| 000 | 01893 a2200529 4500 | ||
|---|---|---|---|
| 005 | 20250518041954.0 | ||
| 264 | 0 | _c20200427 | |
| 008 | 202004s 0 0 eng d | ||
| 022 | _a1878-4186 | ||
| 024 | 7 |
_a10.1016/j.str.2019.04.009 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aPrajapati, Sabin | |
| 245 | 0 | 0 |
_aStructural and Functional Analyses of the Human PDH Complex Suggest a "Division-of-Labor" Mechanism by Local E1 and E3 Clusters. _h[electronic resource] |
| 260 |
_bStructure (London, England : 1993) _c07 2019 |
||
| 300 |
_a1124-1136.e4 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 |
_aAcetyl Coenzyme A _xchemistry |
| 650 | 0 | 4 | _aCatalytic Domain |
| 650 | 0 | 4 | _aCloning, Molecular |
| 650 | 0 | 4 |
_aCoenzyme A _xchemistry |
| 650 | 0 | 4 | _aCryoelectron Microscopy |
| 650 | 0 | 4 |
_aEscherichia coli _xgenetics |
| 650 | 0 | 4 | _aGene Expression |
| 650 | 0 | 4 |
_aGenetic Vectors _xchemistry |
| 650 | 0 | 4 | _aHumans |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 | _aProtein Binding |
| 650 | 0 | 4 | _aProtein Conformation, alpha-Helical |
| 650 | 0 | 4 | _aProtein Conformation, beta-Strand |
| 650 | 0 | 4 | _aProtein Interaction Domains and Motifs |
| 650 | 0 | 4 | _aProtein Multimerization |
| 650 | 0 | 4 |
_aProtein Subunits _xchemistry |
| 650 | 0 | 4 |
_aPyruvate Dehydrogenase Complex _xchemistry |
| 650 | 0 | 4 |
_aRecombinant Proteins _xchemistry |
| 650 | 0 | 4 | _aSubstrate Specificity |
| 650 | 0 | 4 | _aThermodynamics |
| 700 | 1 | _aHaselbach, David | |
| 700 | 1 | _aWittig, Sabine | |
| 700 | 1 | _aPatel, Mulchand S | |
| 700 | 1 | _aChari, Ashwin | |
| 700 | 1 | _aSchmidt, Carla | |
| 700 | 1 | _aStark, Holger | |
| 700 | 1 | _aTittmann, Kai | |
| 773 | 0 |
_tStructure (London, England : 1993) _gvol. 27 _gno. 7 _gp. 1124-1136.e4 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1016/j.str.2019.04.009 _zAvailable from publisher's website |
| 999 |
_c29731256 _d29731256 |
||