CA2899960C - Anti-cd83 antibodies and use thereof - Google Patents
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- CA2899960C CA2899960C CA2899960A CA2899960A CA2899960C CA 2899960 C CA2899960 C CA 2899960C CA 2899960 A CA2899960 A CA 2899960A CA 2899960 A CA2899960 A CA 2899960A CA 2899960 C CA2899960 C CA 2899960C
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Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2803—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the immunoglobulin superfamily
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/06—Immunosuppressants, e.g. drugs for graft rejection
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/545—Medicinal preparations containing antigens or antibodies characterised by the dose, timing or administration schedule
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/32—Immunoglobulins specific features characterized by aspects of specificity or valency specific for a neo-epitope on a complex, e.g. antibody-antigen or ligand-receptor
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/34—Identification of a linear epitope shorter than 20 amino acid residues or of a conformational epitope defined by amino acid residues
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/40—Immunoglobulins specific features characterized by post-translational modification
- C07K2317/41—Glycosylation, sialylation, or fucosylation
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/55—Fab or Fab'
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/60—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments
- C07K2317/62—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments comprising only variable region components
- C07K2317/622—Single chain antibody (scFv)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/60—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments
- C07K2317/62—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments comprising only variable region components
- C07K2317/626—Diabody or triabody
-
- 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
- C07K2317/72—Increased effector function due to an Fc-modification
-
- 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
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
- C07K2317/732—Antibody-dependent cellular cytotoxicity [ADCC]
-
- 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
Landscapes
- Health & Medical Sciences (AREA)
- Immunology (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biochemistry (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Mycology (AREA)
- Microbiology (AREA)
- Epidemiology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Transplantation (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201361759780P | 2013-02-01 | 2013-02-01 | |
| US61/759,780 | 2013-02-01 | ||
| PCT/AU2014/000066 WO2014117220A1 (en) | 2013-02-01 | 2014-01-31 | Anti-cd83 antibodies and use thereof |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CA2899960A1 CA2899960A1 (en) | 2014-08-07 |
| CA2899960C true CA2899960C (en) | 2022-05-03 |
Family
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Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2899960A Active CA2899960C (en) | 2013-02-01 | 2014-01-31 | Anti-cd83 antibodies and use thereof |
Country Status (13)
| Country | Link |
|---|---|
| US (3) | US9840559B2 (OSRAM) |
| EP (2) | EP3626743A1 (OSRAM) |
| JP (2) | JP6539585B2 (OSRAM) |
| KR (2) | KR102449868B1 (OSRAM) |
| CN (1) | CN105531289B (OSRAM) |
| AU (1) | AU2014213009B2 (OSRAM) |
| CA (1) | CA2899960C (OSRAM) |
| DK (1) | DK2951208T3 (OSRAM) |
| ES (1) | ES2762622T3 (OSRAM) |
| MX (1) | MX2015010023A (OSRAM) |
| NZ (1) | NZ711543A (OSRAM) |
| PT (1) | PT2951208T (OSRAM) |
