| 序号 | 专利名 | 申请号 | 申请日 | 公开（公告）号 | 公开（公告）日 | 发明人 |
|---|---|---|---|---|---|---|
| 1 | 胱硫醚β-合酶的纯化 | CN201380027463.0 | 2013-03-25 | CN104540940A | 2015-04-22 | R.G.卡里洛; J.P.克劳斯; T.马坦; D.纳维 |
| 本发明提供用于纯化胱硫醚β-合酶(CBS)蛋白、尤其是其截短的变体的色谱法以及自其制备的组合物和药物组合物。 | ||||||
| 2 | 用于治疗高胱氨酸尿症的胱硫醚β-合酶 | CN201480006554.0 | 2014-01-29 | CN105452457A | 2016-03-30 | J·P·克劳斯; T·马吉坦; E·巴伯李尔 |
| 本发明提供使用人胱硫醚β-合酶(CBS)、其同源物、变体或突变体以治疗高胱氨酸尿症和其它相关疾病和病症的用于酶替代疗法的试剂和方法。 | ||||||
| 3 | シスタチオンβ−シンターゼの精製 | JP2015503433 | 2013-03-25 | JP6146934B2 | 2017-06-21 | カリージョ, リチャード ジー.; クラウス, ジャン ピー.; マイタン, トーマス; ナベー, デイビッド |
| 4 | COMPOSITIONS AND METHODS FOR TREATMENT OF HOMOCYSTINURIA | EP16864878.0 | 2016-11-09 | EP3373922A1 | 2018-09-19 | KRAUS, Jan, P.; MAJTAN, Tomas; BUBLIL, Erez |
| Provided are compositions and methods for enzyme replacement therapy using modified human cystathionine beta synthase (CBS) in the treatment of homocystinuria and related diseases and disorders. | ||||||
| 5 | CYSTATHIONINE BETA-SYNTHASE ENZYME FOR TREATMENT OF HOMOCYSTINURIA | EP14705634.5 | 2014-01-29 | EP2951299B1 | 2017-07-12 | KRAUS, Jan, P.; MAJTAN, Tomas; BUBLIL, Erez |
| The invention provides reagents and methods for enzyme replacement therapy using human cystathionine ²-synthase (CBS) homologues, variants or mutants thereof to treat homocystinuria and other related diseases and disorders. | ||||||
| 6 | COMPOSITIONS AND METHODS FOR TREATMENT OF HOMOCYSTINURIA | US15774755 | 2016-11-09 | US20180318404A1 | 2018-11-08 | Jan P. Kraus; Tomas Majtan; Erez Bublil |
| Provided are compositions and methods for enzyme replacement therapy using modified human cystathionine beta synthase (CBS) in the treatment of homocystinuria and related diseases and disorders. | ||||||
| 7 | Chemically modified cystathionine β-synthase enzyme for treatment of homocystinuria | US15235355 | 2016-08-12 | US10046036B2 | 2018-08-14 | Jan P Kraus; Tomas Majtan; Erez Bublil |
| The invention provides reagents and methods for enzyme replacement therapy using chemically modified species of human cystathionine β-synthase (CBS) to treat homocystinuria and other related diseases and disorders. | ||||||
| 8 | MICROORGANISM PRODUCING O-ACETYL-HOMOSERINE AND METHOD FOR PRODUCING O-ACETYLHOMOSERINE USING THE SAME | US15316475 | 2015-06-05 | US20170137853A1 | 2017-05-18 | Jee Yeon BAE; Hyun Ah KIM; Yong Uk SHIN; So Young KIM; Sang Kyoum KIM; Kwang Ho NA; Ju Hee SEO; Sung Kwang SON; Hye Ryun YOO; Jin Geun CHOI |
| The present disclosure relates to a microorganism producing O-acetylhomoserine with high efficiency and a method for producing O-acetylhomoserine and L-methionine using the microorganism. The present disclosure provides a microorganism producing O-acetylhomoserine having an enhanced activity of a protein which is predicted to export O-acetylhomoserine, and a method for producing O-acetylhomoserine and L-methionine using the microorganism. | ||||||
| 9 | USE OF HYDROGEN SULFIDE SYNTHESIS INHIBITORS FOR CANCER THERAPY | US14967649 | 2015-12-14 | US20160095831A1 | 2016-04-07 | Mark HELLMICH; Jia ZHOU; Csaba SZABO |
| In certain aspects the methods comprise administering an inhibitor of hydrogen sulfide biosynthesis, a cystathionine-β-synthase (CBS) inhibitor, or a hydrogen sulfide neutralizing agent to a patient having a cancer associated with elevated production of hydrogen sulfide. | ||||||
| 10 | Human Cystathionine Beta-Synthase Variants and Methods of Production Thereof | US14663749 | 2015-03-20 | US20160017309A1 | 2016-01-21 | Jan P. KRAUS |
