重组核糖体失活蛋白alpha-苦瓜素的生物学活性分析
|
摘要
植物核糖体失活蛋白(ribosome-inactivating proteins, RIPs)是一类可以将真核细胞28SrRNA的SRL区域的A4324脱去,并破坏延伸因子与核糖体的结合,从而将蛋白质的生物合成抑制在延伸阶段的蛋白质家族。研究表明RIPs具有免疫调节、骨髓净化、抗病毒、抗细菌、抗真菌、抗突变、抗肿瘤等多种活性,并能够增强宿主植物对病原菌的抵抗作用。RIPs在植物界中分布的比较广泛,尤以葫芦科家族(如苦瓜、丝瓜、南瓜)中含量最多。从苦瓜种子中提取的α-苦瓜素因能在体外抑制兔网织红细胞裂解物和小麦胚乳系统的蛋白质翻译过程而被认为是RIPs家族的成员之一。目前对α-苦瓜素的活性研究并不深入,并且该蛋白也尚未得到充分的应用。因此,本研究将大肠杆菌异源表达系统和亲和纯化技术相结合得到了高纯度的α-苦瓜素蛋白,并对其酶活性进行了研究,结果如下：
1.将含有α-苦瓜素基因的重组表达载体pET-MC转化到大肠杆菌Rosetta (DE3) pLysS菌株内,得到了富含a-苦瓜素基因的工程菌株。此外,我们还分析了培养条件(培养时间：6-18h; IPTG诱导剂的浓度：0.5-1.5mM;诱导温度：22-37℃；诱导的菌体浓度OD600:0.6-0.8)对重组蛋白质得率的影响,最终优化出能够使大部分重组α-苦瓜素蛋白在细胞质内积累的培养条件。诱导后的菌液经SDS-PAGE检测后发现重组蛋白的表达量是115mg/L。经Ni-NTA亲和层析后得到的蛋白质产量为85mg/L,即回收率为73.9%, SDS-PAGE检测结果表明重组蛋白的纯度为94.7%。
2.首先用水稻的rRNAs验证重组α-苦瓜素的RNA N-糖苷酶活性,结果发现该酶活性是浓度依赖性的。低浓度蛋白仅仅影响了28S rRNA,并产生了典型的"Endo's fragment";而高浓度蛋白则将RNAs完全降解成弥散条带。我们还发现重组α-苦瓜素对尖镰孢(Fusarium oxysporum L.)和腐皮镰孢(Fusarium solani L.)的生长有较强的抑制作用。此外,α-苦瓜素蛋白也能抑制铜绿脓杆菌(Pseudomonas aeruginosa L.)的生长和繁殖。
3.在DNase-like活性的研究过程中,我们发现该酶活性是浓度依赖性、二价金属离子依赖性、温度敏感型、pH稳定型的。圆二色谱(CD)检测结果表明α-苦瓜素仅仅影响了质粒DNA的碱基堆积作用,但是对DNA的右手螺旋却没有影响。通过点突变技术将对多聚核苷酸：腺嘌呤糖苷酶活性关键的五个氨基酸残基Tyr93、Tyr134、Glu183、Arg186、Trp215突变成Ala,然后通过大肠杆菌异源表达得到纯化的突变体蛋白,并进一步分析DNase-like活性。研究发现Y93A突变体完全丧失了1DNase-like酶活性,而其余4个突变体的酶活性略受影响,充分说明多聚核苷酸：腺嘌呤糖苷酶活性DNase-like酶活性是由不同但是却紧密相关的结构域行使的。
4.为了开发与α-苦瓜素基因紧密连锁的SSR分子标记,我们采用FIASCO (Fast Isolation by AFLP of Sequence COntaining Repeats)扩增和磁珠富集技术从苦瓜基因组DNA内分离出16对多态性的SSR分子标记,并在5个群体(广西、湖南、四川、江西、湖北)共36份材料内进行了多态性检测。这16对引物扩增的等位基因数为3-8,Ho和He的范围分别为0.000-1.000和0.325-0.867,并且这些标记之间不存在严重的连锁不平衡现象。这些SSR标记在苦瓜的近缘属植物西葫芦(Cucurbita pepo L.)、丝瓜(Luffa cylindrical L.)、葫芦(Lagenaria siceraria L.)、黄瓜(Cucumis sativus L.)内具有比较强的通用性。这些标记将为α-苦瓜素基因的定位分析奠定有力的基础,同时也将对苦瓜及近缘种属的分类、亲缘关系的研究,以及育种工作有重要的指导意义。
Ribosome-inactivating proteins (RIPs) are a family of enzyme, which could remove a specific adenine A4324from the highly conserved, surface-exposed, α-sarcin/ricin loop in the28S rRNA of eukaryotic ribosomes. The depurination destroyed the interaction between elongation factors and ribosome, thereby resulting in inactivation of ribosomes and inhibition of protein synthesis. Studies show that RIPs not only have immunomodulatory,"clean-up" of bone marrow, antivirus, antimicrobial, antifungal, antimutagenic, antitumor, but also could effectively enhance the resistance of host plant to pathogens. RIPs are widely distributed in the plant kingdom, especially the Cucurbitaceae family including bitter gourd, sponge gourd and pumpkin. Alpha-Momordicin (α-MC), a RIP isolated from Momordica charantia L., could inhibit protein synthesis in rabbit reticulocyte lysate and wheat endosperm system. Studies on the enzamital activity were not complete, while its applications have not yet been fully developed. In this study, the highly purified α-MC was obtained from E.coli heterologous expression system coupled with Ni-NTA affinity chromatography. Researches on the enzymatic activities of α-MC were as followes:
1. We have constructed the recombinant expression vector pET-MC and transformed it into E. coli Rosetta (DE3) pLysS strain. After optimizing the cultural condition by varying induction time (6-18h), IPTG concentration (0.5-1.5mM), culture temperature (22-37℃), and the cell concentration (0.6-1.0for OD600), the recombinant α-MC protein was mostly present in the soluble fraction. Subsequently, α-MC protein was recovered from the bacterial cells using Ni-NTA affinity chromatography. The protein concentration was estimated to be85mg/L with Bradford method. SDS-PAGE electrophoresis showed the94.7%purity and the recovery of73.9%.
2. Results showed that the RNA N-glycosidase activity was concentration-dependent. Only the28S rRNA was affected when being incubated with low concentrations of a-MC, releasing the typical "Endo's fragment". With the increase of protein concentration, total rRNAs were completely degraded, as smear bands appearing on the agarose gel. The antifungal activity towards F. oxysporum and F. solan were tested from both molecular and cell levels. In addition, a-MC could also effectively inhibit the growth of P. aeruginosa.
3. The DNase-like activity of a-MC towards plasmid was concentration-dependent, metal-dependent, temperature-sensitive, and pH-stable. Circular dichroism was used to detect the conformational change in plamid DNA. To explore the relationship between the DNase-like activity and polynucleotide:adenosine glycosidase activity, five amino acids critical for the polynucleotide:adenosine glycosidase activity were mutated to alanine, respectively. After prokaryotic expression and affinity purification, five homogenous mutant proteins were obtained. The DNase-like activity was completely lost in the Y93A mutant. However, the DNase-like activity was more or less affected in the other four mutants. We speculated that the polynucleotide: adenosine glycosidase activity and DNase-like activity might be implemented by distinct but related domains.
4. In order to develop SSR markers linked with a-MC gene, the FIASCO technology was utilized to isolate microsatellites from bitter melon genomic DNA. In total,16loci showed polymorphic in36accessions collected from five populations (Guangxi, Hunan, Sichuan, Jiangxi, and Hubei). These loci contained three to eight alleles, with He and Ho ranging from0.325to0.867and from0.000to1.000, respectively. No significant linkage disequilibrium was found between these polymorphic loci. These markers could also amplify corresponding fragments in Cucurbita pepo L., Luffa cylindrical L., Lagenaria siceraria L., and Cucumis sativus L. These marks will facilitate the mapping of a-MC gene, and are also useful for genus classification, relation studies, as well as the molecular marker assisting breeding of bitter melon and other closely related species.
