AU2014233537A1 - Extracellular matrix-binding synthetic peptidoglycans - Google Patents
Extracellular matrix-binding synthetic peptidoglycans Download PDFInfo
- Publication number
- AU2014233537A1 AU2014233537A1 AU2014233537A AU2014233537A AU2014233537A1 AU 2014233537 A1 AU2014233537 A1 AU 2014233537A1 AU 2014233537 A AU2014233537 A AU 2014233537A AU 2014233537 A AU2014233537 A AU 2014233537A AU 2014233537 A1 AU2014233537 A1 AU 2014233537A1
- Authority
- AU
- Australia
- Prior art keywords
- synthetic peptidoglycan
- binding peptide
- collagen
- hyaluronic acid
- glycan
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Abandoned
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Landscapes
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Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201361798916P | 2013-03-15 | 2013-03-15 | |
| US61/798,916 | 2013-03-15 | ||
| PCT/US2014/029596 WO2014144969A1 (en) | 2013-03-15 | 2014-03-14 | Extracellular matrix-binding synthetic peptidoglycans |
Publications (1)
| Publication Number | Publication Date |
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| AU2014233537A1 true AU2014233537A1 (en) | 2015-09-10 |
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Families Citing this family (19)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| HUE044239T2 (hu) | 2008-03-27 | 2019-10-28 | Purdue Research Foundation | Kollagén-kötõ szintetikus peptidoglikánok, elõállításuk és alkalmazási eljárásaik |
| HUE031596T2 (en) | 2011-05-24 | 2017-07-28 | Symic Ip Llc | Synthetic peptidoglycans that bind hyaluronic acid, their production and use |
| WO2014144969A1 (en) | 2013-03-15 | 2014-09-18 | Purdue Research Foundation | Extracellular matrix-binding synthetic peptidoglycans |
| WO2015164822A1 (en) | 2014-04-25 | 2015-10-29 | Purdue Research Foundation | Collagen binding synthetic peptidoglycans for treatment of endothelial dysfunction |
| WO2015175565A2 (en) | 2014-05-12 | 2015-11-19 | Purdue Research Foundation | Selectin and icam/vcam peptide ligand conjugates |
| JP6516235B2 (ja) * | 2014-10-31 | 2019-05-22 | 国立大学法人富山大学 | キメラタンパク質及びそれを用いたミクログリア活性阻害剤 |
| JP6693728B2 (ja) * | 2014-11-14 | 2020-05-13 | 興和株式会社 | 新規な機能性ペプチド |
| WO2016100846A1 (en) | 2014-12-19 | 2016-06-23 | Northwestern University | Thromboresistant-anticoagulant extracellular matrix |
| WO2016161333A2 (en) * | 2015-04-01 | 2016-10-06 | Purdue Research Foundation | Compositions comprising bioconjugates |
| BR112017021970A2 (pt) * | 2015-04-17 | 2018-07-10 | Symic Ip Llc | bioconjugados e usos dos mesmos |
| US10463745B2 (en) * | 2015-05-12 | 2019-11-05 | Northwestern University | Materials for tissue regeneration |
| EP3512561A4 (en) * | 2016-09-16 | 2020-10-07 | Glycologix, LLC | SULFATED GLYCOSAMINOGLYCAN BIOMATERIALS AS PROTEOGLYCAN MIMETICS |
| CN111050778B (zh) | 2017-07-07 | 2024-09-10 | 斯米克Ip有限公司 | 具有化学修饰的骨架的生物缀合物 |
| WO2019010485A1 (en) * | 2017-07-07 | 2019-01-10 | Symic Ip, Llc | TREATMENT OF FIBROSIS |
| AU2018298224B2 (en) | 2017-07-07 | 2024-08-15 | Symic Ip, Llc | Synthetic bioconjugates |
| WO2019075213A1 (en) | 2017-10-11 | 2019-04-18 | Northwestern University | HEPARIN CONJUGATED TO PEPTIDES BINDING TO COLLAGEN FOR TARGETING BIOLOGICAL AND SYNTHETIC FABRICS |
