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Projection structure and oligomeric properties of a bacterial core protein translocase
59/59 checkable references clean · checked 2026-07-22
Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
The 59 checked references that resolve
resolves10.1073/pnas.88.15.6545
Reconstitution of a protein translocation system containing purified SecY, SecE, and SecA from Escherichia coli.
resolves10.1038/33967
Three-dimensional map of the plasma membrane H+-ATPase in the open conformation
resolves10.1021/bi00061a021
Purified Escherichia coli preprotein translocase catalyzes multiple cycles of precursor protein translocation
resolves10.1126/science.278.5346.2123
Alignment of Conduits for the Nascent Polypeptide Chain in the Ribosome-Sec61 Complex
resolves10.1016/0092-8674(90)90111-Q
The purified E. coli integral membrane protein is sufficient for reconstitution of SecA-dependent precursor protein translocation
resolves10.1016/0092-8674(88)90227-9
SecA protein is required for secretory protein translocation into E. coli membrane vesicles
resolves10.1021/bi00191a026
F0 Membrane Domain of ATP Synthase from Bovine Heart Mitochondria: Purification, Subunit Composition, and Reconstitution with F1-ATPase
resolves10.1074/jbc.270.34.20106
SecYEG and SecA Are the Stoichiometric Components of Preprotein Translocase
resolves10.1093/emboj/16.10.2756
Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme
resolves10.1093/emboj/16.16.4871
The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling
resolves10.1093/emboj/18.12.3263
The PrlA and PrlG phenotypes are caused by a loosened association among the translocase SecYEG subunits
resolves10.1007/978-3-642-71114-5_3
Specific Volumes of Biological Macromolecules and Some Other Molecules of Biological Interest
resolves10.1016/S0092-8674(94)90582-7
SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
resolves10.1016/0092-8674(95)90143-4
SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF
resolves10.1006/jmbi.1996.0328
Electron-crystallographic Refinement of the Structure of Bacteriorhodopsin
resolves10.1016/S0092-8674(00)81391-4
Oligomeric Rings of the Sec61p Complex Induced by Ligands Required for Protein Translocation
resolves10.1016/0304-3991(86)90203-2
Structure of purple membrane from halobacterium halobium: recording, measurement and evaluation of electron micrographs at 3.5 Å resolution
resolves10.1016/S0022-2836(05)80271-2
Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
resolves10.1006/jmbi.1998.2070
Characterisation of an improved two-dimensional p22121 crystal from bovine rhodopsin
resolves10.1128/jb.154.1.253-260.1983
Mutations in a new gene, secB, cause defective protein localization in Escherichia coli
resolves10.1016/S0092-8674(00)81206-4
The Preprotein Translocation Channel of the Outer Membrane of Mitochondria
resolves10.1038/227680a0
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
resolves10.1002/j.1460-2075.1989.tb03458.x
SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli.
resolves10.1016/0092-8674(90)90742-W
The ATPase activity of secA is regulated by acidic phospholipids, secY, and the leader and mature domains of precursor proteins
resolves10.1093/emboj/19.5.852
SecYEG assembles into a tetramer to form the active protein translocation channel
resolves10.1016/S1097-2765(00)00118-0
The Structure of Ribosome-Channel Complexes Engaged in Protein Translocation
resolves10.1006/jmbi.1998.2413
The bacterial SecY/E translocation complex forms channel-like structures similar to those of the eukaryotic sec61p complex
resolves10.1006/jmbi.1996.0399
Over-production of Proteins inEscherichia coli: Mutant Hosts that Allow Synthesis of some Membrane Proteins and Globular Proteins at High Levels
resolves10.1074/jbc.274.29.20110
Interaction of BiP with the J-domain of the Sec63p Component of the Endoplasmic Reticulum Protein Translocation Complex
resolves10.1002/j.1460-2075.1994.tb06628.x
Disruption of the gene encoding p12 (SecG) reveals the direct involvement and important function of SecG in the protein translocation of Escherichia coli at low temperature.
resolves10.1128/jb.150.2.686-691.1982
Identification of a new gene (secA) and gene product involved in the secretion of envelope proteins in Escherichia coli
resolves10.1016/S0092-8674(00)80443-2
Protein Translocation in the Three Domains of Life: Variations on a Theme
resolves10.1093/emboj/19.8.1900
Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA
resolves10.1002/j.1460-2075.1996.tb00906.x
Targeting of signal sequenceless proteins for export in Escherichia coli with altered protein translocase.
resolves10.1146/annurev.bi.65.070196.001415
PROTEIN TRANSPORT ACROSS THE EUKARYOTIC ENDOPLASMIC RETICULUM AND BACTERIAL INNER MEMBRANES
resolves10.1038/24421
Three-dimensional structure of the plant photosystem II reaction centre at 8 Å resolution
resolves10.1101/gad.3.7.1035
The secE gene encodes an integral membrane protein required for protein export in Escherichia coli.
resolves10.1007/BFb0115597
Simultaneous radial and wavelength analysis with the Optima XL-A analytical ultracentrifuge
resolves10.1111/j.1432-1033.1995.tb20624.x
The Influence of Two Anion-transport Inhibitors, 4,4'-Diisothiocyanatodihydrostilbene-2,2'-Disulfonate and 4,4'-Dibenzoylstilbene-2,2'-Disulfonate, on the Self-association of Erythrocyte Band 3 Protein
resolves10.1126/science.283.5405.1176
Three-Dimensional Structure of a Recombinant Gap Junction Membrane Channel
resolves10.1006/jmbi.1994.1445
Analysis of Electron Microscope Images and Electron Diffraction Patterns of Thin Crystals of Ø29 Connectors in Ice
resolves10.1074/jbc.275.4.2472
Non-bilayer Lipids Stimulate the Activity of the Reconstituted Bacterial Protein Translocase
resolves10.1093/emboj/17.13.3631
PrlA4 prevents the rejection of signal sequence defective preproteins by stabilizing the SecA–SecY interaction during the initiation of translocation
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