JP2016532125A5 - - Google Patents
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- JP2016532125A5 JP2016532125A5 JP2016543461A JP2016543461A JP2016532125A5 JP 2016532125 A5 JP2016532125 A5 JP 2016532125A5 JP 2016543461 A JP2016543461 A JP 2016543461A JP 2016543461 A JP2016543461 A JP 2016543461A JP 2016532125 A5 JP2016532125 A5 JP 2016532125A5
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- 108090000765 processed proteins & peptides Proteins 0.000 claims description 59
- 238000000034 method Methods 0.000 claims description 43
- 102000004169 proteins and genes Human genes 0.000 claims description 39
- 108090000623 proteins and genes Proteins 0.000 claims description 39
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 31
- 229920001184 polypeptide Polymers 0.000 claims description 29
- 239000011148 porous material Substances 0.000 claims description 27
- 230000004481 post-translational protein modification Effects 0.000 claims description 23
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 17
- 230000026731 phosphorylation Effects 0.000 claims description 13
- 238000006366 phosphorylation reaction Methods 0.000 claims description 13
- 150000001413 amino acids Chemical class 0.000 claims description 10
- 208000011580 syndromic disease Diseases 0.000 claims description 10
- 108091005703 transmembrane proteins Proteins 0.000 claims description 10
- 102000035160 transmembrane proteins Human genes 0.000 claims description 10
- 208000035475 disorder Diseases 0.000 claims description 9
- 201000010099 disease Diseases 0.000 claims description 8
- 230000004048 modification Effects 0.000 claims description 8
- 238000012986 modification Methods 0.000 claims description 8
- 230000000694 effects Effects 0.000 claims description 7
- 239000012528 membrane Substances 0.000 claims description 6
- 230000015572 biosynthetic process Effects 0.000 claims description 5
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 4
- 230000002159 abnormal effect Effects 0.000 claims description 4
- 125000003636 chemical group Chemical group 0.000 claims description 4
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 claims description 4
- 125000001165 hydrophobic group Chemical group 0.000 claims description 4
- 239000007787 solid Substances 0.000 claims description 4
- 108091034117 Oligonucleotide Proteins 0.000 claims description 3
- 230000013595 glycosylation Effects 0.000 claims description 3
- 238000006206 glycosylation reaction Methods 0.000 claims description 3
- 229920000642 polymer Polymers 0.000 claims description 3
- ODHCTXKNWHHXJC-VKHMYHEASA-N 5-oxo-L-proline Chemical compound OC(=O)[C@@H]1CCC(=O)N1 ODHCTXKNWHHXJC-VKHMYHEASA-N 0.000 claims description 2
- 230000005730 ADP ribosylation Effects 0.000 claims description 2
- 206010003591 Ataxia Diseases 0.000 claims description 2
- 208000032791 BCR-ABL1 positive chronic myelogenous leukemia Diseases 0.000 claims description 2
- 201000010717 Bruton-type agammaglobulinemia Diseases 0.000 claims description 2
- 241000282461 Canis lupus Species 0.000 claims description 2
- 208000010833 Chronic myeloid leukaemia Diseases 0.000 claims description 2
- 206010010539 Congenital megacolon Diseases 0.000 claims description 2
- 108010006464 Hemolysin Proteins Proteins 0.000 claims description 2
- 208000004592 Hirschsprung disease Diseases 0.000 claims description 2
- 108010014603 Leukocidins Proteins 0.000 claims description 2
- 108090001030 Lipoproteins Proteins 0.000 claims description 2
- 102000004895 Lipoproteins Human genes 0.000 claims description 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims description 2
- 239000004472 Lysine Substances 0.000 claims description 2
- 208000021642 Muscular disease Diseases 0.000 claims description 2
- 241000187480 Mycobacterium smegmatis Species 0.000 claims description 2
- 208000033761 Myelogenous Chronic BCR-ABL Positive Leukemia Diseases 0.000 claims description 2
- 208000033833 Myelomonocytic Chronic Leukemia Diseases 0.000 claims description 2
- 201000009623 Myopathy Diseases 0.000 claims description 2
- 241000588653 Neisseria Species 0.000 claims description 2
- 206010028980 Neoplasm Diseases 0.000 claims description 2
