| 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 | 玉米ZmTrxh基因及其应用 | CN201410068709.5 | 2014-02-27 | CN104877973A | 2015-09-02 | 徐明良; 刘青青; 蒋璐; 陶永富; 刘欢欢; 叶建荣; 杨琴; 张琰; 张睿 |
| 本发明公开了一种玉米ZmTrxh基因及其应用。本发明公开的一种蛋白，为如下（1）或（2）所示：（1）SEQ ID No.2所示的蛋白；（2）将SEQ ID No.2所示的氨基酸序列经过一个或几个氨基酸残基的取代和/或缺失和/或添加且功能相同的蛋白质。本发明公开的玉米抗甘蔗花叶病毒病的主效基因ZmTrxh可提高玉米对甘蔗花叶病毒病的抗性。 | ||||||
| 2 | 生产含二硫键的蛋白质的宿主细胞和方法 | CN200980110335.6 | 2009-03-24 | CN102016047A | 2011-04-13 | J-Y·F·迪布瓦; R·H·M·库文; J·M·范迪尔 |
| 本发明提供了遗传修饰的芽孢杆菌宿主细胞，所述细胞具有降低的细胞质还原酶活性，例如降低的TrxA活性，以及编码异源葡萄球菌氧化酶的核酸。本发明还提供了使用本发明的宿主细胞生产含二硫键的蛋白质的方法，以及使用本发明的宿主细胞改进蛋白质折叠的方法。 | ||||||
| 3 | 含有硫氧还蛋白的皮肤外用剂组合物 | CN201380048674.2 | 2013-11-13 | CN104684568A | 2015-06-03 | 金志映; 黄俊永; 金英韶; 韩相勋 |
| 本发明涉及一种含有硫氧还蛋白的皮肤外用剂组合物。更具体地，涉及一种含有硫氧还蛋白，从而能够提供优异的皮肤保湿力改善效果、皮脂调节效果、毛孔收缩效果、通过血循环改善的脸色改善等的整体皮肤状态的改善效果的组合物。 | ||||||
| 4 | 生产含二硫键的蛋白质的宿主细胞和方法 | CN200980110335.6 | 2009-03-24 | CN102016047B | 2014-05-28 | J-Y·F·迪布瓦; R·H·M·库文; J·M·范迪尔 |
| 本发明提供了遗传修饰的芽孢杆菌宿主细胞，所述细胞具有降低的细胞质还原酶活性，例如降低的TrxA活性，以及编码异源葡萄球菌氧化酶的核酸。本发明还提供了使用本发明的宿主细胞生产含二硫键的蛋白质的方法，以及使用本发明的宿主细胞改进蛋白质折叠的方法。 | ||||||
| 5 | 用硫氧还蛋白减轻空气传播性和接触性变应原的变应原性 | CN00804968.8 | 2000-01-25 | CN1350547A | 2002-05-22 | B·B·布坎南; G·德瓦尔; R·M·洛萨诺; J·H·翁; B·C·伊; O·L·弗里克 |
| 硫氧还蛋白(一种小型二巯基蛋白)是变应原蛋白,特别是存在于花粉和动物和植物来源的变应原性蛋白质的一种特异性还原剂。其所有靶向的蛋白质含有二硫(S－S)键,它被硫氧还蛋白还原到巯基(SH)水平。其靶向的蛋白质具有变应原活性,而且在氧化(S－S)状态较不易被消化,当被还原(SH态)时,它们丧失其变应原性,和/或变得更可消化。当被NADPH通过NADP－硫氧还蛋白还原酶(生理条件)或通过硫辛酸化学还原剂激活(还原)时,硫氧还蛋白实现这种还原作用。过敏的狗进行的皮肤试验显示,在注射前用还原的硫氧还蛋白处理花粉消除了或降低了花粉的变应原性。研究显示被硫氧还蛋白还原后,花粉蛋白的消化提高。已被硫氧还蛋白还原的花粉蛋白是有效和安全的免疫治疗剂,可用于降低或消除动物在接触非还原花粉蛋白质时会发生的过敏反应。 | ||||||
| 6 | COMPOSITION FOR EXTERNAL USE SKIN PREPARATION, CONTAINING THIOREDOXIN | US14431853 | 2013-11-13 | US20150250700A1 | 2015-09-10 | Ji Yeong Kim; Joon Young Hwang; Young So Kim; Sang Hoon Han |
| The present invention relates to a composition for an external use skin preparation, containing thioredoxin, and more specifically, to a composition which contains thioredoxin thereby providing an overall improvement in skin condition such as a remarkable improvement in skin moisturization, sebum control, pore contraction, an improvement in skin color through blood circulation improvement, and the like. | ||||||
| 7 | Preventive or Therapeutic Agent for Inflammatory Ocular-Surface Diseases | US11885020 | 2006-02-24 | US20090280100A1 | 2009-11-12 | Junji Yodoi; Hajime Nakamura; Shigeru Kinoshita; Chie Sotozono |
| [Problems] The present invention aims to provide a preventive or therapeutic agent for inflammatory ocular-surface diseases.[Means for Solving Problems] The present invention provides a preventive or therapeutic agent for inflammatory ocular-surface diseases, which comprises polypeptides of thioredoxin superfamily as an active ingredient. | ||||||
| 8 | Growth factor for hair and skin treatment | US11385200 | 2006-03-21 | US20070224150A1 | 2007-09-27 | Yongji Chung |
| The present invention relates to a method of treatment for slowing the progress of skin aging comprising contacting the skin with an amount effective to slow skin aging of a composition comprising one or more compounds selected from the group consisting of EGF, bFGF, IGF-1, KGF, TGF-β3, TRX, VEGF, TRX, aFGF, FGF-10, copper peptide, acetyl hexapeptide, palmitoyl pentapeptide, CPP, and UDN glycoprotein. | ||||||
| 9 | Method for producing by cell-free protein synthesis system using thioredoxin-fused protein expression vector | US10992360 | 2004-11-19 | US20050255542A1 | 2005-11-17 | Mikako Shirouzu; Goushi Ishihara; Mihoro Saeki; Mie Goto; Kaori Tajima; Takanori Kigawa; Shigeyuki Yokoyama |