1.将含有α-苦瓜素基因的重组表达载体pET-MC转化到大肠杆菌Rosetta (DE3) pLysS菌株内,得到了富含a-苦瓜素基因的工程菌株。此外,我们还分析了培养条件(培养时间：6-18h; IPTG诱导剂的浓度：0.5-1.5mM;诱导温度：22-37℃；诱导的菌体浓度OD600:0.6-0.8)对重组蛋白质得率的影响,最终优化出能够使大部分重组α-苦瓜素蛋白在细胞质内积累的培养条件。诱导后的菌液经SDS-PAGE检测后发现重组蛋白的表达量是115mg/L。经Ni-NTA亲和层析后得到的蛋白质产量为85mg/L,即回收率为73.9%, SDS-PAGE检测结果表明重组蛋白的纯度为94.7%。
2.首先用水稻的rRNAs验证重组α-苦瓜素的RNA N-糖苷酶活性,结果发现该酶活性是浓度依赖性的。低浓度蛋白仅仅影响了28S rRNA,并产生了典型的"Endo's fragment";而高浓度蛋白则将RNAs完全降解成弥散条带。我们还发现重组α-苦瓜素对尖镰孢(Fusarium oxysporum L.)和腐皮镰孢(Fusarium solani L.)的生长有较强的抑制作用。此外,α-苦瓜素蛋白也能抑制铜绿脓杆菌(Pseudomonas aeruginosa L.)的生长和繁殖。
3.在DNase-like活性的研究过程中,我们发现该酶活性是浓度依赖性、二价金属离子依赖性、温度敏感型、pH稳定型的。圆二色谱(CD)检测结果表明α-苦瓜素仅仅影响了质粒DNA的碱基堆积作用,但是对DNA的右手螺旋却没有影响。通过点突变技术将对多聚核苷酸：腺嘌呤糖苷酶活性关键的五个氨基酸残基Tyr93、Tyr134、Glu183、Arg186、Trp215突变成Ala,然后通过大肠杆菌异源表达得到纯化的突变体蛋白,并进一步分析DNase-like活性。研究发现Y93A突变体完全丧失了1DNase-like酶活性,而其余4个突变体的酶活性略受影响,充分说明多聚核苷酸：腺嘌呤糖苷酶活性DNase-like酶活性是由不同但是却紧密相关的结构域行使的。
4.为了开发与α-苦瓜素基因紧密连锁的SSR分子标记,我们采用FIASCO (Fast Isolation by AFLP of Sequence COntaining Repeats)扩增和磁珠富集技术从苦瓜基因组DNA内分离出16对多态性的SSR分子标记,并在5个群体(广西、湖南、四川、江西、湖北)共36份材料内进行了多态性检测。这16对引物扩增的等位基因数为3-8,Ho和He的范围分别为0.000-1.000和0.325-0.867,并且这些标记之间不存在严重的连锁不平衡现象。这些SSR标记在苦瓜的近缘属植物西葫芦(Cucurbita pepo L.)、丝瓜(Luffa cylindrical L.)、葫芦(Lagenaria siceraria L.)、黄瓜(Cucumis sativus L.)内具有比较强的通用性。这些标记将为α-苦瓜素基因的定位分析奠定有力的基础,同时也将对苦瓜及近缘种属的分类、亲缘关系的研究,以及育种工作有重要的指导意义。
Ribosome-inactivating proteins (RIPs) are a family of enzyme, which could remove a specific adenine A4324from the highly conserved, surface-exposed, α-sarcin/ricin loop in the28S rRNA of eukaryotic ribosomes. The depurination destroyed the interaction between elongation factors and ribosome, thereby resulting in inactivation of ribosomes and inhibition of protein synthesis. Studies show that RIPs not only have immunomodulatory,"clean-up" of bone marrow, antivirus, antimicrobial, antifungal, antimutagenic, antitumor, but also could effectively enhance the resistance of host plant to pathogens. RIPs are widely distributed in the plant kingdom, especially the Cucurbitaceae family including bitter gourd, sponge gourd and pumpkin. Alpha-Momordicin (α-MC), a RIP isolated from Momordica charantia L., could inhibit protein synthesis in rabbit reticulocyte lysate and wheat endosperm system. Studies on the enzamital activity were not complete, while its applications have not yet been fully developed. In this study, the highly purified α-MC was obtained from E.coli heterologous expression system coupled with Ni-NTA affinity chromatography. Researches on the enzymatic activities of α-MC were as followes:
1. We have constructed the recombinant expression vector pET-MC and transformed it into E. coli Rosetta (DE3) pLysS strain. After optimizing the cultural condition by varying induction time (6-18h), IPTG concentration (0.5-1.5mM), culture temperature (22-37℃), and the cell concentration (0.6-1.0for OD600), the recombinant α-MC protein was mostly present in the soluble fraction. Subsequently, α-MC protein was recovered from the bacterial cells using Ni-NTA affinity chromatography. The protein concentration was estimated to be85mg/L with Bradford method. SDS-PAGE electrophoresis showed the94.7%purity and the recovery of73.9%.
2. Results showed that the RNA N-glycosidase activity was concentration-dependent. Only the28S rRNA was affected when being incubated with low concentrations of a-MC, releasing the typical "Endo's fragment". With the increase of protein concentration, total rRNAs were completely degraded, as smear bands appearing on the agarose gel. The antifungal activity towards F. oxysporum and F. solan were tested from both molecular and cell levels. In addition, a-MC could also effectively inhibit the growth of P. aeruginosa.
3. The DNase-like activity of a-MC towards plasmid was concentration-dependent, metal-dependent, temperature-sensitive, and pH-stable. Circular dichroism was used to detect the conformational change in plamid DNA. To explore the relationship between the DNase-like activity and polynucleotide:adenosine glycosidase activity, five amino acids critical for the polynucleotide:adenosine glycosidase activity were mutated to alanine, respectively. After prokaryotic expression and affinity purification, five homogenous mutant proteins were obtained. The DNase-like activity was completely lost in the Y93A mutant. However, the DNase-like activity was more or less affected in the other four mutants. We speculated that the polynucleotide: adenosine glycosidase activity and DNase-like activity might be implemented by distinct but related domains.
4. In order to develop SSR markers linked with a-MC gene, the FIASCO technology was utilized to isolate microsatellites from bitter melon genomic DNA. In total,16loci showed polymorphic in36accessions collected from five populations (Guangxi, Hunan, Sichuan, Jiangxi, and Hubei). These loci contained three to eight alleles, with He and Ho ranging from0.325to0.867and from0.000to1.000, respectively. No significant linkage disequilibrium was found between these polymorphic loci. These markers could also amplify corresponding fragments in Cucurbita pepo L., Luffa cylindrical L., Lagenaria siceraria L., and Cucumis sativus L. These marks will facilitate the mapping of a-MC gene, and are also useful for genus classification, relation studies, as well as the molecular marker assisting breeding of bitter melon and other closely related species.
引文
陈禅友,兰红,李亚木,戴希刚.苦瓜种质资源ISSR遗传多态性分析.长江蔬菜,2012,(12)：19-22.
陈燕平,汪钟信,邓望喜.杀虫植物苦瓜的研究进展.湖北植保,2001,(6)：7-9.
程雪,胡进耀,苏智先.丝瓜核糖体失活蛋白的研究进展综述.西华师范大学学报,2004,25(2)：207-209.
褚嘉佑等,褚嘉佑,杨爱德,王辨明,胡忠,张和君,史良如,曲京华,罗兰英,郭仁.抗人T细胞单克隆抗体与商陆毒蛋白结合物的制备及其抗白血病细胞活性.细胞与分子免疫学杂志,1988,(3)：58.
傅明辉,田洁.苦瓜籽核糖体失活蛋白的分离纯化及抗氧化活性的研究.中国生化药物杂志,2002，3：134-136.
黄春萍,张宏,张晓喻.植物抗真菌蛋白的分类及抗菌机制研究进展.国外医药(抗生素分册),2007,(4)：167-171.
黄如葵,孙德利,张曼,方锋学,罗海玲.苦瓜遗传多样性的形态学性状聚类分析.广西农业科学,2008,(3)：351-356.
贾茗娴,尹惠琼,王跃华,章金刚。蓖麻毒素检测技术研究进展.生物技术通讯,2011,22(5)：747-750.
李建国.核糖体失活蛋白的研究进展.分子植物育种,2005,(4)：566-570.
李向东,刘望夷.核糖体失活蛋白的结构功能与分布.细胞生物学杂志,1997,19(2)：69-75.
林育泉,刘思,周鹏.新型抗病毒抗肿瘤苦瓜蛋白MAP30的研究进展.华南热带农业大学学报,2005,11(4)：24-29.
毛兴平.苦瓜AFLP分子标记反应体系的建立.广西热带农业,2010,(6)：9-14.
齐文波,徐中平,徐誉泰,宋剑秋,张英慧,王海仁.苦瓜素的分离纯化与抗肿瘤活性的研究.离子交换与吸附,1999,15(1)：59-63.
蘧艳峰,郭素堂,袁静明.细胞毒素Gelonin的结构功能及其在抗癌治疗中的应用前景.肿瘤研究与临床,2006,18(2)：139-140.
孙海燕,胡家恕,汪俏梅.苦瓜的核糖体失活蛋白.2004,26(3)：247-251.
孙亚卿,邵金旺,张少英.甜菜基因工程研究进展及其展望.中国农学通报,23(4)：27-32.
王庆华,于长春,徐誉泰,王海仁.α-苦瓜素和β-苦瓜素的研究进展.中草药,1995,26(5)：266-267.
王为,王长彪,刘方,陈浩东,王林,王春英,张香娣,王玉红,王坤波.棉花非冗余性EST-SSR新标记的开发及其评价.作物学报,2012,1443-1451.
王绪.苦瓜性别分化相关分子标记的研究.南宁：广西大学,2007.
徐振武,陈陵际.天花粉蛋白对人结肠癌SW—I116裸鼠的体内实验研究.浙江肿瘤,1997,3(2)：110-111.
杨洲平,黄乾明,刘一江,陈平.不同苦瓜品种MAP30基因的克隆及序列分析.四川农业大学学报,2007,25(1)：58-62.
袁燕,毛宇,黄晓麒,戴晓畅.核糖体失活蛋白研究新进展.天然产物研究与开发,2007,19(1)：169-174.
张君毅,郭巧生.磁珠富集法分离半夏微卫星序列.中国中药杂志,2009, 34(12)：1479-1482.
张智,孙素荣,马纪,张富春.植物中的核糖体失活蛋白及其抗病毒机制.植物生理学通讯,2005,41(4)：537-541.
Bagga S, Seth D, Batra JK. The cytotoxic activity of ribosome-inactivating protein saporin-6 is attributed to its rRNA N-glycosidase and internucleosomal DNA fragmentation activities. J. Biol. Chem.,2003,278:4813-4820.
Bai Y, Watt B, Wahome PG, Mantis NJ, Robertus JD. Identification of new classes of ricin toxin inhibitors by virtual screening. Toxicon,2010,56(4):526-534.
Balconi C, Lanzanova C, Conti E, Triulzi T, Forlani F, Cattaneo M, Lupotto E. Fusarium head blight evaluation in wheat transgenic plants expressing the maize b-32 antifungal gene. Eur. J. Plant Pathol.,2007,117(2):129-140.
Barbieri L, Ferreras JM, Barraco A, Ricci P, Stirpe F. Some ribosome-inactivating proteins depurinate ribosomal RNA at multiple sites. Biochem. J.,1992,286(Pt 1):1-4.
Barbieri L, Valbonesi P, Bonora E, Gorini P, Bolognesi A, Stirpe F. Polynucleotide:adenosine glycosidase activity of ribosome-inactivating proteins:effect on DNA, RNA and poly (A). Nucleic Acids Res.,1997,25(3):518-522.
Barbieri L, Polito L, Bolognesi A, Ciani M, Pelosi E, Farini V, Jha AK, Sharma N, Vivanco JM, Chambery A, Parente A, Stirpe F. Ribosome-inactivating proteins in edible plants and purification and characterization of a new ribosome-inactivating protein from Cucurbita moschata. Biochim Biophys Acta,2006,1760:783-792.
Barbieri L, Valbonesi P, Righi F, Zuccheri G, Monti F, Gorini P, Samori B, Stirpe F. Polynucleotide: adenosine glycosidase is the sole activity of ribosome-inactivating proteins on DNA. J. Biochem.,2000,128:883-889.
Basch E, Gabardi S, Ulbricht C. Bitter melon (Momordica charantia):a review of efficacy and safety. Am. J. Health-Syst. Ph.,2003,60(4):356-359.
Battelli MG, Vittoria Scicchitano V, Polito L, Farini V, Barbieri L, Andrea Bolognesi A. Binding and intracellular routing of the plant-toxic lectins, lanceolin and stenodacrylin. BBA-Gen. Subj.,2010,1800(12):1276-1282.
