ReviewBiochimica et biophysica acta2007
Oligomeric states of the SecA and SecYEG core components of the bacterial Sec translocon.
Review in Biochimica et biophysica acta, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 31 citations in OpenAlex.
- Article
- The SecA ATPase motor protein binds to Escherichia coli liposomes only as monomers.Biochimica et biophysica acta. Biomembranes · 2020Article
- An alternate mode of oligomerization for E. coli SecA.Scientific reports · 2017Article
- Escherichia coli SecG is required for residual export mediated by mutant signal sequences and for SecY-SecE complex stability.Journal of bacteriology · 2015Article
- Analysis of SecA dimerization in solution.Biochemistry · 2014Article
- Defining the solution state dimer structure of Escherichia coli SecA using Förster resonance energy transfer.Biochemistry · 2013Article
- Two copies of the SecY channel and acidic lipids are necessary to activate the SecA translocation ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The use of analytical sedimentation velocity to extract thermodynamic linkage.Biophysical chemistry · 2011Article
- A single copy of SecYEG is sufficient for preprotein translocation.The EMBO journal · 2011Article
- Article
- Energetics of SecA dimerization.Journal of molecular biology · 2011Article
- Mapping of the SecA·SecY and SecA·SecG interfaces by site-directed in vivo photocross-linking.The Journal of biological chemistry · 2011Article
- Asp3 mediates multiple protein-protein interactions within the accessory Sec system of Streptococcus gordonii.Molecular microbiology · 2010Article
- Mapping of the signal peptide-binding domain of Escherichia coli SecA using Förster resonance energy transfer.Biochemistry · 2010Article
- Translocation of proteins through the Sec61 and SecYEG channels.Current opinion in cell biology · 2009Review
- Reexamination of the role of the amino terminus of SecA in promoting its dimerization and functional state.Journal of bacteriology · 2008Article
- Article
- Review
- Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA.The EMBO journal · 2007Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Many proteins synthesized in the cytoplasm ultimately function in non-cytoplasmic locations. In Escherichia coli, the general secretory (Sec) pathway transports the vast majority of these proteins. Two fundamental components of the Sec transport pathway are the SecYEG heterotrimeric complex that forms the channel through the cytoplasmic membrane, and SecA, the ATPase that drives the preprotein to and across the membrane. This review focuses on what is known about the oligomeric states of these core Sec components and how the oligomeric state might change during the course of the translocation of a preprotein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.