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Physiological Basis for Conservation of the Signal Recognition Particle Targeting Pathway in <i>Escherichia coli</i>

https://doi.org/10.1128/jb.183.7.2187-2197.2001
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56/56 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.

3 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.

The 56 checked references that resolve
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Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone.
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The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein
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Differential use of the signal recognition particle translocase targeting pathway for inner membrane protein assembly in <i>Escherichia coli</i>
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Assembly of a cytoplasmic membrane protein in <i>Escherichia coli</i> is dependent on the signal recognition particle
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A signal sequence is not required for protein export in prlA mutants of Escherichia coli.
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Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor.
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resolves10.1038/366351a0
GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation
resolves10.1002/j.1460-2075.1996.tb01082.x
Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli.
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The Structure of Multiple Polypeptide Domains Determines the Signal Recognition Particle Targeting Requirement of <i>Escherichia coli</i> Inner Membrane Proteins
resolves10.1038/359744a0
The E. coli ffh gene is necessary for viability and efficient protein export
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An <i>E. coli</i> Ribonucleoprotein Containing 4.5 <i>S</i> RNA Resembles Mammalian Signal Recognition Particle
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resolves10.1074/jbc.274.13.8993
SecA Is Required for the Insertion of Inner Membrane Proteins Targeted by the Escherichia coli Signal Recognition Particle
resolves10.1016/0092-8674(90)90454-M
E. coli 4.5S RNA is part of a ribonucleoprotein particle that has properties related to signal recognition particle
resolves10.1038/340478a0
Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP–binding domains
resolves10.1074/jbc.272.4.2053
FtsY, the Prokaryotic Signal Recognition Particle Receptor Homologue, Is Essential for Biogenesis of Membrane Proteins
resolves10.1016/S0092-8674(00)80787-4
Polypeptide Flux through Bacterial Hsp70
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The dnaK protein modulates the heat-shock response of Escherichia coli
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Levels of DnaK and DnaJ provide tight control of heat shock gene expression and protein repair in <i>Escherichia coli</i>
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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
resolves10.1146/annurev.cb.10.110194.000511
Signal Sequence Recognition and Protein Targeting to the Endoplasmic Reticulum Membrane
resolves10.1101/gad.6.7.1165
DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli.
resolves10.1073/pnas.89.15.7139
Partial loss of function mutations in DnaK, the Escherichia coli homologue of the 70-kDa heat shock proteins, affect highly conserved amino acids implicated in ATP binding and hydrolysis.
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Redundant In Vivo Proteolytic Activities of <i>Escherichia coli</i> Lon and the ClpYQ (HslUV) Protease
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Sequence analysis and phenotypic characterization of groEL mutations that block lambda and T4 bacteriophage growth
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Two classes of extragenic suppressor mutations identify functionally distinct regions of the GroEL chaperone of Escherichia coli
The 3 references without a DOI — listed, not checked
no DOI — not checkedGross C. A. Function and regulation of the heat shock proteins Escherichia coli and Salmonella: cellular and molecular biology 2nd ed. Neidhardt F. C. 1996 1382 1399 American Society for Microbiology Washington D.C.
no DOI — not checkedHarlow E. Lane D. Using antibodies. 1999 Cold Spring Harbor Laboratory Press Cold Spring Harbor N.Y
no DOI — not checkedMiller J. H. A short course in bacterial genetics. 1992 Cold Spring Harbor Laboratory Press Cold Spring Harbor N.Y
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