Begam M, Kumar S, Roy S, Campanella JJ, Kapoor HC. Molecular cloning and functional identification of a ribosome inactivating/antiviral protein from leaves of post-flowering stage of Celosia cristata and its expression in Escherichia coli. Phytochemistry,2006,67(22): 2441-2449.
Benson G. TENDEM REPEATS FINDER:a program to analyze DNA sequences. Nucleic Acids Res.,1999,27(2):573-580.
Bernado P, Modig K, Grela P, Svergun DI, Tchorzewski M, Pons M, Akke M. Structure and dynamics of ribosomal protein L12:an ensemble model based on SAXS and NMR relaxation. Biophys. J.,2010,98,2374-2382.
Bhaskar A, Deb U, Kumar O, Rao PVL. Abrin induced oxida-tive stress mediated DNA damage in human leukemic cells and its reversal by N-acetylcysteine. Toxicol. In Vitro,2008,22(8): 1902-1908.
Bieri S, Potrykus I, Fiitterer J. Expression of active barley seed ribosome-inactivating protein in transgenic wheat. Theor. Appl. Genet.,2000,100(5):755-763.
Brigotti M, Keith G, Pallanca A, Carnicelli D, Alvergna P. Identification of the tRNAs which up-regulate agrostin, barley RIP and PAP-S, three ribosome-inactivating proteins of plant origin. FEBS Lett.,1998,431(2):259-262.
Brigotti M, Alfieri R, Sestili P, Bonelli M, Petronini PG, Guidarelli A, Barbieri L, Stirpe F, Sperti S. Damage to nuclear DNA induced by Shiga toxin 1 and ricin in human endothelial cells. FASEB J.,2002,16:365-372.
Brookfield JFY. A simple new method for estimating null allelc frequency from heterozygote deficiency. Mol. Ecol.,1996,5:453-455.
Chan DSB, Chu LO, Lee KM, Too PHM, Ma KW, Sze KH, Zhu G, Shaw PC, Wong KB. Interaction between trichosanthin, a ribosome-inactivating protein, and the ribosomal stalk protein P2 by chemical shift perturbation and mutagenesis analyses. Nucleic Acids Res., 2007,35:1660-1672.
Chaudhry B, Muller-Uri F, Cameron-Mills V, Gough S, Simpson D, Skriver K, Mundy J. The barley 60 kDa jasmonate-induced protein (JIP60) is a novel ribosome-inactivating protein. Plant J.,2003,6(6):815-824.
Chiou JC, Li XP, Remacha M, Ballesta JPG, Tumer NE.2011. Shiga toxin 1 is more dependent on the P proteins of the ribosomal stalk for depurination activity than Shiga toxin 2. Int. J. Biochem. Cell. Biol.,2011,43:1792-1801.
Cho HJ, Lee SJ, Kim S, Kim BD. Isolation and characterization of cDNAs encoding ribosome inactivating protein from Dianthus sinensis L. Molecules and cells,2000,10(2):135-141.
Choudhary N, Kapoor HC, Lodha ML. Cloning and expression of antiviral/ribosome-inactivating protein from Bougainvillea xbuttiana. J. Biosciences,2008,33(1):91-101.
Chunyang Z, Hui M, Shuming N, Yao D, Lei J, Chen Dieyan C. Quantum dot-labeled trichosanthin. Analyst,2000,125(6):1029-1031.
Corrado G, Scarpettaa M, Aliotob D, Di Maroc A, Politod L, Parentee A, Raoa R. Inducible antiviral activity and rapid production of the Ribosome-Inactivating Protein I from Phytolacca heterotepala in tobacco. Plant Sci.,2008,174(4):467-474.
Dai J, Zhao L, Yang H, Guo H, Fan K, Wang H, Qian W, Zhang D, Li B, Wang H, Guo Y. Identification of a novel functional domain of ricin responsible for its potent toxicity. J. Biol. Chem.,2011,286:12166-12171.
Dai WD, Bonos S, Guo Z, Meyer WA, Day PR, Belanger FC. Expression of pokeweed antiviral proteins in creeping bentgrass. Plant Cell Rep.,2003,21:497-502.
De-la-Pena C, Badri DV, Vivanco JM. Novel role for pectin methylesterase in Arabidopsis:a new function showing ribosome-inactivating protein (RIP) activity. BBA-Gen. Subj.,2008, 1780(5):773-783.
Dey SS, Singh AK, Chandel D, Behera TK. Genetic diversity of bitter gourd (Momordica charantia L.) genotypes revealed by RAPD markers and agronomic traits. Sci. Hortic.,2006, 109:21-28.
Dhara K, Ratha J, Manassero M, Wang XY, Gao S, Banerjee P. Synthesis, crystal structure, magnetic property and oxidative DNA cleavage activity of an octanuclear copper (II) complex showing water-perchlorate helical network, J. Inorg. Biochem.,2007,101:95-103.
Diaconu M, Kothe U, Schlunzen F, Fischer N, Harms JM, Tonevitsky AG, Stark H, Rodnina MV, Wahl MC. Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activation. Cell,2005,121:991-1004.
Di Maro A, Chambery A, Carafa V, Costantini S, Colonna G, Parente A. Structural characterization and comparative modeling of PD-Ls 1-3, type 1 ribosome-inactivating proteins from summer leaves of Phytolacca dioica L. Biochimie,2009,91:352-363.
Endo Y, Wool IG. The site of action of alpha-sarcin on eukaryotic ribosomes. The sequence at the alpha-sarcin cleavage site in 28 S ribosomal ribonucleic acid. J. Biol. Chem.,1982, 257(15):9054-9060.
Endo Y, Tsurugi K.1988. The RNA N-glycosidase activity of ricin A-chain. The characteristics of the enzymatic activity of ricin A-chain with ribosomes and with rRNA. J. Biol. Chem.,1988, 263:8735-8739.
Endo Y, Tsurugi K, Franz H. The site of action of the A-chain of mist letoe lectin I on eukaryotic ribosomes:the RNA N-glycosidase activity of the protein. FEBS Lett,1988,231:378-380.
Excoffier L, Laval G, Schneider S. Arlequin (Version 3.01):An Integrated Software Package for Population Genetics Data Analysis. Computational and Molecular Population Genetics Lab (CMPG) Institute of Zoology University of Berne, Berne, Switzerland.2005.
Feng Z, Li WW, Yeung HW. Crystals of α-momorcharin:a new ribosome-inactivating protein. J. Mol. Biol.,1990,214(3):625-626.
Ferreras JM, Barbieri L, Girbes T, Battelli MG, Rojo MA, Arias FJ, Rocher MA, Soriano F, Mendez E, Stirpe F. Distribution and properties of major ribosome-inactivating proteins (28S rRNA N-glycosidases) of the plant Saponaria officinalis L. (Caryophyllaceae). Biochim Biophys Acta,1993,1216(1):31-42.
Fong WP, Mock WY, Ng TB. Intrinsic ribonuclease activities in ribonuclease and ribosome-inactivating proteins from the seeds of bitter gourd. Int. J. Biochem. Cell B.,2000, 32(5):571-577.
Gatehouse AMR, Barbieri L, Stirpe F, Croy RRD. Effects of ribosome inactivating proteins on insect development-differences between Lepidoptera and Coleoptera. Entomol. Exp. Appl., 1990,54(1):43-51.
Giansanti L, Di Leandro L, Koutris I, Cialfi A, Benedetti E, Laurenti G, Pitari G, Ippoliti R. Ricin and saporin:plant enzymes for the research and the clinics. Curr. Chem. Biol.,2010,4: 99-107.
Girbes T, Ferreras JM, Arias FJ, Stirpe F. Description, distribution, activity and phylogenetic relationship of ribosome-inactivating proteins in plants, fungi and bacteria. Mini-Rev. Med. Chem.,2004,4(5):461-476.
Grela P, Bernado P, Svergun D, Kwiatowski J, Abramczyk D, Grankowski N, Tchorzewski M. Structural relationships among the ribosomal stalk proteins from the three domains of life. J. Mol. Evol.,2008a,67:154-167.
Grela P, Sawa-Makarska J, Gordiyenko Y, Robinson CV, Grankowski N, Tchorzewski M. Structural properties of the human acidic ribosomal P proteins forming the P1-P2 heterocomplex. J. Biol. Chem.,2008b,143:169-177.
Grela P, Krokowski D, Gordiyenko Y, Krowarsch D, Robinson CV, Otlewski J, Grankowski N, Tchorzewski M.2010. Biophysical properties of the eukaryotic ribosomal stalk. Biochemistry,2010,49:924-933.
Grimmer S, Spilsberg B, Hanada K, Sandvig K. Depletion of sphingolipids facilitates endosome to golgi transport of ricin. Traffic,2006,7(9):1243-1253.
Hao Q, Peumans WJ, Van Damme EJ. Type-1 ribosome-inactivating protein from iris (Iris hollandica var. Professor Blaauw) binds specific genomic DNA fragments. Biochem. J., 2001,357(Pt 3):875-880.
Hartley MR, Lord JM. Cytotoxic ribosome-inactivating lectins from plants. BBA)-Proteins & Proteomics,2004,1701(1):1-14.
Hedblom ML, Cawley DB, Boguslawski S, Houston LL. Binding of ricin A chain to rat liver ribosomes:relationship to ribosome inactivation. J. Supramol. Struct.,1978,9:253-268.
Ho WKK, Liu SC, Shaw PC, Yeung HW, Ng TB, Chan WY. Cloning of the cDNA of a-momorcharin:a ribosome-inactivating protein. Biochim Biophys Acta,1991,1088(2): 311-314.
Honjo E, Watanabe K, Tsukamoto T. Real-time kinetic analyses of the interaction of ricin toxin A-chain with ribosomes prove a conformational change involved in complex formation. J. Biochem.,2002,131:267-275.
Hu K, Huang XF, Ke WD, Ding Y. Characterization of 11 new microsatellite loci in taro (Colocasia esculenta). Mol. Ecol. Resour.,2009,9(2):582-584.
Huang MX, Hou P, Wei Q, Xu Y, Chen F. A ribosome-inactivating protein (curcin 2) induced from Jatropha curcas can reduce viral and fungal infection in transgenic tobacco. Plant Growth Regul.,2008,54(2):115-123.
Iordanov, M.S., Pribnow, D., Magun, J.L., Dinh, T.H., Pearson, J.A., Chen, S.L., Magun, B.E., 1997. Ribotoxic stress response:activation of the stress-activated protein kinase JNK1 by inhibitors of the peptidyl transferase reaction and by sequence-speci fic RNA damage to the alpha-sarcin/ricin loop in the 28S rRNA. Mol. Cell. Biol.,1997,17:3373-3381.
