| 000 | 01452 a2200397 4500 | ||
|---|---|---|---|
| 005 | 20250518031551.0 | ||
| 264 | 0 | _c20201019 | |
| 008 | 202010s 0 0 eng d | ||
| 022 | _a2045-2322 | ||
| 024 | 7 |
_a10.1038/s41598-019-41060-0 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aQuintana-Gallardo, Lucía | |
| 245 | 0 | 0 |
_aThe cochaperone CHIP marks Hsp70- and Hsp90-bound substrates for degradation through a very flexible mechanism. _h[electronic resource] |
| 260 |
_bScientific reports _c03 2019 |
||
| 300 |
_a5102 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 | _aChromatography, Gel |
| 650 | 0 | 4 | _aChromatography, Liquid |
| 650 | 0 | 4 | _aCryoelectron Microscopy |
| 650 | 0 | 4 |
_aHSP70 Heat-Shock Proteins _xmetabolism |
| 650 | 0 | 4 |
_aHSP90 Heat-Shock Proteins _xmetabolism |
| 650 | 0 | 4 | _aHumans |
| 650 | 0 | 4 | _aMass Spectrometry |
| 650 | 0 | 4 | _aMicroscopy, Electron, Transmission |
| 650 | 0 | 4 |
_aMolecular Chaperones _xmetabolism |
| 650 | 0 | 4 | _aProtein Folding |
| 650 | 0 | 4 | _aTandem Mass Spectrometry |
| 650 | 0 | 4 |
_aUbiquitination _xgenetics |
| 700 | 1 | _aMartín-Benito, Jaime | |
| 700 | 1 | _aMarcilla, Miguel | |
| 700 | 1 | _aEspadas, Guadalupe | |
| 700 | 1 | _aSabidó, Eduard | |
| 700 | 1 | _aValpuesta, José María | |
| 773 | 0 |
_tScientific reports _gvol. 9 _gno. 1 _gp. 5102 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1038/s41598-019-41060-0 _zAvailable from publisher's website |
| 999 |
_c29516257 _d29516257 |
||