| WO2022256568A1 (en) * | 2021-06-02 | 2022-12-08 | Arizona Board Of Regents On Behalf Of The University Of Arizona | Methods and compositions for localization of growth factors |
| AU2023352919A1 (en) | 2022-09-29 | 2025-03-13 | Adora Animal Health Corporation | Storage stable formulations of sulfated glycosaminoglycans and fragments derived therefrom for the treatment of pain and other medical conditions |
| JPWO2024080183A1 (enExample) * | 2022-10-14 | 2024-04-18 |
Family Cites Families (142)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4683298A (en) | 1985-01-10 | 1987-07-28 | British Columbia Research Council | Process for the preparation of aminated polysaccharide derivatives |
| US5547936A (en) | 1985-06-17 | 1996-08-20 | La Jolla Cancer Research Foundation | Inhibition of cell migration with synthetic peptides |
| FI912858A0 (fi) | 1988-12-20 | 1991-06-13 | Jolla Cancer Res Found | Polypeptidpolymerkonjugat aktiva vid botande av saor. |
| FR2644066B1 (fr) | 1989-03-09 | 1994-05-13 | Therapeutiques Substitutives | Compositions stabilisees comprenant des fgfs, leur procede d'obtention et leurs applications therapeutiques, chirurgicales et cosmetologiques |
| US5693625A (en) | 1989-03-09 | 1997-12-02 | Therapeutiques Substitutives | Method of regenerating cells and tissues using functionalized dextrans |
| EP0567575B1 (en) | 1991-01-14 | 1999-10-13 | New York University | Cytokine-induced protein, tsg-6, dna coding therefor and uses thereof |
| JP2901787B2 (ja) | 1991-07-15 | 1999-06-07 | 日本メジフィジックス株式会社 | 核磁気共鳴造影剤 |
| FR2718023B1 (fr) | 1994-03-30 | 1996-08-14 | Paris Val Marne Universite | Médicament et composition pharmaceutique pour le traitement de lésions du tractus digestif. |
| PT876165E (pt) | 1995-12-18 | 2006-10-31 | Angiotech Biomaterials Corp | Composicoes de polimeros reticulados e processos para a sua utilizacao |
| CA2299687C (en) | 1997-08-04 | 2009-10-27 | Bio Syntech Ltd. | Temperature-controlled ph-dependant formation of ionic polysaccharide gels |
| US5997895A (en) | 1997-09-16 | 1999-12-07 | Integra Lifesciences Corporation | Dural/meningeal repair product using collagen matrix |
| AU762606B2 (en) | 1997-11-21 | 2003-06-26 | Genset S.A. | Chlamydia pneumoniae genomic sequence and polypeptides, fragments thereof and uses thereof, in particular for the diagnosis, prevention and treatment of infection |
| US7691829B2 (en) | 1998-03-24 | 2010-04-06 | Petito George D | Composition and method for healing tissues |
| FR2781485B1 (fr) | 1998-07-21 | 2003-08-08 | Denis Barritault | Polymeres biocompatibles leur procede de preparation et les compositions les contenant |
| JP3103531B2 (ja) | 1998-09-30 | 2000-10-30 | 延也 柳内 | ヒト尿由来細胞接着糖蛋白質及びその製造方法 |
| US6822071B1 (en) | 1998-11-12 | 2004-11-23 | The Regents Of The University Of California | Polypeptides from Chlamydia pneumoniae and their use in the diagnosis, prevention and treatment of disease |
| US6703491B1 (en) | 1999-03-17 | 2004-03-09 | Exelixis, Inc. | Drosophila sequences |
| US6864235B1 (en) | 1999-04-01 | 2005-03-08 | Eva A. Turley | Compositions and methods for treating cellular response to injury and other proliferating cell disorders regulated by hyaladherin and hyaluronans |
| US20110214206A1 (en) | 1999-05-06 | 2011-09-01 | La Rosa Thomas J | Nucleic acid molecules and other molecules associated with plants |
