KR20020033743A - 펩티드 수용체 리게이션 방법 - Google Patents
펩티드 수용체 리게이션 방법 Download PDFInfo
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- KR20020033743A KR20020033743A KR1020027001058A KR20027001058A KR20020033743A KR 20020033743 A KR20020033743 A KR 20020033743A KR 1020027001058 A KR1020027001058 A KR 1020027001058A KR 20027001058 A KR20027001058 A KR 20027001058A KR 20020033743 A KR20020033743 A KR 20020033743A
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- Prior art keywords
- rna
- peptide receptor
- linker
- molecule
- rna molecule
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- 239000005297 pyrex Substances 0.000 description 1
- UMJSCPRVCHMLSP-UHFFFAOYSA-N pyridine Natural products COC1=CC=CN=C1 UMJSCPRVCHMLSP-UHFFFAOYSA-N 0.000 description 1
- 238000010791 quenching Methods 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 238000010992 reflux Methods 0.000 description 1
- 238000010839 reverse transcription Methods 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 239000012146 running buffer Substances 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 150000003349 semicarbazides Chemical class 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000010583 slow cooling Methods 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- YLQBMQCUIZJEEH-UHFFFAOYSA-N tetrahydrofuran Natural products C=1C=COC=1 YLQBMQCUIZJEEH-UHFFFAOYSA-N 0.000 description 1
- 125000003396 thiol group Chemical group [H]S* 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 238000009281 ultraviolet germicidal irradiation Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P19/00—Preparation of compounds containing saccharide radicals
- C12P19/26—Preparation of nitrogen-containing carbohydrates
- C12P19/28—N-glycosides
- C12P19/30—Nucleotides
- C12P19/34—Polynucleotides, e.g. nucleic acids, oligoribonucleotides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
- C07K1/1072—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides by covalent attachment of residues or functional groups
- C07K1/1077—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides by covalent attachment of residues or functional groups by covalent attachment of residues other than amino acids or peptide residues, e.g. sugars, polyols, fatty acids
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K17/00—Carrier-bound or immobilised peptides; Preparation thereof
- C07K17/02—Peptides being immobilised on, or in, an organic carrier
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1003—Extracting or separating nucleic acids from biological samples, e.g. pure separation or isolation methods; Conditions, buffers or apparatuses therefor
- C12N15/1006—Extracting or separating nucleic acids from biological samples, e.g. pure separation or isolation methods; Conditions, buffers or apparatuses therefor by means of a solid support carrier, e.g. particles, polymers
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1034—Isolating an individual clone by screening libraries
- C12N15/1062—Isolating an individual clone by screening libraries mRNA-Display, e.g. polypeptide and encoding template are connected covalently
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1034—Isolating an individual clone by screening libraries
- C12N15/1075—Isolating an individual clone by screening libraries by coupling phenotype to genotype, not provided for in other groups of this subclass
