000 | 01949 a2200565 4500 | ||
---|---|---|---|
005 | 20250517040407.0 | ||
264 | 0 | _c20150814 | |
008 | 201508s 0 0 rus d | ||
022 | _a0026-8984 | ||
024 | 7 |
_a10.7868/S0026898415020068 _2doi |
|
040 |
_aNLM _beng _cNLM |
||
100 | 1 | _aKhmeleva, S A | |
245 | 0 | 0 |
_a[Effect of mutations and modifications of amino acid residues on zinc-induced interaction of the metal-binding domain of β-amyloid with DNA]. _h[electronic resource] |
260 |
_bMolekuliarnaia biologiia _c |
||
300 |
_a507-14 p. _bdigital |
||
500 | _aPublication Type: English Abstract; Journal Article; Research Support, Non-U.S. Gov't | ||
650 | 0 | 4 | _aAmino Acid Substitution |
650 | 0 | 4 |
_aAmyloid beta-Peptides _xchemical synthesis |
650 | 0 | 4 |
_aArginine _xchemistry |
650 | 0 | 4 |
_aAsparagine _xchemistry |
650 | 0 | 4 |
_aAspartic Acid _xchemistry |
650 | 0 | 4 | _aBinding Sites |
650 | 0 | 4 | _aBiosensing Techniques |
650 | 0 | 4 | _aCations, Divalent |
650 | 0 | 4 |
_aCoordination Complexes _xchemistry |
650 | 0 | 4 |
_aDNA _xchemical synthesis |
650 | 0 | 4 |
_aDNA, Single-Stranded _xchemical synthesis |
650 | 0 | 4 |
_aHistidine _xchemistry |
650 | 0 | 4 | _aHumans |
650 | 0 | 4 |
_aPeptide Fragments _xchemical synthesis |
650 | 0 | 4 | _aPhosphorylation |
650 | 0 | 4 | _aProtein Binding |
650 | 0 | 4 | _aProtein Multimerization |
650 | 0 | 4 |
_aSerine _xchemistry |
650 | 0 | 4 | _aSolutions |
650 | 0 | 4 | _aStructure-Activity Relationship |
650 | 0 | 4 | _aSurface Plasmon Resonance |
650 | 0 | 4 | _aToxicity Tests |
650 | 0 | 4 |
_aZinc _xchemistry |
700 | 1 | _aMezentsev, Y V | |
700 | 1 | _aKozin, S A | |
700 | 1 | _aMitkevich, V A | |
700 | 1 | _aMedvedev, A E | |
700 | 1 | _aIvanov, A S | |
700 | 1 | _aBodoev, N V | |
700 | 1 | _aMakarov, A A | |
700 | 1 | _aRadko, S P | |
773 | 0 |
_tMolekuliarnaia biologiia _gvol. 49 _gno. 3 _gp. 507-14 |
|
856 | 4 | 0 |
_uhttps://doi.org/10.7868/S0026898415020068 _zAvailable from publisher's website |
999 |
_c25013788 _d25013788 |