| A fusion protein of thioredoxin with a target protein is expressed in a cell-free protein synthesis system to thereby synthesize at least a part of the fusion protein as a soluble protein. It is preferable that the target protein is a highly hydrophobic protein such as a membrane protein. In particular, a membrane protein such a G protein-coupled receptor can be produced in a state being highly soluble and capable of forming a biologically active three dimensional structure. Also, provided a recombinant vector for producing such a membrane protein in a cell-free protein synthesis system. | ||||||
| 10 | Thioredoxin increases redox-cycling of anticancer agents thereby sensitizes cancer cells to apoptosis | US10970370 | 2004-10-21 | US20050208037A1 | 2005-09-22 | Ravi Dashnamoorthy; Kumuda Das |
| The present invention provides for treatment of cancer by enhancing the effectiveness of anticancer agents. The present invention therefore provides methods of increasing the apoptotic potential of anticancer drugs by increasing the expression of the cellular redox protein thioredoxin or thioredoxin-like molecules and thereby sensitizing the cancer to the anticancer agent. The present invention also provides methods of ameliorating negative side-effects of an anticancer therapy comprising a thioredoxin or a thioredoxin-like molecule and an anticancer therapy. | ||||||
| 11 | Stabilization of hypoallergenic, hyperdigestible previously reduced proteins | US10698824 | 2003-10-30 | US20040091578A1 | 2004-05-13 | Bob B. Buchanan; Susumu Morigasaki; Gregorio del Val; Oscar L. Frick |
| Disulfide proteins showed mitigated allergenicity and increased digestibility by pepsin following reduction by thioredoxin. The sulfhydryl groups newly formed on reduction by thioredoxin (at 4null C.) or dithiothreitol (DTT) (at 55null C.) were blocked with a physiological disulfide, such as cystamine or oxidized glutathione (GSSG) to obtain stable forms of the disarmed allergen. When derivatized with cystamine, BLG was separated from its oxidized and reduced forms on non-reducing SDS-PAGE and appeared to lack sulfhydryl groups. Although less effective GSSG, gave similar results. Allergenicity of the two derivatives was compared with that of the oxidized, reduced and reoxidized forms of BLG by skin testing dogs from a colony sensitized to cow's milk. Both the cystamine and GSSG derivatized BLG showed decreased allergenicity and increased sensitivity to pepsin as compared to controls. The reoxidized form resembled the derivatives in having lower allergenicity. The thioredoxin- and DTT-reduced forms showed hypoallergenic, hyperdigestible properties, most effectively when the reduced proteins were heated at 55null C. Whole milk subjected to these procedures showed results similar to those obtained with pure BLG. Other proteins are similarly stabilized. Stable forms of such disarmed, hypoallergenic and hyperdigestible disulfide protein allergens or just hypoallergenic or just hyperdigestible protein allergens are useful in foods as well as clinical preparations. | ||||||
| 12 | Use of thiol redox proteins for reducing protein intramolecular disulfide bonds, for improving the quality of cereal products, dough and baked goods and for inactivating snake, bee and scorpion toxins | US10464793 | 2003-06-17 | US20030215542A1 | 2003-11-20 | Bob B. Buchanan; Boihon C. Yee; Joshua H. Wong; Rosa M. Lozano; Karoly Kobrehel; Jin-An Jiao; Sungho Shin |