- 208000015914 Non-Hodgkin lymphomas Diseases 0.000 claims description 2
- 108010013381 Porins Proteins 0.000 claims description 2
- 102000004022 Protein-Tyrosine Kinases Human genes 0.000 claims description 2
- 108090000412 Protein-Tyrosine Kinases Proteins 0.000 claims description 2
- ODHCTXKNWHHXJC-GSVOUGTGSA-N Pyroglutamic acid Natural products OC(=O)[C@H]1CCC(=O)N1 ODHCTXKNWHHXJC-GSVOUGTGSA-N 0.000 claims description 2
- 208000006265 Renal cell carcinoma Diseases 0.000 claims description 2
- 230000006295 S-nitrosylation Effects 0.000 claims description 2
- 206010043189 Telangiectasia Diseases 0.000 claims description 2
- 108010073429 Type V Secretion Systems Proteins 0.000 claims description 2
- 206010049644 Williams syndrome Diseases 0.000 claims description 2
- 208000023940 X-Linked Combined Immunodeficiency disease Diseases 0.000 claims description 2
- 208000016349 X-linked agammaglobulinemia Diseases 0.000 claims description 2
- 230000021736 acetylation Effects 0.000 claims description 2
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- ODHCTXKNWHHXJC-UHFFFAOYSA-N acide pyroglutamique Natural products OC(=O)C1CCC(=O)N1 ODHCTXKNWHHXJC-UHFFFAOYSA-N 0.000 claims description 2
- 230000010933 acylation Effects 0.000 claims description 2
- 238000005917 acylation reaction Methods 0.000 claims description 2
- 230000006154 adenylylation Effects 0.000 claims description 2
- 230000029936 alkylation Effects 0.000 claims description 2
- 238000005804 alkylation reaction Methods 0.000 claims description 2
- 230000009435 amidation Effects 0.000 claims description 2
- 238000007112 amidation reaction Methods 0.000 claims description 2
- 230000031709 bromination Effects 0.000 claims description 2
- 238000005893 bromination reaction Methods 0.000 claims description 2
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- 235000012000 cholesterol Nutrition 0.000 claims description 2
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- 230000006329 citrullination Effects 0.000 claims description 2
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- 230000006126 farnesylation Effects 0.000 claims description 2
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- 230000004927 fusion Effects 0.000 claims description 2
- 230000006251 gamma-carboxylation Effects 0.000 claims description 2
- 230000006130 geranylgeranylation Effects 0.000 claims description 2
- 229960003180 glutathione Drugs 0.000 claims description 2
- 239000003228 hemolysin Substances 0.000 claims description 2
- 230000006149 hemylation Effects 0.000 claims description 2
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- 230000026045 iodination Effects 0.000 claims description 2
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- 230000006122 isoprenylation Effects 0.000 claims description 2
- 230000006144 lipoylation Effects 0.000 claims description 2
- 230000017538 malonylation Effects 0.000 claims description 2
- 238000005259 measurement Methods 0.000 claims description 2
- 201000006938 muscular dystrophy Diseases 0.000 claims description 2
- 230000003274 myotonic effect Effects 0.000 claims description 2
- 230000007498 myristoylation Effects 0.000 claims description 2
- 230000005257 nucleotidylation Effects 0.000 claims description 2
- 108010014203 outer membrane phospholipase A Proteins 0.000 claims description 2
- 230000003647 oxidation Effects 0.000 claims description 2
- 238000007254 oxidation reaction Methods 0.000 claims description 2
- 230000026792 palmitoylation Effects 0.000 claims description 2
- 230000005261 phosphopantetheinylation Effects 0.000 claims description 2
- 102000007739 porin activity proteins Human genes 0.000 claims description 2
- 230000013823 prenylation Effects 0.000 claims description 2
- 210000003625 skull Anatomy 0.000 claims description 2
- 125000002730 succinyl group Chemical group C(CCC(=O)*)(=O)* 0.000 claims description 2
- 230000035322 succinylation Effects 0.000 claims description 2
- 238000010613 succinylation reaction Methods 0.000 claims description 2
- 230000010741 sumoylation Effects 0.000 claims description 2
- 208000009056 telangiectasis Diseases 0.000 claims description 2
