JP2016505826A5 - - Google Patents
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- JP2016505826A5 JP2016505826A5 JP2015545941A JP2015545941A JP2016505826A5 JP 2016505826 A5 JP2016505826 A5 JP 2016505826A5 JP 2015545941 A JP2015545941 A JP 2015545941A JP 2015545941 A JP2015545941 A JP 2015545941A JP 2016505826 A5 JP2016505826 A5 JP 2016505826A5
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Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201261735516P | 2012-12-10 | 2012-12-10 | |
| US61/735,516 | 2012-12-10 | ||
| US201361794685P | 2013-03-15 | 2013-03-15 | |
| US61/794,685 | 2013-03-15 | ||
| PCT/US2013/074218 WO2014093406A1 (en) | 2012-12-10 | 2013-12-10 | Methods for screening |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2016505826A JP2016505826A (ja) | 2016-02-25 |
| JP2016505826A5 true JP2016505826A5 (OSRAM) | 2017-02-02 |
Family
ID=49883268
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2015545941A Ceased JP2016505826A (ja) | 2012-12-10 | 2013-12-10 | スクリーニングの方法 |
| JP2015545938A Pending JP2016505251A (ja) | 2012-12-10 | 2013-12-10 | リポカリン融合パートナー |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2015545938A Pending JP2016505251A (ja) | 2012-12-10 | 2013-12-10 | リポカリン融合パートナー |
Country Status (11)
| Country | Link |
|---|---|
| US (4) | US10156559B2 (OSRAM) |
| EP (2) | EP2928913A1 (OSRAM) |
| JP (2) | JP2016505826A (OSRAM) |
| CN (2) | CN105189540A (OSRAM) |
| AU (2) | AU2013359429A1 (OSRAM) |
| BR (2) | BR112015013525A2 (OSRAM) |
| CA (2) | CA2913029A1 (OSRAM) |
| IL (2) | IL239261A0 (OSRAM) |
| RU (2) | RU2015126651A (OSRAM) |
| SG (2) | SG11201504600UA (OSRAM) |
| WO (2) | WO2014093406A1 (OSRAM) |
Families Citing this family (29)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP3165533B1 (en) | 2010-05-11 | 2020-04-08 | Fred Hutchinson Cancer Research Center | Chlorotoxin variants, conjugates and methods for their use |
| CN108524919A (zh) | 2012-05-17 | 2018-09-14 | 延伸生物科学股份有限公司 | 用于改进的药物递送的载体 |
| CA2913029A1 (en) | 2012-12-10 | 2014-06-19 | Fred Hutchinson Cancer Research Center | Lipocalin fusion partners |
| US11559580B1 (en) | 2013-09-17 | 2023-01-24 | Blaze Bioscience, Inc. | Tissue-homing peptide conjugates and methods of use thereof |
| KR101576904B1 (ko) | 2014-07-31 | 2015-12-14 | (주)케어젠 | 파골세포 분화 및 활성 억제능을 갖는 펩타이드 및 이의 용도 |
| US9616109B2 (en) | 2014-10-22 | 2017-04-11 | Extend Biosciences, Inc. | Insulin vitamin D conjugates |
| US9789197B2 (en) | 2014-10-22 | 2017-10-17 | Extend Biosciences, Inc. | RNAi vitamin D conjugates |
| WO2016065042A1 (en) | 2014-10-22 | 2016-04-28 | Extend Biosciences, Inc. | Therapeutic vitamin d conjugates |
| CA2980838A1 (en) * | 2015-05-18 | 2016-11-24 | Pieris Pharmaceuticals Gmbh | Anti-cancer fusion polypeptide |
| CN107847554A (zh) * | 2015-06-26 | 2018-03-27 | 弗莱德哈钦森癌症研究中心 | 治疗性肽及其使用方法 |
| JP2018521994A (ja) * | 2015-06-26 | 2018-08-09 | フレッド ハッチンソン キャンサー リサーチ センター | 治療用ペプチドおよびそれらの使用方法 |
| JP6966424B2 (ja) * | 2015-09-09 | 2021-11-17 | フレッド ハッチンソン キャンサー リサーチ センター | 軟骨ホーミングペプチド |
| PT3362470T (pt) * | 2015-10-13 | 2021-12-10 | Hope City | Recetores de antigénios quiméricos que contêm um domínio de clorotoxina |