| Methods of reducing cystine containing animal and plant proteins, and improving dough and baked goods' characteristics is provided which includes the steps of mixing dough ingredients with a thiol redox protein to form a dough and baking the dough to form a baked good. The method of the present invention preferably uses reduced thioredoxin with wheat flour which imparts a stronger dough and higher loaf volumes. Methods for reducing snake, bee and scorpion toxin proteins with a thiol redox (SH) agent and thereby inactivating the protein or detoxifying the protein in an individual are also provided. Protease inhibitors, including the Kunitz and Bowman-Birk trypsin inhibitors of soybean, were also reduced by the NADP/thioredoxin system (NADPH, thioredoxin, and NADP-thioredoxin reductase) from either E. coli or wheat germ. When reduced by thioredoxin, the Kunitz and Bowman-Birk soybean trypsin inhibitors lose their ability to inhibit trypsin. Moreover, the reduced form of the inhibitors showed increased susceptibility to heat and proteolysis by either subtilisin or a protease preparation from germinating wheat seeds. The 2S albumin of castor seed endosperm was reduced by thioredoxin from either wheat germ or E. coli. Thioredoxin was reduced by either NADPH and NADP-thioredoxin reductase or dithiothreitol. Analyses showed that thioredoxin actively reduced the intramolecular disulfides of the 2S large subunit, but was ineffective in reducing the intermolecular disulfides that connect the large to the small subunit. A novel cystine containing protein that inhibits pullulanase was isolated. The protein was reduced by thioredoxin and upon reduction its inhibitory activity was destroyed or greatly reduced. | ||||||
| 13 | Neutralization of food allergens by thioredoxin | US326976 | 1994-10-21 | US5792506A | 1998-08-11 | Bob B. Buchanan; Karoly Kobrehel; Boihon C. Yee; Rosa Lozano; Oscar L. Frick; Richard W. Ermel |
| Thioredoxin, a small dithiol protein, is a specific reductant for major allergenic proteins present in widely used foods from animal and plant sources. All targeted allergenic proteins contain disulfide (S--S) bonds that are reduced to the sulfhydryl (SH) level by thioredoxin. The proteins are allergenically active in the oxidized (S--S) state. When reduced (SH state), they lose their allergenicity. Thioredoxin achieved this reduction when activated (reduced) either by NADPH via NADP-thioredoxin reductase (physiological conditions) or by dithiothreitol, a chemical reductant. Skin tests and feeding experiments carried out with sensitized dogs showed that treatment of the food with reduced thioredoxin prior to ingestion eliminated or decreased the allergenicity of the food. | ||||||
| 14 | Method for maintaining gut epithelial cells by treatment with a cytokine such as interleukin 11 | US941372 | 1992-09-02 | US5460810A | 1995-10-24 | David A. Williams; Steven C. Clark |
| A method for reducing damage or depletion of gut epithelial cells (e.g., as a result of radiation therapy or chemotherapy) by administration of one or more of the following cytokines: interleukin 11 (IL-11), interleukin 6 (IL-6), leukemia inhibitory factor/cholinergic differentiation factor (LIF/CDF), oncostatin M (OSM), or ciliary neurotrophic factor (CNTF). | ||||||
| 15 | Peptide and protein fusions to thioredoxin and thioredoxin-like molecules | US921848 | 1992-07-28 | US5292646A | 1994-03-08 | John McCoy; Edward R. LaVallie |