- 210000005239 tubule Anatomy 0.000 claims description 2
- 238000007792 addition Methods 0.000 claims 4
- 238000001814 protein method Methods 0.000 claims 1
- 108020004414 DNA Proteins 0.000 description 9
- 239000002773 nucleotide Substances 0.000 description 5
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 4
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 3
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 102000008130 Cyclic AMP-Dependent Protein Kinases Human genes 0.000 description 2
- 108010049894 Cyclic AMP-Dependent Protein Kinases Proteins 0.000 description 2
- 102000053602 DNA Human genes 0.000 description 2
- 238000001712 DNA sequencing Methods 0.000 description 2
- OIRDTQYFTABQOQ-KQYNXXCUSA-N adenosine Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O OIRDTQYFTABQOQ-KQYNXXCUSA-N 0.000 description 2
- 230000003197 catalytic effect Effects 0.000 description 2
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- 238000004949 mass spectrometry Methods 0.000 description 2
- 230000006432 protein unfolding Effects 0.000 description 2
- 230000010076 replication Effects 0.000 description 2
- 230000005945 translocation Effects 0.000 description 2
- 101710092462 Alpha-hemolysin Proteins 0.000 description 1
- 239000002126 C01EB10 - Adenosine Substances 0.000 description 1
- 230000008836 DNA modification Effects 0.000 description 1
- 108010021466 Mutant Proteins Proteins 0.000 description 1
- 102000008300 Mutant Proteins Human genes 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
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- 230000001973 epigenetic effect Effects 0.000 description 1
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- 239000003446 ligand Substances 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 230000006320 pegylation Effects 0.000 description 1
- 108010060709 protein kinase inhibitor peptide (5-24) Proteins 0.000 description 1
- 230000009822 protein phosphorylation Effects 0.000 description 1
- 230000007398 protein translocation Effects 0.000 description 1
- 238000000575 proteomic method Methods 0.000 description 1
- CCOXWRVWKFVFDG-UHFFFAOYSA-N pyrimidine-2-carbaldehyde Chemical compound O=CC1=NC=CC=N1 CCOXWRVWKFVFDG-UHFFFAOYSA-N 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 230000011664 signaling Effects 0.000 description 1
- 238000004557 single molecule detection Methods 0.000 description 1
- 230000007704 transition Effects 0.000 description 1
- 238000000539 two dimensional gel electrophoresis Methods 0.000 description 1
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GBGB1316849.7A GB201316849D0 (en) | 2013-09-23 | 2013-09-23 | Method |
| GB1316849.7 | 2013-09-23 | ||
| US201361896933P | 2013-10-29 | 2013-10-29 | |
| US61/896,933 | 2013-10-29 | ||
| PCT/GB2014/052873 WO2015040423A1 (en) | 2013-09-23 | 2014-09-22 | Method |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2016532125A JP2016532125A (ja) | 2016-10-13 |
| JP2016532125A5 true JP2016532125A5 (enExample) | 2017-11-02 |
| JP6707453B2 JP6707453B2 (ja) | 2020-06-10 |
Family
ID=49553252
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2016543461A Active JP6707453B2 (ja) | 2013-09-23 | 2014-09-22 | ペプチド、ポリペプチドまたはタンパク質中の１個または複数の翻訳後修飾（ｐｔｍ）の存在、非存在、数または位置を決定する方法 |
Country Status (8)
| Country | Link |
|---|---|
| US (2) | US10712254B2 (enExample) |
| EP (1) | EP3049814B1 (enExample) |
| JP (1) | JP6707453B2 (enExample) |
| CN (1) | CN105765387B (enExample) |
| AU (1) | AU2014322867B2 (enExample) |
| CA (1) | CA2924752C (enExample) |
| GB (1) | GB201316849D0 (enExample) |
| WO (1) | WO2015040423A1 (enExample) |
Families Citing this family (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB201316849D0 (en) * | 2013-09-23 | 2013-11-06 | Isis Innovation | Method |
| GB201614455D0 (en) * | 2016-08-24 | 2016-10-05 | Univ Oxford Innovation Ltd | Biomarkers |
| BR112021004675A2 (pt) | 2018-09-11 | 2021-06-01 | Rijksuniversiteit Groningen | nanoporos biológicos com diâmetros de poros ajustáveis e usos dos mesmos como ferramentas analíticas |
| CN109300501B (zh) * | 2018-09-20 | 2021-02-02 | 国家卫生健康委科学技术研究所 | 蛋白质三维结构预测方法及用其构建的预测云平台 |
