TWI700093B - 雙重ｖ區類抗體蛋白質之用途 - Google Patents
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| TWI803876B (zh) * | 2011-03-28 | 2023-06-01 | 法商賽諾菲公司 | 具有交叉結合區定向之雙重可變區類抗體結合蛋白 |
| EP2916866B1 (de) * | 2012-11-06 | 2018-04-04 | Bayer Pharma Aktiengesellschaft | Formulierung für bispecific t-cell-engangers (bites) |
| TWI679019B (zh) | 2013-04-29 | 2019-12-11 | 法商賽諾菲公司 | 抗ｉｌ－４／抗ｉｌ－１３之雙特異性抗體調配物 |
| TW201542226A (zh) * | 2014-02-12 | 2015-11-16 | Sanofi Sa | 抗－ｉｌ－４／抗－ｉｌ－１３雙特異性抗體／聚麩胺酸配製物 |
| TW201628647A (zh) * | 2014-06-27 | 2016-08-16 | 賽諾菲公司 | 抗－ｉｌ４－ｉｌ１３雙特異性抗體 |
| MA40164A (fr) * | 2014-06-27 | 2017-05-03 | Sanofi Sa | Anticorps bispécifiques anti-il4-il13 |
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| CN120204385A (zh) | 2019-05-24 | 2025-06-27 | 赛诺菲 | 治疗系统性硬化症的方法 |
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| US4450254A (en) | 1980-11-03 | 1984-05-22 | Standard Oil Company | Impact improvement of high nitrile resins |
| US4315929A (en) | 1981-01-27 | 1982-02-16 | The United States Of America As Represented By The Secretary Of Agriculture | Method of controlling the European corn borer with trewiasine |
| US4313946A (en) | 1981-01-27 | 1982-02-02 | The United States Of America As Represented By The Secretary Of Agriculture | Chemotherapeutically active maytansinoids from Trewia nudiflora |
| JPS57192389A (en) | 1981-05-20 | 1982-11-26 | Takeda Chem Ind Ltd | Novel maytansinoid |
| US4640835A (en) | 1981-10-30 | 1987-02-03 | Nippon Chemiphar Company, Ltd. | Plasminogen activator derivatives |
| US4716111A (en) | 1982-08-11 | 1987-12-29 | Trustees Of Boston University | Process for producing human antibodies |
| US4560655A (en) | 1982-12-16 | 1985-12-24 | Immunex Corporation | Serum-free cell culture medium and process for making same |
| US4657866A (en) | 1982-12-21 | 1987-04-14 | Sudhir Kumar | Serum-free, synthetic, completely chemically defined tissue culture media |
| GB8308235D0 (en) | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US4767704A (en) | 1983-10-07 | 1988-08-30 | Columbia University In The City Of New York | Protein-free culture medium |
| US4496689A (en) | 1983-12-27 | 1985-01-29 | Miles Laboratories, Inc. | Covalently attached complex of alpha-1-proteinase inhibitor with a water soluble polymer |
| US5807715A (en) | 1984-08-27 | 1998-09-15 | The Board Of Trustees Of The Leland Stanford Junior University | Methods and transformed mammalian lymphocyte cells for producing functional antigen-binding protein including chimeric immunoglobulin |
| EP0216846B2 (en) | 1985-04-01 | 1995-04-26 | Celltech Limited | Transformed myeloma cell-line and a process for the expression of a gene coding for a eukaryotic polypeptide employing same |
| US4737456A (en) | 1985-05-09 | 1988-04-12 | Syntex (U.S.A.) Inc. | Reducing interference in ligand-receptor binding assays |
| EP0206448B1 (en) | 1985-06-19 | 1990-11-14 | Ajinomoto Co., Inc. | Hemoglobin combined with a poly(alkylene oxide) |
| US4676980A (en) | 1985-09-23 | 1987-06-30 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Target specific cross-linked heteroantibodies |
| US5618920A (en) | 1985-11-01 | 1997-04-08 | Xoma Corporation | Modular assembly of antibody genes, antibodies prepared thereby and use |
| GB8601597D0 (en) | 1986-01-23 | 1986-02-26 | Wilson R H | Nucleotide sequences |
| EP0272253A4 (en) | 1986-03-07 | 1990-02-05 | Massachusetts Inst Technology | METHOD FOR IMPROVING GLYCOPROTE INSTABILITY. |
| GB8607679D0 (en) | 1986-03-27 | 1986-04-30 | Winter G P | Recombinant dna product |
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| US4791192A (en) | 1986-06-26 | 1988-12-13 | Takeda Chemical Industries, Ltd. | Chemically modified protein with polyethyleneglycol |