| US20090087878A9 (en) | 1999-05-06 | 2009-04-02 | La Rosa Thomas J | Nucleic acid molecules associated with plants |
| FR2794976B1 (fr) | 1999-06-16 | 2004-05-07 | Solutions | Compositions pharmaceutiques a action cicatrisante ou anti-complementaire comprenant un derive de dextrane |
| EP1218027B1 (en) | 1999-09-15 | 2010-01-20 | The Bruce H. DeWoolfson Irrevocable Family Trust | Composition for stabilizing corneal tissue during or after orthokeratological lens wear |
| FR2799465B1 (fr) | 1999-10-12 | 2004-02-13 | Centre Nat Rech Scient | Peptides ayant une activite de stimulation de la reponse immunitaire et de regeneration tissulaire |
| US20030158302A1 (en) | 1999-12-09 | 2003-08-21 | Cyric Chaput | Mineral-polymer hybrid composition |
| EP1237585B1 (en) | 1999-12-09 | 2003-06-18 | Biosyntech Canada Inc. | Mineral-polymer hybrid composition |
| WO2002017955A1 (en) | 2000-08-30 | 2002-03-07 | University Of Delaware | Delivery system for heparin-binding growth factors |
| US7803905B2 (en) | 2000-08-31 | 2010-09-28 | University Of Delaware | Bioactive peptide for cell adhesion |
| AU2002211517A1 (en) | 2000-10-04 | 2002-04-15 | California Institute Of Technology | Magnetic resonance imaging agents for in vivo labeling and detection of amyloid deposits |
| AU2002221370A1 (en) | 2000-11-15 | 2002-05-27 | Bio Syntech Canada Inc | Method for restoring a damaged or degenerated intervertebral disc |
| US20040236092A1 (en) | 2001-07-13 | 2004-11-25 | Roman Dziarski | Peptidologlycan recognition protein encoding nucleic acids and methods of use thereof |
| AU2002323217B2 (en) | 2001-08-15 | 2008-04-10 | Brown University Research Foundation | Treatment of muscular dystrophies and related disorders |
| DE60238858D1 (de) | 2001-11-15 | 2011-02-17 | Biosyntech Canada Inc | Zusammensetzung und verfahren um chitosan unter neutralen bedingungen homogen zu modifizieren oder vernetzen |
| US20090158452A1 (en) | 2001-12-04 | 2009-06-18 | Johnson Richard G | Transgenic plants with enhanced agronomic traits |
| US20090100536A1 (en) | 2001-12-04 | 2009-04-16 | Monsanto Company | Transgenic plants with enhanced agronomic traits |
| US20050108791A1 (en) | 2001-12-04 | 2005-05-19 | Edgerton Michael D. | Transgenic plants with improved phenotypes |
| WO2003075848A2 (en) | 2002-03-08 | 2003-09-18 | Zymogenetics, Inc. | Inhibitors for use in hemostasis |
| US7666852B2 (en) | 2002-04-22 | 2010-02-23 | Agenta Biotechnologies, Inc. | Wound and cutaneous injury healing with a nucleic acid encoding a proteoglycan polypeptide |
| JP2005185101A (ja) | 2002-05-30 | 2005-07-14 | National Institute Of Agrobiological Sciences | 植物の全長cDNAおよびその利用 |
| US8673333B2 (en) | 2002-09-25 | 2014-03-18 | The Johns Hopkins University | Cross-linked polymer matrices, and methods of making and using same |
| US7862831B2 (en) | 2002-10-09 | 2011-01-04 | Synthasome, Inc. | Method and material for enhanced tissue-biomaterial integration |
| US20090183270A1 (en) | 2002-10-02 | 2009-07-16 | Adams Thomas R | Transgenic plants with enhanced agronomic traits |
| JP2006501846A (ja) | 2002-10-04 | 2006-01-19 | リージェンツ オブ ザ ユニバーシティ オブ ミネソタ | ローソニア・イントラセルラリス由来の核酸およびポリペプチド配列ならびに使用方法 |
