| 000 | 01631 a2200445 4500 | ||
|---|---|---|---|
| 005 | 20250515025755.0 | ||
| 264 | 0 | _c20060726 | |
| 008 | 200607s 0 0 eng d | ||
| 022 | _a0027-8424 | ||
| 024 | 7 |
_a10.1073/pnas.0600195103 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aKubota, Susumu | |
| 245 | 0 | 0 |
_aCytosolic chaperonin protects folding intermediates of Gbeta from aggregation by recognizing hydrophobic beta-strands. _h[electronic resource] |
| 260 |
_bProceedings of the National Academy of Sciences of the United States of America _cMay 2006 |
||
| 300 |
_a8360-5 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article | ||
| 650 | 0 | 4 |
_aActins _xmetabolism |
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 | _aAnimals |
| 650 | 0 | 4 | _aCattle |
| 650 | 0 | 4 |
_aChaperonin 60 _xmetabolism |
| 650 | 0 | 4 | _aChaperonin Containing TCP-1 |
| 650 | 0 | 4 |
_aChaperonins _xchemistry |
| 650 | 0 | 4 |
_aGTP-Binding Proteins _xmetabolism |
| 650 | 0 | 4 | _aHumans |
| 650 | 0 | 4 | _aHydrophobic and Hydrophilic Interactions |
| 650 | 0 | 4 | _aMale |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 | _aProtein Binding |
| 650 | 0 | 4 | _aProtein Folding |
| 650 | 0 | 4 | _aProtein Structure, Secondary |
| 650 | 0 | 4 | _aProtein Structure, Tertiary |
| 650 | 0 | 4 |
_aProtein Subunits _xmetabolism |
| 650 | 0 | 4 | _aSequence Alignment |
| 700 | 1 | _aKubota, Hiroshi | |
| 700 | 1 | _aNagata, Kazuhiro | |
| 773 | 0 |
_tProceedings of the National Academy of Sciences of the United States of America _gvol. 103 _gno. 22 _gp. 8360-5 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1073/pnas.0600195103 _zAvailable from publisher's website |
| 999 |
_c16315984 _d16315984 |
||