000 | 01939 a2200565 4500 | ||
---|---|---|---|
005 | 20250513204341.0 | ||
264 | 0 | _c20000403 | |
008 | 200004s 0 0 eng d | ||
022 | _a0092-8674 | ||
024 | 7 |
_a10.1016/s0092-8674(00)80692-3 _2doi |
|
040 |
_aNLM _beng _cNLM |
||
100 | 1 | _aFarr, G W | |
245 | 0 | 0 |
_aMultivalent binding of nonnative substrate proteins by the chaperonin GroEL. _h[electronic resource] |
260 |
_bCell _cMar 2000 |
||
300 |
_a561-73 p. _bdigital |
||
500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. | ||
650 | 0 | 4 |
_aAdenosine Triphosphate _xmetabolism |
650 | 0 | 4 | _aAnimals |
650 | 0 | 4 |
_aBacterial Proteins _xchemistry |
650 | 0 | 4 | _aBinding Sites |
650 | 0 | 4 | _aCattle |
650 | 0 | 4 |
_aChaperonin 10 _xchemistry |
650 | 0 | 4 |
_aChaperonin 60 _xchemistry |
650 | 0 | 4 | _aChemical Phenomena |
650 | 0 | 4 | _aChemistry, Physical |
650 | 0 | 4 | _aCryoelectron Microscopy |
650 | 0 | 4 |
_aCystine _xphysiology |
650 | 0 | 4 |
_aEscherichia coli _xmetabolism |
650 | 0 | 4 |
_aEthylmaleimide _xpharmacology |
650 | 0 | 4 | _aImage Processing, Computer-Assisted |
650 | 0 | 4 | _aMacromolecular Substances |
650 | 0 | 4 |
_aMalate Dehydrogenase _xchemistry |
650 | 0 | 4 | _aModels, Molecular |
650 | 0 | 4 |
_aPeptides _xchemistry |
650 | 0 | 4 | _aProtein Binding |
650 | 0 | 4 | _aProtein Conformation |
650 | 0 | 4 | _aProtein Folding |
650 | 0 | 4 | _aProtein Structure, Tertiary |
650 | 0 | 4 |
_aRibulose-Bisphosphate Carboxylase _xchemistry |
650 | 0 | 4 | _aStructure-Activity Relationship |
650 | 0 | 4 |
_aThiosulfate Sulfurtransferase _xchemistry |
700 | 1 | _aFurtak, K | |
700 | 1 | _aRowland, M B | |
700 | 1 | _aRanson, N A | |
700 | 1 | _aSaibil, H R | |
700 | 1 | _aKirchhausen, T | |
700 | 1 | _aHorwich, A L | |
773 | 0 |
_tCell _gvol. 100 _gno. 5 _gp. 561-73 |
|
856 | 4 | 0 |
_uhttps://doi.org/10.1016/s0092-8674(00)80692-3 _zAvailable from publisher's website |
999 |
_c10675822 _d10675822 |