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Biomedical Technology (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Molecular Biology (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Microbiology (AREA)
- Plant Pathology (AREA)
- Physics & Mathematics (AREA)
- Crystallography & Structural Chemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Bioinformatics & Computational Biology (AREA)
- Analytical Chemistry (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US14583499P | 1999-07-27 | 1999-07-27 | |
| US60/145,834 | 1999-07-27 | ||
| PCT/US2000/019653 WO2001007657A1 (en) | 1999-07-27 | 2000-07-19 | Peptide acceptor ligation methods |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| KR20020033743A true KR20020033743A (ko) | 2002-05-07 |
Family
ID=22514769
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| KR1020027001058A Withdrawn KR20020033743A (ko) | 1999-07-27 | 2000-07-19 | 펩티드 수용체 리게이션 방법 |
Country Status (16)
| Country | Link |
|---|---|
| US (3) | US6429300B1 (https=) |
| EP (2) | EP1196637B1 (https=) |
| JP (2) | JP4766808B2 (https=) |
| KR (1) | KR20020033743A (https=) |
| AT (2) | ATE360706T1 (https=) |
| AU (2) | AU781783B2 (https=) |
| CA (2) | CA2377468C (https=) |
| CY (1) | CY1113185T1 (https=) |
| DE (1) | DE60034566T2 (https=) |
| DK (2) | DK1870417T3 (https=) |
| ES (2) | ES2284508T3 (https=) |
| HK (1) | HK1045334A1 (https=) |
| IL (1) | IL147037A0 (https=) |
| NO (1) | NO20020348D0 (https=) |
| PT (2) | PT1870417E (https=) |
| WO (1) | WO2001007657A1 (https=) |
Families Citing this family (104)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2001007657A1 (en) * | 1999-07-27 | 2001-02-01 | Phylos, Inc. | Peptide acceptor ligation methods |
| CA2397091A1 (en) | 2000-01-11 | 2001-07-19 | Markus Schweitzer | Biomolecules having multiple attachment moieties for binding to a substrate surface |
| AU2001262152A1 (en) * | 2000-03-31 | 2001-10-08 | Memorec Stoffel Gmbh | Method for extracting nucleic acids |
| US7410761B2 (en) * | 2000-05-19 | 2008-08-12 | Proteonova, Inc. | System for rapid identification and selection of nucleic acids and polypeptides, and method thereof |
| US20040229271A1 (en) * | 2000-05-19 | 2004-11-18 | Williams Richard B. | Compositions and methods for the identification and selection of nucleic acids and polypeptides |
| US6962781B1 (en) * | 2000-05-19 | 2005-11-08 | Proteonova, Inc. | In vitro evolution of nucleic acids and encoded polypeptide |
| AU2001295005A1 (en) * | 2000-08-11 | 2002-02-25 | Nanogen, Inc. | Macromolecules having hydrazide attachment moieties and reagents for their production |
| US7129229B2 (en) | 2000-08-11 | 2006-10-31 | Nanogen Recognomics Gmbh | Hydrazide building blocks and hydrazide modified biomolecules |
| JP4963142B2 (ja) * | 2000-12-14 | 2012-06-27 | 学校法人慶應義塾 | 遺伝子型と表現型の対応付け分子とその構成要素、および対応付け分子の製造方法と利用方法 |
| US20060234231A1 (en) * | 2001-06-20 | 2006-10-19 | Nuevolution A/S | Microarrays displaying encoded molecules |
| EP1401850A1 (en) | 2001-06-20 | 2004-03-31 | Nuevolution A/S | Nucleoside derivatives for library preparation |
| US6893822B2 (en) | 2001-07-19 | 2005-05-17 | Nanogen Recognomics Gmbh | Enzymatic modification of a nucleic acid-synthetic binding unit conjugate |
| WO2003012146A1 (en) * | 2001-07-31 | 2003-02-13 | Phylos, Inc. | Modular assembly of nucleic acid-protein fusion multimers |
| DE10147074A1 (de) * | 2001-09-25 | 2003-05-08 | Beru Ag | Verfahren zum Betreiben einer aus mehreren Heizelementen bestehenden mehrstufigen elektrischen Heizung |
