| scholarly article | Q13442814 |
| P2093 | author name string | Linda L Randall | |
| Simon J S Hardy | |||
| Yuying Suo | |||
| P2860 | cites work | Direct identification of the site of binding on the chaperone SecB for the amino terminus of the translocon motor SecA. | Q42739776 |
| Sites of interaction between SecA and the chaperone SecB, two proteins involved in export | Q43095210 | ||
| Asymmetric binding between SecA and SecB two symmetric proteins: implications for function in export. | Q52563568 | ||
| Conformational changes of the chaperone SecB upon binding to a model substrate--bovine pancreatic trypsin inhibitor (BPTI). | Q54354833 | ||
| Mutations of the molecular chaperone protein SecB which alter the interaction between SecB and maltose-binding protein. | Q54663164 | ||
| Mapping of the docking of SecA onto the chaperone SecB by site-directed spin labeling: insight into the mechanism of ligand transfer during protein export | Q81230421 | ||
| Crystal structure of the bacterial protein export chaperone secB | Q27628763 | ||
| Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA | Q27639672 | ||
| Structural determinants of SecB recognition by SecA in bacterial protein translocation | Q27642253 | ||
| SecA, the motor of the secretion machine, binds diverse partners on one interactive surface | Q30485740 | ||
| Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labeling | Q30496200 | ||
| Orientation of SecA and SecB in complex, derived from disulfide cross-linking | Q30497880 | ||
| Direct demonstration that homotetrameric chaperone SecB undergoes a dynamic dimer-tetramer equilibrium | Q31664450 | ||
| Dimeric SecA couples the preprotein translocation in an asymmetric manner | Q33815223 | ||
| Identification and interpretation of complexity in sedimentation velocity boundaries | Q33915169 | ||
| Calorimetric analyses of the interaction between SecB and its ligands | Q36280993 | ||
| Complex behavior in solution of homodimeric SecA. | Q36639172 | ||
| Stoichiometry of SecYEG in the active translocase of Escherichia coli varies with precursor species | Q37031742 | ||
| Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands | Q41866614 | ||
| Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export | Q41904736 | ||
| Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by SecB requires two protomers of SecA | Q42078600 | ||
| P433 | issue | 4 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 887-900 | |
| P577 | publication date | 2014-12-19 | |
| P1433 | published in | Journal of Molecular Biology | Q925779 |
| P1476 | title | The basis of asymmetry in the SecA:SecB complex | |
| P478 | volume | 427 |
| Q57056828 | Co-assembly of SecYEG and SecA fully restores the properties of the native translocon |
| Q36942421 | Conserved SecA Signal Peptide-Binding Site Revealed by Engineered Protein Chimeras and Förster Resonance Energy Transfer |
| Q47286801 | Penetration into Membrane of Amino-terminal Region of SecA when Associated with SecYEG in Active Complexes |
| Q39021695 | Protein export through the bacterial Sec pathway. |
| Q50307534 | SecA functions in vivo as a discrete anti-parallel dimer to promote protein transport |
| Q47374398 | The Sec System: Protein Export in Escherichia coli |
| Q48149538 | secA, secD, secF, yajC, and yidC contribute to the adhesion regulation of Vibrio alginolyticus |
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