| US20050069572A1 (en) | 2002-10-09 | 2005-03-31 | Jennifer Elisseeff | Multi-layered polymerizing hydrogels for tissue regeneration |
| FR2846659B1 (fr) | 2002-10-30 | 2005-02-18 | Centre Nat Rech Scient | Fragments peptidiques du facteur harp inhibant l'angiogenese |
| WO2004045542A2 (en) | 2002-11-15 | 2004-06-03 | Arizona Board Of Regents Arizona State University | Therapeutic bioconjugates |
| US8404681B2 (en) | 2003-03-24 | 2013-03-26 | Luitpold Pharmaceuticals, Inc. | Xanthones, thioxanthones and acridinones as DNA-PK inhibitors |
| US8198020B2 (en) | 2003-08-22 | 2012-06-12 | Potentia Pharmaceuticals, Inc. | Compositions and methods for enhancing phagocytosis or phagocyte activity |
| PL1677807T3 (pl) | 2003-10-28 | 2011-05-31 | Organes Tissus Regeneration Reparation Remplacement Otr3 | Zastosowanie polimerów bio-kompatybilnych do wytwarzania kompozycji lub wyrobu medycznego |
| FR2861308A1 (fr) | 2003-10-28 | 2005-04-29 | Organes Tissus Regeneration Re | Utilisation de polymeres biocompatibles pour la preparation d'une composition pharmaceutique, dermatologique ou cosmetique destinee a la prevention, au soulagement ou au traitement des genes, desagrements et douleurs |
| WO2005055800A2 (en) | 2003-12-15 | 2005-06-23 | Technion Research & Development Foundation Ltd. | Therapeutic drug-eluting endoluminal covering |
| EP2289567A3 (en) | 2003-12-22 | 2011-06-22 | Regentis Biomaterials Ltd. | Matrix comprising naturally-occurring crosslinked protein backbone |
| US7842667B2 (en) | 2003-12-22 | 2010-11-30 | Regentis Biomaterials Ltd. | Matrix composed of a naturally-occurring protein backbone cross linked by a synthetic polymer and methods of generating and using same |
| US7709439B2 (en) | 2004-02-20 | 2010-05-04 | Boston Scientific Scimed, Inc. | Biomaterials for enhanced healing |
| US20060041961A1 (en) | 2004-03-25 | 2006-02-23 | Abad Mark S | Genes and uses for pant improvement |
| EP1758931A1 (en) | 2004-05-31 | 2007-03-07 | National University of Singapore | Peptides derived from decorin leucine rich repeats and uses thereof |
| US20060075522A1 (en) | 2004-07-31 | 2006-04-06 | Jaclyn Cleveland | Genes and uses for plant improvement |
| WO2006036681A2 (en) | 2004-09-22 | 2006-04-06 | Cartilix, Inc. | Cartilage filling device |
| EP1804844A4 (en) | 2004-09-29 | 2012-02-29 | Univ Singapore | COMPOSITE, PROCESS FOR ITS MANUFACTURE AND ITS APPLICATIONS |
| US20060241022A1 (en) | 2004-10-06 | 2006-10-26 | Bowen Benjamin P | Selectin targeting bioconjugates |
| WO2006047758A1 (en) | 2004-10-27 | 2006-05-04 | Massachusetts Institute Of Technology | Novel technique to fabricate molded structures having a patterned porosity |
| WO2007044026A2 (en) | 2004-11-23 | 2007-04-19 | The Johns Hopkins University | Compositions comprising modified collagen and uses therefore |
| WO2006089167A1 (en) | 2005-02-18 | 2006-08-24 | Cartilix, Inc. | Glucosamine materials |
| WO2006089119A2 (en) | 2005-02-18 | 2006-08-24 | Cartilix, Inc. | Biological adhesive |
| CA2598251A1 (en) | 2005-03-04 | 2006-09-14 | Northwestern University | Angiogenic heparin binding peptide amphiphiles |
| GB2424223C (en) | 2005-03-07 | 2011-02-02 | Massachusetts Inst Technology | Biomaterial. |
| EP1863404A2 (en) | 2005-03-30 | 2007-12-12 | Cartilix, Inc. | Coated medical device |