| AU2002356984A1 (en) * | 2001-11-16 | 2003-06-10 | Proteonova, Inc. | Selection and evolution of nucleic acids and polypeptides |
| US7125669B2 (en) * | 2001-11-27 | 2006-10-24 | Compound Therapeutics, Inc. | Solid-phase immobilization of proteins and peptides |
| DE20200926U1 (de) * | 2002-01-23 | 2002-04-18 | Hegenscheidt-MFD GmbH & Co. KG, 41812 Erkelenz | Festwalzgerät einer Festwalzmaschine für Kurbelwellen |
| AU2003218629A1 (en) * | 2002-03-15 | 2003-09-29 | Nuevolution A/S | A building block forming a c-c or a c-hetero atom bond uponreaction |
| EP1487978B1 (en) * | 2002-03-15 | 2008-11-19 | Nuevolution A/S | An improved method for synthesising templated molecules |
| US20050221318A1 (en) * | 2002-03-15 | 2005-10-06 | Gouliaev Alex H | Building block forming a c-c bond upon reaction |
| AU2003214033A1 (en) * | 2002-03-15 | 2003-09-29 | Nuevolution A/S | A building block capable of transferring a functional entity |
| WO2004013070A2 (en) | 2002-08-01 | 2004-02-12 | Nuevolution A/S | Multi-step synthesis of templated molecules |
| AU2003256857A1 (en) * | 2002-08-08 | 2004-02-25 | Dharmacon, Inc. | Short interfering rnas having a hairpin structure containing a non-nucleotide loop |
| PT2348125T (pt) | 2002-10-30 | 2017-08-29 | Nuevolution As | Método para a síntese de um complexo bifuncional |
| AU2003291964A1 (en) | 2002-12-19 | 2004-07-14 | Nuevolution A/S | Quasirandom structure and function guided synthesis methods |
| US20070026397A1 (en) * | 2003-02-21 | 2007-02-01 | Nuevolution A/S | Method for producing second-generation library |
| EP1597394A2 (en) * | 2003-02-21 | 2005-11-23 | Nuevolution A/S | A method for obtaining structural information about an encoded molecule |
| DE602004019764D1 (de) * | 2003-03-20 | 2009-04-16 | Nuevolution As | Ligationsvermittelnde codierung von kleinen molekülen |
| WO2004110964A2 (en) * | 2003-06-16 | 2004-12-23 | Nuevolution A/S | Encoded molecules by translation (emt) |
| US20050095627A1 (en) * | 2003-09-03 | 2005-05-05 | The Salk Institute For Biological Studies | Multiple antigen detection assays and reagents |
| EP1670939B1 (en) * | 2003-09-18 | 2009-11-04 | Nuevolution A/S | A method for obtaining structural information concerning an encoded molecule and method for selecting compounds |
| CN1906307B (zh) * | 2003-11-20 | 2011-08-24 | 圣诺菲·帕斯图尔公司 | 纯化百日咳毒素的方法及其中有用的肽 |
| CN1946417A (zh) | 2003-12-05 | 2007-04-11 | 阿德内克休斯治疗公司 | 2型血管内皮生长因子受体的抑制剂 |
| AU2004314705A1 (en) * | 2003-12-12 | 2005-08-11 | Proteonova, Inc. | System and methods for nucleic acid and polypeptide selection |
| EP1723255B1 (en) * | 2004-02-17 | 2010-12-29 | Nuevolution A/S | Method for enrichment involving elimination by mismatch hybridisation |
| DE602005017370D1 (de) * | 2004-03-22 | 2009-12-10 | Nuevolution As | Ligationscodierung unter verwendung von oligonukleotidbausteinen |
| CA2467321A1 (en) * | 2004-05-14 | 2005-11-14 | Paul J. Santerre | Polymeric coupling agents and pharmaceutically-active polymers made therefrom |
| WO2006041194A1 (ja) | 2004-10-15 | 2006-04-20 | Japan Science And Technology Agency | ｍＲＮＡ－ピューロマイシン－タンパク質連結体作製用リンカー |
| EP2261257B1 (en) | 2005-01-12 | 2018-07-11 | Proteonova, Inc. | Method for making targeted therapeutic agents |
| US10206998B2 (en) | 2005-01-12 | 2019-02-19 | Proteonova, Inc. | Modular targeted therapeutic agents and methods of making same |
| EP1951890A4 (en) | 2005-11-16 | 2009-06-24 | Ambrx Inc | PROCESSES AND COMPOSITIONS WITH NON-NATURAL AMINO ACIDS |