| WO (1) | WO2014117220A1 (OSRAM) |
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| JP6539585B2 (ja) * | 2013-02-01 | 2019-07-03 | デンドロサイト バイオテック ピーティーワイ リミテッド | 抗ｃｄ８３抗体及びその使用 |
| CA2965170A1 (en) * | 2014-10-23 | 2016-04-28 | Dendrocyte Biotech Pty Ltd | Cd83 binding proteins and uses thereof |
| CA3074379A1 (en) * | 2017-09-13 | 2019-03-21 | Kira Biotech Pty Limited | Treatment method |
| AU2019226101A1 (en) * | 2018-02-23 | 2020-09-17 | H. Lee Moffitt Cancer Center And Research Institute Inc. | CD83-binding chimeric antigen receptors |
| EP4004051A4 (en) | 2019-07-19 | 2023-08-23 | Oncoresponse, Inc. | IMMUNOMODULATORY ANTIBODIES AND METHODS OF USE THEREOF |
| JP7701908B2 (ja) * | 2019-08-16 | 2025-07-02 | エイチ リー モフィット キャンサー センター アンド リサーチ インスティテュート インコーポレイテッド | 抗ｃｄ３８キメラ抗原受容体を発現する制御性ｔ細胞 |
| CN117547553A (zh) * | 2023-11-21 | 2024-02-13 | 中国人民解放军陆军特色医学中心 | Cd83+、cd83+pd-l1+间充质干细胞及其制备方法和应用 |
Family Cites Families (74)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4593089A (en) | 1980-07-30 | 1986-06-03 | Abbott Laboratories | Fluorescent polarization immunoassay utilizing substituted triazinylaminofluorescein aminoglycosides |
| US4554101A (en) | 1981-01-09 | 1985-11-19 | New York Blood Center, Inc. | Identification and preparation of epitopes on antigens and allergens on the basis of hydrophilicity |
| GB8308235D0 (en) | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| 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 |
| US4751190A (en) | 1985-07-22 | 1988-06-14 | Abbott Laboratories | Fluorescence polarization immunoassay and reagents for use therein |
| 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 |
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| EP0302894B1 (en) | 1986-04-28 | 1992-11-19 | Endotronics Inc. | Method of culturing leukocytes |
| US5260203A (en) | 1986-09-02 | 1993-11-09 | Enzon, Inc. | Single polypeptide chain binding molecules |
| US4946778A (en) | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| 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 |
| US6291158B1 (en) | 1989-05-16 | 2001-09-18 | Scripps Research Institute | Method for tapping the immunological repertoire |
| US5859205A (en) | 1989-12-21 | 1999-01-12 | Celltech Limited | Humanised antibodies |
| WO1994004679A1 (en) | 1991-06-14 | 1994-03-03 | Genentech, Inc. | Method for making humanized antibodies |
| US5565332A (en) | 1991-09-23 | 1996-10-15 | Medical Research Council | Production of chimeric antibodies - a combinatorial approach |
| ES2227512T3 (es) | 1991-12-02 | 2005-04-01 | Medical Research Council | Produccion de anticuerpos contra auto-antigenos a partir de repertorios de segmentos de anticuerpos fijados en un fago. |
| DE4211351A1 (de) | 1992-04-04 | 1993-10-07 | Behringwerke Ag | Verfahren zur Analyse partikelverstärkter Agglutinationsreaktionen auf Zentrifugalanalysatoren durch Bestimmung der Trübungsaufhellung |
| EP0569141A3 (en) | 1992-04-14 | 1994-10-26 | Hybritech Inc | Method for inhibiting the growth of multidrug-resistant tumors by antibodies. |
| US5316920A (en) | 1992-04-17 | 1994-05-31 | Dana-Faber Cancer Institute, Inc. | Lymphocyte activation antigen HB15, a member of the immunoglobulin superfamily |
| US5710262A (en) | 1992-04-17 | 1998-01-20 | Dana-Faber Cancer Institute, Inc. | Nucleic acid encoding HB15 polypeptides |
| US20080152586A1 (en) | 1992-09-25 | 2008-06-26 | Avipep Pty Limited | High avidity polyvalent and polyspecific reagents |
| US5844094A (en) | 1992-09-25 | 1998-12-01 | Commonwealth Scientific And Industrial Research Organization | Target binding polypeptide |
| WO1994009817A1 (en) | 1992-11-04 | 1994-05-11 | City Of Hope | Novel antibody construct |