| EP3373952A4 (en) * | 2015-11-10 | 2019-05-22 | Fred Hutchinson Cancer Research Center | NKG2D decoys |
| CN105348392B (zh) * | 2015-11-18 | 2019-08-02 | 北京华金瑞清生物医药技术有限公司 | 一种Nav1.7抑制剂及其改造方法 |
| EP3442555A4 (en) * | 2016-04-15 | 2020-04-01 | Blaze Bioscience, Inc. | METHOD FOR TREATING BREAST CANCER |
| AU2017250359B2 (en) | 2016-04-15 | 2022-06-16 | Blaze Bioscience, Inc. | Methods of treating breast cancer |
| WO2018039283A1 (en) * | 2016-08-22 | 2018-03-01 | Fred Hutchinson Cancer Research Center | Peptides and methods of use thereof |
| EP4529966A3 (en) | 2016-08-29 | 2025-06-18 | Fred Hutchinson Cancer Center | Chelating platform for delivery of radionuclides |
| CN106699866A (zh) * | 2016-12-13 | 2017-05-24 | 山西农业大学 | 一种鸡细胞外脂肪酸结合蛋白、原核表达及其纯化方法 |
| WO2018136614A1 (en) | 2017-01-18 | 2018-07-26 | Fred Hutchinson Cancer Research Center | Peptide compositions and methods of use thereof for disrupting tead interactions |
| CN110475565A (zh) * | 2017-03-16 | 2019-11-19 | 光明之火生物科学公司 | 软骨归巢肽缀合物及其使用方法 |
| WO2018232122A1 (en) | 2017-06-15 | 2018-12-20 | Blaze Bioscience, Inc. | Renal-homing peptide conjugates and methods of use thereof |
| CN107739410B (zh) * | 2017-10-18 | 2021-07-30 | 南京鼓楼医院 | CD3单链抗体-iRGD融合蛋白、制备及其作为抗肿瘤药物的应用 |
| CA3086040A1 (en) | 2017-12-19 | 2019-06-27 | Blaze Bioscience, Inc. | Tumor homing and cell penetrating peptide-immuno-oncology agent complexes and methods of use thereof |
| WO2019178573A1 (en) * | 2018-03-16 | 2019-09-19 | Blaze Bioscience, Inc. | Truncated cartilage-homing peptides and peptide complexes and methods of use thereof |
| WO2021126341A1 (en) * | 2019-12-19 | 2021-06-24 | Blaze Bioscience, Inc. | Methods of treating vascular lesions and malformations |
| CN115329965B (zh) * | 2022-08-16 | 2025-08-01 | 北京有竹居网络技术有限公司 | 数据处理方法和电子设备 |
| IL319526A (en) | 2022-09-30 | 2025-05-01 | Extend Biosciences Inc | Long-acting parathyroid hormone |
Family Cites Families (118)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4444744A (en) | 1980-03-03 | 1984-04-24 | Goldenberg Milton David | Tumor localization and therapy with labeled antibodies to cell surface antigens |
| DE3407582A1 (de) | 1984-03-01 | 1985-09-05 | Dornier System Gmbh, 7990 Friedrichshafen | Schaltungsanordnung fuer einen regelkreis |
| AU617652B2 (en) | 1986-09-19 | 1991-12-05 | Scripps Clinic And Research Foundation | Monoclonal paratopic molecule directed to human ganglioside gd2 |
| US5591829A (en) | 1987-05-29 | 1997-01-07 | Matsushita; Shuzo | Antibodies modified with toxic substance |
| US5051364A (en) | 1989-02-16 | 1991-09-24 | The Salk Institute For Biological Studies | Anti-lipocortin-I and anti-lipocortin-II monoclonal antibodies |
| DE3909799A1 (de) | 1989-03-24 | 1990-09-27 | Behringwerke Ag | Monoklonale antikoerper (mak) gegen tumorassoziierte antigene, ihre herstellung und verwendung |
| ATE135373T1 (de) | 1989-09-08 | 1996-03-15 | Univ Johns Hopkins | Modifikationen der struktur des egf-rezeptor-gens in menschlichen glioma |
| US5223253A (en) | 1989-09-28 | 1993-06-29 | American Home Products Corporation | Bovine vaccine compositions and method for preventing trichomonas infections using same |
