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Dissecting the Translocase and Integrase Functions of the <i>Escherichia coli</i> Secyeg Translocon
34/34 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 34 checked references that resolve
resolves10.1083/jcb.108.5.1637
In vitro membrane assembly of a polytopic, transmembrane protein results in an enzymatically active conformation.
resolves10.1074/jbc.271.49.31196
FtsH (HflB) Is an ATP-dependent Protease Selectively Acting on SecY and Some Other Membrane Proteins
resolves10.1128/jb.172.12.7005-7010.1990
Characterization of cold-sensitive secY mutants of Escherichia coli
resolves10.1073/pnas.91.10.4539
A cytoplasmic domain is important for the formation of a SecY-SecE translocator complex.
resolves10.1093/emboj/19.1.134
Discrimination between SRP‐ and SecA/SecB‐dependent substrates involves selective recognition of nascent chains by SRP and trigger factor
resolves10.1074/jbc.273.22.13898
Requirements for the Translocation of Elongation-arrested, Ribosome-associated OmpA across the Plasma Membrane ofEscherichia coli
resolves10.1016/S0014-5793(96)01354-3
Assembly of a cytoplasmic membrane protein in <i>Escherichia coli</i> is dependent on the signal recognition particle
resolves10.1073/pnas.95.25.14646
Differential use of the signal recognition particle translocase targeting pathway for inner membrane protein assembly in
<i>Escherichia coli</i>
resolves10.1073/pnas.85.23.8953
SecA suppresses the temperature-sensitive SecY24 defect in protein translocation in Escherichia coli membrane vesicles.
resolves10.1128/jb.179.12.4003-4012.1997
Comparative characterization of SecA from the alpha-subclass purple bacterium Rhodobacter capsulatus and Escherichia coli reveals differences in membrane and precursor specificity
resolves10.1016/S0021-9258(18)99951-5
Identification of a soluble SecA/SecB complex by means of a subfractionated cell-free export system.
resolves10.1016/S0014-5793(97)00376-1
Subunit interactions in the <i>Escherichia coli</i> protein translocase: SecE and SecG associate independently with SecY
resolves10.1091/mbc.10.7.2163
In Vitro Studies with Purified Components Reveal Signal Recognition Particle (SRP) and SecA/SecB as Constituents of Two Independent Protein-targeting Pathways of<i>Escherichia coli</i>
resolves10.1002/j.1460-2075.1994.tb06511.x
An alternative protein targeting pathway in Escherichia coli: studies on the role of FtsY.
resolves10.1111/j.1432-1033.1995.766_3.x
The Functional Integration of a Polytopic Membrane Protein of <i>Escherichia coli</i> is Dependent on the Bacterial Signal‐Recognition Particle
resolves10.1006/plas.1994.1032
The pKSM710 Vector Cassette Provides Tightly Regulated lac and T7lac Promoters and Strategies for Manipulating N-Terminal Protein Sequences
resolves10.1093/emboj/16.21.6384
SecY and SecA interact to allow SecA insertion and protein translocation across the Escherichia coli plasma membrane
resolves10.1073/pnas.81.23.7421
In vitro translocation of bacterial proteins across the plasma membrane of Escherichia coli.
resolves10.1074/jbc.273.20.12451
A Mutation in the Escherichia coli secY Gene That Produces Distinct Effects on Inner Membrane Protein Insertion and Protein Export
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.
resolves10.1016/S0092-8674(00)81083-1
Inversion of the Membrane Topology of SecG Coupled with SecA-Dependent Preprotein Translocation
resolves10.1128/jb.176.20.6410-6413.1994
Gene fusion analysis of membrane protein topology: a direct comparison of alkaline phosphatase and beta-lactamase fusions
resolves10.1074/jbc.274.13.8993
SecA Is Required for the Insertion of Inner Membrane Proteins Targeted by the Escherichia coli Signal Recognition Particle
resolves10.1002/j.1460-2075.1991.tb07699.x
One of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery.
resolves10.1074/jbc.272.4.2053
FtsY, the Prokaryotic Signal Recognition Particle Receptor Homologue, Is Essential for Biogenesis of Membrane Proteins
resolves10.1046/j.1365-2958.1998.00937.x
Coupled structure change of SecA and SecG revealed by the synthetic lethality of the <i>secAcsR11</i> and Δ<i>secG</i>::<i>kan</i> double mutant
resolves10.1111/j.1432-1033.1992.tb17111.x
Biochemical analysis of the biogenesis and function of the <i>Escherichia coli</i> export factor SecY
resolves10.1016/S0300-9084(97)82744-7
Protein translocation functions of Escherichia coli SecY: In vitro characterization of cold-sensitive secY mutants
resolves10.1074/jbc.271.21.12394
Insertion of the Polytopic Membrane Protein MalF Is Dependent on the Bacterial Secretion Machinery
resolves10.1016/S0092-8674(00)81839-5
The E. coli Signal Recognition Particle Is Required for the Insertion of a Subset of Inner Membrane Proteins
resolves10.1093/emboj/17.9.2504
The Escherichia coli SRP and SecB targeting pathways converge at the translocon
resolves10.1016/S0021-9258(18)35796-X
Membrane insertion of the mannitol permease of Escherichia coli occurs under conditions of impaired SecA function.
resolves10.1016/S0021-9258(18)89669-7
Effects of two sec genes on protein assembly into the plasma membrane of Escherichia coli.
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