JP2012522501A5 - - Google Patents
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- JP2012522501A5 JP2012522501A5 JP2012502830A JP2012502830A JP2012522501A5 JP 2012522501 A5 JP2012522501 A5 JP 2012522501A5 JP 2012502830 A JP2012502830 A JP 2012502830A JP 2012502830 A JP2012502830 A JP 2012502830A JP 2012522501 A5 JP2012522501 A5 JP 2012522501A5
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- Prior art keywords
- amino acid
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- 235000001014 amino acid Nutrition 0.000 claims 123
- 125000003275 alpha amino acid group Chemical group 0.000 claims 117
- 238000006467 substitution reaction Methods 0.000 claims 113
- 150000007523 nucleic acids Chemical class 0.000 claims 42
- 108020004707 nucleic acids Proteins 0.000 claims 39
- 102000039446 nucleic acids Human genes 0.000 claims 39
- 101710143275 Single-stranded DNA cytosine deaminase Proteins 0.000 claims 23
- 102100022433 Single-stranded DNA cytosine deaminase Human genes 0.000 claims 23
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims 19
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 claims 17
- 108090000623 proteins and genes Proteins 0.000 claims 16
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 claims 15
- 235000004279 alanine Nutrition 0.000 claims 15
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 claims 14
- 229940024606 amino acid Drugs 0.000 claims 14
- 150000001413 amino acids Chemical class 0.000 claims 14
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 claims 13
- 239000004471 Glycine Substances 0.000 claims 13
- 235000013922 glutamic acid Nutrition 0.000 claims 13
- 239000004220 glutamic acid Substances 0.000 claims 13
- 235000018102 proteins Nutrition 0.000 claims 12
- 102000004169 proteins and genes Human genes 0.000 claims 12
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 claims 11
- 235000003704 aspartic acid Nutrition 0.000 claims 11
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 claims 11
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 claims 10
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims 10
- 239000004472 Lysine Substances 0.000 claims 10
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 claims 10
- 229960000310 isoleucine Drugs 0.000 claims 10
- 238000000034 method Methods 0.000 claims 9
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 claims 9
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 claims 8
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 claims 8
- 239000004475 Arginine Substances 0.000 claims 7
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 claims 7
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims 7
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims 7
- 210000004027 cell Anatomy 0.000 claims 7
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 claims 7
- 125000000539 amino acid group Chemical group 0.000 claims 6
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 claims 4
- 108020004705 Codon Proteins 0.000 claims 4
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 claims 4
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 claims 4
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 claims 4
- 239000004473 Threonine Substances 0.000 claims 4
- 235000009582 asparagine Nutrition 0.000 claims 4
- 229960001230 asparagine Drugs 0.000 claims 4
- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 claims 4
- 229930182817 methionine Natural products 0.000 claims 4
- 101000755690 Homo sapiens Single-stranded DNA cytosine deaminase Proteins 0.000 claims 3
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 claims 3
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 claims 3
- 241001465754 Metazoa Species 0.000 claims 3
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 claims 3
- 238000006243 chemical reaction Methods 0.000 claims 3
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 claims 3