| US5650489A (en) | 1990-07-02 | 1997-07-22 | The Arizona Board Of Regents | Random bio-oligomer library, a method of synthesis thereof, and a method of use thereof |
| GB2250993B (en) | 1990-11-21 | 1995-02-15 | Inst Nat Sante Rech Med | Stromelysin-3 and its application in the diagnosis and treatment of malignant breast cancer |
| US5750376A (en) | 1991-07-08 | 1998-05-12 | Neurospheres Holdings Ltd. | In vitro growth and proliferation of genetically modified multipotent neural stem cells and their progeny |
| ATE275197T1 (de) | 1991-09-20 | 2004-09-15 | Amgen Inc | Glial neurotrophe faktor |
| US5314992A (en) | 1991-11-25 | 1994-05-24 | Trustees Of Dartmouth College | Lipocortin-1 receptor protein and its uses |
| WO1993023075A1 (en) | 1992-05-14 | 1993-11-25 | Oncologix, Inc. | Treatment of vascular leakage syndrome and collagenase induced disease by administration of matrix metalloproteinase inhibitors |
| RU2148401C1 (ru) | 1993-01-13 | 2000-05-10 | Канзер Рисерч Кампейн Технолоджи, Лтд. | Фармацевтическая композиция с антиопухолевой активностью и способ ее получения |
| US5626862A (en) | 1994-08-02 | 1997-05-06 | Massachusetts Institute Of Technology | Controlled local delivery of chemotherapeutic agents for treating solid tumors |
| US5688773A (en) | 1994-08-17 | 1997-11-18 | The General Hospital Corporation | Method of selectively destroying neoplastic cells |
| US5985822A (en) | 1994-12-09 | 1999-11-16 | The Scripps Research Institute | Inhibition of glial cell proliferation with N-CAM homophilic peptides |
| US5756340A (en) | 1995-05-08 | 1998-05-26 | The Regents Of The University Of California | Insect control with multiple toxins |
| JP3809502B2 (ja) | 1995-05-30 | 2006-08-16 | 二郎 有川 | ハンタウィルス抗原蛋白質およびモノクローナル抗体 |
| JPH0971599A (ja) | 1995-09-06 | 1997-03-18 | Nippon Seibutsu Kagaku Kenkyusho | 鶏貧血ウイルス(cav)感染鶏血清と高い反応性を示すポリペプチド及びこのポリペプチドに対する抗体、鶏貧血ウイルス感染の診断法及びワクチン |
| US6667156B2 (en) | 1995-12-27 | 2003-12-23 | Uab Research Foundation | Diagnosis and treatment of neuroectodermal tumors |
| US5905027A (en) | 1995-12-27 | 1999-05-18 | Uab Research Foundation | Method of diagnosing and treating gliomas |
| AU2889097A (en) * | 1996-05-10 | 1997-12-05 | Novartis Ag | Identification of members of combinatorial libraries by mass spectrometry |
| US6130101A (en) | 1997-09-23 | 2000-10-10 | Molecular Probes, Inc. | Sulfonated xanthene derivatives |
| EP1055684A4 (en) | 1997-12-05 | 2002-12-04 | Kyogo Itoh | TUMORANTIGENS IN THE FORM OF PEPTIDE DERIVATIVES |
| GB9809776D0 (en) * | 1998-05-07 | 1998-07-08 | Nycomed Imaging As | Method |
| WO2000009502A1 (en) | 1998-08-12 | 2000-02-24 | Daiichi Pure Chemicals Co., Ltd. | Fluorescent labelling reagents |
| US6703381B1 (en) | 1998-08-14 | 2004-03-09 | Nobex Corporation | Methods for delivery therapeutic compounds across the blood-brain barrier |
| AU755334C (en) * | 1998-08-25 | 2004-02-26 | University Of Washington | Rapid quantitative analysis of proteins or protein function in complex mixtures |
| US6214986B1 (en) | 1998-10-07 | 2001-04-10 | Isis Pharmaceuticals, Inc. | Antisense modulation of bcl-x expression |
| US6629040B1 (en) * | 1999-03-19 | 2003-09-30 | University Of Washington | Isotope distribution encoded tags for protein identification |