| US4946778A (en) | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| GB8717430D0 (en) | 1987-07-23 | 1987-08-26 | Celltech Ltd | Recombinant dna product |
| IL89489A0 (en) | 1988-03-09 | 1989-09-10 | Hybritech Inc | Chimeric antibodies directed against human carcinoembryonic antigen |
| EP0362371A4 (en) | 1988-04-15 | 1990-10-24 | Protein Design Labs, Inc. | Il-2 receptor-specific chimeric antibodies |
| ATE119198T1 (de) | 1988-04-16 | 1995-03-15 | Celltech Ltd | Verfahren zur herstellung von proteinen mittels rekombinanter dna. |
| AU631802B2 (en) | 1988-06-14 | 1992-12-10 | Cetus Oncology Corporation | Coupling agents and sterically hindered disulfide linked conjugates prepared therefrom |
| US5223409A (en) | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
| US6048728A (en) | 1988-09-23 | 2000-04-11 | Chiron Corporation | Cell culture medium for enhanced cell growth, culture longevity, and product expression |
| US5534617A (en) | 1988-10-28 | 1996-07-09 | Genentech, Inc. | Human growth hormone variants having greater affinity for human growth hormone receptor at site 1 |
| WO1990005144A1 (en) | 1988-11-11 | 1990-05-17 | Medical Research Council | Single domain ligands, receptors comprising said ligands, methods for their production, and use of said ligands and receptors |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| ZA902949B (en) | 1989-05-05 | 1992-02-26 | Res Dev Foundation | A novel antibody delivery system for biological response modifiers |
| IL94611A (en) | 1989-06-05 | 1994-12-29 | Organogenesis Inc | Medium for cell cultures containing insulin or growth factor similar to insulin, transferrin or iron ion, triiodothyronine or thyroxine and method of use |
| US5413923A (en) | 1989-07-25 | 1995-05-09 | Cell Genesys, Inc. | Homologous recombination for universal donor cells and chimeric mammalian hosts |
| FR2650598B1 (fr) | 1989-08-03 | 1994-06-03 | Rhone Poulenc Sante | Derives de l'albumine a fonction therapeutique |
| GB8928874D0 (en) | 1989-12-21 | 1990-02-28 | Celltech Ltd | Humanised antibodies |
| DE69133566T2 (de) | 1990-01-12 | 2007-12-06 | Amgen Fremont Inc. | Bildung von xenogenen Antikörpern |
| US5314995A (en) | 1990-01-22 | 1994-05-24 | Oncogen | Therapeutic interleukin-2-antibody based fusion proteins |
| WO1991014438A1 (en) | 1990-03-20 | 1991-10-03 | The Trustees Of Columbia University In The City Of New York | Chimeric antibodies with receptor binding ligands in place of their constant region |
| GB9015198D0 (en) | 1990-07-10 | 1990-08-29 | Brien Caroline J O | Binding substance |
| US5633425A (en) | 1990-08-29 | 1997-05-27 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
| KR100272077B1 (ko) | 1990-08-29 | 2000-11-15 | 젠팜인터내셔날,인코포레이티드 | 이종 항체를 생산할 수 있는 전이유전자를 가진 인간이외의 동물 |
| US5814318A (en) | 1990-08-29 | 1998-09-29 | Genpharm International Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5625126A (en) | 1990-08-29 | 1997-04-29 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5661016A (en) | 1990-08-29 | 1997-08-26 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| US5122469A (en) | 1990-10-03 | 1992-06-16 | Genentech, Inc. | Method for culturing Chinese hamster ovary cells to improve production of recombinant proteins |
| ATE218889T1 (de) | 1990-11-09 | 2002-06-15 | Stephen D Gillies | Cytokine immunokonjugate |
| DE69233482T2 (de) | 1991-05-17 | 2006-01-12 | Merck & Co., Inc. | Verfahren zur Verminderung der Immunogenität der variablen Antikörperdomänen |
| US5565332A (en) | 1991-09-23 | 1996-10-15 | Medical Research Council | Production of chimeric antibodies - a combinatorial approach |