| Human cystathionine β-synthase variants are disclosed, as well as a method to produce recombinant human cystathionine β-synthase and variants thereof. More particularly, the role of both the N-terminal and C-terminal regions of human CBS has been studied, and a variety of truncation mutants and modified CBS homologues are described. In addition, a method to express and purify recombinant human cystathionine β-synthase (CBS) and variants thereof which have only one or two additional amino acid residues at the N-terminus are described. | ||||||
| 11 | Human Cystathionine Beta-Synthase Variants and Methods of Production Thereof | US13826024 | 2013-03-14 | US20140023630A1 | 2014-01-23 | Jan P. KRAUS; Jana OLIVERIUSOVA |
| Human cystathionine β-synthase variants are disclosed, as well as a method to produce recombinant human cystathionine β-synthase and variants thereof. More particularly, the role of both the N-terminal and C-terminal regions of human CBS has been studied, and a variety of truncation mutants and modified CBS homologues are described. In addition, a method to express and purify recombinant human cystathionine β-synthase (CBS) and variants thereof which have only one or two additional amino acid residues at the N-terminus are described. | ||||||
| 12 | Purification of Cystathionine Beta-Synthase | US13830494 | 2013-03-14 | US20130251700A1 | 2013-09-26 | Richard G. CARRILLO; Jan P. KRAUS; Thomas MAJTAN; David NAVEH |
| This invention provides chromatographic methods for the purification of a cystathionine β-Synthase (CBS) protein, particularly truncated variants thereof and compositions and pharmaceutical compositions prepared therefrom. | ||||||
| 13 | Human cystathionine β-synthase variants and methods of production thereof | US10464811 | 2003-06-17 | US07485307B2 | 2009-02-03 | Jan P. Kraus; Jana Oliveriusova |
| Human cystathionine β-synthase variants are disclosed, as well as a method to produce recombinant human cystathionine β-synthase and variants thereof. More particularly, the role of both the N-terminal and C-terminal regions of human CBS has been studied, and a variety of truncation mutants and modified CBS homologues are described. In addition, a method to express and purify recombinant human cystathionine β-synthase (CBS) and variants thereof which have only one or two additional amino acid residues at the N-terminus are described. | ||||||
| 14 | CHEMICALLY MODIFIED CYSTATHIONINE BETA-SYNTHASE ENZYME FOR TREATMENT OF HOMOCYSTINURIA | US16025652 | 2018-07-02 | US20180311325A1 | 2018-11-01 | Jan P. Kraus; Tomas Majtan; Erez Bublil |
| The invention provides reagents and methods for enzyme replacement therapy using chemically modified species of human cystathionine β-synthase (CBS) to treat homocystinuria and other related diseases and disorders. | ||||||
| 15 | Human Cystathionine Beta-Synthase Variants and Methods of Production Thereof | US15458081 | 2017-03-14 | US20170253865A1 | 2017-09-07 | Jan P. KRAUS |
| Human cystathionine β-synthase variants are disclosed, as well as a method to produce recombinant human cystathionine β-synthase and variants thereof. More particularly, the role of both the N-terminal and C-terminal regions of human CBS has been studied, and a variety of truncation mutants and modified CBS homologues are described. In addition, a method to express and purify recombinant human cystathionine β-synthase (CBS) and variants thereof which have only one or two additional amino acid residues at the N-terminus are described. | ||||||
| 16 | METHIONINE METABOLITES PREDICT AGGRESSIVE CANCER PROGRESSION | US14617016 | 2015-02-09 | US20150204882A1 | 2015-07-23 | Neil A. Bhowmick; Diptiman Choudhury |
