000 | 01982 a2200529 4500 | ||
---|---|---|---|
005 | 20250516074139.0 | ||
264 | 0 | _c20120611 | |
008 | 201206s 0 0 eng d | ||
022 | _a1932-6203 | ||
024 | 7 |
_a10.1371/journal.pone.0030257 _2doi |
|
040 |
_aNLM _beng _cNLM |
||
100 | 1 | _aNagaraj, Ram H | |
245 | 0 | 0 |
_aHydroimidazolone modification of the conserved Arg12 in small heat shock proteins: studies on the structure and chaperone function using mutant mimics. _h[electronic resource] |
260 |
_bPloS one _c2012 |
||
300 |
_ae30257 p. _bdigital |
||
500 | _aPublication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't | ||
650 | 0 | 4 | _aAmino Acid Sequence |
650 | 0 | 4 |
_aArginine _xchemistry |
650 | 0 | 4 |
_aBinding Sites _xgenetics |
650 | 0 | 4 | _aCircular Dichroism |
650 | 0 | 4 | _aElectrophoresis, Polyacrylamide Gel |
650 | 0 | 4 |
_aHSP27 Heat-Shock Proteins _xchemistry |
650 | 0 | 4 |
_aImidazoles _xchemistry |
650 | 0 | 4 | _aKinetics |
650 | 0 | 4 |
_aMolecular Chaperones _xchemistry |
650 | 0 | 4 | _aMolecular Sequence Data |
650 | 0 | 4 | _aMolecular Structure |
650 | 0 | 4 | _aMutation |
650 | 0 | 4 |
_aProtein Binding _xdrug effects |
650 | 0 | 4 |
_aProtein Structure, Secondary _xdrug effects |
650 | 0 | 4 |
_aProtein Structure, Tertiary _xdrug effects |
650 | 0 | 4 |
_aPyruvaldehyde _xpharmacology |
650 | 0 | 4 |
_aRecombinant Proteins _xchemistry |
650 | 0 | 4 | _aSequence Homology, Amino Acid |
650 | 0 | 4 | _aSpectrometry, Fluorescence |
650 | 0 | 4 | _aThermodynamics |
650 | 0 | 4 |
_aalpha-Crystallin A Chain _xchemistry |
650 | 0 | 4 |
_aalpha-Crystallin B Chain _xchemistry |
700 | 1 | _aPanda, Alok Kumar | |
700 | 1 | _aShanthakumar, Shilpa | |
700 | 1 | _aSanthoshkumar, Puttur | |
700 | 1 | _aPasupuleti, NagaRekha | |
700 | 1 | _aWang, Benlian | |
700 | 1 | _aBiswas, Ashis | |
773 | 0 |
_tPloS one _gvol. 7 _gno. 1 _gp. e30257 |
|
856 | 4 | 0 |
_uhttps://doi.org/10.1371/journal.pone.0030257 _zAvailable from publisher's website |
999 |
_c21486553 _d21486553 |