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1、生物化工专业翻译1.AbstractAmyloiddisorderscausedebilitatingillnessesthroughtheformationoftoxicproteinaggregates.Themechanismsofamyloidtoxicityandthenatureofspeciesresponsibleformediatingcellulardysfunctionremainunclear.Here,usingp2-microglobulin(
2、32m)asamodelsystem,weshowthatthedisruptiono
3、fmembranesbyamyloidfibrilsiscausedbythemolecularsheddingofmembrane・activeoligomersinaprocessthatisdependentonpH.UsingthioflavinT(ThT)fluorescenee,NMR,EMandfluoresceneecorrelationspectroscopy(FCS),weshowthatfibrildisassemblyatpH6.4resultsintheformationofnormativesphericaloligomersth
4、atdisruptsyntheticmembranes.Bycontrast,fibrildissociationatpH7.4resultsintheformationofnontoxic,nativemonomers•Chemicalcross-linkingorinteractionwithhsp70increasesthekineticstabilityoffibrilsanddecreasestheircapacitytocausemembranedisruptionandcellulardysfunction.Theresultsdemonstr
5、atehowpHcanmodulatethedeleteriouseffectsofpreformedamyloidaggregatesandsuggestwhyendocytictraffickingthroughacidiccompartmentsmaybeakeyfactorinamyloiddisease.抽象淀粉样蛋白疾病引起通过毒性蛋白聚集体的形成衰弱的疾病。淀粉样蛋白的毒性的机制，负责调解细胞功能障碍品种的性质仍然不清楚。在这里，用B2微球蛋白(P2M),其为模型系统，我们表明，膜的由淀粉样蛋白原纤维的破坏是通过膜-活性低聚物的分子屮脱落的处理
6、是依赖于pH值而引起的。使用硫磺素T(ThT的)荧光,NMREM和荧光相关光谱(FCS),我们表明，原纤维的拆卸，在pH6.4的结果屮的非天然寡聚球形扰乱合成膜的形成。相比Z下，原纤维解离，在pH7.4的结果在无毒，天然单体的形成。化学交联或相互作用与HSP70增加纤维的动力学稳定性，并降低它们的容量以使膜破坏和细胞功能障碍。结果表明如何pH值可以调节预形成的淀粉样蛋白聚集体的有害作用，并说明为什么通过酸性隔室的内吞贩卖可以是在淀粉样蛋白病的关键因素。2.AbstractDuringthelastdecade,severalpiecesofconvincin
7、gevideneewerepublishedindicatingthatagingoflivingorganismsisprogrammed,beingaparticularcaseofprogrammeddeathoforganism(phenoptosis).Amongthem,thefollowingobservationscanbementioned[1].Speciesweredescribedthatshownegligibleaging.Inmammals,thenakedmoleratisthemostimpressiveexample・Th
8、isisarodentofmousesizelivingatleast10-foldIongerthanamouseandhavingfecundityhigherthanamouseandnoage-relateddiseases[2].Insomespecieswithhighagingrate,genesresponsibleforactiveorganizationofagingbypoisoningoftheorganismwithendogenousmetaboliteshavebeenidentified[3].Inwomen,standard
9、deviationsdividedbythemean