| SE9901387D0 (sv) | 1999-04-19 | 1999-04-19 | Astra Ab | New pharmaceutical foromaulations |
| US6849714B1 (en) | 1999-05-17 | 2005-02-01 | Conjuchem, Inc. | Protection of endogenous therapeutic peptides from peptidase activity through conjugation to blood components |
| CA2384429A1 (en) | 1999-09-14 | 2001-03-22 | Michael K. Bahr | Magnetic nanoparticles having biochemical activity, method for the production thereof and their use |
| AUPQ339899A0 (en) * | 1999-10-13 | 1999-11-04 | University Of Queensland, The | Novel molecules |
| AU4305101A (en) | 1999-11-22 | 2001-06-04 | Research Foundation Of The State University Of New York, The | Magnetic nanoparticles for selective therapy |
| DE10020376A1 (de) | 2000-04-26 | 2001-11-08 | Inst Zelltechnologie E V | Dynamische Marker |
| AU2002220265A1 (en) | 2000-11-03 | 2002-05-15 | University Of Vermont And State Agricultural College | Compositions for inhibiting grb7 |
| US20020077921A1 (en) | 2000-12-15 | 2002-06-20 | Paul-David Morrison | Method and apparatus for an interactive catalog |
| WO2002069896A2 (en) | 2001-03-01 | 2002-09-12 | Northwest Hospital | Connexin enhances chemotherapy-induced apoptosis in human cancer cells inhibiting tumor cell proliferation |
| WO2003008583A2 (en) | 2001-03-02 | 2003-01-30 | Sagres Discovery | Novel compositions and methods for cancer |
| US20030021810A1 (en) | 2001-06-26 | 2003-01-30 | Sontheimer Harald W. | Chlorotoxin inhibition of cell invasion, cancer metastasis, angiogenesis and tissue remodeling |
| GB0115581D0 (en) * | 2001-06-26 | 2001-08-15 | Glaxo Group Ltd | Method of mass spectometry |
| WO2003029462A1 (en) * | 2001-09-27 | 2003-04-10 | Pieris Proteolab Ag | Muteins of human neutrophil gelatinase-associated lipocalin and related proteins |
| US6972326B2 (en) | 2001-12-03 | 2005-12-06 | Molecular Probes, Inc. | Labeling of immobilized proteins using dipyrrometheneboron difluoride dyes |
| EP1480665A2 (en) | 2002-02-04 | 2004-12-01 | Auburn University | Peptides for recognition and targeting of glial cell tumors |
| US20030232013A1 (en) | 2002-02-22 | 2003-12-18 | Gary Sieckman | Therapeutic and diagnostic targeting of cancers cells with tumor homing peptides |
| MXPA04011871A (es) | 2002-05-31 | 2005-07-26 | Transmolecular Inc | Quimioterapia en combinacion con clorotoxina. |
| US20060088899A1 (en) | 2002-05-31 | 2006-04-27 | Alvarez Vernon L | Combination chemotherapy with chlorotoxin |
| US7563600B2 (en) * | 2002-09-12 | 2009-07-21 | Combimatrix Corporation | Microarray synthesis and assembly of gene-length polynucleotides |
| US7560160B2 (en) | 2002-11-25 | 2009-07-14 | Materials Modification, Inc. | Multifunctional particulate material, fluid, and composition |
| US20040101822A1 (en) | 2002-11-26 | 2004-05-27 | Ulrich Wiesner | Fluorescent silica-based nanoparticles |
| CN1791671A (zh) * | 2003-03-21 | 2006-06-21 | 先灵公司 | 靶配体的筛选方法 |
| US20050059038A1 (en) * | 2003-03-21 | 2005-03-17 | Adams Steven P. | Method of screening for target ligands |
| WO2005099774A2 (en) | 2004-04-06 | 2005-10-27 | Transmolecular, Inc. | Diagnosis and treatment of myeloid and lymphoid cell cancers |