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 claims 3
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims 3
- 239000004474 valine Substances 0.000 claims 3
- 108091028043 Nucleic acid sequence Proteins 0.000 claims 2
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 claims 2
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 claims 2
- 238000003556 assay Methods 0.000 claims 2
- 210000003719 b-lymphocyte Anatomy 0.000 claims 2
- 230000000694 effects Effects 0.000 claims 2
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 claims 2
- 230000001939 inductive effect Effects 0.000 claims 2
- 230000035772 mutation Effects 0.000 claims 2
- 239000002773 nucleotide Substances 0.000 claims 2
- 125000003729 nucleotide group Chemical group 0.000 claims 2
- 230000009261 transgenic effect Effects 0.000 claims 2
- 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 claims 2
- 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 1
- 102220488785 ADP-ribosylation factor 1_N52A_mutation Human genes 0.000 claims 1
- 241000894006 Bacteria Species 0.000 claims 1
- 101000755699 Bos taurus Single-stranded DNA cytosine deaminase Proteins 0.000 claims 1
- 241000282836 Camelus dromedarius Species 0.000 claims 1
- 241000283707 Capra Species 0.000 claims 1
- 102100026846 Cytidine deaminase Human genes 0.000 claims 1
- 108010031325 Cytidine deaminase Proteins 0.000 claims 1
- 102220557633 DNA-directed RNA polymerase I subunit RPA12_Q14H_mutation Human genes 0.000 claims 1
- 241000287828 Gallus gallus Species 0.000 claims 1
- 241000699666 Mus <mouse, genus> Species 0.000 claims 1
- 101000755751 Mus musculus Single-stranded DNA cytosine deaminase Proteins 0.000 claims 1
- 102000008300 Mutant Proteins Human genes 0.000 claims 1
- 108010021466 Mutant Proteins Proteins 0.000 claims 1
- 102220527891 NADH-cytochrome b5 reductase 2_K10Q_mutation Human genes 0.000 claims 1
- 241000283973 Oryctolagus cuniculus Species 0.000 claims 1
- 102220517097 Protease-associated domain-containing protein 1_A39P_mutation Human genes 0.000 claims 1
- 102220469611 Protein unc-13 homolog A_D67A_mutation Human genes 0.000 claims 1
- 241000700159 Rattus Species 0.000 claims 1
- 239000002253 acid Substances 0.000 claims 1
- 230000004913 activation Effects 0.000 claims 1
- 230000001580 bacterial effect Effects 0.000 claims 1
- 230000015572 biosynthetic process Effects 0.000 claims 1
- 210000004899 c-terminal region Anatomy 0.000 claims 1
- 229940106109 canineaid Drugs 0.000 claims 1
- 239000013611 chromosomal DNA Substances 0.000 claims 1
- 235000018417 cysteine Nutrition 0.000 claims 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims 1
- 210000003527 eukaryotic cell Anatomy 0.000 claims 1
- 239000013604 expression vector Substances 0.000 claims 1
- 108020001507 fusion proteins Proteins 0.000 claims 1
- 102000037865 fusion proteins Human genes 0.000 claims 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims 1
- 230000037431 insertion Effects 0.000 claims 1
- 238000003780 insertion Methods 0.000 claims 1
- 238000002955 isolation Methods 0.000 claims 1
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 claims 1
- 210000004962 mammalian cell Anatomy 0.000 claims 1
- 238000004519 manufacturing process Methods 0.000 claims 1
- 210000001236 prokaryotic cell Anatomy 0.000 claims 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 claims 1
- 102200016465 rs104894275 Human genes 0.000 claims 1
- 102220199342 rs1057521133 Human genes 0.000 claims 1
- 102220005306 rs33926796 Human genes 0.000 claims 1
- 102220324961 rs61730095 Human genes 0.000 claims 1
- 102220026962 rs63750005 Human genes 0.000 claims 1
- 230000000392 somatic effect Effects 0.000 claims 1
- 239000013598 vector Substances 0.000 claims 1
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US16634909P | 2009-04-03 | 2009-04-03 | |
| US61/166,349 | 2009-04-03 | ||
