| scholarly article | Q13442814 |
| P2093 | author name string | Priya Bariya | |
| Linda L Randall | |||
| P2860 | cites work | SecB: a chaperone from Escherichia coli | Q74420415 |
| SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocation | Q24596484 | ||
| X-ray structure of a protein-conducting channel | Q27642744 | ||
| Structural Basis for Signal-Sequence Recognition by the Translocase Motor SecA as Determined by NMR | Q27649095 | ||
| Conformational transition of Sec machinery inferred from bacterial SecYE structures | Q27652527 | ||
| Structure and function of a membrane component SecDF that enhances protein export | Q27667802 | ||
| Structural basis for the antifolding activity of a molecular chaperone | Q27726706 | ||
| Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels | Q29547813 | ||
| Folding of β-barrel membrane proteins in lipid bilayers - Unassisted and assisted folding and insertion | Q30152928 | ||
| The soluble, periplasmic domain of OmpA folds as an independent unit and displays chaperone activity by reducing the self-association propensity of the unfolded OmpA transmembrane β-barrel | Q30155509 | ||
| Folding and assembly of beta-barrel membrane proteins | Q30160417 | ||
| 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 | ||
| SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli | Q33562047 | ||
| A novel membrane protein involved in protein translocation across the cytoplasmic membrane of Escherichia coli. | Q34058655 | ||
| Escherichia coli SecB protein associates with exported protein precursors in vivo | Q34290053 | ||
| SecB, one small chaperone in the complex milieu of the cell | Q35021874 | ||
| The basis of asymmetry in the SecA:SecB complex | Q35207949 | ||
| Export of periplasmic galactose-binding protein in Escherichia coli depends on the chaperone SecB. | Q35582444 | ||
| Role of the leader peptide of maltose-binding protein in two steps of the export process | Q36224664 | ||
| Determination of the binding frame within a physiological ligand for the chaperone SecB. | Q36278522 | ||
| Determination of the binding frame of the chaperone SecB within the physiological ligand oligopeptide-binding protein | Q36280530 | ||
| The interaction between the chaperone SecB and its ligands: evidence for multiple subsites for binding | Q36280717 | ||
| Calorimetric analyses of the interaction between SecB and its ligands | Q36280993 | ||
| Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY. | Q36321596 | ||
| Evidence for specificity at an early step in protein export in Escherichia coli | Q36361933 | ||
| Stoichiometry of SecYEG in the active translocase of Escherichia coli varies with precursor species | Q37031742 | ||
| Membrane protein insertion and proton-motive-force-dependent secretion through the bacterial holo-translocon SecYEG-SecDF-YajC-YidC. | Q37687646 | ||
| SecB protein: a cytosolic export factor that associates with nascent exported proteins | Q37949462 | ||
| Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase | Q38314889 | ||
| SecD is involved in the release of translocated secretory proteins from the cytoplasmic membrane of Escherichia coli | Q38322783 | ||
| The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein | Q38347439 | ||
| Multicopy suppression of cold-sensitive sec mutations in Escherichia coli | Q39838135 | ||
| Involvement of SecB, a chaperone, in the export of ribose-binding protein | Q39935707 | ||
| A new "gel-like" phase in dodecyl maltoside-lipid mixtures: implications in solubilization and reconstitution studies. | Q40225154 | ||
| Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands | Q41866614 | ||
| Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by SecB requires two protomers of SecA | Q42078600 | ||
| The variable subdomain of Escherichia coli SecA functions to regulate SecA ATPase activity and ADP release | Q42152267 | ||
| A "push and slide" mechanism allows sequence-insensitive translocation of secretory proteins by the SecA ATPase | Q42209016 | ||
| Characterization of membrane-associated and soluble states of SecA protein from wild-type and SecA51(TS) mutant strains of Escherichia coli | Q43424522 | ||
| Organization of the receptor-kinase signaling array that regulates Escherichia coli chemotaxis | Q44064990 | ||
| The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins | Q44686930 | ||
| Nucleotide exchange from the high-affinity ATP-binding site in SecA is the rate-limiting step in the ATPase cycle of the soluble enzyme and occurs through a specialized conformational state | Q44925080 | ||
| The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation. | Q46008320 | ||
| ΔμH+ and ATP function at different steps of the catalytic cycle of preprotein translocase | Q46481993 | ||
| The Sec System: Protein Export in Escherichia coli | Q47374398 | ||
| Remote Coupled Drastic β-Barrel to β-Sheet Transition of the Protein Translocation Motor | Q49340799 | ||
| Charged amino acids in a preprotein inhibit SecA-dependent protein translocation. | Q51798035 | ||
| Asymmetric binding between SecA and SecB two symmetric proteins: implications for function in export. | Q52563568 | ||
| In vitro analysis of the process of translocation of OmpA across the Escherichia coli cytoplasmic membrane. A translocation intermediate accumulates transiently in the absence of the proton motive force. | Q54340916 | ||
| SecA supports a constant rate of preprotein translocation. | Q54467339 | ||
| Mapping of the Binding Frame for the Chaperone SecB within a Natural Ligand, Galactose-binding Protein | Q54601274 | ||
| Retardation of folding as a possible means of suppression of a mutation in the leader sequence of an exported protein. | Q54740268 | ||
| Structure-based working model of SecDF, a proton-driven bacterial protein translocation factor. | Q55282553 | ||
| Dynamic action of the Sec machinery during initiation, protein translocation and termination. | Q55513394 | ||
| Orientation of membrane vesicles from Escherichia coli prepared by different procedures | Q70048133 | ||
| Sidedness of native membrane vesicles of Escherichia coli and orientation of the reconstituted lactose: H+ carrier | Q70368087 | ||
| Short hydrophobic segments in the mature domain of ProOmpA determine its stepwise movement during translocation across the cytoplasmic membrane of Escherichia coli | Q73084746 | ||
| P433 | issue | 1 | |
| P407 | language of work or name | English | Q1860 |
| P577 | publication date | 2018-12-07 | |
| P1433 | published in | Journal of Bacteriology | Q478419 |
| P1476 | title | Co-assembly of SecYEG and SecA fully restores the properties of the native translocon | |
| P478 | volume | 201 |
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