| US8415325B2 (en) | 2005-03-31 | 2013-04-09 | University Of Delaware | Cell-mediated delivery and targeted erosion of noncovalently crosslinked hydrogels |
| US7737131B2 (en) | 2005-03-31 | 2010-06-15 | University Of Delaware | Multifunctional and biologically active matrices from multicomponent polymeric solutions |
| US7732427B2 (en) | 2005-03-31 | 2010-06-08 | University Of Delaware | Multifunctional and biologically active matrices from multicomponent polymeric solutions |
| US8338390B2 (en) | 2005-03-31 | 2012-12-25 | University Of Delaware | Multifunctional and biologically active matrices from multicomponent polymeric solutions |
| US8367639B2 (en) | 2005-03-31 | 2013-02-05 | University Of Delaware | Hydrogels with covalent and noncovalent crosslinks |
| EP1882392A4 (en) | 2005-05-10 | 2009-07-01 | Monsanto Technology Llc | GENES AND THEIR USES FOR PLANT IMPROVEMENTS |
| JP5140579B2 (ja) | 2005-06-08 | 2013-02-06 | カンジェーン コーポレイション | 病原菌に対する生体防御を増強するヒアルロン酸結合性ペプチド |
| US20080069774A1 (en) | 2005-11-17 | 2008-03-20 | Lance Liotta | Proteomic antisense molecular shield and targeting |
| JP2009529374A (ja) | 2006-03-07 | 2009-08-20 | アクスル インターナショナル | 治療及び癒着防止用生物活性スキャホールド |
| US20070212385A1 (en) | 2006-03-13 | 2007-09-13 | David Nathaniel E | Fluidic Tissue Augmentation Compositions and Methods |
| JP2009529967A (ja) | 2006-03-15 | 2009-08-27 | サーモディクス,インコーポレイティド | 天然生分解性ポリサッカライドの疎水性誘導体及びそれらの使用 |
| WO2008034648A1 (en) | 2006-04-05 | 2008-03-27 | Metanomics Gmbh | Process for the production of a fine chemical |
| GB0610395D0 (en) | 2006-05-25 | 2006-07-05 | Ge Healthcare Ltd | Novel imaging agents |
| US20090162436A1 (en) | 2006-06-14 | 2009-06-25 | Carson Daniel D | Compositions and methods for repair of tissues |
| WO2010033564A1 (en) | 2008-09-17 | 2010-03-25 | Ceres, Inc. | Transgenic plants having increased biomass |
| PT2484375T (pt) | 2006-09-26 | 2018-07-09 | Infectious Disease Res Inst | Composição para vacina contendo adjuvante sintético |
| US7592009B2 (en) * | 2006-10-10 | 2009-09-22 | Ecole Polytechnique Federale De Lausanne (Epfl) | Polypeptide ligands for targeting cartilage and methods of use thereof |
| US8114835B2 (en) | 2006-11-09 | 2012-02-14 | Northwestern University | Self-assembling peptide amphiphiles for tissue engineering |
| US8114834B2 (en) | 2006-11-09 | 2012-02-14 | Northwestern University | Self-assembling peptide amphiphiles |
| US20100222546A1 (en) | 2006-11-28 | 2010-09-02 | David Crich | Methods for the preparation of functionalized peptides, proteins and carbohydrates and their conjugates |
| US8188220B2 (en) | 2006-12-06 | 2012-05-29 | Sanford-Burnham Medical Research Institute | Methods and compositions related to targeting wounds, regenerating tissue, and tumors |
| WO2008070179A2 (en) | 2006-12-06 | 2008-06-12 | Monsanto Technology, Llc | Genes and uses for plant improvement |
| PL2497505T3 (pl) | 2007-04-16 | 2017-02-28 | Regentis Biomaterials Ltd. | Kompozycje i sposoby tworzenia rusztowania |
| US20100119577A1 (en) | 2007-05-06 | 2010-05-13 | Byoung-Hyun Min | Therapeutic composite for cartilage disorder using extracellular matrix (ecm) scaffold |
| US20100191215A1 (en) | 2007-06-12 | 2010-07-29 | By-Pass ,Inc. | Pressure pulse actuating device for delivery systems |