| WO1993008829A1 (en) | 1991-11-04 | 1993-05-13 | The Regents Of The University Of California | Compositions that mediate killing of hiv-infected cells |
| AU3178993A (en) | 1991-11-25 | 1993-06-28 | Enzon, Inc. | Multivalent antigen-binding proteins |
| ATE408012T1 (de) | 1991-12-02 | 2008-09-15 | Medical Res Council | Herstellung von autoantikörpern auf phagenoberflächen ausgehend von antikörpersegmentbibliotheken |
| US5869619A (en) | 1991-12-13 | 1999-02-09 | Xoma Corporation | Modified antibody variable domains |
| FR2686899B1 (fr) | 1992-01-31 | 1995-09-01 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides biologiquement actifs, leur preparation et compositions pharmaceutiques les contenant. |
| FR2686901A1 (fr) | 1992-01-31 | 1993-08-06 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides antithrombotiques, leur preparation et compositions pharmaceutiques les contenant. |
| ATE419355T1 (de) | 1992-02-06 | 2009-01-15 | Novartis Vaccines & Diagnostic | Marker für krebs und biosynthetisches bindeprotein dafür |
| ES2149768T3 (es) | 1992-03-25 | 2000-11-16 | Immunogen Inc | Conjugados de agentes enlazantes de celulas derivados de cc-1065. |
| WO1993021319A1 (en) | 1992-04-08 | 1993-10-28 | Cetus Oncology Corporation | HUMANIZED C-erbB-2 SPECIFIC ANTIBODIES |
| ZA932522B (en) | 1992-04-10 | 1993-12-20 | Res Dev Foundation | Immunotoxins directed against c-erbB-2(HER/neu) related surface antigens |
| EP0749475A4 (en) | 1992-08-26 | 1997-05-07 | Harvard College | USE OF CYTOKINE IP-10 AS ANTI-TUMOR AGENT |
| US5639641A (en) | 1992-09-09 | 1997-06-17 | Immunogen Inc. | Resurfacing of rodent antibodies |
| DE69427974T2 (de) | 1993-04-29 | 2001-12-06 | Unilever N.V., Rotterdam | Herstellung von antikörpern oder funktionstüchtig gemachten teilen davon, abgeleitet von schweren ketten von immunglobulinen von camelidae |
| US5928904A (en) | 1993-09-07 | 1999-07-27 | Smithkline Beecham Corporation | DNA encoding recombinant IL4 antibodies useful in treatment of IL4 mediated disorders |
| US5705154A (en) | 1995-03-08 | 1998-01-06 | Schering Corporation | Humanized monoclonal antibodies against human interleukin-4 |
| US6165463A (en) | 1997-10-16 | 2000-12-26 | Inhale Therapeutic Systems, Inc. | Dispersible antibody compositions and methods for their preparation and use |
| JP4312259B2 (ja) | 1995-04-27 | 2009-08-12 | アムジェン フレモント インク． | 免疫したゼノマウス（ＸｅｎｏＭｏｕｓｅ）に由来するヒト抗体 |
| EP0823941A4 (en) | 1995-04-28 | 2001-09-19 | Abgenix Inc | HUMAN ANTIBODIES DERIVED FROM IMMUNIZED XENO MOUSES |
| BR9606706A (pt) | 1995-10-16 | 1999-04-06 | Unilever Nv | Análogo de fragmento de anticorpo biespecífico ou bivalente uso processo para produzir o mesmo |
| US6664227B1 (en) | 1996-03-01 | 2003-12-16 | Genetics Institute, Llc | Treatment of fibrosis by antagonism of IL-13 and IL-13 receptor chains |
| WO1997033899A1 (en) | 1996-03-14 | 1997-09-18 | Human Genome Sciences, Inc. | Apoptosis inducing molecule i |
| WO1997034631A1 (en) | 1996-03-18 | 1997-09-25 | Board Of Regents, The University Of Texas System | Immunoglobin-like domains with increased half lives |
| EP0904278A4 (en) | 1996-03-22 | 1999-09-15 | Human Genome Sciences Inc | MOLECULE II INDUCER OF APOPTOSIS |
| JPH11507843A (ja) | 1996-03-28 | 1999-07-13 | ザ・ジョンズ・ホプキンス・ユニバーシティー | タンパク質の可溶性二価および多価ヘテロ二量体類縁体 |
| US5916771A (en) | 1996-10-11 | 1999-06-29 | Abgenix, Inc. | Production of a multimeric protein by cell fusion method |
| WO1998023289A1 (en) | 1996-11-27 | 1998-06-04 | The General Hospital Corporation | MODULATION OF IgG BINDING TO FcRn |
| DE69738539T2 (de) | 1996-12-03 | 2009-03-26 | Amgen Fremont Inc. | Vollkommen humane Antikörper die EGFR binden |
