参考文献/References:
[1] Flom G,Behal R H,Rosen L,等.Sti1二聚体形成序列以及与Hsp70和Hsp90作用的序列[J].生物化学杂志,2007,404(1):159-167.(英文版)
[2] Gaiser A M,Brandt F,Richter K.从线虫分离的非典型Hop 蛋白具有与Hsc70或Hsp90形成复合体的作用[J].分子生物学杂志,2009,391(3):621-634.(英文版)
[3] Prodromou C,Siligardi G,O’Brien R,等.含有TPR 结构域的共分子伴侣蛋白具有调节Hsp90 ATPase 活性的功能[J].欧洲分子生物学协会杂志,1999,18(3):754-762.(英文版)
[4] Richter K,Muschler P,Hainzl O,等.Sti1是Hsp90 ATPase功能的非竞争性抑制剂,在ATP酶循环中二者结合可阻止Hsp90的N-端的二聚体化[J].生物化学杂志,2003,278(12):10328-10333.(英文版)
[5] Hessling M,Richter K,Buchner J.ATP诱导分子伴侣蛋白Hsp90结构循环变化的剖析[J].天然结构与分子生物学,2009,16(3):287-293.(英文版)
[6] Chang H C,Nathan D F,Lindquist S.Hsp90共伴侣蛋白Sti1(p60)在体内的作用[J].分子和细胞生物学,1997,17(1):318-325.(英文版).
[7] Ran F,Bali M,Michels C A.通过非诱导的组成型等位基因突变确定Hsp90/Hsp70分子伴侣机器调节酵母MAL基因激活因子[J].遗传学,2008,179(1):331-343.(英文版)
[8] Johnson B D,Schumacher R J,Ross E D,等.Hop在蛋白折叠时调节Hsp70与Hsp90的作用[J].生物化学杂志,1998,273(6):3679-3686.(英文版)
[9] Wegele H,Wandinger S K,Schmid A B,等.受调节蛋白从分子伴侣Hsp70转移到Hsp90[J].分子生物学杂志,2006,356(3):802-811.(英文版)
[10] Mir S S,Fiedler D,Cashikar A G.Ssd1是酵母耐热蛋白Hsp104是酵母蛋白降解过程中的调节蛋白[J].分子和细胞生物学,2009,29(1):187-200.(英文版)
[11] Hernández T J,Papandreou N,Chomilier J.序列分析显示两端带内含子的 TPR-DP单元可能源于真核蛋白Hop和Hip的TPR-DP结构域以及原核蛋白GerD[J].细胞胁迫和分子伴侣,2009,14(3):281-289.(英文版).
[12] 刘士德,李明华,张建华,等.多头绒泡菌14-3-3蛋白激活酵母Gal4蛋白调节的基因与其二聚体结合结构域及磷酸化位点有关[J].微生物学文献集,2009,192(1):33-40.(英文版)
[13] 欧阳秋玲,刘士德,张建华,等.采用酵母双杂交法筛选PSRPK相关蛋白基因[J].深圳大学学报理工版,2006,23(3):222-229.
[14] Shai Shaham.细胞生物学方法[M].纽约:学术出版社,2005:9-41.(英文版)
[15] Brychzy A,Rein T,Winklhofer K F,等.连接2个TPR和1个J结构域的共伴侣因子Tpr2调节Hsp70/Hsp90 分子伴侣系统[J].欧洲分子生物学协会杂志,2003,22(14):3613-3623.(英文版)
[16] LIN Jiu-sheng,Wilson M A.含有一个非典型34肽重复序列的大肠杆菌硫氧还蛋白类似蛋白YbbN是Groel负调控因子.生物化学杂志,2011,286(22):19459-19469.(英文版)
[17] Krukenberg K A,Frster F,Rice L M,等.大肠杆菌Hsp90在溶液中展现多种构像:透视Hsp90的构像动力学[J].结构,2008,16(5):755-765.(英文版)
[18] Ingmer H,Brndsted L.蛋白酶在细菌病理中的作用[J].微生物学研究,2009,160(9):704-710.(英文版)
[19] Switala J,O’Neil J O,Loewen P C.大肠杆菌过氧化氢酶HPII具有提高抗变性的功能[J].生物化学,1999,38(13):3895-3901.(英文版)
[20] Anand A,Duk B T,Singh S,等.氧化还原反应调节VHb(透明颤菌血红蛋白)与抗氧化蛋白的作用:氧胁迫下VHb生物合成调节的新发现[J].生物化学杂志,2010,426(3):271-280.(英文版)
[1] Flom G,Behal R H,Rosen L,et al.Definition of the minimal fragments of Sti1 required for dimerization,interaction with Hsp70 and Hsp90 and in vivo functions[J].The Biochemical Journal,2007,404(1):159-167.