Jiao YZ, Liu WY. Low-density lipoprotein receptor-related protein 1 is an essential receptor for trichosanthin in 2 choriocarcinoma cell lines. Biochem. Bioph. Res. Co.,2010,391(4): 1579-1584.
Kim JK, Jang IC, Wu R, Zuo WN, Boston RS, Lee YH. Co-expression of a modified maize ribosome-inactivating protein and a rice basic chitinase gene in transgenic rice plants confers enhanced resistance to sheath blight. Transgenic Res.,2003,12(4):475-484.
Kowalski M, Guindon J, Brazas L, Moore C, Entwistle J, Cizeau J, Jewet MA, Macdonald GC. A phase Ⅱ study of oportuzumab monatox:an immunotoxin therapy for patients with noninvasive urothelial carcinoma in situ previously treated with bacillus Calmette-Guerin. J. Urol.,2012,188:1712-1718.
Lee-Huang S, Huang PL, Sun Y, Chen HC, Kung HF, Huang PL, Murphy WJ. Inhibition of MDA-MB-231 human breast tumor xenografls and HER2 expression by anti-tumor agents GAP31 and MAP30. Anticancer Res.,2000,20:653-659.
Lee KM, Yu CWH, Chiu TYH, Sze KH, Shaw PC, Wong KB. Solution structure of the dimerization domain of the eukaryotic stalk P1/P2 complex reveals the structural organization of eukaryotic stalk complex. Nucleic Acids Res.,2012,40:3172-3182.
Li JJ, Geyer R, Tan W. Using molecular beacons as a sensitive fluorescence assay for enzymatic cleavage of single-stranded DNA, Nucleic. Acids Res.,2000,28:e52.
Li XP, Chiou JC, Remacha M, Ballesta JPG, Turner NE. A two-step binding model proposed for the electrostatic interactions of ricin a chain with ribosomes. Biochemistry,2009,48: 3853-3863.
Lindauer M, Wong J, Magun B.2010. Ricin toxin activates the NALP3 in flammasome. Toxins (Basel),2010,2:1500-1514.
Ling J, Liu W, Wang TP. Cleavage of supercoiled double-stranded DNA by several ribosome-inactivating proteins in vitro. FEBS Lett.,1994,345(2):143-146.
Ling J, Li XD, Wu X, Liu WY. Topological requirements for recognition and cleavage of DNA by ribosome-inactivating proteins. Biol. Chem. Hoppe Seyler,1995,376(11):637-641.
Liu H, Naismith J. An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol. BMC Biotechnol.,2008,8:91-100.
Liu R, Yang J, Liu WY. Isolation and enzymatic characterization of lamjapin, the first ribosome-inactivating protein from cryptogamic algal plant (Laminaria japonica A). European Journal of Biochemistry,2002,269(19):4746-4752.
Lodge JK, Kaniewski WK, Turner NE. Broad-spectrum virus resistance in transgenic plants expressing pokeweed antiviral protein. Proc. Natl. Acad. Sci.,1993,90:7089-7093.
Logemann J, Jach G, Tommerup H, Mundy J, Schell J. Expression of a barley ribosome-inactivating protein leads to increased fungal protection in transgenic tobacco plants. Nat. Biotechnol.,1992,10(3):305-308.
M Hamdi M, Chikh-Rouhou H, Boughalleb N, de Galarreta JIR. Ribosome Inactivating Protein of barley enhanced resistance to Rhizoctonia solani in transgenic potato cultivar 'Desiree'in greenhouse conditions. Biotechnol. Agron. Soc. Environ.,2013,17(1):20-26.
Massiah AJ, Hartley MR. Wheat ribosome-inactivating proteins:seed and leaf forms with different specificities and cofactor requirements. Planta,1995,197(4):633-640.
May KL, Li XP, Azorin FM, Ballesta J, Grela P, Tchorzewski M, Turner NE. The P1/P2 proteins of the human ribosomal stalk are required for ribosome binding and depurination by ricin in human cells. FEBS J.,2012,279:3925-3936.
McCluskey AJ, Bolewska-Pedyczak E, Jarvik N, Chen G, Sidhu SS, Gariepy J.2012. Charged and hydrophobic surfaces on the A chain of shiga-like toxin 1 recognize the C-terminal domain of ribosomal stalk proteins. PLoS ONE,2012,7:e31191.
McGrath MS, Hwang KM, Caldwell SE, Gaston I, Luk KC, Wu P, Ng VL, Crowe S, Daniels J, Marsh J, Deihart T, Lekas PU, Uennaari JC, Yeung HW, Lifson JF. GLQ223:an inhibitor of human immunodeficiency virus replication in acutely and chronically infected cells of lympho-cyte and mononuclear phagocyte lineage. Proc. Natl. Acad. Sci.,1989,86(8): 2844-2848.
Morais JKS, Gomes VM, Oliveira JTA, Santos IS, Da Cunha M, Oliveira HD, Oliveira HP, Sousa DOB, Vasconcelos IM. Soybean toxin (SBTX), a protein from soybeans that inhibits the life cycle of plant and human pathogenic fungi. J. Agric. Food Chem.,2010,58: 10356-10363.
Ng TB, Lam JSY, Wong JH, Lam SK, Ngai PHK, Wang HX, Chu KT, Chan WY. Differential abilities of the mushroom ribosome-inactivating proteins hypsin and velutin to perturb normal development of cultured mouse embryos. Toxicology in vitro,2010,24(4): 1250-1257.
Nielsen K, Boston RS. Ribosome-inactivating proteins:a plant perspective. Annu. Rev. Plant Biol., 2001,52(1):785-816.
Nielsen T, Thrane C, Christophersen C, Anthoni U, S(?)rensen J. Structure, production characteristics and fungal antagonism of tensin-a new antifungal cyclic lipopeptide from Pseudomonas fluorescens strain 96.578. J. Appl. Microbiol.,2000,89(6):992-1001.
Pan L, Xia Q, Quan Z, Liu H, Ke W, Ding Y. Development of novel EST-SSRs from sacred lotus (Nelumbo nucifera Gaertn) and their utilization for the genetic diversity analysis of N. nucifera. J. Hered.,2010,101(1):71-82.
Parente D, Raucci G, Celano B, Pacilli A, Zanoni L, Canevari S, Adobati E, Colnaghi MI, Dosio F, Arpicco S, Cattel L, Mele A, Santis RD. Clavin, a Type-1 Ribosome-Inactivating Protein from Aspergillus clavatus IF0 8605. European Journal of Biochemistry,1996,239(2): 272-280.
Parikh BA, Coetzer C, Tumer NE. Pokeweed antiviral protein regulates the stability of its own mRNA by a mechanism that requires depurination but can be separated from depurination of the a-sarcin/ricin loop of rRNA. J. Biol. Chem.,2002,277(44):41428-41437.
Park S, Stevens NM, Vivanco JM. Enzymatic specificity of three ribosome-inactivating proteins against fungal ribosomes, and correlation with antifungal activity. Planta,2002,216(2): 227-234.
Park SC, Kim JY, Lee JK, Hwang I, Cheong H, Nah JW, Hahm KS, Park Y. Antifungal mechanism of a novel antifungal pro-tein from pumpkin rinds against various fungal pathogens. J. Agric. Food Chem.,2009,57(19):9299-9304.
Park SW, Vepachedu R, Sharma N, Vivanco JM. Ribosome-inactivating proteins in plant biology. Planta,2004,219:1093-1096.
Pemberton JM, Slate J, Bancroft DR, Barrett JA. Nonamplifying alleles at microsatellite loci:a caution for parentage and population studies. Mol. Ecol.,1995,4(2):249-252.
Peumans WJ, Hao Q, van Damme EJM. Ribosome-inactivating proteins from plants:more than RNA N-glycosidases. FASEB J.,2001,15(9):1493-1506.
Pitipanapong J, Chitprasertb S, Gotoc M, Jiratchariyakuld W, Sasakic M, Shotipruka A. New approach for extraction of charantin from Momordica charantia with pressurized liquid extraction. Sep. Purif. Technol.,2007,52(3):416-422.
Puri M, Kaur I, Kanwar RK, Gupta RC, Chauhan A, Kanwar JR. Ribosome inactivating protein (RIPs) from Momordica charantia for antiviral therapy. Curr. Mol. Med.,2009,9(9): 1080-1094.
Puri M, Kaur I, Perugini MA, Gupta RC. Ribosome-inactivating proteins:current status and biomedical applications. Drug Discov. Today,2012,17(13-14):774-783.
Quan Z, Pan L, Ke WD, Ding Y. Polymorphic microsatellite markers in Euryale ferox Salisb.(Nymphaeaceae). Mol. Ecol. Resour.,2009,9(1):330-332.
Remi Shih NJ, McDonald KA, Dandekar AM, Girbes T, Iglesias R, Jackman AP. A novel type-1 ribosome-inactivating protein isolated from the supernatant of transformed suspension cultures of Trichosanthes kirilowii. Plant Cell Rep.,1998,17(6):531-537.
Reinbothe S, Reinbothe C, Lehmann J, Becker W, Apel K, Parthier B. JIP60, a methyl jasmonate-induced ribosome-inactivating protein involved in plant stress reactions. Proc. Natl. Acad. Sci.,1994,91(15):7012-7016.
Rice WR. Analyzing tables of statistical tests. Evolution,1989,43(1):223-225.
Robertus JD, Monzingo AF. The structure of ribosome inactivating proteins. Mini Rev. Med. Chem.,2004,4:477-486.
Sandvig K, van Deurs B. Entry of ricin and Shiga toxin into cells:molecular mechanisms and medical perspectives. EMBO J.,2000,19(22):5943-5950.
Selitrennikoff CP. Antifungal proteins. Appl. Environ. Microbiol.,2001,67(7):2883-2894.
Sha O, Kwong WH, Cho EYP, Yew DTW, Ng TB. Different neuronal toxicity of single-chain ribosome-inactivating proteins on the rat retina. Toxicon,2008,51(1):45-53.
Shahidi-Noghabi S, Van Damme EJM, Smagghe G. Expression of Sambucus nigra agglutinin (SNA-I') from elderberry bark in transgenic tobacco plants results in enhanced resistance to different insect species. Transgenic Res.,2009,18(2):249-259.
