000 | 01981 a2200589 4500 | ||
---|---|---|---|
005 | 20250515053753.0 | ||
264 | 0 | _c20070611 | |
008 | 200706s 0 0 eng d | ||
022 | _a1357-2725 | ||
024 | 7 |
_a10.1016/j.biocel.2006.11.006 _2doi |
|
040 |
_aNLM _beng _cNLM |
||
100 | 1 | _aNicoll, W S | |
245 | 0 | 0 |
_aCytosolic and ER J-domains of mammalian and parasitic origin can functionally interact with DnaK. _h[electronic resource] |
260 |
_bThe international journal of biochemistry & cell biology _c2007 |
||
300 |
_a736-51 p. _bdigital |
||
500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
650 | 0 | 4 | _aAmino Acid Sequence |
650 | 0 | 4 | _aAmino Acid Substitution |
650 | 0 | 4 | _aAnimals |
650 | 0 | 4 | _aBase Sequence |
650 | 0 | 4 | _aBinding Sites |
650 | 0 | 4 |
_aCytosol _xmetabolism |
650 | 0 | 4 |
_aEndoplasmic Reticulum _xmetabolism |
650 | 0 | 4 |
_aEscherichia coli _xgenetics |
650 | 0 | 4 |
_aEscherichia coli Proteins _xchemistry |
650 | 0 | 4 | _aGenetic Complementation Test |
650 | 0 | 4 |
_aHSP40 Heat-Shock Proteins _xgenetics |
650 | 0 | 4 |
_aHSP70 Heat-Shock Proteins _xchemistry |
650 | 0 | 4 | _aHumans |
650 | 0 | 4 | _aMice |
650 | 0 | 4 | _aMolecular Sequence Data |
650 | 0 | 4 | _aMutation |
650 | 0 | 4 |
_aNeoplasm Proteins _xgenetics |
650 | 0 | 4 | _aPhylogeny |
650 | 0 | 4 | _aProtein Binding |
650 | 0 | 4 | _aProtein Structure, Tertiary |
650 | 0 | 4 |
_aProtozoan Proteins _xgenetics |
650 | 0 | 4 | _aSequence Homology, Amino Acid |
650 | 0 | 4 | _aTemperature |
700 | 1 | _aBotha, M | |
700 | 1 | _aMcNamara, C | |
700 | 1 | _aSchlange, M | |
700 | 1 | _aPesce, E-R | |
700 | 1 | _aBoshoff, A | |
700 | 1 | _aLudewig, M H | |
700 | 1 | _aZimmermann, R | |
700 | 1 | _aCheetham, M E | |
700 | 1 | _aChapple, J P | |
700 | 1 | _aBlatch, G L | |
773 | 0 |
_tThe international journal of biochemistry & cell biology _gvol. 39 _gno. 4 _gp. 736-51 |
|
856 | 4 | 0 |
_uhttps://doi.org/10.1016/j.biocel.2006.11.006 _zAvailable from publisher's website |
999 |
_c16803098 _d16803098 |