000 | 01844 a2200529 4500 | ||
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005 | 20250513220104.0 | ||
264 | 0 | _c20000907 | |
008 | 200009s 0 0 eng d | ||
022 | _a0036-8075 | ||
024 | 7 |
_a10.1126/science.289.5483.1317 _2doi |
|
040 |
_aNLM _beng _cNLM |
||
100 | 1 | _aSerio, T R | |
245 | 0 | 0 |
_aNucleated conformational conversion and the replication of conformational information by a prion determinant. _h[electronic resource] |
260 |
_bScience (New York, N.Y.) _cAug 2000 |
||
300 |
_a1317-21 p. _bdigital |
||
500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. | ||
650 | 0 | 4 |
_aAmyloid _xchemistry |
650 | 0 | 4 |
_aBiopolymers _xchemistry |
650 | 0 | 4 | _aCentrifugation, Density Gradient |
650 | 0 | 4 | _aCircular Dichroism |
650 | 0 | 4 | _aElectrophoresis, Polyacrylamide Gel |
650 | 0 | 4 |
_aEndopeptidases _xmetabolism |
650 | 0 | 4 |
_aFungal Proteins _xchemistry |
650 | 0 | 4 | _aKinetics |
650 | 0 | 4 | _aLight |
650 | 0 | 4 | _aMicelles |
650 | 0 | 4 | _aMicroscopy, Atomic Force |
650 | 0 | 4 | _aMicroscopy, Electron |
650 | 0 | 4 | _aModels, Chemical |
650 | 0 | 4 | _aPeptide Termination Factors |
650 | 0 | 4 |
_aPrions _xchemistry |
650 | 0 | 4 | _aProtein Conformation |
650 | 0 | 4 | _aProtein Folding |
650 | 0 | 4 | _aSaccharomyces cerevisiae Proteins |
650 | 0 | 4 | _aScattering, Radiation |
650 | 0 | 4 | _aSolubility |
650 | 0 | 4 | _aSonication |
700 | 1 | _aCashikar, A G | |
700 | 1 | _aKowal, A S | |
700 | 1 | _aSawicki, G J | |
700 | 1 | _aMoslehi, J J | |
700 | 1 | _aSerpell, L | |
700 | 1 | _aArnsdorf, M F | |
700 | 1 | _aLindquist, S L | |
773 | 0 |
_tScience (New York, N.Y.) _gvol. 289 _gno. 5483 _gp. 1317-21 |
|
856 | 4 | 0 |
_uhttps://doi.org/10.1126/science.289.5483.1317 _zAvailable from publisher's website |
999 |
_c10906360 _d10906360 |