| US5516637A (en) | 1994-06-10 | 1996-05-14 | Dade International Inc. | Method involving display of protein binding pairs on the surface of bacterial pili and bacteriophage |
| US5731168A (en) | 1995-03-01 | 1998-03-24 | Genentech, Inc. | Method for making heteromultimeric polypeptides |
| US6113898A (en) | 1995-06-07 | 2000-09-05 | Idec Pharmaceuticals Corporation | Human B7.1-specific primatized antibodies and transfectomas expressing said antibodies |
| CA2229043C (en) | 1995-08-18 | 2016-06-07 | Morphosys Gesellschaft Fur Proteinoptimierung Mbh | Protein/(poly)peptide libraries |
| GB9603256D0 (en) | 1996-02-16 | 1996-04-17 | Wellcome Found | Antibodies |
| US6541213B1 (en) | 1996-03-29 | 2003-04-01 | University Of Washington | Microscale diffusion immunoassay |
| US6699658B1 (en) | 1996-05-31 | 2004-03-02 | Board Of Trustees Of The University Of Illinois | Yeast cell surface display of proteins and uses thereof |
| CA2244326C (en) | 1997-08-11 | 2006-03-28 | Shinichi Eda | Microparticle enhanced light scattering agglutination assay and microparticle reagents therefor |
| ATE419009T1 (de) | 1997-10-31 | 2009-01-15 | Genentech Inc | Methoden und zusammensetzungen bestehend aus glykoprotein-glykoformen |
| PT2180007E (pt) | 1998-04-20 | 2013-11-25 | Roche Glycart Ag | Engenharia de glicosilação de anticorpos para melhorar a citotoxicidade celular dependente de anticorpos |
| US6562622B1 (en) | 1998-05-08 | 2003-05-13 | Diatech Pty, Ltd | Continuous in vitro evolution |
| ES2278463T3 (es) | 1998-12-08 | 2007-08-01 | Biovation Limited | Metodo para reducir la inmunogenicidad de proteinas. |
| WO2000042430A1 (en) | 1999-01-15 | 2000-07-20 | Medtox Scientific, Inc. | Lateral flow test strip |
| US6737056B1 (en) | 1999-01-15 | 2004-05-18 | Genentech, Inc. | Polypeptide variants with altered effector function |
| AU781547B2 (en) * | 1999-04-14 | 2005-05-26 | Government Of The United States Of America, As Represented By The Secretary Of The Department Of Health And Human Services, The | Compositions containing immunotoxins and agents that inhibit dendritic cell maturation for inducing immune tolerance to a graft |
| US7270969B2 (en) | 1999-05-05 | 2007-09-18 | Phylogica Limited | Methods of constructing and screening diverse expression libraries |
| DK1355919T3 (da) | 2000-12-12 | 2011-03-14 | Medimmune Llc | Molekyler med længere halveringstider, sammensætninger og anvendelser deraf |
| MXPA05000511A (es) | 2001-07-12 | 2005-09-30 | Jefferson Foote | Anticuepros super humanizados. |
| JP4264348B2 (ja) | 2001-08-20 | 2009-05-13 | プロテオム システムズ リミテッド | 診断検査方法および装置 |
| AR039067A1 (es) * | 2001-11-09 | 2005-02-09 | Pfizer Prod Inc | Anticuerpos para cd40 |
| EP1480598A4 (en) * | 2001-11-21 | 2006-03-22 | Celltech R & D Inc | HANDLING CYTOKINE RATES USING CD83 GENE PRODUCTS |
| US20040185040A1 (en) | 2001-11-21 | 2004-09-23 | Celltech R & D Limited | Modulating immune responses |
| US7317091B2 (en) | 2002-03-01 | 2008-01-08 | Xencor, Inc. | Optimized Fc variants |
| AU2002950779A0 (en) | 2002-08-15 | 2002-09-12 | The Corporation Of The Trustees Of The Order Of The Sisters Of Mercy In Queensland | A method of immunomodulation |
| US7217797B2 (en) | 2002-10-15 | 2007-05-15 | Pdl Biopharma, Inc. | Alteration of FcRn binding affinities or serum half-lives of antibodies by mutagenesis |
| EP1565753A2 (en) | 2002-11-21 | 2005-08-24 | The University Of Leicester | Bodily fluid markers of tissue hypoxia |
| AU2003300817A1 (en) * | 2002-11-21 | 2004-06-18 | Celltech R And D, Inc. | Modulating immune responses |
| US7169898B2 (en) * | 2002-12-04 | 2007-01-30 | Alexander Steinkasserer | Soluble CD83 proteins and use thereof for the treatment or prevention of a disease or medical condition caused by dysfunction or undesired function of a cellular immune response involving T cells |