| JP2007516693A (ja) | 2003-06-09 | 2007-06-28 | ザ・リージェンツ・オブ・ザ・ユニバーシティ・オブ・ミシガン | 癌の治療および診断のための組成物および方法 |
| DE10328251A1 (de) | 2003-06-24 | 2005-01-13 | Toximed Gmbh | Pharmazeutischer Wirkstoff |
| US20070275902A1 (en) | 2003-11-26 | 2007-11-29 | Transmolecular, Inc. | Treatment of Phosphatidylinositol Phospholipid Disorders |
| EP1544296B8 (fr) * | 2003-12-18 | 2009-08-05 | Biomethodes | Procédé de mutagenèse dirigée massive |
| US20080153746A1 (en) | 2004-04-06 | 2008-06-26 | Transmolecular, Inc. | Diagnosis and Treatment of Myeloid and Lymphoid Cell Cancers |
| JP2007536260A (ja) | 2004-05-06 | 2007-12-13 | ザ・トラスティーズ・オブ・コロンビア・ユニバーシティ・イン・ザ・シティ・オブ・ニューヨーク | 虚血性および腎毒性障害の軽減および改善用ngal |
| EP1771573A4 (en) | 2004-07-21 | 2009-02-18 | Ambrx Inc | BIOSYNTHETIC POLYPEPTIDES OBTAINED FROM NON-NATURALLY CITED AMINO ACIDS |
| US20090209615A1 (en) * | 2004-09-27 | 2009-08-20 | Stuart Lipton | Inhibitors of matrix metalloproteinases to treat neurological disorders |
| GB0422901D0 (en) * | 2004-10-14 | 2004-11-17 | Ares Trading Sa | Lipocalin protein |
| KR100681763B1 (ko) | 2005-02-28 | 2007-02-15 | 재단법인 목암생명공학연구소 | 인간 리포칼린 2를 유효성분으로 포함하는 암 전이 억제용약학적 조성물, 이를 이용한 암 전이 억제 방법 |
| GB0504767D0 (en) * | 2005-03-08 | 2005-04-13 | Ares Trading Sa | Lipocalin protein |
| US7462446B2 (en) | 2005-03-18 | 2008-12-09 | University Of Washington | Magnetic nanoparticle compositions and methods |
| US20070037232A1 (en) | 2005-03-31 | 2007-02-15 | Barasch Jonathan M | Detection of NGAL in chronic renal disease |
| WO2006110585A2 (en) | 2005-04-07 | 2006-10-19 | Novartis Vaccines And Diagnostics Inc. | Cancer-related genes (prlr) |
| US20060286089A1 (en) | 2005-04-08 | 2006-12-21 | Xcyte Therapies, Inc. | Compositions and methods for the treatment of burns and sepsis |
| EP1877428B1 (en) | 2005-04-22 | 2011-03-16 | University of Washington | Cyanine- chlorotoxin conjugate and method for intra-operative visualization of cancer |
| US7833979B2 (en) | 2005-04-22 | 2010-11-16 | Amgen Inc. | Toxin peptide therapeutic agents |
| KR101285904B1 (ko) | 2005-08-18 | 2013-07-15 | 암브룩스, 인코포레이티드 | tRNA 조성물 및 이의 용도 |
| US20070237714A1 (en) | 2006-03-31 | 2007-10-11 | Alvarez Vernon L | Diagnosis and treatment of tumors |
| WO2007137163A2 (en) | 2006-05-19 | 2007-11-29 | Georgia Tech Research Corporation | Abc transporter ligand |
| CN100564517C (zh) | 2006-09-21 | 2009-12-02 | 武汉大学 | 一种蝎抗神经胶质瘤肽及其制备方法和应用 |
| CN101003788A (zh) | 2006-09-21 | 2007-07-25 | 武汉大学 | 一种蝎抗肿瘤转移肽及其制备方法和应用 |
| TW200833840A (en) | 2006-10-25 | 2008-08-16 | Amgen Inc | Toxin peptide therapeutic agents |
| ES2362386T3 (es) | 2007-06-21 | 2011-07-04 | Technische Universität München | Proteínas activas biológicas que tienen estabilidad aumentada in vivo y/o in vitro. |
| US20090004105A1 (en) | 2007-06-27 | 2009-01-01 | Zhen Cheng | Molecular imaging of matrix metalloproteinase expression using labeled chlorotoxin |
| WO2009021136A1 (en) | 2007-08-07 | 2009-02-12 | Transmolecular, Inc. | Chlorotoxins as drug carriers |
| US20110283260A1 (en) | 2007-08-31 | 2011-11-17 | Iosemantics, Llc | Quality assurance tools for use with source code and a semantic model |