| HUE056836T2 (hu) | 2005-12-01 | 2022-03-28 | Nuevolution As | Enzimatikus kódolási eljárások nagy könyvtárak hatékony szintéziséhez |
| US7749957B2 (en) | 2006-04-06 | 2010-07-06 | E.I. Du Pont De Nemours And Company | Clay-binding peptides and methods of use |
| CA2670471A1 (en) | 2006-11-22 | 2008-06-05 | Adnexus, A Bristol-Myers Squibb R&D Company (A Delaware Corporation) | Targeted therapeutics based on engineered proteins for tyrosine kinases receptors, including igf-ir |
| AU2008216303A1 (en) | 2007-02-12 | 2008-08-21 | Proteonova, Inc. | Generation of library of soluble random polypeptides linked to mRNA |
| US7951559B2 (en) * | 2007-07-25 | 2011-05-31 | E.I. Du Pont De Nemours And Company | Recombinant peptide production using a cross-linkable solubility tag |
| US7678883B2 (en) * | 2007-07-25 | 2010-03-16 | E.I. Du Pont De Nemours And Company | Solubility tags for the expression and purification of bioactive peptides |
| US7829311B2 (en) | 2007-07-25 | 2010-11-09 | E.I. Du Pont De Nemours And Company | Ketosteroid isomerase inclusion body tag engineered to be acid-resistant by replacing aspartates with glutamate |
| US7794963B2 (en) | 2007-11-02 | 2010-09-14 | E.I. Du Pont De Nemours And Company | Use of tetracysteine tags in fluorescence-activated cell sorting analysis of prokaryotic cells producing peptides or proteins |
| US8883146B2 (en) | 2007-11-30 | 2014-11-11 | Abbvie Inc. | Protein formulations and methods of making same |
| TWI543768B (zh) | 2007-11-30 | 2016-08-01 | 艾伯維生物技術有限責任公司 | 蛋白質調配物及製造其之方法 |
| CN102007145A (zh) | 2008-02-14 | 2011-04-06 | 百时美施贵宝公司 | 基于结合egfr的工程化蛋白质的靶向治疗剂 |
| EP2283132B1 (en) * | 2008-05-02 | 2016-10-26 | Epicentre Technologies Corporation | Selective 5' ligation tagging of rna |
| PL2274331T3 (pl) | 2008-05-02 | 2014-04-30 | Novartis Ag | Ulepszone cząsteczki wiążące oparte na fibronektynie i ich zastosowanie |
| PE20091931A1 (es) | 2008-05-22 | 2009-12-31 | Bristol Myers Squibb Co | Proteinas de dominio de armazon basadas en fibronectina multivalentes |
| EP3629022A1 (en) | 2008-07-25 | 2020-04-01 | Richard W. Wagner | Protein screening methods |
| MX2011003381A (es) * | 2008-09-30 | 2011-04-21 | Abbott Lab | Metodo mejorado para despliegue de arn. |
| TWI496582B (zh) | 2008-11-24 | 2015-08-21 | 必治妥美雅史谷比公司 | 雙重專一性之ｅｇｆｒ／ｉｇｆｉｒ結合分子 |
| US20100158822A1 (en) | 2008-12-18 | 2010-06-24 | E .I. Du Pont De Nemours And Company | Peptides that bind to silica-coated particles |
| US20100158846A1 (en) * | 2008-12-18 | 2010-06-24 | E. I. Du Pont De Nemours And Company | Hair-binding peptides |
| US8287845B2 (en) * | 2008-12-18 | 2012-10-16 | E I Du Pont De Nemours And Company | Hair-binding peptides |
| US20100158837A1 (en) | 2008-12-18 | 2010-06-24 | E. I. Du Pont De Nemours And Company | Iron oxide-binding peptides |
| US20100247590A1 (en) * | 2009-03-30 | 2010-09-30 | Johnson & Johnson | Peptide-Based Systems For Delivery Of Cosmetic Agents |
| US8481678B2 (en) | 2009-03-30 | 2013-07-09 | E I Du Pont De Nemours And Company | Peptide-based tooth whitening reagents |
| JP5733784B2 (ja) * | 2009-09-24 | 2015-06-10 | 国立大学法人埼玉大学 | ｃＤＮＡ／ｍＲＮＡ−タンパク質連結体の効率的合成法 |
| WO2011051327A2 (en) | 2009-10-30 | 2011-05-05 | Novartis Ag | Small antibody-like single chain proteins |
| WO2011051466A1 (en) | 2009-11-02 | 2011-05-05 | Novartis Ag | Anti-idiotypic fibronectin-based binding molecules and uses thereof |