| PCT/IB2010/000958 WO2010113039A1 (en) | 2009-04-03 | 2010-04-05 | Mutants of activation-induced cytidine deaminase (aid) and methods of use |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2012522501A JP2012522501A (ja) | 2012-09-27 |
| JP2012522501A5 true JP2012522501A5 (enExample) | 2013-05-02 |
| JP5683566B2 JP5683566B2 (ja) | 2015-03-11 |
Family
ID=42617524
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2012502830A Expired - Fee Related JP5683566B2 (ja) | 2009-04-03 | 2010-04-05 | 活性化誘導シチジンデアミナーゼ（ａｉｄ）の変異体及び使用方法 |
Country Status (10)
| Country | Link |
|---|---|
| US (1) | US9683226B2 (enExample) |
| EP (1) | EP2414507B1 (enExample) |
| JP (1) | JP5683566B2 (enExample) |
| CN (1) | CN102482639B (enExample) |
| AU (1) | AU2010230985B2 (enExample) |
| CA (1) | CA2757178C (enExample) |
| DK (1) | DK2414507T3 (enExample) |
| ES (1) | ES2498765T3 (enExample) |
| RU (1) | RU2537264C2 (enExample) |
| WO (1) | WO2010113039A1 (enExample) |
Families Citing this family (37)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2007067032A1 (en) | 2005-12-09 | 2007-06-14 | Academisch Medisch Cemtrum Bij De Universiteit Van Amsterdam | Means and methods for influencing the stability of cells |
| CA3015416C (en) | 2005-12-09 | 2022-10-11 | Academisch Medisch Centrum Bij De Universiteit Van Amsterdam | Means and methods for influencing the stability of antibody producing cells |
| US9445581B2 (en) | 2012-03-28 | 2016-09-20 | Kymab Limited | Animal models and therapeutic molecules |
| DK2792236T4 (da) | 2009-07-08 | 2023-05-15 | Kymab Ltd | Dyremodeller og terapeutiske molekyler |
| ES2666584T3 (es) * | 2009-07-15 | 2018-05-07 | Aimm Therapeutics B.V. | Medios y métodos para producir anticuerpos de alta afinidad |
| EP2638155A1 (en) | 2010-11-08 | 2013-09-18 | Kymab Limited | Cells & vertebrates for enhanced somatic hypermutation and class switch recombination |
| RU2585153C2 (ru) | 2010-12-02 | 2016-05-27 | Аимм Терапьютикс Б.В. | Средства и способы получения высокоаффинных антител |
| EP2670848B1 (en) | 2011-02-06 | 2016-02-03 | Yeda Research and Development Co. Ltd | Affinity maturated t cell receptors and use thereof |
| BR112014006394A2 (pt) | 2011-09-19 | 2017-03-28 | Kymab Ltd | manipulação de diversidade genética de imunoglobulina e terapêuticos multi-anticorpos |
| WO2013045916A1 (en) | 2011-09-26 | 2013-04-04 | Kymab Limited | Chimaeric surrogate light chains (slc) comprising human vpreb |
| US9253965B2 (en) | 2012-03-28 | 2016-02-09 | Kymab Limited | Animal models and therapeutic molecules |
| US10251377B2 (en) | 2012-03-28 | 2019-04-09 | Kymab Limited | Transgenic non-human vertebrate for the expression of class-switched, fully human, antibodies |
| GB2502127A (en) | 2012-05-17 | 2013-11-20 | Kymab Ltd | Multivalent antibodies and in vivo methods for their production |
| CN103031295B (zh) * | 2012-12-10 | 2015-01-28 | 浙江工业大学 | 冬虫夏草胞苷脱氨酶、编码基因及其应用 |
| PL225333B1 (pl) * | 2013-01-14 | 2017-03-31 | Inst Chemii Bioorganicznej Polskiej Akademii Nauk | Preparat wykazujący aktywność ludzkiej deaminazy cytydyny indukowanej aktywacją limfocytów B (AID) oraz sposób otrzymywania tego preparatu w systemie bakteryjnym |
| US9788534B2 (en) | 2013-03-18 | 2017-10-17 | Kymab Limited | Animal models and therapeutic molecules |
| US9783618B2 (en) | 2013-05-01 | 2017-10-10 | Kymab Limited | Manipulation of immunoglobulin gene diversity and multi-antibody therapeutics |
| US11707056B2 (en) | 2013-05-02 | 2023-07-25 | Kymab Limited | Animals, repertoires and methods |
| US9783593B2 (en) | 2013-05-02 | 2017-10-10 | Kymab Limited | Antibodies, variable domains and chains tailored for human use |
| CA2925723A1 (en) | 2013-10-01 | 2015-04-09 | Kymab Limited | Animal models and therapeutic molecules |
| DK3099709T3 (da) | 2014-01-31 | 2020-02-03 | Aimm Therapeutics Bv | Midler og fremgangsmåder til fremstilling af stabile antistoffer |
| CN104263755B (zh) * | 2014-07-03 | 2017-02-15 | 成都中联生科基因科技有限公司 | 一种利用dna损伤修复机制使单克隆抗体细胞株进行体内快速进化的新方法 |
