| 000 | 01675 a2200481 4500 | ||
|---|---|---|---|
| 005 | 20250513182617.0 | ||
| 264 | 0 | _c19990520 | |
| 008 | 199905s 0 0 eng d | ||
| 022 | _a0092-8674 | ||
| 024 | 7 |
_a10.1016/s0092-8674(00)80743-6 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aSpiess, C | |
| 245 | 0 | 0 |
_aA temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. _h[electronic resource] |
| 260 |
_bCell _cApr 1999 |
||
| 300 |
_a339-47 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 |
_aAmylases _xchemistry |
| 650 | 0 | 4 |
_aBacterial Proteins _xchemistry |
| 650 | 0 | 4 |
_aChaperonins _xmetabolism |
| 650 | 0 | 4 | _aDNA Primers |
| 650 | 0 | 4 |
_aEndopeptidases _xmetabolism |
| 650 | 0 | 4 |
_aEscherichia coli _xchemistry |
| 650 | 0 | 4 | _aEscherichia coli Proteins |
| 650 | 0 | 4 | _aGene Deletion |
| 650 | 0 | 4 | _aGene Expression Regulation, Bacterial |
| 650 | 0 | 4 | _aGene Expression Regulation, Enzymologic |
| 650 | 0 | 4 | _aHeat-Shock Proteins |
| 650 | 0 | 4 | _aIn Vitro Techniques |
| 650 | 0 | 4 | _aLac Operon |
| 650 | 0 | 4 |
_aMutation _xphysiology |
| 650 | 0 | 4 | _aPeriplasmic Proteins |
| 650 | 0 | 4 |
_aProtein Disulfide-Isomerases _xgenetics |
| 650 | 0 | 4 | _aProtein Folding |
| 650 | 0 | 4 |
_aSerine Endopeptidases _xchemistry |
| 650 | 0 | 4 | _aSubstrate Specificity |
| 650 | 0 | 4 | _aTemperature |
| 650 | 0 | 4 |
_aTranscription, Genetic _xphysiology |
| 650 | 0 | 4 |
_aalpha-Amylases _xmetabolism |
| 700 | 1 | _aBeil, A | |
| 700 | 1 | _aEhrmann, M | |
| 773 | 0 |
_tCell _gvol. 97 _gno. 3 _gp. 339-47 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1016/s0092-8674(00)80743-6 _zAvailable from publisher's website |
| 999 |
_c10278709 _d10278709 |
||