| WO2011092233A1 (en) | 2010-01-29 | 2011-08-04 | Novartis Ag | Yeast mating to produce high-affinity combinations of fibronectin-based binders |
| JP2013519869A (ja) | 2010-02-10 | 2013-05-30 | ノバルティス アーゲー | 筋肉成長のための方法および化合物 |
| WO2011126370A1 (en) * | 2010-04-09 | 2011-10-13 | Universiteit Utrecht Holding B.V. | Recombinant multimeric influenza proteins |
| WO2011127933A1 (en) | 2010-04-16 | 2011-10-20 | Nuevolution A/S | Bi-functional complexes and methods for making and using such complexes |
| TW201138808A (en) | 2010-05-03 | 2011-11-16 | Bristol Myers Squibb Co | Serum albumin binding molecules |
| ES2573108T3 (es) | 2010-05-26 | 2016-06-06 | Bristol-Myers Squibb Company | Proteínas de armazón a base de fibronectina que tienen estabilidad mejorada |
| CN107903321A (zh) | 2010-07-30 | 2018-04-13 | 诺华有限公司 | 纤连蛋白摇篮分子和其库 |
| DE102010056289A1 (de) | 2010-12-24 | 2012-06-28 | Geneart Ag | Verfahren zur Herstellung von Leseraster-korrekten Fragment-Bibliotheken |
| ES2873375T3 (es) | 2011-03-15 | 2021-11-03 | X Body Inc | Métodos de cribado de anticuerpos |
| PT3415619T (pt) | 2011-04-28 | 2021-03-22 | Univ Leland Stanford Junior | Identificação de polinucleótidos associados a uma amostra |
| CA2843955A1 (en) | 2011-08-01 | 2013-02-07 | The General Hospital Corporation | Protein and peptide libraries |
| AU2012323316B2 (en) | 2011-10-11 | 2017-08-10 | Viela Bio, Inc. | CD40L-specific Tn3-derived scaffolds and methods of use thereof |
| CN104105708B (zh) | 2011-12-05 | 2018-04-03 | X博迪生物科学公司 | PDGF受体β结合多肽 |
| JP6020865B2 (ja) * | 2013-03-13 | 2016-11-02 | 国立大学法人 東京大学 | 核酸リンカー |
| ES2920601T3 (es) | 2013-06-28 | 2022-08-05 | X Body Inc | Descubrimiento de antígenos objetivo, cribados fenotípicos y uso de los mismos para la identificación de epítopos objetivo específicos de células objetivo |
| CN103382579B (zh) * | 2013-07-06 | 2015-10-21 | 中国科学院成都生物研究所 | 一种体外筛选多肽的方法 |
| WO2015042528A1 (en) | 2013-09-23 | 2015-03-26 | X-Body Biosciences, Inc. | Methods and compositions for generation of binding agents against cell surface antigens |
| US20150184214A1 (en) * | 2013-12-31 | 2015-07-02 | Roche Nimblegen, Inc. | Enrichment of full length oligonucleotides via transcription/translation mediated purification |
| US10421958B2 (en) | 2014-02-05 | 2019-09-24 | Molecular Templates, Inc. | Methods of screening, selecting, and identifying cytotoxic recombinant polypeptides based on an interim diminution of ribotoxicity |
| EP3129401B1 (en) | 2014-03-20 | 2019-06-12 | Bristol-Myers Squibb Company | Serum albumin-binding fibronectin type iii domains |
| JP6478392B2 (ja) * | 2014-12-26 | 2019-03-06 | 国立研究開発法人産業技術総合研究所 | 核酸リンカー |
| EP3842451A1 (en) | 2015-03-12 | 2021-06-30 | MedImmune, LLC | Method of purifying albumin-fusion proteins |
| EP3708580B1 (en) | 2015-09-23 | 2023-11-01 | Bristol-Myers Squibb Company | Fast-off rate serum albumin binding fibronectin type iii domains |
| AU2017259794B2 (en) | 2016-05-02 | 2023-04-13 | Encodia, Inc. | Macromolecule analysis employing nucleic acid encoding |
| EP3472355A4 (en) | 2016-06-15 | 2020-07-29 | Genecapture, Inc. | COMPOSITIONS, METHODS AND DEVICES INCLUDING ROD LOOP MOLECULES-SENSORS |
| WO2018005559A1 (en) | 2016-06-27 | 2018-01-04 | Juno Therapeutics, Inc. | Method of identifying peptide epitopes, molecules that bind such epitopes and related uses |
| MA45491A (fr) | 2016-06-27 | 2019-05-01 | Juno Therapeutics Inc | Épitopes à restriction cmh-e, molécules de liaison et procédés et utilisations associés |