| US6277375B1 (en) | 1997-03-03 | 2001-08-21 | Board Of Regents, The University Of Texas System | Immunoglobulin-like domains with increased half-lives |
| BRPI9809391B8 (pt) | 1997-04-14 | 2021-05-25 | Amgen Res Munich Gmbh | processo para a produção de um receptor de antígeno anti-humano, anticorpo humano e composição farmacêutica |
| US6235883B1 (en) | 1997-05-05 | 2001-05-22 | Abgenix, Inc. | Human monoclonal antibodies to epidermal growth factor receptor |
| DK1272647T3 (en) | 2000-04-11 | 2014-12-15 | Genentech Inc | Multivalent antibodies and uses thereof |
| CA2405550A1 (en) | 2000-04-12 | 2001-10-25 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| WO2001090192A2 (en) | 2000-05-24 | 2001-11-29 | Imclone Systems Incorporated | Bispecific immunoglobulin-like antigen binding proteins and method of production |
| WO2002008293A2 (en) | 2000-07-25 | 2002-01-31 | Immunomedics Inc. | Multivalent target binding protein |
| US6333410B1 (en) | 2000-08-18 | 2001-12-25 | Immunogen, Inc. | Process for the preparation and purification of thiol-containing maytansinoids |
| US20040023338A1 (en) | 2001-10-26 | 2004-02-05 | Heavner George A. | IL-4 mutein proteins, antibodies, compositions, methods and uses |
| CA2464695A1 (en) | 2001-10-26 | 2003-05-01 | Centocor, Inc. | Il-13 mutein proteins, antibodies, compositions, methods and uses |
| CA2480777A1 (en) | 2002-05-01 | 2003-11-13 | Regeneron Pharmaceuticals, Inc. | Methods of using cytokine antagonists to treat hiv infection and aids |
| FR2840614B1 (fr) | 2002-06-07 | 2004-08-27 | Flamel Tech Sa | Polyaminoacides fonctionnalises par de l'alpha-tocopherol et leurs applications notamment therapeutiques |
| US20040033228A1 (en) | 2002-08-16 | 2004-02-19 | Hans-Juergen Krause | Formulation of human antibodies for treating TNF-alpha associated disorders |
| EP1618181B1 (en) | 2003-04-22 | 2014-10-15 | IBC Pharmaceuticals | Polyvalent protein complex |
| BRPI0412418A (pt) | 2003-07-10 | 2006-08-22 | Wyeth Corp | expressão recombinante de protease de cisteìna de streptococcus pyogenes e composições imunogênicas da mesma |
| GB0407315D0 (en) | 2003-07-15 | 2004-05-05 | Cambridge Antibody Tech | Human antibody molecules |
| PL1711528T3 (pl) | 2003-12-23 | 2012-11-30 | Genentech Inc | Leczenie nowotworu nowymi przeciwciałami monoklonalnymi anty-IL13 |
| US7652146B2 (en) | 2004-02-06 | 2010-01-26 | Bristol-Myers Squibb Company | Process for preparing 2-aminothiazole-5-carboxamides useful as kinase inhibitors |
| US7666583B2 (en) | 2004-02-19 | 2010-02-23 | Yale University | Identification of cancer protein biomarkers using proteomic techniques |
| CA2554596A1 (en) | 2004-02-27 | 2005-09-15 | Regeneron Pharmaceuticals, Inc. | Il-4/il-13 specific polypetides and therapeutic uses thereof |
| GB0411186D0 (en) | 2004-05-19 | 2004-06-23 | Celltech R&D Ltd | Biological products |
| CA2568428C (en) | 2004-05-25 | 2020-12-29 | Attenuon, Llc | Ligands binding the complex of urokinase-type plasminogen activator (upa) and its receptor (upar) that inhibit downstream upar interactions: identification and use in diagnosis or therapy |
| AR049390A1 (es) | 2004-06-09 | 2006-07-26 | Wyeth Corp | Anticuerpos contra la interleuquina-13 humana y usos de los mismos |
| US20060148009A1 (en) | 2004-10-12 | 2006-07-06 | Xencor, Inc. | Prediction and assessment of immunogenicity |
| WO2006117910A1 (ja) | 2005-04-28 | 2006-11-09 | Mochida Pharmaceutical Co., Ltd. | 抗血小板膜糖蛋白質ⅵモノクローナル抗体 |
| GB0514319D0 (en) | 2005-07-13 | 2006-06-14 | Secr Defence | Antibodies for anthrax |
| US7612181B2 (en) | 2005-08-19 | 2009-11-03 | Abbott Laboratories | Dual variable domain immunoglobulin and uses thereof |
| JP2009510046A (ja) | 2005-09-30 | 2009-03-12 | メドイミューン・リミテッド | インターロイキン−１３抗体組成物 |
