03 |
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