Sharma N, Park SW, Vepachedu R., Barbieri L, Ciani M, Stirpe F., Brett J., Savary BJ, Vivanco JM. Isolation and characterization of an RIP (ribosome-inactivating protein)-like protein from tobacco with dual enzymatic activity. Plant Physiol.,2004,134(1):171-181.
Sikriwal D, Batra JK. Ribosome inactivating proteins and apoptosis, in:JM. Lord, M.R. Hartley (Eds.), Toxic plant proteins, Heidelberg,2010, pp.167-189.
Stirpe F, Olsnes S, Pihl A. Gelonin, a new inhibitor of protein synthesis, nontoxic to intact cells. Isolation, characterization, and preparation of cytotoxic complexes with concanavalin A. J. Biol. Chem.,1980,255(14):6947-6953.
Stirpe F, Barbieri L, Battelli MG, Soria M, Lappi DA. Ribosome-Inactivating Proteins from Plants: Present Status and Future Prospects. Nat. Biotechnol.,1992,10(4):405-412.
Stirpe F, Barbieri L, Gorini P, Valbonesi P, Bolognesi A, Polito L. Activities associated with the presence of ribosome-inactivating proteins increase in senescent and stressed leaves. FEBS Lett.,1996,382(3):309-312.
Stirpe F. Ribosome-inactivating proteins. Toxicon,2004,44(4):371-383.
Stirpe F, Bolognesi A, Bortolotti M, Farini V, Lubelli C, Pelosi E, Polito L, Dozza B, Strocchi P, Chambery A, Parente A, Barbieri L. Characterization of highly toxic type 2 ribosome-inactivating proteins from Adenia lanceolata and Adenia stenodactyla (Passifloraceae). Toxicon,2007,50(1):94-105.
Stirpe F. Ribosome-inactivating proteins:from toxins to useful proteins. Toxicon,2013,67(1): 12-16.
Song SK, Choi Y, Moon YH, Kim SG, Choi YD, Lee JS. Systemic induction of a Phytolacca insularis antiviral protein gene by mechanical wounding, jasmonic acid, and abscisic acid. Plant Mol. Biol.,2000,43(4):439-450.
Too PH, Ma MK, Mak AN, Wong YT, Tung CK, Zhu G, Au SW, Wong KB, Shaw PC. The C-terminal fragment of the ribosomal P protein complexed to trichosanthin reveals the interaction between the ribosome-inactivating protein and the ribosome. Nucleic Acids Res., 2009,37:602-610.
Uma Maheswari PM, Palaniandavar M. DNA binding and cleavage properties of certain tetrammine ruthenium (Ⅱ) complexes of modified 1,10-phenanthrolines-effect of hydrogen- -bonding on DNA-binding affinity, J. Inorg. Biochem.,2004,98:219-230.
Van Ooseterhaut C, Hutchinson WF, Wills DPM, Shipley P. MICRO-CHECKER:software for identifying and correcting genotyping errors in microsatellite data. Mol. Ecol. Notes,2004,4: 535-538.
Virgilio M, Lombardi A, Caliandro R, Fabbrini MS. (2010) Ribosome-inactivating proteins:from plant defense to tumor attack. Toxins,2010,2(11):2699-2737.
Vivanco JM, Savary BJ, Flores HE. Characterization of Two Novel Type Ⅰ Ribosome-Inactivating Proteins from the Storage Roots of the Andean CropMirabilis expansa. Plant Physiol.,1999, 119(4):1447-1456.
Wang JH, Tam SC, Huang H, Ouyang DY, Wang YY, Zheng YT. Site-directed PEGylation of trichosanthin retained its anti-HIV activity with reduced potency in vitro. Biochem. Bioph. Res. Co.,2004,317(4):965-971.
Wang P, Turner NE. Pokeweed antiviral protein cleaves double-stranded supercoiled DNA using the same active site required to depurinate rRNA, Nucleic. Acids Res.,1999,27:1900-1905.
Wang SZ, Zhang YB, Liu HG, He Y, Yan JJ, Wu ZH, Ding Y. Molecular cloning and functional analysis of a recombinant ribosome-inactivating protein (alpha-momorcharm) from Momordica charantia. Appl. Microbiol. Biot.,2012,96(4):939-950.
Walsh TA, Morgan AE, Hey TD. Characterization and molecular cloning of a proenzyme form of a ribosome-inactivating protein from maize. Novel mechanism of proenzyme activation by proteolytic removal of a 2.8-kilodalton internal peptide segment. J. Biol. Chem.,1991, 266(34):23422-23427.
Walter R, Epperson BK.2001. Geographic pattern of genetic variation in Pinus resinosa:area of greatest diversity is not the origin of postglacial populations. Mol. Ecol.,2001,10:103-111.
Weber JL. Informativeness of human (dC-dA)-(dG-dT)n polymorphisms. Genomics,1990,7: 524-530.
Weber JL, May PE. Abundant class of human DNA polymorphisms which can be typed using the poly-merase chain reaction. Am. J. Hum. Genet.,1989,44:388-396.
Wong JH, Ng TB, Cheung RCF, Ye XJ, Wang HX, Lam SK, Lin P, Chan YS, Fang EF, Ngai PHK, Xia LX, Ye XY, Jiang Y, Liu F. Proteins with antifungal properties and other medicinal applications from plants and mushrooms. Appl. Microbiol. Biotechnol.,2010,87: 1-15.
Wu ZH, Wang SZ, Hu JH, Li F, Ke WD, Ding Y. Development and characterization of microsatellite markers for Sagittaria trifolia var. sinensis (Alismataceae). Am. J. Bot.,2011. 98(2):e36-e38.
Xu H, He WJ, Liu WY. A novel ribotoxin with ribonuclease activity that specifically cleaves a single phosphodiester bond in rat 28S ribosomal RNA and inactivates ribosome. Arch. Biochem. Biophys.,2004,427(1):30-40.
Yan Q, Li XP, Turner NE. N-glycosylation Does Not Affect the Catalytic Activity of Ricin A Chain but Stimulates Cytotoxicity by Promoting Its Transport Out of the Endoplasmic Reticulum. Traffic,2012,13(11):1508-1521.
Yeung HW, Li WW, Chan WY, Law LK, Ng TB. Alpha and beta momorcharins. International Journal of Peptide and Protein Research,1986,28(5):518-524.
Zarling JM, Moran PA, Haffar O, Sias J, Richman DD, Spina CA, Myers DE, Kuebelbeck V, Ledbetter JA, Uckun FM. Inhibition of HIV replication by pokeweed antiviral protein targeted to CD4+cells by monoclonal antibodies. Nature (London),1990,347:92-95.
Zheng J, Lei N, He Q, Hu W, Jin JG, Meng Y, Deng N, Meng YF, Zhang CJ, Shen F. PEGylation is effective in reducing immunogenicity, immunotoxicity, and hepatotoxicity of a-momorcharin in vivo. Immunopharm. Immunot.,2012,34(5):866-873.
Zhu F, Zhang P, Meng YF, Xu F, Zhang DW, Cheng J, Lin HH, Xi DH. Alpha-momorcharin, a RIP produced by bitter melon, enhances defense response in tobacco plants against diverse plant viruses and shows antifungal activity in vitro. Planta,2013,237(1):77-88.
Zhu G, Huang Q, Qian M, Tang Y. Crystal structure of a-momorcharin in 80% acetonitrile-water mixture. BBA-Protein Structure and Molecular Enzymology,2001,1548(1):152-158.
Zhu LN, Kong DM, Li XZ, Wang GY, Wang J, Jin YW. DNA cleavage activities of tetraazamacrocyclic oxamido nickel (II) complexes. Polyhedron,2010,29:574-580.
陈燕平,汪钟信,邓望喜.杀虫植物苦瓜的研究进展.湖北植保,2001,(6)：7-9.
程雪,胡进耀,苏智先.丝瓜核糖体失活蛋白的研究进展综述.西华师范大学学报,2004,25(2)：207-209.
褚嘉佑等,褚嘉佑,杨爱德,王辨明,胡忠,张和君,史良如,曲京华,罗兰英,郭仁.抗人T细胞单克隆抗体与商陆毒蛋白结合物的制备及其抗白血病细胞活性.细胞与分子免疫学杂志,1988,(3)：58.
傅明辉,田洁.苦瓜籽核糖体失活蛋白的分离纯化及抗氧化活性的研究.中国生化药物杂志,2002，3：134-136.
黄春萍,张宏,张晓喻.植物抗真菌蛋白的分类及抗菌机制研究进展.国外医药(抗生素分册),2007,(4)：167-171.
黄如葵,孙德利,张曼,方锋学,罗海玲.苦瓜遗传多样性的形态学性状聚类分析.广西农业科学,2008,(3)：351-356.
贾茗娴,尹惠琼,王跃华,章金刚。蓖麻毒素检测技术研究进展.生物技术通讯,2011,22(5)：747-750.
李建国.核糖体失活蛋白的研究进展.分子植物育种,2005,(4)：566-570.
李向东,刘望夷.核糖体失活蛋白的结构功能与分布.细胞生物学杂志,1997,19(2)：69-75.
林育泉,刘思,周鹏.新型抗病毒抗肿瘤苦瓜蛋白MAP30的研究进展.华南热带农业大学学报,2005,11(4)：24-29.
毛兴平.苦瓜AFLP分子标记反应体系的建立.广西热带农业,2010,(6)：9-14.
齐文波,徐中平,徐誉泰,宋剑秋,张英慧,王海仁.苦瓜素的分离纯化与抗肿瘤活性的研究.离子交换与吸附,1999,15(1)：59-63.
蘧艳峰,郭素堂,袁静明.细胞毒素Gelonin的结构功能及其在抗癌治疗中的应用前景.肿瘤研究与临床,2006,18(2)：139-140.
孙海燕,胡家恕,汪俏梅.苦瓜的核糖体失活蛋白.2004,26(3)：247-251.
孙亚卿,邵金旺,张少英.甜菜基因工程研究进展及其展望.中国农学通报,23(4)：27-32.
王庆华,于长春,徐誉泰,王海仁.α-苦瓜素和β-苦瓜素的研究进展.中草药,1995,26(5)：266-267.
王为,王长彪,刘方,陈浩东,王林,王春英,张香娣,王玉红,王坤波.棉花非冗余性EST-SSR新标记的开发及其评价.作物学报,2012,1443-1451.
王绪.苦瓜性别分化相关分子标记的研究.南宁：广西大学,2007.
徐振武,陈陵际.天花粉蛋白对人结肠癌SW—I116裸鼠的体内实验研究.浙江肿瘤,1997,3(2)：110-111.
