| 000 | 01463 a2200409 4500 | ||
|---|---|---|---|
| 005 | 20250513161904.0 | ||
| 264 | 0 | _c19990305 | |
| 008 | 199903s 0 0 eng d | ||
| 022 | _a0014-2956 | ||
| 024 | 7 |
_a10.1046/j.1432-1327.1999.00053.x _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aFouchaq, B | |
| 245 | 0 | 0 |
_aOligomerization of the 17-kDa peptide-binding domain of the molecular chaperone HSC70. _h[electronic resource] |
| 260 |
_bEuropean journal of biochemistry _cJan 1999 |
||
| 300 |
_a379-84 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 |
_aAdenosine Triphosphatases _xanalysis |
| 650 | 0 | 4 |
_aApoproteins _xpharmacology |
| 650 | 0 | 4 | _aBinding Sites |
| 650 | 0 | 4 |
_aCarrier Proteins _xgenetics |
| 650 | 0 | 4 | _aChromatography, Gel |
| 650 | 0 | 4 |
_aCytochrome c Group _xpharmacology |
| 650 | 0 | 4 | _aCytochromes c |
| 650 | 0 | 4 | _aHSC70 Heat-Shock Proteins |
| 650 | 0 | 4 |
_aHSP70 Heat-Shock Proteins _xgenetics |
| 650 | 0 | 4 | _aModels, Theoretical |
| 650 | 0 | 4 | _aMutation |
| 650 | 0 | 4 |
_aPeptide Fragments _xgenetics |
| 650 | 0 | 4 | _aProtein Binding |
| 650 | 0 | 4 | _aProtein Structure, Secondary |
| 650 | 0 | 4 | _aUltracentrifugation |
| 700 | 1 | _aBenaroudj, N | |
| 700 | 1 | _aEbel, C | |
| 700 | 1 | _aLadjimi, M M | |
| 773 | 0 |
_tEuropean journal of biochemistry _gvol. 259 _gno. 1-2 _gp. 379-84 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1046/j.1432-1327.1999.00053.x _zAvailable from publisher's website |
| 999 |
_c9876252 _d9876252 |
||