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Structure of a complex of the ATPase SecA and the protein-translocation channel
61/61 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.
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The 61 checked references that resolve
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Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
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SRP‐dependent co‐translational targeting and SecA‐dependent translocation analyzed as individual steps in the export of a bacterial protein
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SecA Is Required for the Insertion of Inner Membrane Proteins Targeted by the Escherichia coli Signal Recognition Particle
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Sec‐dependent membrane protein biogenesis: SecYEG, preprotein hydrophobicity and translocation kinetics control the stop‐transfer function
resolves10.1016/j.cell.2007.02.036
Protein Translocation Is Mediated by Oligomers of the SecY Complex with One SecY Copy Forming the Channel
resolves10.1093/emboj/cdg418
Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase
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Mapping an Interface of SecY (PrlA) and SecE (PrlG) by Using Synthetic Phenotypes and In Vivo Cross-Linking
resolves10.1038/sj.emboj.7600804
Investigating the SecY plug movement at the SecYEG translocation channel
resolves10.1016/S0092-8674(00)81738-9
Signal Sequence Recognition in Posttranslational Protein Transport across the Yeast ER Membrane
resolves10.1016/0092-8674(90)90111-Q
The purified E. coli integral membrane protein is sufficient for reconstitution of SecA-dependent precursor protein translocation
resolves10.1073/pnas.88.15.6545
Reconstitution of a protein translocation system containing purified SecY, SecE, and SecA from Escherichia coli.
resolves10.1016/S0092-8674(94)90582-7
SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
resolves10.1126/science.1074424
Nucleotide Control of Interdomain Interactions in the Conformational Reaction Cycle of SecA
resolves10.1093/emboj/cdf471
Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane
resolves10.1074/jbc.M413947200
The Bacterial ATPase SecA Functions as a Monomer in Protein Translocation
resolves10.1038/sj.emboj.7601661
Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA
resolves10.1038/nsmb1166
Co- and post-translational translocation through the protein-conducting channel: analogous mechanisms at work?
resolves10.1016/j.jmb.2006.08.044
A Novel Dimer Interface and Conformational Changes Revealed by an X-ray Structure of B. subtilis SecA
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A defined mutation in the protein export gene within the spc ribosomal protein operon of Escherichia coli: isolation and characterization of a new temperature‐sensitive secY mutant.
resolves10.1073/pnas.081617398
An essential amino acid residue in the protein translocation channel revealed by targeted random mutagenesis of SecY
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Roles of the C-Terminal End of SecY in Protein Translocation and Viability of
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resolves10.1074/jbc.M204436200
Superactive SecY Variants That Fulfill the Essential Translocation Function with a Reduced Cellular Quantity
resolves10.1038/334173a0
Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membranes
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
resolves10.1016/S0092-8674(00)80716-3
Crystal Structures of Complexes of PcrA DNA Helicase with a DNA Substrate Indicate an Inchworm Mechanism
resolves10.1016/S0092-8674(00)81083-1
Inversion of the Membrane Topology of SecG Coupled with SecA-Dependent Preprotein Translocation
resolves10.1021/bi034331a
Nearest Neighbor Analysis of the SecYEG Complex. 1. Identification of a SecY−SecG Interface
resolves10.1038/nature00827
Three-dimensional structure of the bacterial protein-translocation complex SecYEG
resolves10.1016/j.jmb.2005.08.005
Atomic Model of the E.coli Membrane-bound Protein Translocation Complex SecYEG
resolves10.1016/j.jmb.2008.06.049
SecA, the Motor of the Secretion Machine, Binds Diverse Partners on One Interactive Surface
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The binding cascade of SecB to SecA to SecYE mediates preprotein targeting to the E. coli plasma membrane
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Structural Basis for Signal-Sequence Recognition by the Translocase Motor SecA as Determined by NMR
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Targeting of signal sequenceless proteins for export in Escherichia coli with altered protein translocase.
resolves10.1038/nsb980
Structural determinants of SecB recognition by SecA in bacterial protein translocation
resolves10.1016/S0092-8674(00)00028-3
The Sec61p Complex Mediates the Integration of a Membrane Protein by Allowing Lipid Partitioning of the Transmembrane Domain
resolves10.1038/nature07439
A role for the two-helix finger of the SecA ATPase in protein translocation
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Isolation and analysis of dominant secA mutations in Escherichia coli
resolves10.1046/j.1365-2958.1999.01686.x
A molecular switch in SecA protein couples ATP hydrolysis to protein translocation
resolves10.1016/S0969-2126(01)00570-6
Crystal Structures of the HslVU Peptidase–ATPase Complex Reveal an ATP-Dependent Proteolysis Mechanism
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Role of the processing pore of the ClpX AAA+ ATPase in the recognition and engagement of specific protein substrates
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Loops in the Central Channel of ClpA Chaperone Mediate Protein Binding, Unfolding, and Translocation
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Central Pore Residues Mediate the p97/VCP Activity Required for ERAD
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Diverse Pore Loops of the AAA+ ClpX Machine Mediate Unassisted and Adaptor-Dependent Recognition of ssrA-Tagged Substrates
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The Long α-Helix of SecA Is Important for the ATPase Coupling of Translocation
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Improved methods for building protein models in electron density maps and the location of errors in these models
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Improved Fourier coefficients for maps using phases from partial structures with errors
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Considerations for the refinement of low-resolution crystal structures
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Determining the Structure of an Unliganded and Fully Glycosylated SIV gp120 Envelope Glycoprotein
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ConSurf: Identification of Functional Regions in Proteins
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The 2 references without a DOI — listed, not checked
no DOI — not checkedCollaborative Computational Project, 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760–763 (1994)
no DOI — not checkedDeLano, W. L. The PyMOL Molecular Graphics System. < http://www.pymol.org > (2002)
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