| This invention provides a fusion molecule comprising a DNA sequence encoding a thioredoxin-like protein fused to the DNA sequence encoding a selected heterologous peptide or protein. The peptide or protein may be fused to the amino terminus of the thioredoxin-like molecule, the carboxyl terminus of the thioredoxin-like molecule, or within the thioredoxin-like molecule, for example at the active-site loop of said molecule. Expression of this fusion molecule under the control of a regulatory sequence capable of directing its expression in a desired host cell, produces high levels of stable and soluble fusion protein. The fusion protein, located in the bacterial cytoplasm, may be selectively released from the cell by osmotic shock or freeze/thaw procedures. It may be optionally cleaved to liberate the soluble, correctly folded heterologous protein from the thioredoxin-like portion. | ||||||
| 16 | Method for treating cancer therapy radiation damage or arteriosclerosis using human ADF | US589616 | 1990-09-28 | US5210073A | 1993-05-11 | Junji Yodoi; Atsushi Uchida; Yutaka Tagaya; Akira Mitsui; Tadashi Hirakawa |
| A composition and method for the treatment of inflammation, rheumatism, autoimmune disease, ischemic damage of organs, drug toxicity and arteriosclerosis comprising human ADF is disclosed. | ||||||
| 17 | 티오레독신을 함유하는 피부 외용제 조성물 | KR1020120127891 | 2012-11-13 | KR1020140060928A | 2014-05-21 | 김지영; 황준영; 김영소; 한상훈 |
| The present invention relates to a composition comprising thioredoxin for external skin application and, more specifically, to a composition which comprises thioredoxin, thereby providing an overall improvement in skin conditions such as an excellent improvement in skin moisturization, sebum control, pore contraction, and an improvement in skin color through a blood circulation improvement. | ||||||
| 18 | ＴＲＸ-ＴＸＮＩＰ 복합체 변형 단백질의 결정화 방법 및 그의 입체구조 | KR1020130082514 | 2013-07-12 | KR101636932B1 | 2016-07-07 | 김명희; 황중원; 오태광 |
| 본발명은 TXNIP 변형단백질, 상기 TXNIP 변형단백질의제조방법, 상기변형단백질을코딩하는폴리뉴클레오티드, 상기폴리뉴클레오티드를포함하는발현벡터, 상기발현벡터가도입된형질전환체, 상기 TXNIP 변형단백질을이용한 TRX-TXNIP 복합체변형단백질의결정화방법, 및상기 TRX 및 TXNIP 간의상호작용을조절하는물질, TRX 활성저해제및 TXNIP 기능을조절하는물질을스크리닝하는방법에관한것이다. | ||||||
| 19 | ＴＲＸ-ＴＸＮＩＰ 복합체 변형 단백질의 결정화 방법 및 그의 입체구조 | KR1020130082514 | 2013-07-12 | KR1020140009079A | 2014-01-22 | 김명희; 황중원; 오태광 |
| The present invention relates to TXNIP modified protein; a production method of the TXNIP modified protein; a polynucleotide coding the TXNIP modified protein; an expression vector including the polynucleotide; a transformant in which the expression vector is transduced; a crystallization method for TRX-TXNIP complex modified protein using the TXNIP modified protein; a material controlling the interaction between TRX and TXNIP; and a screening method for a TRX activation inhibitor and a material controlling functions TXNIP. | ||||||
| 20 | Method for crystallization of TRX-TXNIP complex mutein and 3D structure thereof | US14414370 | 2013-07-12 | US09732126B2 | 2017-08-15 | Myung Hee Kim; Jung Won Hwang; Tae Kwang Oh |
| The present invention relates to a modified TXNIP protein, a method for preparing the modified TXNIP protein, a polynucleotide encoding the modified protein, an expression vector including the polynucleotide, a transformant introduced with the expression vector, a method for crystallizing a modified TRX-TXNIP complex using the modified TXNIP protein, and a method for screening a substance regulating interaction between TRX and TXNIP, an inhibitor of TRX activity, or a substance regulating TXNIP function. | ||||||
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