| US20090075281A1 (en) | 2007-07-10 | 2009-03-19 | Regents Of The University Of California | Mtbe genes |
| US7993679B2 (en) | 2007-09-25 | 2011-08-09 | Integra Lifesciences Corporation | Flowable wound matrix and its preparation and use |
| US20100210509A1 (en) | 2007-10-09 | 2010-08-19 | Postech Academy-Industry Foundation | Long acting hyaluronic acid - peptide conjugate |
| WO2009099580A2 (en) | 2008-02-05 | 2009-08-13 | Monsanto Technology, Llc | Isolated novel nucleic acid and protein molecules from soy and methods of using those molecules to generate transgenic plants with enhanced agronomic traits |
| HUE044239T2 (hu) * | 2008-03-27 | 2019-10-28 | Purdue Research Foundation | Kollagén-kötõ szintetikus peptidoglikánok, elõállításuk és alkalmazási eljárásaik |
| CN102177180A (zh) | 2008-04-04 | 2011-09-07 | 犹他州大学研究基金会 | 烷基化半合成的糖胺聚糖醚及其制备和使用方法 |
| US8343942B2 (en) | 2008-04-04 | 2013-01-01 | University Of Utah Research Foundation | Methods for treating interstitial cystitis |
| US20100004196A1 (en) | 2008-06-17 | 2010-01-07 | Hopitaux Universitaires De Geneve | Heparan sulfate proteoglycan composition and use thereof |
| WO2010011857A2 (en) | 2008-07-23 | 2010-01-28 | The Johns Hopkins University | Parenteral administration of a glucosamine |
| US20110269208A1 (en) | 2008-08-15 | 2011-11-03 | The Trustees Of The University Of Pennsylvania | Cross-linked polymer network formed by sequential cross-linking |
| FR2936247B1 (fr) | 2008-09-24 | 2010-10-22 | Ct Hospitalier Universitaire De Dijon | Proteines recombinantes a activite hemostatique capables d'induire l'agregation plaquettaire. |
| US9072688B2 (en) | 2008-10-31 | 2015-07-07 | The Invention Science Fund I, Llc | Compositions and methods for therapeutic delivery with frozen particles |
| EP2358758B1 (de) | 2008-11-28 | 2012-09-05 | Zetascience GmbH | Bioaktives hydrogel |
| KR101062068B1 (ko) | 2008-12-01 | 2011-09-02 | 포항공과대학교 산학협력단 | 유착방지용 조성물 |
| IL195764A0 (en) | 2008-12-07 | 2009-11-18 | Technion Res & Dev Foundation | Compositions and methods for drug delivery |
| WO2010083179A2 (en) | 2009-01-16 | 2010-07-22 | Monsanto Technology Llc | Isolated novel nucleic acid and protein molecules from soybeans and methods of using those molecules to generate transgenic plants with enhanced agronomic traits |
| BRPI1013179A2 (pt) | 2009-03-30 | 2019-09-24 | Prometheus Laboratories Inc | peptídeo sintético, métodos para detectar um anticorpo de proteína anti-citrulinado em uma amostra biológica, para realizar um ensaio para ajudar no diagnóstico ou prognóstico de artrite reumatóide, para melhorar a sensibilidade de diagnosticar ou prognosticar artrite reumatóide, ensaio para diagnosticar ou prognosticar artrite reumatóide, kit, e, método para identificar um peptídeo que é imunologicamente reativo com um anticorpo de proteína anti-citrulinado |
| WO2010115156A2 (en) | 2009-04-03 | 2010-10-07 | Synthetic Genomics, Inc. | Endophytic fungus and uses therefor |
| AU2010236584A1 (en) | 2009-04-13 | 2011-11-10 | Northwestern University | Novel peptide-based scaffolds for cartilage regeneration and methods for their use |
| FI20095452A0 (fi) | 2009-04-23 | 2009-04-23 | Suomen Punainen Risti Veripalv | Uudet haaraiset sokerianalyysit |