杨洲平,黄乾明,刘一江,陈平.不同苦瓜品种MAP30基因的克隆及序列分析.四川农业大学学报,2007,25(1)：58-62.
袁燕,毛宇,黄晓麒,戴晓畅.核糖体失活蛋白研究新进展.天然产物研究与开发,2007,19(1)：169-174.
张君毅,郭巧生.磁珠富集法分离半夏微卫星序列.中国中药杂志,2009, 34(12)：1479-1482.
张智,孙素荣,马纪,张富春.植物中的核糖体失活蛋白及其抗病毒机制.植物生理学通讯,2005,41(4)：537-541.
Bagga S, Seth D, Batra JK. The cytotoxic activity of ribosome-inactivating protein saporin-6 is attributed to its rRNA N-glycosidase and internucleosomal DNA fragmentation activities. J. Biol. Chem.,2003,278:4813-4820.
Bai Y, Watt B, Wahome PG, Mantis NJ, Robertus JD. Identification of new classes of ricin toxin inhibitors by virtual screening. Toxicon,2010,56(4):526-534.
Balconi C, Lanzanova C, Conti E, Triulzi T, Forlani F, Cattaneo M, Lupotto E. Fusarium head blight evaluation in wheat transgenic plants expressing the maize b-32 antifungal gene. Eur. J. Plant Pathol.,2007,117(2):129-140.
Barbieri L, Ferreras JM, Barraco A, Ricci P, Stirpe F. Some ribosome-inactivating proteins depurinate ribosomal RNA at multiple sites. Biochem. J.,1992,286(Pt 1):1-4.
Barbieri L, Valbonesi P, Bonora E, Gorini P, Bolognesi A, Stirpe F. Polynucleotide:adenosine glycosidase activity of ribosome-inactivating proteins:effect on DNA, RNA and poly (A). Nucleic Acids Res.,1997,25(3):518-522.
Barbieri L, Polito L, Bolognesi A, Ciani M, Pelosi E, Farini V, Jha AK, Sharma N, Vivanco JM, Chambery A, Parente A, Stirpe F. Ribosome-inactivating proteins in edible plants and purification and characterization of a new ribosome-inactivating protein from Cucurbita moschata. Biochim Biophys Acta,2006,1760:783-792.
Barbieri L, Valbonesi P, Righi F, Zuccheri G, Monti F, Gorini P, Samori B, Stirpe F. Polynucleotide: adenosine glycosidase is the sole activity of ribosome-inactivating proteins on DNA. J. Biochem.,2000,128:883-889.
Basch E, Gabardi S, Ulbricht C. Bitter melon (Momordica charantia):a review of efficacy and safety. Am. J. Health-Syst. Ph.,2003,60(4):356-359.
Battelli MG, Vittoria Scicchitano V, Polito L, Farini V, Barbieri L, Andrea Bolognesi A. Binding and intracellular routing of the plant-toxic lectins, lanceolin and stenodacrylin. BBA-Gen. Subj.,2010,1800(12):1276-1282.
Begam M, Kumar S, Roy S, Campanella JJ, Kapoor HC. Molecular cloning and functional identification of a ribosome inactivating/antiviral protein from leaves of post-flowering stage of Celosia cristata and its expression in Escherichia coli. Phytochemistry,2006,67(22): 2441-2449.
Benson G. TENDEM REPEATS FINDER:a program to analyze DNA sequences. Nucleic Acids Res.,1999,27(2):573-580.
Bernado P, Modig K, Grela P, Svergun DI, Tchorzewski M, Pons M, Akke M. Structure and dynamics of ribosomal protein L12:an ensemble model based on SAXS and NMR relaxation. Biophys. J.,2010,98,2374-2382.
Bhaskar A, Deb U, Kumar O, Rao PVL. Abrin induced oxida-tive stress mediated DNA damage in human leukemic cells and its reversal by N-acetylcysteine. Toxicol. In Vitro,2008,22(8): 1902-1908.
Bieri S, Potrykus I, Fiitterer J. Expression of active barley seed ribosome-inactivating protein in transgenic wheat. Theor. Appl. Genet.,2000,100(5):755-763.
Brigotti M, Keith G, Pallanca A, Carnicelli D, Alvergna P. Identification of the tRNAs which up-regulate agrostin, barley RIP and PAP-S, three ribosome-inactivating proteins of plant origin. FEBS Lett.,1998,431(2):259-262.
Brigotti M, Alfieri R, Sestili P, Bonelli M, Petronini PG, Guidarelli A, Barbieri L, Stirpe F, Sperti S. Damage to nuclear DNA induced by Shiga toxin 1 and ricin in human endothelial cells. FASEB J.,2002,16:365-372.
Brookfield JFY. A simple new method for estimating null allelc frequency from heterozygote deficiency. Mol. Ecol.,1996,5:453-455.
Chan DSB, Chu LO, Lee KM, Too PHM, Ma KW, Sze KH, Zhu G, Shaw PC, Wong KB. Interaction between trichosanthin, a ribosome-inactivating protein, and the ribosomal stalk protein P2 by chemical shift perturbation and mutagenesis analyses. Nucleic Acids Res., 2007,35:1660-1672.
Chaudhry B, Muller-Uri F, Cameron-Mills V, Gough S, Simpson D, Skriver K, Mundy J. The barley 60 kDa jasmonate-induced protein (JIP60) is a novel ribosome-inactivating protein. Plant J.,2003,6(6):815-824.
Chiou JC, Li XP, Remacha M, Ballesta JPG, Tumer NE.2011. Shiga toxin 1 is more dependent on the P proteins of the ribosomal stalk for depurination activity than Shiga toxin 2. Int. J. Biochem. Cell. Biol.,2011,43:1792-1801.
Cho HJ, Lee SJ, Kim S, Kim BD. Isolation and characterization of cDNAs encoding ribosome inactivating protein from Dianthus sinensis L. Molecules and cells,2000,10(2):135-141.
Choudhary N, Kapoor HC, Lodha ML. Cloning and expression of antiviral/ribosome-inactivating protein from Bougainvillea xbuttiana. J. Biosciences,2008,33(1):91-101.
Chunyang Z, Hui M, Shuming N, Yao D, Lei J, Chen Dieyan C. Quantum dot-labeled trichosanthin. Analyst,2000,125(6):1029-1031.
Corrado G, Scarpettaa M, Aliotob D, Di Maroc A, Politod L, Parentee A, Raoa R. Inducible antiviral activity and rapid production of the Ribosome-Inactivating Protein I from Phytolacca heterotepala in tobacco. Plant Sci.,2008,174(4):467-474.
Dai J, Zhao L, Yang H, Guo H, Fan K, Wang H, Qian W, Zhang D, Li B, Wang H, Guo Y. Identification of a novel functional domain of ricin responsible for its potent toxicity. J. Biol. Chem.,2011,286:12166-12171.
Dai WD, Bonos S, Guo Z, Meyer WA, Day PR, Belanger FC. Expression of pokeweed antiviral proteins in creeping bentgrass. Plant Cell Rep.,2003,21:497-502.
De-la-Pena C, Badri DV, Vivanco JM. Novel role for pectin methylesterase in Arabidopsis:a new function showing ribosome-inactivating protein (RIP) activity. BBA-Gen. Subj.,2008, 1780(5):773-783.
Dey SS, Singh AK, Chandel D, Behera TK. Genetic diversity of bitter gourd (Momordica charantia L.) genotypes revealed by RAPD markers and agronomic traits. Sci. Hortic.,2006, 109:21-28.
Dhara K, Ratha J, Manassero M, Wang XY, Gao S, Banerjee P. Synthesis, crystal structure, magnetic property and oxidative DNA cleavage activity of an octanuclear copper (II) complex showing water-perchlorate helical network, J. Inorg. Biochem.,2007,101:95-103.
Diaconu M, Kothe U, Schlunzen F, Fischer N, Harms JM, Tonevitsky AG, Stark H, Rodnina MV, Wahl MC. Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activation. Cell,2005,121:991-1004.
Di Maro A, Chambery A, Carafa V, Costantini S, Colonna G, Parente A. Structural characterization and comparative modeling of PD-Ls 1-3, type 1 ribosome-inactivating proteins from summer leaves of Phytolacca dioica L. Biochimie,2009,91:352-363.
Endo Y, Wool IG. The site of action of alpha-sarcin on eukaryotic ribosomes. The sequence at the alpha-sarcin cleavage site in 28 S ribosomal ribonucleic acid. J. Biol. Chem.,1982, 257(15):9054-9060.
Endo Y, Tsurugi K.1988. The RNA N-glycosidase activity of ricin A-chain. The characteristics of the enzymatic activity of ricin A-chain with ribosomes and with rRNA. J. Biol. Chem.,1988, 263:8735-8739.
Endo Y, Tsurugi K, Franz H. The site of action of the A-chain of mist letoe lectin I on eukaryotic ribosomes:the RNA N-glycosidase activity of the protein. FEBS Lett,1988,231:378-380.
Excoffier L, Laval G, Schneider S. Arlequin (Version 3.01):An Integrated Software Package for Population Genetics Data Analysis. Computational and Molecular Population Genetics Lab (CMPG) Institute of Zoology University of Berne, Berne, Switzerland.2005.
Feng Z, Li WW, Yeung HW. Crystals of α-momorcharin:a new ribosome-inactivating protein. J. Mol. Biol.,1990,214(3):625-626.
Ferreras JM, Barbieri L, Girbes T, Battelli MG, Rojo MA, Arias FJ, Rocher MA, Soriano F, Mendez E, Stirpe F. Distribution and properties of major ribosome-inactivating proteins (28S rRNA N-glycosidases) of the plant Saponaria officinalis L. (Caryophyllaceae). Biochim Biophys Acta,1993,1216(1):31-42.
Fong WP, Mock WY, Ng TB. Intrinsic ribonuclease activities in ribonuclease and ribosome-inactivating proteins from the seeds of bitter gourd. Int. J. Biochem. Cell B.,2000, 32(5):571-577.
Gatehouse AMR, Barbieri L, Stirpe F, Croy RRD. Effects of ribosome inactivating proteins on insect development-differences between Lepidoptera and Coleoptera. Entomol. Exp. Appl., 1990,54(1):43-51.
Giansanti L, Di Leandro L, Koutris I, Cialfi A, Benedetti E, Laurenti G, Pitari G, Ippoliti R. Ricin and saporin:plant enzymes for the research and the clinics. Curr. Chem. Biol.,2010,4: 99-107.