| The invention relates to the use of enzymes, nanorods, and nanoelectronic devices to detect cysteine level in a patient sample and relates to the use of the detected cysteine level to predict cancer recurrence in the patient and to prescribe and/or administer an appropriate therapy to a subject. The invention is directed to systems and methods of detecting cysteine level in a sample from a subject, wherein the systems or methods can further comprise measuring at least one additional parameter, such as PSA level, Gleason score and clinical stage. The invention is directed to systems and methods of predicting the probability of a recurrence of a cancer in a subject, wherein the systems or methods can further comprise measuring at least one additional parameter, such as PSA level, Gleason score and clinical stage. The invention further comprises prescribing and/or administering an appropriate therapy to a subject based on the predicted probability of recurrence. | ||||||
| 17 | Human cystathionine β-synthase variants and methods of production thereof | US13221379 | 2011-08-30 | US08398989B2 | 2013-03-19 | Jan P. Kraus; Jana Oliveriusova |
| Human cystathionine β-synthase variants are disclosed, as well as a method to produce recombinant human cystathionine β-synthase and variants thereof. More particularly, the role of both the N-terminal and C-terminal regions of human CBS has been studied, and a variety of truncation mutants and modified CBS homologues are described. In addition, a method to express and purify recombinant human cystathionine β-synthase (CBS) and variants thereof which have only one or two additional amino acid residues at the N-terminus are described. | ||||||
| 18 | Human cystathionine β-synthase variants and methods of production thereof | US12359287 | 2009-01-24 | US08007787B2 | 2011-08-30 | Jan P. Kraus |
| Human cystathionine β-synthase variants are disclosed, as well as a method to produce recombinant human cystathionine β-synthase and variants thereof. More particularly, the role of both the N-terminal and C-terminal regions of human CBS has been studied, and a variety of truncation mutants and modified CBS homologues are described. In addition, a method to express and purify recombinant human cystathionine β-synthase (CBS) and variants thereof which have only one or two additional amino acid residues at the N-terminus are described. | ||||||
| 19 | Human Cystathionine beta-Synthase Variants and Methods of Production Thereof | US12359287 | 2009-01-24 | US20100166725A1 | 2010-07-01 | Jan P. Kraus; Jana Oliveriusova |
| Human cystathionine β-synthase variants are disclosed, as well as a method to produce recombinant human cystathionine β-synthase and variants thereof. More particularly, the role of both the N-terminal and C-terminal regions of human CBS has been studied, and a variety of truncation mutants and modified CBS homologues are described. In addition, a method to express and purify recombinant human cystathionine β-synthase (CBS) and variants thereof which have only one or two additional amino acid residues at the N-terminus are described. | ||||||
| 20 | Human cystathionine β-synthase variants and methods of production thereof | US15015477 | 2016-02-04 | US09631188B2 | 2017-04-25 | Jan P. Kraus |
| Human cystathionine β-synthase variants are disclosed, as well as a method to produce recombinant human cystathionine β-synthase and variants thereof. More particularly, the role of both the N-terminal and C-terminal regions of human CBS has been studied, and a variety of truncation mutants and modified CBS homologues are described. In addition, a method to express and purify recombinant human cystathionine β-synthase (CBS) and variants thereof which have only one or two additional amino acid residues at the N-terminus are described. | ||||||
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