| CN101918041A (zh) | 2007-10-12 | 2010-12-15 | 超分子有限公司 | 用于肿瘤诊断和治疗的氯毒素剂的系统性给药 |
| JP5746861B2 (ja) | 2007-10-19 | 2015-07-08 | アボット・ラボラトリーズAbbott Laboratories | 哺乳動物のngalに結合する抗体及びその使用 |
| US8846036B2 (en) | 2007-10-19 | 2014-09-30 | Abbott Laboratories | Antibodies that bind to mammalian NGAL and uses thereof |
| US20090123946A1 (en) | 2007-10-19 | 2009-05-14 | Abbott Laboratories | Immunoassays and kits for the detection of ngal |
| US20090124022A1 (en) | 2007-10-19 | 2009-05-14 | Abbott Laboratories | Antibodies that bind to mammalian ngal and uses thereof |
| US20090269777A1 (en) | 2007-10-19 | 2009-10-29 | Abbott Laboratories | Immunoassays and kits for the detection of ngal |
| US20090123970A1 (en) | 2007-10-19 | 2009-05-14 | Abbott Laboratories | Glycosylated mammalian ngal and use thereof |
| US20090176274A1 (en) | 2007-10-19 | 2009-07-09 | Abbott Laboratories | Glycosylated mammalian ngal and use thereof |
| PL2215481T5 (pl) | 2007-11-15 | 2017-10-31 | Bioporto Diagnostics As | Zastosowanie diagnostyczne indywidualnych postaci cząsteczkowych biomarkera |
| CA2749108C (en) | 2008-01-18 | 2017-06-27 | Visen Medical, Inc. | Intramolecularly-quenched fluorescent imaging agents |
| WO2009108762A2 (en) | 2008-02-26 | 2009-09-03 | The Penn State Research Foundation | Methods and compositions for treatment of retinoid-responsive conditions |
| US8093060B2 (en) | 2008-02-28 | 2012-01-10 | Canon Kabushiki Kaisha | Multisite phosphorylated peptide (protein) recognizing compound and detection method, imaging method, alzheimer's disease diagnosing method and reagent kit using the same |
| EP3673922A1 (en) | 2008-03-14 | 2020-07-01 | VisEn Medical, Inc. | Integrin targeting agents and methods of using same |
| CA2718854A1 (en) | 2008-03-20 | 2009-09-24 | Transmolecular, Inc. | Inhibition of angiogenesis |
| GB0807831D0 (en) | 2008-04-29 | 2008-06-04 | Cambridge Entpr Ltd | Agents for imaging cell death |
| CN101270158B (zh) | 2008-04-30 | 2010-12-22 | 武汉大学 | 一种靶向抗神经胶质瘤蛋白及制备方法和用途 |
| BRPI0912683A2 (pt) | 2008-05-15 | 2016-01-26 | Transmolecular Inc | tratamento de tumores metastáticos |
| JP2009300110A (ja) | 2008-06-10 | 2009-12-24 | Olympus Corp | 移植細胞の光学的検出方法又はイメージング方法 |
| JP5711118B2 (ja) * | 2008-06-24 | 2015-04-30 | テクニッシュ ウニヴェルジテート ミュンヘン | 所与の標的に対してアフィニティーを有するhNGALおよび類縁タンパク質のムテイン |
| US20100098637A1 (en) | 2008-09-23 | 2010-04-22 | The Regents Of The University Of Michigan | Dye-loaded nanoparticle |
| CN101381405B (zh) | 2008-09-24 | 2011-07-27 | 武汉摩尔生物科技有限公司 | 基因工程肿瘤靶向kct-w1多肽及制备方法和用途 |
| JP2010085108A (ja) | 2008-09-29 | 2010-04-15 | Nano Factory:Kk | 生体光イメージング用プローブ |
| US20100105150A1 (en) | 2008-10-24 | 2010-04-29 | Abbott Laboratories | Isolated human autoantibodies to neutrophil gelatinase-associated lipocalin (ngal) and methods and kits for the detection of human autoantibodies to ngal |
| US20100331650A1 (en) * | 2009-06-25 | 2010-12-30 | Roche Diagnostics Operations, Inc. | Episodic blood glucose monitoring system with an interactive graphical user interface and methods thereof |
| US10191060B2 (en) | 2009-11-09 | 2019-01-29 | University Of Washington | Functionalized chromophoric polymer dots and bioconjugates thereof |