| CA3057419A1 (en) | 2017-03-21 | 2018-09-27 | Fujifilm Corporation | Peptide compound and method for producing same, composition for screening use, and method for selecting peptide compound |
| MX2020004559A (es) * | 2017-10-31 | 2020-10-05 | Encodia Inc | Kits para análisis utilizando codificación y/o etiqueta de ácido nucleico. |
| RU2020112854A (ru) | 2017-11-30 | 2021-12-30 | Арракис Терапьютикс, Инк. | Фотозонды, связывающие нуклеиновые кислоты, и способы их применения |
| CN111971292B (zh) | 2018-02-02 | 2024-12-13 | 波纹疗法公司 | 包含类固醇二聚体的玻璃制剂及其用途 |
| TWI830718B (zh) * | 2018-02-09 | 2024-02-01 | 日商住友化學股份有限公司 | 核酸分子之製造方法 |
| EP3778914A4 (en) * | 2018-03-30 | 2022-01-19 | Sumitomo Chemical Company, Ltd. | Method for producing single-strand rna |
| WO2019236644A1 (en) * | 2018-06-05 | 2019-12-12 | Arrakis Therapeutics, Inc. | Encoded libraries and methods of use for screening nucleic acid targets |
| WO2020154815A1 (en) | 2019-02-01 | 2020-08-06 | Ripple Therapeutics Corporation | Crystalline forms of dexamethasone dimers and uses thereof |
| WO2021024041A1 (en) | 2019-08-07 | 2021-02-11 | Ripple Therapeutics Corporation | Controlled release drug dimers |
| MX2022013665A (es) | 2020-05-01 | 2022-11-30 | Ripple Therapeutics Corp | Composiciones y metodos heterodimeros para el tratamiento de trastornos oculares. |
Family Cites Families (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2001007657A1 (en) * | 1999-07-27 | 2001-02-01 | Phylos, Inc. | Peptide acceptor ligation methods |
| US5391723A (en) * | 1989-05-31 | 1995-02-21 | Neorx Corporation | Oligonucleotide conjugates |
| US5843701A (en) * | 1990-08-02 | 1998-12-01 | Nexstar Pharmaceticals, Inc. | Systematic polypeptide evolution by reverse translation |
| AU8124694A (en) * | 1993-10-29 | 1995-05-22 | Affymax Technologies N.V. | In vitro peptide and antibody display libraries |
| DE19646372C1 (de) * | 1995-11-11 | 1997-06-19 | Evotec Biosystems Gmbh | Genotyp und Phänotyp koppelnde Verbindung |
| AU714486B2 (en) * | 1995-11-21 | 2000-01-06 | Yale University | Unimolecular segment amplification and detection |
| US6117635A (en) * | 1996-07-16 | 2000-09-12 | Intergen Company | Nucleic acid amplification oligonucleotides with molecular energy transfer labels and methods based thereon |
| US5842701A (en) * | 1996-10-08 | 1998-12-01 | Smith International, Inc. | Dual functioning seal for rock bits |
| CA2268353A1 (en) | 1996-10-10 | 1998-04-16 | Henrik Garoff | Alphavirus-retrovirus vectors |
| DE69730157T2 (de) * | 1996-10-17 | 2005-07-28 | Mitsubishi Chemical Corp. | Molekül, welches genotyp und phänotyp zusammenführt und dessen anwendungen |
| US6261804B1 (en) | 1997-01-21 | 2001-07-17 | The General Hospital Corporation | Selection of proteins using RNA-protein fusions |
| DK1712623T3 (da) | 1997-01-21 | 2012-02-06 | Gen Hospital Corp | Udvælgelse af proteiner ved anvendelse af RNA-proteinfusioner |
| US5935791A (en) * | 1997-09-23 | 1999-08-10 | Becton, Dickinson And Company | Detection of nucleic acids by fluorescence quenching |
| DE69800415T2 (de) * | 1997-12-22 | 2001-07-19 | Genset, Paris | Prostatakrebs-gen |
| US5985575A (en) | 1998-05-20 | 1999-11-16 | Wisconsin Alumni Research Foundation | Tethered function assay for protein function |
| AU779653B2 (en) * | 1999-08-27 | 2005-02-03 | Bristol-Myers Squibb Company | Methods for encoding and sorting in vitro translated proteins |
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