| CA3134796A1 (en) * | 2019-04-09 | 2020-10-15 | Oxford Nanopore Technologies Limited | Pore |
| CN112147185B (zh) * | 2019-06-29 | 2022-07-01 | 清华大学 | 一种控制多肽穿过纳米孔速度的方法及其应用 |
| BR112022009402A2 (pt) * | 2019-11-19 | 2022-08-09 | Univ Groningen | Nanoporos artificiais e usos e métodos relacionados com os mesmos |
| CN118011004A (zh) * | 2019-12-02 | 2024-05-10 | 牛津纳米孔科技公开有限公司 | 使用纳米孔表征靶多肽的方法 |
| NL2024579B1 (en) * | 2019-12-24 | 2021-09-06 | Univ Delft Tech | Protein and peptide fingerprinting and sequencing by nanopore translocation of peptide-oligonucleotide complexes |
| CN112480204A (zh) * | 2020-04-13 | 2021-03-12 | 南京大学 | 一种采用Aerolysin纳米孔道的蛋白质/多肽测序方法 |
| IL320502A (en) | 2022-10-28 | 2025-06-01 | Univ Groningen | Nanopore-based protein efflux |
| WO2024165853A1 (en) | 2023-02-07 | 2024-08-15 | Oxford University Innovation Limited | Method of characterising a peptide, polypeptide or protein using a nanopore |
| WO2025003492A1 (en) | 2023-06-30 | 2025-01-02 | Ecole Polytechnique Federale De Lausanne (Epfl) | Uses of aerolysin nanopores |
Family Cites Families (20)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6267872B1 (en) | 1998-11-06 | 2001-07-31 | The Regents Of The University Of California | Miniature support for thin films containing single channels or nanopores and methods for using same |
| US7744816B2 (en) * | 2002-05-01 | 2010-06-29 | Intel Corporation | Methods and device for biomolecule characterization |
| US8278055B2 (en) * | 2002-05-01 | 2012-10-02 | Intel Corporation | Methods and device for analyte characterization |
| GB0505971D0 (en) | 2005-03-23 | 2005-04-27 | Isis Innovation | Delivery of molecules to a lipid bilayer |
| GB0523282D0 (en) | 2005-11-15 | 2005-12-21 | Isis Innovation | Methods using pores |
| NZ579083A (en) | 2007-02-20 | 2012-07-27 | Oxford Nanopore Tech Ltd | Lipid bilayer sensor system |
| GB2453377A (en) | 2007-10-05 | 2009-04-08 | Isis Innovation | Transmembrane protein pores and molecular adapters therefore. |
| GB0724736D0 (en) | 2007-12-19 | 2008-01-30 | Oxford Nanolabs Ltd | Formation of layers of amphiphilic molecules |
| US9447152B2 (en) | 2008-07-07 | 2016-09-20 | Oxford Nanopore Technologies Limited | Base-detecting pore |
| US20110229877A1 (en) | 2008-07-07 | 2011-09-22 | Oxford Nanopore Technologies Limited | Enzyme-pore constructs |
| GB0820927D0 (en) * | 2008-11-14 | 2008-12-24 | Isis Innovation | Method |
| CA2750874A1 (en) | 2009-01-30 | 2010-08-05 | Oxford Nanopore Technologies Limited | Hybridization linkers |
| GB0905140D0 (en) | 2009-03-25 | 2009-05-06 | Isis Innovation | Method |
| BR112012013074B1 (pt) | 2009-12-01 | 2018-09-18 | Oxford Nanopore Technologies Limited | instrumento de análise e módulo para realizar análise bioquímica, e, método para operar um instrumento de análise para realizar análise bioquímica |
| AU2012264497B2 (en) * | 2011-05-27 | 2017-06-15 | Oxford Nanopore Technologies Limited | Coupling method |
| US10139417B2 (en) * | 2012-02-01 | 2018-11-27 | Arizona Board Of Regents On Behalf Of Arizona State University | Systems, apparatuses and methods for reading an amino acid sequence |
| AU2013220156B2 (en) * | 2012-02-15 | 2018-08-09 | Oxford Nanopore Technologies Limited | Aptamer method |
| JP6312607B2 (ja) * | 2012-02-16 | 2018-04-18 | ザ リージェンツ オブ ザ ユニバーシティ オブ カリフォルニア | 酵素仲介タンパク質トランスロケーションのためのナノポアセンサー |
| NL2009191C2 (en) | 2012-07-16 | 2014-01-20 | Univ Delft Tech | Single molecule protein sequencing. |
| GB201316849D0 (en) * | 2013-09-23 | 2013-11-06 | Isis Innovation | Method |
-
2013
- 2013-09-23 GB GBGB1316849.7A patent/GB201316849D0/en not_active Ceased
-
2014
- 2014-09-22 EP EP14772216.9A patent/EP3049814B1/en active Active
- 2014-09-22 CA CA2924752A patent/CA2924752C/en active Active
- 2014-09-22 US US15/023,652 patent/US10712254B2/en active Active
- 2014-09-22 AU AU2014322867A patent/AU2014322867B2/en active Active
- 2014-09-22 CN CN201480063812.9A patent/CN105765387B/zh active Active
- 2014-09-22 WO PCT/GB2014/052873 patent/WO2015040423A1/en not_active Ceased
- 2014-09-22 JP JP2016543461A patent/JP6707453B2/ja active Active
-
2020
- 2020-05-27 US US16/884,367 patent/US11592382B2/en active Active
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