Girbes T, Ferreras JM, Arias FJ, Stirpe F. Description, distribution, activity and phylogenetic relationship of ribosome-inactivating proteins in plants, fungi and bacteria. Mini-Rev. Med. Chem.,2004,4(5):461-476.
Grela P, Bernado P, Svergun D, Kwiatowski J, Abramczyk D, Grankowski N, Tchorzewski M. Structural relationships among the ribosomal stalk proteins from the three domains of life. J. Mol. Evol.,2008a,67:154-167.
Grela P, Sawa-Makarska J, Gordiyenko Y, Robinson CV, Grankowski N, Tchorzewski M. Structural properties of the human acidic ribosomal P proteins forming the P1-P2 heterocomplex. J. Biol. Chem.,2008b,143:169-177.
Grela P, Krokowski D, Gordiyenko Y, Krowarsch D, Robinson CV, Otlewski J, Grankowski N, Tchorzewski M.2010. Biophysical properties of the eukaryotic ribosomal stalk. Biochemistry,2010,49:924-933.
Grimmer S, Spilsberg B, Hanada K, Sandvig K. Depletion of sphingolipids facilitates endosome to golgi transport of ricin. Traffic,2006,7(9):1243-1253.
Hao Q, Peumans WJ, Van Damme EJ. Type-1 ribosome-inactivating protein from iris (Iris hollandica var. Professor Blaauw) binds specific genomic DNA fragments. Biochem. J., 2001,357(Pt 3):875-880.
Hartley MR, Lord JM. Cytotoxic ribosome-inactivating lectins from plants. BBA)-Proteins & Proteomics,2004,1701(1):1-14.
Hedblom ML, Cawley DB, Boguslawski S, Houston LL. Binding of ricin A chain to rat liver ribosomes:relationship to ribosome inactivation. J. Supramol. Struct.,1978,9:253-268.
Ho WKK, Liu SC, Shaw PC, Yeung HW, Ng TB, Chan WY. Cloning of the cDNA of a-momorcharin:a ribosome-inactivating protein. Biochim Biophys Acta,1991,1088(2): 311-314.
Honjo E, Watanabe K, Tsukamoto T. Real-time kinetic analyses of the interaction of ricin toxin A-chain with ribosomes prove a conformational change involved in complex formation. J. Biochem.,2002,131:267-275.
Hu K, Huang XF, Ke WD, Ding Y. Characterization of 11 new microsatellite loci in taro (Colocasia esculenta). Mol. Ecol. Resour.,2009,9(2):582-584.
Huang MX, Hou P, Wei Q, Xu Y, Chen F. A ribosome-inactivating protein (curcin 2) induced from Jatropha curcas can reduce viral and fungal infection in transgenic tobacco. Plant Growth Regul.,2008,54(2):115-123.
Iordanov, M.S., Pribnow, D., Magun, J.L., Dinh, T.H., Pearson, J.A., Chen, S.L., Magun, B.E., 1997. Ribotoxic stress response:activation of the stress-activated protein kinase JNK1 by inhibitors of the peptidyl transferase reaction and by sequence-speci fic RNA damage to the alpha-sarcin/ricin loop in the 28S rRNA. Mol. Cell. Biol.,1997,17:3373-3381.
Jiao YZ, Liu WY. Low-density lipoprotein receptor-related protein 1 is an essential receptor for trichosanthin in 2 choriocarcinoma cell lines. Biochem. Bioph. Res. Co.,2010,391(4): 1579-1584.
Kim JK, Jang IC, Wu R, Zuo WN, Boston RS, Lee YH. Co-expression of a modified maize ribosome-inactivating protein and a rice basic chitinase gene in transgenic rice plants confers enhanced resistance to sheath blight. Transgenic Res.,2003,12(4):475-484.
Kowalski M, Guindon J, Brazas L, Moore C, Entwistle J, Cizeau J, Jewet MA, Macdonald GC. A phase Ⅱ study of oportuzumab monatox:an immunotoxin therapy for patients with noninvasive urothelial carcinoma in situ previously treated with bacillus Calmette-Guerin. J. Urol.,2012,188:1712-1718.
Lee-Huang S, Huang PL, Sun Y, Chen HC, Kung HF, Huang PL, Murphy WJ. Inhibition of MDA-MB-231 human breast tumor xenografls and HER2 expression by anti-tumor agents GAP31 and MAP30. Anticancer Res.,2000,20:653-659.
Lee KM, Yu CWH, Chiu TYH, Sze KH, Shaw PC, Wong KB. Solution structure of the dimerization domain of the eukaryotic stalk P1/P2 complex reveals the structural organization of eukaryotic stalk complex. Nucleic Acids Res.,2012,40:3172-3182.
Li JJ, Geyer R, Tan W. Using molecular beacons as a sensitive fluorescence assay for enzymatic cleavage of single-stranded DNA, Nucleic. Acids Res.,2000,28:e52.
Li XP, Chiou JC, Remacha M, Ballesta JPG, Turner NE. A two-step binding model proposed for the electrostatic interactions of ricin a chain with ribosomes. Biochemistry,2009,48: 3853-3863.
Lindauer M, Wong J, Magun B.2010. Ricin toxin activates the NALP3 in flammasome. Toxins (Basel),2010,2:1500-1514.
Ling J, Liu W, Wang TP. Cleavage of supercoiled double-stranded DNA by several ribosome-inactivating proteins in vitro. FEBS Lett.,1994,345(2):143-146.
Ling J, Li XD, Wu X, Liu WY. Topological requirements for recognition and cleavage of DNA by ribosome-inactivating proteins. Biol. Chem. Hoppe Seyler,1995,376(11):637-641.
Liu H, Naismith J. An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol. BMC Biotechnol.,2008,8:91-100.
Liu R, Yang J, Liu WY. Isolation and enzymatic characterization of lamjapin, the first ribosome-inactivating protein from cryptogamic algal plant (Laminaria japonica A). European Journal of Biochemistry,2002,269(19):4746-4752.
Lodge JK, Kaniewski WK, Turner NE. Broad-spectrum virus resistance in transgenic plants expressing pokeweed antiviral protein. Proc. Natl. Acad. Sci.,1993,90:7089-7093.
Logemann J, Jach G, Tommerup H, Mundy J, Schell J. Expression of a barley ribosome-inactivating protein leads to increased fungal protection in transgenic tobacco plants. Nat. Biotechnol.,1992,10(3):305-308.
M Hamdi M, Chikh-Rouhou H, Boughalleb N, de Galarreta JIR. Ribosome Inactivating Protein of barley enhanced resistance to Rhizoctonia solani in transgenic potato cultivar 'Desiree'in greenhouse conditions. Biotechnol. Agron. Soc. Environ.,2013,17(1):20-26.
Massiah AJ, Hartley MR. Wheat ribosome-inactivating proteins:seed and leaf forms with different specificities and cofactor requirements. Planta,1995,197(4):633-640.
May KL, Li XP, Azorin FM, Ballesta J, Grela P, Tchorzewski M, Turner NE. The P1/P2 proteins of the human ribosomal stalk are required for ribosome binding and depurination by ricin in human cells. FEBS J.,2012,279:3925-3936.
McCluskey AJ, Bolewska-Pedyczak E, Jarvik N, Chen G, Sidhu SS, Gariepy J.2012. Charged and hydrophobic surfaces on the A chain of shiga-like toxin 1 recognize the C-terminal domain of ribosomal stalk proteins. PLoS ONE,2012,7:e31191.
McGrath MS, Hwang KM, Caldwell SE, Gaston I, Luk KC, Wu P, Ng VL, Crowe S, Daniels J, Marsh J, Deihart T, Lekas PU, Uennaari JC, Yeung HW, Lifson JF. GLQ223:an inhibitor of human immunodeficiency virus replication in acutely and chronically infected cells of lympho-cyte and mononuclear phagocyte lineage. Proc. Natl. Acad. Sci.,1989,86(8): 2844-2848.
Morais JKS, Gomes VM, Oliveira JTA, Santos IS, Da Cunha M, Oliveira HD, Oliveira HP, Sousa DOB, Vasconcelos IM. Soybean toxin (SBTX), a protein from soybeans that inhibits the life cycle of plant and human pathogenic fungi. J. Agric. Food Chem.,2010,58: 10356-10363.
Ng TB, Lam JSY, Wong JH, Lam SK, Ngai PHK, Wang HX, Chu KT, Chan WY. Differential abilities of the mushroom ribosome-inactivating proteins hypsin and velutin to perturb normal development of cultured mouse embryos. Toxicology in vitro,2010,24(4): 1250-1257.
Nielsen K, Boston RS. Ribosome-inactivating proteins:a plant perspective. Annu. Rev. Plant Biol., 2001,52(1):785-816.
Nielsen T, Thrane C, Christophersen C, Anthoni U, S(?)rensen J. Structure, production characteristics and fungal antagonism of tensin-a new antifungal cyclic lipopeptide from Pseudomonas fluorescens strain 96.578. J. Appl. Microbiol.,2000,89(6):992-1001.
Pan L, Xia Q, Quan Z, Liu H, Ke W, Ding Y. Development of novel EST-SSRs from sacred lotus (Nelumbo nucifera Gaertn) and their utilization for the genetic diversity analysis of N. nucifera. J. Hered.,2010,101(1):71-82.
Parente D, Raucci G, Celano B, Pacilli A, Zanoni L, Canevari S, Adobati E, Colnaghi MI, Dosio F, Arpicco S, Cattel L, Mele A, Santis RD. Clavin, a Type-1 Ribosome-Inactivating Protein from Aspergillus clavatus IF0 8605. European Journal of Biochemistry,1996,239(2): 272-280.
Parikh BA, Coetzer C, Tumer NE. Pokeweed antiviral protein regulates the stability of its own mRNA by a mechanism that requires depurination but can be separated from depurination of the a-sarcin/ricin loop of rRNA. J. Biol. Chem.,2002,277(44):41428-41437.
Park S, Stevens NM, Vivanco JM. Enzymatic specificity of three ribosome-inactivating proteins against fungal ribosomes, and correlation with antifungal activity. Planta,2002,216(2): 227-234.
Park SC, Kim JY, Lee JK, Hwang I, Cheong H, Nah JW, Hahm KS, Park Y. Antifungal mechanism of a novel antifungal pro-tein from pumpkin rinds against various fungal pathogens. J. Agric. Food Chem.,2009,57(19):9299-9304.
Park SW, Vepachedu R, Sharma N, Vivanco JM. Ribosome-inactivating proteins in plant biology. Planta,2004,219:1093-1096.