[2] Gaiser A M,Brandt F,Richter K.The non-canonical Hop protein from Caenorhabditis elegans exerts essential functions and forms binary complexes with either Hsc70 or Hsp90[J].Journal of Molecular Biology,2009,391(3):621-634.
[3] Prodromou C,Siligardi G,O’Brien R,et al.Regulation of Hsp90 ATPase activity by tetratricopeptide repeat(TPR)-domain co-chaperones[J].European Molecular Biology Organization Journal,1999,18(3):754-762.
[4] Richter K,Muschler P,Hainzl O,et al.Sti1 is a non-competitive inhibitor of the Hsp90 ATPase.Binding prevents the N-terminal dimerization reaction during the atpase cycle[J].The Journal of Biological Chemistry,2003,278(12):10328-10333.
[5] Hessling M,Richter K,Buchner J.Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90[J].Nature Structural and Molecular Biology,2009,16(3):287-293.
[6] Chang H C,Nathan D F,Lindquist S.In vivo analysis of the Hsp90 cochaperone Sti1(p60)[J].Molecular and Cellular Biology,1997,17(1):318-325.
[7] Ran F,Bali M,Michels C A.Hsp90/Hsp70 chaperone machine regulation of the Saccharomyces MAL-activator as determined in vivo using noninducible and constitutive mutant alleles[J].Genetics,2008,179(1):331-343.
[8] Johnson B D,Schumacher R J,Ross E D,et al.Hop modulates Hsp70/Hsp90 interactions in protein folding[J].The Journal of Biological Chemistry,1998,273(6):3679-3686.
[9] Wegele H,Wandinger S K,Schmid A B,et al.Substrate transfer from the chaperone Hsp70 to Hsp90[J].Journal of Molecular Biology,2006,356(3):802-811.
[10] Mir S S,Fiedler D,Cashikar A G.Ssd1 is required for thermotolerance and Hsp104-mediated protein disaggregation in Saccharomyces cerevisiae[J].Molecular and Cellular Biology,2009,29(1):187-200.
[11] Hernández T J,Papandreou N,Chomilier J.Sequence analyses reveal that a TPR-DP module,surrounded by recombinable flanking introns,could be at the origin of eukaryotic Hop and Hip TPR-DP domains and prokaryotic GerD proteins[J].Cell Stress and Chaperones,2009,14(3):281-289.
[12] LIU Shi-de,LI Ming-hua,ZHANG Jian-hua,et al.Activation of the transcription of Gal4-regulated genes by Physarum 14-3-3 in yeast is related to dimer-binding motif-2 and three phosphorylation sites[J].Archives of Microbiology,2009,192(1):33-40
[13] OUYANG Qiu-ling,LIU Shi-de,ZHANG Jian-hua,et al.Screening of the PSRPK-related protein genes with yeast two-hybrid method[J].Journal of Shenzhen University Science and Engineering,2006,23(3):222-229.(in Chinese)
[14] Shai Shaham.Methods in Cell Biology[M].New York:Academic Press,2005:9-41.
[15] Brychzy A,Rein T,Winklhofer K F,et al.Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system[J].European Molecular Biology Organization Journal,2003,22(14):3613-3623.
[16] LIN Jiu-sheng,Wilson M A.Escherichia coli thioredoxin -like protein YbbN contain an atypical tetratricopeptide repeat motif and is a negative regulator of Groel[J].The Journal of Biological Chemistry,2011,286(22):19459-19469.
[17] Krukenberg K A,Frster F,Rice L M,et al.Multiple conformations of E.coli Hsp90 in solution:insights into the conformational dynamics of Hsp90[J].Structure,2008,16(5):755-765.
[18] Ingmer H,Brndsted L.Proteases in bacterial pathogenesis[J].Research in Microbiology,2009,160(9):704-710.
[19] Switala J,O’Neil J O,Loewen P C.Catalase HPII from Escherichia coli exhibits enhanced resistance to denaturation[J].Biochemistry,1999,38(13):3895-3901.
[20] Anand A,Duk B T,Singh S,et al.Redox-mediated interactions of VHb(Vitreoscilla haemoglobin) with OxyR:novel regulation of VHb biosynthesis under oxidative stress[J].The Biochemical Journal,2010,426(3):271-280.
相似文献/References:
[1]张建华,刘士德,刑苗.多头绒泡菌G2期cDNA表达文库的构建[J].深圳大学学报理工版,2005,22(1):50.
ZHANG Jian-hua,LIU Shi-de,and XING Miao.Construction of a cDNA expression library of Physarum polycephalum at G2phase[J].Journal of Shenzhen University Science and Engineering,2005,22(No.4(283-376)):50.