| WO2004063351A2 (en) | 2003-01-09 | 2004-07-29 | Macrogenics, Inc. | IDENTIFICATION AND ENGINEERING OF ANTIBODIES WITH VARIANT Fc REGIONS AND METHODS OF USING SAME |
| CN1822857A (zh) | 2003-06-02 | 2006-08-23 | 阿莱克申药物公司 | 去免疫原性抗cd3抗体 |
| WO2005037867A1 (en) | 2003-10-15 | 2005-04-28 | Pdl Biopharma, Inc. | ALTERATION OF Fc-FUSION PROTEIN SERUM HALF-LIVES BY MUTAGENESIS OF POSITIONS 250, 314 AND/OR 428 OF THE HEAVY CHAIN CONSTANT REGION OF IG |
| JP4653109B2 (ja) | 2003-11-05 | 2011-03-16 | ロシュ グリクアート アクチェンゲゼルシャフト | 高められたＦｃレセプター結合親和性及びエフェクター機能をもつＣＤ２０抗体 |
| US8802820B2 (en) | 2004-11-12 | 2014-08-12 | Xencor, Inc. | Fc variants with altered binding to FcRn |
| US20070135620A1 (en) | 2004-11-12 | 2007-06-14 | Xencor, Inc. | Fc variants with altered binding to FcRn |
| JP2008523083A (ja) | 2004-12-08 | 2008-07-03 | イムノメディクス， インコーポレイテッド | 炎症性疾患および免疫調節不全疾患、感染性疾患、病的血管新生およびがんの免疫療法および検出のための方法および組成物 |
| WO2006102720A1 (en) | 2005-03-31 | 2006-10-05 | Telethon Institute For Child Health Research | Isolation of inhibitor of ires-mediated translation |
| KR20170086700A (ko) * | 2005-04-08 | 2017-07-26 | 아르고스 쎄라퓨틱스 인코포레이티드 | 수지상 세포 조성물 및 방법 |
| EP1945668A4 (en) | 2005-08-15 | 2009-07-22 | Arana Therapeutics Ltd | SYNTHETIC ANTIBODIES WITH FRAMEWORK REGIONS OF NEUWELTPRIMATEN |
| WO2007150020A1 (en) * | 2006-06-23 | 2007-12-27 | Simon Paul M | Targeted immune conjugates |
| EP1985305A1 (en) | 2007-04-24 | 2008-10-29 | Vivalis | Duck embryonic derived stem cell lines for the production of viral vaccines |
| EP1995309A1 (en) | 2007-05-21 | 2008-11-26 | Vivalis | Recombinant protein production in avian EBx® cells |
| EP2207803B1 (en) * | 2008-06-25 | 2013-05-01 | Korea Research Institute of Bioscience and Biotechnology | Cd9-specific human antibodies |
| AR074369A1 (es) | 2008-11-20 | 2011-01-12 | Genentech Inc | Anticuerpos anti-unc 5b (receptor de netrina) y metodos de uso |
| US20120195900A1 (en) | 2010-12-22 | 2012-08-02 | Abbott Laboratories | Tri-variable domain binding proteins and uses thereof |
| JP2013040160A (ja) | 2011-07-01 | 2013-02-28 | Genentech Inc | 自己免疫疾患を治療するための抗ｃｄ８３アゴニスト抗体の使用 |
| JP6539585B2 (ja) | 2013-02-01 | 2019-07-03 | デンドロサイト バイオテック ピーティーワイ リミテッド | 抗ｃｄ８３抗体及びその使用 |
| CA2965170A1 (en) | 2014-10-23 | 2016-04-28 | Dendrocyte Biotech Pty Ltd | Cd83 binding proteins and uses thereof |
| CA3074379A1 (en) | 2017-09-13 | 2019-03-21 | Kira Biotech Pty Limited | Treatment method |
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2019
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2020
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| CN105531289A (zh) | 2016-04-27 |
| US20200339684A1 (en) | 2020-10-29 |
| US20180201681A1 (en) | 2018-07-19 |
| MX2015010023A (es) | 2017-11-17 |
| US10781255B2 (en) | 2020-09-22 |
| EP2951208B1 (en) | 2019-11-13 |
| AU2014213009A1 (en) | 2015-09-17 |
| EP3626743A1 (en) | 2020-03-25 |
| KR102449868B1 (ko) | 2022-10-04 |
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| NZ711543A (en) | 2020-08-28 |
| US9840559B2 (en) | 2017-12-12 |
| JP2019076102A (ja) | 2019-05-23 |
| KR20150135250A (ko) | 2015-12-02 |
| US11725054B2 (en) | 2023-08-15 |
| PT2951208T (pt) | 2019-12-30 |
| KR20200120967A (ko) | 2020-10-22 |
| JP6539585B2 (ja) | 2019-07-03 |
| CA2899960A1 (en) | 2014-08-07 |
| EP2951208A1 (en) | 2015-12-09 |
| CN105531289B (zh) | 2019-02-22 |
| KR102204127B1 (ko) | 2021-01-20 |
| AU2014213009B2 (en) | 2019-01-03 |
| ES2762622T3 (es) | 2020-05-25 |
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| US20150376277A1 (en) | 2015-12-31 |
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| JP2016507521A (ja) | 2016-03-10 |
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