Pemberton JM, Slate J, Bancroft DR, Barrett JA. Nonamplifying alleles at microsatellite loci:a caution for parentage and population studies. Mol. Ecol.,1995,4(2):249-252.
Peumans WJ, Hao Q, van Damme EJM. Ribosome-inactivating proteins from plants:more than RNA N-glycosidases. FASEB J.,2001,15(9):1493-1506.
Pitipanapong J, Chitprasertb S, Gotoc M, Jiratchariyakuld W, Sasakic M, Shotipruka A. New approach for extraction of charantin from Momordica charantia with pressurized liquid extraction. Sep. Purif. Technol.,2007,52(3):416-422.
Puri M, Kaur I, Kanwar RK, Gupta RC, Chauhan A, Kanwar JR. Ribosome inactivating protein (RIPs) from Momordica charantia for antiviral therapy. Curr. Mol. Med.,2009,9(9): 1080-1094.
Puri M, Kaur I, Perugini MA, Gupta RC. Ribosome-inactivating proteins:current status and biomedical applications. Drug Discov. Today,2012,17(13-14):774-783.
Quan Z, Pan L, Ke WD, Ding Y. Polymorphic microsatellite markers in Euryale ferox Salisb.(Nymphaeaceae). Mol. Ecol. Resour.,2009,9(1):330-332.
Remi Shih NJ, McDonald KA, Dandekar AM, Girbes T, Iglesias R, Jackman AP. A novel type-1 ribosome-inactivating protein isolated from the supernatant of transformed suspension cultures of Trichosanthes kirilowii. Plant Cell Rep.,1998,17(6):531-537.
Reinbothe S, Reinbothe C, Lehmann J, Becker W, Apel K, Parthier B. JIP60, a methyl jasmonate-induced ribosome-inactivating protein involved in plant stress reactions. Proc. Natl. Acad. Sci.,1994,91(15):7012-7016.
Rice WR. Analyzing tables of statistical tests. Evolution,1989,43(1):223-225.
Robertus JD, Monzingo AF. The structure of ribosome inactivating proteins. Mini Rev. Med. Chem.,2004,4:477-486.
Sandvig K, van Deurs B. Entry of ricin and Shiga toxin into cells:molecular mechanisms and medical perspectives. EMBO J.,2000,19(22):5943-5950.
Selitrennikoff CP. Antifungal proteins. Appl. Environ. Microbiol.,2001,67(7):2883-2894.
Sha O, Kwong WH, Cho EYP, Yew DTW, Ng TB. Different neuronal toxicity of single-chain ribosome-inactivating proteins on the rat retina. Toxicon,2008,51(1):45-53.
Shahidi-Noghabi S, Van Damme EJM, Smagghe G. Expression of Sambucus nigra agglutinin (SNA-I') from elderberry bark in transgenic tobacco plants results in enhanced resistance to different insect species. Transgenic Res.,2009,18(2):249-259.
Sharma N, Park SW, Vepachedu R., Barbieri L, Ciani M, Stirpe F., Brett J., Savary BJ, Vivanco JM. Isolation and characterization of an RIP (ribosome-inactivating protein)-like protein from tobacco with dual enzymatic activity. Plant Physiol.,2004,134(1):171-181.
Sikriwal D, Batra JK. Ribosome inactivating proteins and apoptosis, in:JM. Lord, M.R. Hartley (Eds.), Toxic plant proteins, Heidelberg,2010, pp.167-189.
Stirpe F, Olsnes S, Pihl A. Gelonin, a new inhibitor of protein synthesis, nontoxic to intact cells. Isolation, characterization, and preparation of cytotoxic complexes with concanavalin A. J. Biol. Chem.,1980,255(14):6947-6953.
Stirpe F, Barbieri L, Battelli MG, Soria M, Lappi DA. Ribosome-Inactivating Proteins from Plants: Present Status and Future Prospects. Nat. Biotechnol.,1992,10(4):405-412.
Stirpe F, Barbieri L, Gorini P, Valbonesi P, Bolognesi A, Polito L. Activities associated with the presence of ribosome-inactivating proteins increase in senescent and stressed leaves. FEBS Lett.,1996,382(3):309-312.
Stirpe F. Ribosome-inactivating proteins. Toxicon,2004,44(4):371-383.
Stirpe F, Bolognesi A, Bortolotti M, Farini V, Lubelli C, Pelosi E, Polito L, Dozza B, Strocchi P, Chambery A, Parente A, Barbieri L. Characterization of highly toxic type 2 ribosome-inactivating proteins from Adenia lanceolata and Adenia stenodactyla (Passifloraceae). Toxicon,2007,50(1):94-105.
Stirpe F. Ribosome-inactivating proteins:from toxins to useful proteins. Toxicon,2013,67(1): 12-16.
Song SK, Choi Y, Moon YH, Kim SG, Choi YD, Lee JS. Systemic induction of a Phytolacca insularis antiviral protein gene by mechanical wounding, jasmonic acid, and abscisic acid. Plant Mol. Biol.,2000,43(4):439-450.
Too PH, Ma MK, Mak AN, Wong YT, Tung CK, Zhu G, Au SW, Wong KB, Shaw PC. The C-terminal fragment of the ribosomal P protein complexed to trichosanthin reveals the interaction between the ribosome-inactivating protein and the ribosome. Nucleic Acids Res., 2009,37:602-610.
Uma Maheswari PM, Palaniandavar M. DNA binding and cleavage properties of certain tetrammine ruthenium (Ⅱ) complexes of modified 1,10-phenanthrolines-effect of hydrogen- -bonding on DNA-binding affinity, J. Inorg. Biochem.,2004,98:219-230.
Van Ooseterhaut C, Hutchinson WF, Wills DPM, Shipley P. MICRO-CHECKER:software for identifying and correcting genotyping errors in microsatellite data. Mol. Ecol. Notes,2004,4: 535-538.
Virgilio M, Lombardi A, Caliandro R, Fabbrini MS. (2010) Ribosome-inactivating proteins:from plant defense to tumor attack. Toxins,2010,2(11):2699-2737.
Vivanco JM, Savary BJ, Flores HE. Characterization of Two Novel Type Ⅰ Ribosome-Inactivating Proteins from the Storage Roots of the Andean CropMirabilis expansa. Plant Physiol.,1999, 119(4):1447-1456.
Wang JH, Tam SC, Huang H, Ouyang DY, Wang YY, Zheng YT. Site-directed PEGylation of trichosanthin retained its anti-HIV activity with reduced potency in vitro. Biochem. Bioph. Res. Co.,2004,317(4):965-971.
Wang P, Turner NE. Pokeweed antiviral protein cleaves double-stranded supercoiled DNA using the same active site required to depurinate rRNA, Nucleic. Acids Res.,1999,27:1900-1905.
Wang SZ, Zhang YB, Liu HG, He Y, Yan JJ, Wu ZH, Ding Y. Molecular cloning and functional analysis of a recombinant ribosome-inactivating protein (alpha-momorcharm) from Momordica charantia. Appl. Microbiol. Biot.,2012,96(4):939-950.
Walsh TA, Morgan AE, Hey TD. Characterization and molecular cloning of a proenzyme form of a ribosome-inactivating protein from maize. Novel mechanism of proenzyme activation by proteolytic removal of a 2.8-kilodalton internal peptide segment. J. Biol. Chem.,1991, 266(34):23422-23427.
Walter R, Epperson BK.2001. Geographic pattern of genetic variation in Pinus resinosa:area of greatest diversity is not the origin of postglacial populations. Mol. Ecol.,2001,10:103-111.
Weber JL. Informativeness of human (dC-dA)-(dG-dT)n polymorphisms. Genomics,1990,7: 524-530.
Weber JL, May PE. Abundant class of human DNA polymorphisms which can be typed using the poly-merase chain reaction. Am. J. Hum. Genet.,1989,44:388-396.
Wong JH, Ng TB, Cheung RCF, Ye XJ, Wang HX, Lam SK, Lin P, Chan YS, Fang EF, Ngai PHK, Xia LX, Ye XY, Jiang Y, Liu F. Proteins with antifungal properties and other medicinal applications from plants and mushrooms. Appl. Microbiol. Biotechnol.,2010,87: 1-15.
Wu ZH, Wang SZ, Hu JH, Li F, Ke WD, Ding Y. Development and characterization of microsatellite markers for Sagittaria trifolia var. sinensis (Alismataceae). Am. J. Bot.,2011. 98(2):e36-e38.
Xu H, He WJ, Liu WY. A novel ribotoxin with ribonuclease activity that specifically cleaves a single phosphodiester bond in rat 28S ribosomal RNA and inactivates ribosome. Arch. Biochem. Biophys.,2004,427(1):30-40.
Yan Q, Li XP, Turner NE. N-glycosylation Does Not Affect the Catalytic Activity of Ricin A Chain but Stimulates Cytotoxicity by Promoting Its Transport Out of the Endoplasmic Reticulum. Traffic,2012,13(11):1508-1521.
Yeung HW, Li WW, Chan WY, Law LK, Ng TB. Alpha and beta momorcharins. International Journal of Peptide and Protein Research,1986,28(5):518-524.
Zarling JM, Moran PA, Haffar O, Sias J, Richman DD, Spina CA, Myers DE, Kuebelbeck V, Ledbetter JA, Uckun FM. Inhibition of HIV replication by pokeweed antiviral protein targeted to CD4+cells by monoclonal antibodies. Nature (London),1990,347:92-95.
Zheng J, Lei N, He Q, Hu W, Jin JG, Meng Y, Deng N, Meng YF, Zhang CJ, Shen F. PEGylation is effective in reducing immunogenicity, immunotoxicity, and hepatotoxicity of a-momorcharin in vivo. Immunopharm. Immunot.,2012,34(5):866-873.
Zhu F, Zhang P, Meng YF, Xu F, Zhang DW, Cheng J, Lin HH, Xi DH. Alpha-momorcharin, a RIP produced by bitter melon, enhances defense response in tobacco plants against diverse plant viruses and shows antifungal activity in vitro. Planta,2013,237(1):77-88.
Zhu G, Huang Q, Qian M, Tang Y. Crystal structure of a-momorcharin in 80% acetonitrile-water mixture. BBA-Protein Structure and Molecular Enzymology,2001,1548(1):152-158.
Zhu LN, Kong DM, Li XZ, Wang GY, Wang J, Jin YW. DNA cleavage activities of tetraazamacrocyclic oxamido nickel (II) complexes. Polyhedron,2010,29:574-580.