000 | 01618 a2200433 4500 | ||
---|---|---|---|
005 | 20250513200220.0 | ||
264 | 0 | _c19991230 | |
008 | 199912s 0 0 eng d | ||
022 | _a1084-9521 | ||
024 | 7 |
_a10.1006/scdb.1999.0320 _2doi |
|
040 |
_aNLM _beng _cNLM |
||
100 | 1 | _aArgon, Y | |
245 | 0 | 0 |
_aGRP94, an ER chaperone with protein and peptide binding properties. _h[electronic resource] |
260 |
_bSeminars in cell & developmental biology _cOct 1999 |
||
300 |
_a495-505 p. _bdigital |
||
500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.; Review | ||
650 | 0 | 4 |
_aAdenosine Triphosphate _xmetabolism |
650 | 0 | 4 | _aAmino Acid Sequence |
650 | 0 | 4 | _aAnimals |
650 | 0 | 4 | _aAntigen Presentation |
650 | 0 | 4 |
_aCalcium _xmetabolism |
650 | 0 | 4 |
_aCancer Vaccines _xchemistry |
650 | 0 | 4 |
_aEndoplasmic Reticulum _xmetabolism |
650 | 0 | 4 | _aGene Expression Regulation |
650 | 0 | 4 |
_aHSP70 Heat-Shock Proteins _xchemistry |
650 | 0 | 4 |
_aHSP90 Heat-Shock Proteins _xchemistry |
650 | 0 | 4 |
_aMembrane Proteins _xchemistry |
650 | 0 | 4 | _aMice |
650 | 0 | 4 |
_aMolecular Chaperones _xchemistry |
650 | 0 | 4 | _aMolecular Sequence Data |
650 | 0 | 4 |
_aPeptides _xmetabolism |
650 | 0 | 4 | _aProtein Binding |
650 | 0 | 4 | _aProtein Folding |
650 | 0 | 4 | _aProtein Processing, Post-Translational |
650 | 0 | 4 | _aSequence Homology, Amino Acid |
700 | 1 | _aSimen, B B | |
773 | 0 |
_tSeminars in cell & developmental biology _gvol. 10 _gno. 5 _gp. 495-505 |
|
856 | 4 | 0 |
_uhttps://doi.org/10.1006/scdb.1999.0320 _zAvailable from publisher's website |
999 |
_c10553705 _d10553705 |