| US20120100106A1 (en) | 2009-05-04 | 2012-04-26 | Purdue Research Foundation | Collagen-binding synthetic peptidoglycans for wound healing |
| GB0909671D0 (en) | 2009-06-04 | 2009-07-22 | Xention Discovery Ltd | Compounds |
| EP2499167A4 (en) | 2009-11-09 | 2013-07-10 | Univ Drexel | COMPOSITIONS AND METHODS FOR TREATING AN ILLNESS OR MALFUNCTION IN SOFT TISSUE |
| EA201290442A1 (ru) | 2009-12-04 | 2012-11-30 | Юклид Системз Корпорэйшн | Композиция и способы профилактики и лечения макулярной дегенерации, диабетической ретинопатии и диабетического макулярного отека |
| US8846020B2 (en) | 2009-12-16 | 2014-09-30 | Regentis Biomaterials Ltd. | Scaffolds formed from polymer-protein conjugates, methods of generating same and uses thereof |
| WO2011094149A1 (en) | 2010-01-26 | 2011-08-04 | University Of Utah Research Foundation | Methods for treating or preventing the spread of cancer using semi-synthetic glycosaminoglycosan ethers |
| EP3569241A1 (en) | 2010-02-26 | 2019-11-20 | Vascular Biosciences, Inc. | Car peptide for homing, diagnosis & targeted therapy for pulmonary and fibrotic disorders |
| ES2742218T3 (es) | 2010-06-23 | 2020-02-13 | Purdue Research Foundation | Peptidoglicanos sintéticos que se enlazan al colágeno destinados a ser utilizados en operaciones vasculares |
| US9173919B2 (en) | 2011-02-16 | 2015-11-03 | Purdue Research Foundation | Collagen-targeted nanoparticles |
| WO2012149515A2 (en) | 2011-04-29 | 2012-11-01 | Northwestern University | Novel vegf mimetic peptide-based scaffolds for therapeutic angiogenesis and methods for their use |
| HUE031596T2 (en) | 2011-05-24 | 2017-07-28 | Symic Ip Llc | Synthetic peptidoglycans that bind hyaluronic acid, their production and use |
| WO2013110056A1 (en) | 2012-01-19 | 2013-07-25 | The Johns Hopkins University | Biomaterials comprising hyaluronic acid binding peptides and bifunctional biopolymer molecules for hyaluronic acid retention and tissue engineering applications |
| US9540428B2 (en) | 2012-07-03 | 2017-01-10 | Ecole Polytechnique Federale De Lausanne (Epfl) | Extracellular matrix heparin-binding domains |
| WO2014028209A1 (en) | 2012-08-14 | 2014-02-20 | The Trustees Of The University Of Pennsylvania | Stabilizing shear-thinning hydrogels |
| WO2014038866A1 (ko) | 2012-09-05 | 2014-03-13 | 아주대학교산학협력단 | 연골세포 유래 세포외 기질막을 이용한 신생혈관질환 치료용 조성물 및 각막 또는 결막 이식재 |
| DE102012108560B4 (de) | 2012-09-13 | 2018-12-20 | Leibniz-Institut Für Polymerforschung Dresden E.V. | Nichtkovalente selbstorganisierende Hydrogelmatrix für biotechnologische Anwendungen |
| CN104870020A (zh) | 2012-10-19 | 2015-08-26 | 康奈尔大学 | 用于关节软骨的仿生型界面润滑剂 |
| EP2915001A4 (en) | 2012-11-01 | 2016-05-04 | Univ Johns Hopkins | CONTACT LENS SURFACE MODIFICATION WITH A HYALURONIC ACID BINDING PEPTIDE FOR THE ACCUMULATION AND STORAGE OF HYALURONIC ACID |
| US20140186350A1 (en) | 2012-12-18 | 2014-07-03 | Novartis Ag | Compositions and methods for long acting molecules |
| WO2014144969A1 (en) | 2013-03-15 | 2014-09-18 | Purdue Research Foundation | Extracellular matrix-binding synthetic peptidoglycans |
| WO2014171084A1 (ja) | 2013-04-16 | 2014-10-23 | パナソニックIpマネジメント株式会社 | 電力変換装置、電力変換方法、モータシステム、3相モータ |
| WO2015022326A1 (en) | 2013-08-12 | 2015-02-19 | Xiber Science Gmbh | Peptides as active agents for treating primary graft dysfunction |
