生物谷報道:朊病毒,,有人認為該稱為蛋白感染子,因為它是一種蛋白質(zhì),,但卻具有自身復制能力,,并可以將正常蛋白變成異常的蛋白,具有病毒相似的特征,,因此成為研究熱點,。以前認為朊病毒是引發(fā)瘋牛病的主要蛋白,后來在正常的的神經(jīng)系統(tǒng)內(nèi)也發(fā)現(xiàn)了它,,而近年研究又發(fā)現(xiàn)它與神經(jīng)細胞的生長和凋亡有關(guān),,下邊附有生物谷以前的相關(guān)報道。而且發(fā)現(xiàn)在低等的生物,,如酵母中也有存在類似朊病毒行為的蛋白,,這似乎表現(xiàn)朊病毒無處不在,包括極低等的生物中,。今天剛剛出版的Nature上,,以及近來發(fā)表現(xiàn)PNAS等刊物上有許多相關(guān)的研究。生物谷將最新的文獻收集整理,,供大家分享,。
Supattapone S.Prion protein conversion in vitro.
J Mol Med. 2004 Mar 10
|Full text(html)|
DeMarco ML, Daggett V.From conversion to aggregation: protofibril formation of the prion protein.
Proc Natl Acad Sci U S A. 2004 Feb 24;101(8):2293-8.
|Full text(html)|PDF
Scheibel T, Bloom J, Lindquist SL.The elongation of yeast prion fibers involves separable steps of association and conversion.
Proc Natl Acad Sci U S A. 2004 Feb 24;101(8):2287-92.
|Full text(html)| PDF
Goodman L.Assessing risk is the business of prion disease research.
J Clin Invest. 2004 Feb;113(4):494.
|Full text(html)| PDF
DeMarco ML, Daggett V.From conversion to aggregation: Protofibril formation of the prion protein.Proc Natl Acad Sci U S A. 2004 Feb 13
PDF
Favereaux A, Perret-Liaudet A, Vital A.Extraneural pathologic prion protein.
N Engl J Med. 2004 Feb 12;350(7):732-3;
|Full text(html)| PDF
Apetri AC, Surewicz KA, Surewicz WK.The effect ofdisease-associated mutations on the folding pathway of human prion protein.
J Biol Chem. 2004 Feb 2 PDF
Protein-only transmission of three yeast prion strains
CHIH-YEN KING & RUBEN DIAZ-AVALOS
Nature 428, 319–323 (2004); doi:10.1038/nature02391
| First Paragraph | Full Text (HTML / PDF) |
Conformational variations in an infectious protein determine prion strain differences
MOTOMASA TANAKA, PETER CHIEN, NARIMAN NABER, ROGER COOKE & JONATHAN S. WEISSMAN
Nature 428, 323–328 (2004); doi:10.1038/nature02392
| First Paragraph | Full Text (HTML / PDF) |
Cell biology: The strain of being a prion
MICK F. TUITE
Prions are remarkable infectious agents associated with certain brain diseases. But they also occur in fungi, experiments with which now provide plausible answers to some critical questions about prion biology.
Nature 428, 265–267 (2004); doi:10.1038/428265a
| Full Text (HTML / PDF) |