| CN101921769B (zh) | 2010-01-11 | 2012-07-25 | 山西大学 | 一种重组腺病毒及其制备方法和应用 |
| WO2011094671A2 (en) | 2010-01-29 | 2011-08-04 | The Uab Research Foundation | N-terminally conjugated polypeptides for targeted therapy and diagnosis |
| HRP20171291T1 (hr) | 2010-02-04 | 2017-10-20 | Morphotek, Inc. | Polipeptidi i konjugati klorotoksina i njihove uporabe |
| CN101824084A (zh) | 2010-04-08 | 2010-09-08 | 山西大学 | 靶向性抗胶质瘤蛋白质及其应用 |
| EP3165533B1 (en) | 2010-05-11 | 2020-04-08 | Fred Hutchinson Cancer Research Center | Chlorotoxin variants, conjugates and methods for their use |
| DK2606061T3 (da) * | 2010-08-16 | 2017-11-06 | Pieris Pharmaceuticals Gmbh | Bindingsproteiner til hepcidin |
| EP3604549A1 (en) * | 2010-11-08 | 2020-02-05 | The Board of Trustees of the Leland Stanford Junior University | Fusion proteins comprising an engineered knottin peptide and uses thereof |
| US10436803B2 (en) * | 2010-12-28 | 2019-10-08 | Quest Diagnostics Investments Incorporated | Quantitation of insulin by tandem mass spectrometry of insulin B chain |
| MX360438B (es) * | 2011-09-07 | 2018-11-01 | X Chem Inc | Metodos para etiquetar bibliotecas codificadas por adn. |
| CA2913029A1 (en) | 2012-12-10 | 2014-06-19 | Fred Hutchinson Cancer Research Center | Lipocalin fusion partners |
-
2013
- 2013-12-10 CA CA2913029A patent/CA2913029A1/en not_active Abandoned
- 2013-12-10 JP JP2015545941A patent/JP2016505826A/ja not_active Ceased
- 2013-12-10 SG SG11201504600UA patent/SG11201504600UA/en unknown
- 2013-12-10 BR BR112015013525A patent/BR112015013525A2/pt not_active IP Right Cessation
- 2013-12-10 AU AU2013359429A patent/AU2013359429A1/en not_active Abandoned
- 2013-12-10 US US14/651,175 patent/US10156559B2/en active Active
- 2013-12-10 US US14/651,172 patent/US20150316536A1/en not_active Abandoned
- 2013-12-10 RU RU2015126651A patent/RU2015126651A/ru not_active Application Discontinuation
- 2013-12-10 CN CN201380072523.0A patent/CN105189540A/zh active Pending
- 2013-12-10 EP EP13814341.7A patent/EP2928913A1/en not_active Withdrawn
- 2013-12-10 US US14/102,396 patent/US20140179560A1/en not_active Abandoned
- 2013-12-10 SG SG11201504602VA patent/SG11201504602VA/en unknown
- 2013-12-10 RU RU2015126650A patent/RU2015126650A/ru not_active Application Discontinuation
- 2013-12-10 EP EP13814726.9A patent/EP2928914A1/en not_active Withdrawn
- 2013-12-10 WO PCT/US2013/074218 patent/WO2014093406A1/en not_active Ceased
- 2013-12-10 BR BR112015013515A patent/BR112015013515A2/pt not_active IP Right Cessation
- 2013-12-10 CN CN201380072527.9A patent/CN105008393A/zh active Pending
- 2013-12-10 AU AU2013359426A patent/AU2013359426A1/en not_active Abandoned
- 2013-12-10 JP JP2015545938A patent/JP2016505251A/ja active Pending
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- 2013-12-10 WO PCT/US2013/074215 patent/WO2014093403A1/en not_active Ceased
-
2015
- 2015-06-07 IL IL239261A patent/IL239261A0/en unknown
- 2015-06-07 IL IL239262A patent/IL239262A0/en unknown
-
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- 2018-12-11 US US16/216,625 patent/US20190101528A1/en not_active Abandoned
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