| DE102013113156A1 (de) | 2013-11-28 | 2015-05-28 | Freie Universität Berlin | Verbindung und Verfahren zur selektiven Radiomarkierung von Polypeptiden mittels Festphasensynthese |
| WO2015164822A1 (en) | 2014-04-25 | 2015-10-29 | Purdue Research Foundation | Collagen binding synthetic peptidoglycans for treatment of endothelial dysfunction |
| WO2015175565A2 (en) | 2014-05-12 | 2015-11-19 | Purdue Research Foundation | Selectin and icam/vcam peptide ligand conjugates |
| WO2016061145A1 (en) | 2014-10-13 | 2016-04-21 | Symic Biomedical, Inc. | Synthetic proteoglycans for preventing tissue adhesion |
| US20170368192A1 (en) | 2014-10-13 | 2017-12-28 | Symic Ip, Llc | Luminal vessel coating for arteriovenous fistula |
| WO2016065083A1 (en) | 2014-10-21 | 2016-04-28 | Symic Biomedical, Inc. | Peptidoglycans comprising collagen-binding peptides for treating gastroesophageal injury |
| WO2016161333A2 (en) | 2015-04-01 | 2016-10-06 | Purdue Research Foundation | Compositions comprising bioconjugates |
| BR112017021970A2 (pt) | 2015-04-17 | 2018-07-10 | Symic Ip Llc | bioconjugados e usos dos mesmos |
| US20170112941A1 (en) | 2015-10-13 | 2017-04-27 | Symic Ip, Llc | Ve-cadherin binding bioconjugate |
-
2014
- 2014-03-14 WO PCT/US2014/029596 patent/WO2014144969A1/en not_active Ceased
- 2014-03-14 MX MX2015012608A patent/MX2015012608A/es unknown
- 2014-03-14 HK HK16108333.1A patent/HK1220217A1/zh unknown
- 2014-03-14 BR BR112015022917A patent/BR112015022917A2/pt not_active Application Discontinuation
- 2014-03-14 EP EP14764351.4A patent/EP2970509B1/en not_active Not-in-force
- 2014-03-14 JP JP2016503156A patent/JP6603650B2/ja not_active Expired - Fee Related
- 2014-03-14 KR KR1020157028095A patent/KR20150130419A/ko not_active Withdrawn
- 2014-03-14 US US14/214,220 patent/US9200039B2/en active Active
- 2014-03-14 SG SG11201506966RA patent/SG11201506966RA/en unknown
- 2014-03-14 AU AU2014233537A patent/AU2014233537A1/en not_active Abandoned
- 2014-03-14 EA EA201591454A patent/EA201591454A1/ru unknown
- 2014-03-14 CA CA2903450A patent/CA2903450A1/en not_active Abandoned
-
2015
- 2015-09-01 ZA ZA2015/06391A patent/ZA201506391B/en unknown
- 2015-09-02 IL IL241054A patent/IL241054A0/en unknown
- 2015-11-13 US US14/940,990 patent/US9872887B2/en active Active
-
2017
- 2017-12-18 US US15/845,955 patent/US20190022175A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| CA2903450A1 (en) | 2014-09-18 |
| KR20150130419A (ko) | 2015-11-23 |
| WO2014144969A1 (en) | 2014-09-18 |
| ZA201506391B (en) | 2017-09-27 |
| EP2970509B1 (en) | 2020-05-13 |
| HK1220217A1 (zh) | 2017-04-28 |
| US20190022175A1 (en) | 2019-01-24 |
| US20140288002A1 (en) | 2014-09-25 |
| US9872887B2 (en) | 2018-01-23 |
| JP2016516065A (ja) | 2016-06-02 |
| US20160129076A1 (en) | 2016-05-12 |
| IL241054A0 (en) | 2015-11-30 |
| MX2015012608A (es) | 2016-07-06 |
| SG11201506966RA (en) | 2015-10-29 |
| US9200039B2 (en) | 2015-12-01 |
| EA201591454A1 (ru) | 2015-12-30 |
| EP2970509A4 (en) | 2016-11-02 |
| EP2970509A1 (en) | 2016-01-20 |
| BR112015022917A2 (pt) | 2017-07-18 |
| JP6603650B2 (ja) | 2019-11-06 |
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| MK5 | Application lapsed section 142(2)(e) - patent request and compl. specification not accepted |