| MY144906A (en) | 2005-10-21 | 2011-11-30 | Novartis Ag | Human antibodies against il13 and therapeutic uses |
| GB0600488D0 (en) | 2006-01-11 | 2006-02-22 | Glaxo Group Ltd | Immunoglobulins |
| AU2007209202A1 (en) | 2006-01-24 | 2007-08-02 | Domantis Limited | Ligands that bind IL-4 and/or IL-13 |
| CA2646626A1 (en) | 2006-03-22 | 2007-09-27 | Apogenix Gmbh | Antibody specific for human il-4 for the treatment of cancer |
| MY161894A (en) * | 2006-09-08 | 2017-05-15 | Abbvie Bahamas Ltd | Interleukin-13 binding proteins |
| CA2672878A1 (en) * | 2006-12-15 | 2008-06-26 | Centocor Ortho Biotech Inc. | Methods and compositions for treating il-4 or il-13 related fibrosis related pathologies |
| CN101600457B (zh) | 2007-01-09 | 2014-01-08 | 惠氏公司 | 抗il-13抗体调配物和其用途 |
| BRPI0817664A2 (pt) * | 2007-10-12 | 2015-03-24 | Massachusetts Inst Technology | Nanopartículas, método para preparar nanopartículas e método para tratar terapeuticamente ou profilaticamente um indivíduo |
| US9308257B2 (en) | 2007-11-28 | 2016-04-12 | Medimmune, Llc | Protein formulation |
| DE112008003232T5 (de) * | 2007-11-30 | 2011-02-24 | Glaxo Group Limited, Greenford | Antigen-Bindungskonstrukte |
| EP2196476A1 (en) | 2008-12-10 | 2010-06-16 | Novartis Ag | Antibody formulation |
| WO2011017070A1 (en) | 2009-07-28 | 2011-02-10 | Merck Sharp & Dohme Corp. | Methods for producing high concentration lyophilized pharmaceutical formulations |
| PL3037104T3 (pl) * | 2009-10-20 | 2020-11-16 | Abbvie Inc. | Izolacja i oczyszczanie przeciwciał anty-il-13 z zastosowaniem chromatografii powinowactwa z białkiem a |
| EP3431485B2 (en) * | 2010-10-01 | 2024-09-04 | ModernaTX, Inc. | Engineered nucleic acids and methods of use thereof |
| EP2686014A1 (en) | 2011-03-16 | 2014-01-22 | Sanofi | Uses of a dual v region antibody-like protein |
| TWI803876B (zh) | 2011-03-28 | 2023-06-01 | 法商賽諾菲公司 | 具有交叉結合區定向之雙重可變區類抗體結合蛋白 |
| TWI679019B (zh) | 2013-04-29 | 2019-12-11 | 法商賽諾菲公司 | 抗ｉｌ－４／抗ｉｌ－１３之雙特異性抗體調配物 |
-
2012
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- 2012-03-15 US US14/003,496 patent/US20130344074A1/en not_active Abandoned
- 2012-03-15 WO PCT/US2012/029147 patent/WO2012125775A1/en not_active Ceased
- 2012-03-15 TW TW101108867A patent/TWI700093B/zh active
- 2012-03-15 AR ARP120100851A patent/AR085911A1/es unknown
- 2012-03-15 JP JP2013558155A patent/JP2014510730A/ja active Pending
- 2012-03-15 TW TW106101119A patent/TWI719112B/zh active
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- 2012-03-15 EP EP17151270.0A patent/EP3235508B1/en active Active
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2021
- 2021-04-07 US US17/224,861 patent/US20210221882A1/en not_active Abandoned
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2009052081A2 (en) * | 2007-10-15 | 2009-04-23 | Sanofi-Aventis | Antibodies that bind il-4 and/or il-13 and their uses |
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Also Published As
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| AR085911A1 (es) | 2013-11-06 |
| JP2014510730A (ja) | 2014-05-01 |
| JP6121598B2 (ja) | 2017-04-26 |
| EP3235508B1 (en) | 2020-12-30 |
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| US11008389B2 (en) | 2021-05-18 |
| PL3235508T3 (pl) | 2021-07-12 |
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| EP2686014A1 (en) | 2014-01-22 |
| US20210221882A1 (en) | 2021-07-22 |
| TW201300127A (zh) | 2013-01-01 |
| JP2017137336A (ja) | 2017-08-10 |
| US20130344074A1 (en) | 2013-12-26 |
| JP2016196485A (ja) | 2016-11-24 |
| TW201731529A (zh) | 2017-09-16 |
| JP6480970B2 (ja) | 2019-03-13 |
| EP3235508A1 (en) | 2017-10-25 |
| US20170029498A1 (en) | 2017-02-02 |
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