| US10968444B2 (en) * | 2017-05-22 | 2021-04-06 | Abzyme Therapeutics Llc | Methods for generating bispecific functional agents |
| US10704040B2 (en) * | 2017-05-22 | 2020-07-07 | Abzyme Therapeutics Llc | Triple-mode system for antibody maturation, surface display and secretion |
| CN107177625B (zh) * | 2017-05-26 | 2021-05-25 | 中国农业科学院植物保护研究所 | 一种定点突变的人工载体系统及定点突变方法 |
| US10961525B2 (en) * | 2017-07-05 | 2021-03-30 | The Trustees Of The University Of Pennsylvania | Hyperactive AID/APOBEC and hmC dominant TET enzymes |
| CN109402096B (zh) * | 2018-11-20 | 2021-01-01 | 中国科学院生物物理研究所 | 一种aid酶突变体及其应用 |
| WO2020148206A1 (en) * | 2019-01-14 | 2020-07-23 | INSERM (Institut National de la Santé et de la Recherche Médicale) | Methods and kits for generating and selecting a variant of a binding protein with increased binding affinity and/or specificity |
| WO2020206325A2 (en) * | 2019-04-05 | 2020-10-08 | The Broad Institute, Inc. | A pseudo-random dna editor for efficient and continuous nucleotide diversification in human cells |
| CN110734900B (zh) * | 2019-11-06 | 2022-09-30 | 上海科技大学 | 一种胞嘧啶碱基编辑工具及其用途 |
| CN111518794B (zh) * | 2020-04-13 | 2023-05-16 | 中山大学 | 基于激活诱导性胞苷脱氨酶的诱导突变蛋白的制备和用途 |
| IL276599A (en) | 2020-08-09 | 2022-03-01 | Yeda Res & Dev | T cell receptor unique to mage-a1 and its uses |
| CN112708650A (zh) * | 2020-12-31 | 2021-04-27 | 河南巨龙生物工程股份有限公司 | 一种缩短胞苷发酵迟滞期的方法 |
| CN113073094B (zh) * | 2021-03-29 | 2023-03-28 | 中山大学 | 基于胞苷脱氨酶LjCDA1L1_4a及其突变体的单碱基突变系统 |
| CN115094127A (zh) * | 2022-02-22 | 2022-09-23 | 中国科学院深圳先进技术研究院 | 一种原位检测蛋白质与脱氧核糖核苷酸结合位置的方法 |
| EP4491723A1 (en) * | 2022-03-08 | 2025-01-15 | Institute Of Genetics And Developmental Biology, Chinese Academy Of Sciences | Cytosine deaminase and use thereof in base editing |
| WO2025119295A1 (zh) * | 2023-12-05 | 2025-06-12 | 广州瑞风生物科技有限公司 | 脱氨酶、融合蛋白、核酸、药物组合物及其应用 |
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| EP1506288B1 (en) * | 2002-05-10 | 2013-04-17 | Medical Research Council | Activation induced deaminase (aid) |
| US20050287648A1 (en) * | 2002-08-05 | 2005-12-29 | University Of Rochester | Protein Transducing Domain/Deaminase Chimeric Proteins, Related Compounds, and Uses Thereof |
| US7393923B2 (en) | 2004-11-08 | 2008-07-01 | The Regents Of The University Of California | Red-shifted fluorescent proteins mPlum and mRaspberry and polynucleotides encoding the same |
| JP4482693B2 (ja) * | 2005-08-29 | 2010-06-16 | 国立大学法人 岡山大学 | 抗体産生細胞の特異的選択方法 |
| GB0607063D0 (en) * | 2006-04-07 | 2006-05-17 | Cellcentric Ltd | Compositions and methods for epigenetic modification of nucleic acid sequences in vivo |
| US20090075378A1 (en) * | 2007-02-20 | 2009-03-19 | Anaptysbio, Inc. | Somatic hypermutation systems |
| US7803582B2 (en) * | 2007-03-17 | 2010-09-28 | Hongzhan Xu | Recombinant vector and use in gene therapy |
| US8095350B2 (en) * | 2007-12-21 | 2012-01-10 | Xiaojiang Chen | Three-dimensional structure of the APOBEC 2 structure, uses thereof, and methods for treating chronic and infectious diseases |
| US7981655B2 (en) * | 2008-02-07 | 2011-07-19 | Regents Of The University Of Minnesota | Modified cytosine deaminases |
| EP2098536A1 (en) * | 2008-03-05 | 2009-09-09 | 4-Antibody AG | Isolation and identification of antigen- or ligand-specific binding proteins |
-
2010
- 2010-04-05 AU AU2010230985A patent/AU2010230985B2/en active Active
- 2010-04-05 CA CA2757178A patent/CA2757178C/en active Active
- 2010-04-05 ES ES10723293.6T patent/ES2498765T3/es active Active
- 2010-04-05 CN CN201080023311.XA patent/CN102482639B/zh active Active
- 2010-04-05 DK DK10723293.6T patent/DK2414507T3/da active
- 2010-04-05 JP JP2012502830A patent/JP5683566B2/ja not_active Expired - Fee Related
- 2010-04-05 US US13/262,187 patent/US9683226B2/en active Active
- 2010-04-05 RU RU2011144569/10A patent/RU2537264C2/ru active
- 2010-04-05 WO PCT/IB2010/000958 patent/WO2010113039A1/en not_active Ceased
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