Reference health
Different modes of SecY–SecA interactions revealed by site-directed <i>in vivo</i> photo-cross-linking
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.
2 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
resolves10.1016/j.bbamcr.2004.06.003
Structure and function of SecA, the preprotein translocase nanomotor
resolves10.1093/emboj/16.21.6384
SecY and SecA interact to allow SecA insertion and protein translocation across the Escherichia coli plasma membrane
resolves10.1016/S0092-8674(94)90582-7
SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
resolves10.1002/j.1460-2075.1987.tb02670.x
Topology analysis of the SecY protein, an integral membrane protein involved in protein export in Escherichia coli.
resolves10.1083/jcb.200412019
Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY
resolves10.1093/emboj/19.5.852
SecYEG assembles into a tetramer to form the active protein translocation channel
resolves10.1038/nature00827
Three-dimensional structure of the bacterial protein-translocation complex SecYEG
resolves10.1074/jbc.M300230200
Fluorescence Resonance Energy Transfer Analysis of Protein Translocase
resolves10.1093/emboj/cdg418
Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase
resolves10.1038/nature04133
Structure of the E. coli protein-conducting channel bound to a translating ribosome
resolves10.1074/jbc.270.34.20106
SecYEG and SecA Are the Stoichiometric Components of Preprotein Translocase
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.
resolves10.1128/jb.179.18.5699-5704.1997
In vivo cross-linking of the SecA and SecY subunits of the Escherichia coli preprotein translocase
resolves10.1074/jbc.272.17.11302
Identification of a Region of Interaction between Escherichia coli SecA and SecY Proteins
resolves10.1021/bi034331a
Nearest Neighbor Analysis of the SecYEG Complex. 1. Identification of a SecY−SecG Interface
resolves10.1021/bi034333v
Nearest Neighbor Analysis of the SecYEG Complex. 2. Identification of a SecY−SecE Cytosolic Interface
resolves10.1016/S0014-5793(02)03202-7
SecY–SecY and SecY–SecG contacts revealed by site‐specific crosslinking
resolves10.1016/S0300-9084(97)82744-7
Protein translocation functions of Escherichia coli SecY: In vitro characterization of cold-sensitive secY mutants
resolves10.1073/pnas.081617398
An essential amino acid residue in the protein translocation channel revealed by targeted random mutagenesis of SecY
resolves10.1128/JB.185.2.405-412.2003
Biochemical Characterization of a Mutationally Altered Protein Translocase: Proton Motive Force Stimulation of the Initiation Phase of Translocation
resolves10.1128/JB.184.8.2243-2250.2002
Roles of the C-Terminal End of SecY in Protein Translocation and Viability of
<i>Escherichia coli</i>
resolves10.1128/jb.172.12.7005-7010.1990
Characterization of cold-sensitive secY mutants of Escherichia coli
resolves10.1046/j.1365-2443.2000.00388.x
Genetic dissection of SecA: suppressor mutations against the <i>secY205</i> translocase defect
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
resolves10.1074/jbc.M204436200
Superactive SecY Variants That Fulfill the Essential Translocation Function with a Reduced Cellular Quantity
resolves10.1073/pnas.172226299
Addition of a photocrosslinking amino acid to the genetic code of
<i>Escherichia</i>
<i>coli</i>
resolves10.1002/1439-7633(20021104)3:11<1135::AID-CBIC1135>3.0.CO;2-M
In Vivo Photocrosslinking with Unnatural Amino Acid Mutagenesis
resolves10.1073/pnas.87.21.8227
Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery.
resolves10.1002/j.1460-2075.1993.tb06013.x
PrlA suppressor mutations cluster in regions corresponding to three distinct topological domains.
resolves10.1007/BF00301061
Genetic analysis of SecY: additional export-defective mutations and factors affecting their phenotypes
resolves10.1128/JB.182.12.3377-3382.2000
A Mutation in
<i>secY</i>
That Causes Enhanced SecA Insertion and Impaired Late Functions in Protein Translocation
resolves10.1128/JB.186.12.3960-3969.2004
Mutational Analysis of Transmembrane Regions 3 and 4 of SecY, a Central Component of Protein Translocase
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
resolves10.1016/j.jmb.2006.07.017
Identification of Two Interaction Sites in SecY that Are Important for the Functional Interaction with SecA
resolves10.1093/emboj/18.12.3263
The PrlA and PrlG phenotypes are caused by a loosened association among the translocase SecYEG subunits
resolves10.1074/jbc.M001100200
Distinct Membrane Binding Properties of N- and C-terminal Domains of Escherichia coli SecA ATPase
resolves10.1021/bi047488r
Conformational State of the SecYEG-Bound SecA Probed by Single Tryptophan Fluorescence Spectroscopy
resolves10.1074/jbc.M413947200
The Bacterial ATPase SecA Functions as a Monomer in Protein Translocation
resolves10.1128/JB.188.1.335-338.2006
SecA Dimer Cross-Linked at Its Subunit Interface Is Functional for Protein Translocation
resolves10.1016/0006-291X(90)92083-C
Secy protein, a membrane-embedded secretion factor of E. coli, is cleaved by the ompT protease in vitro
resolves10.1016/0378-1119(85)90120-9
Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectors
resolves10.1038/nmeth0505-377
Photo-cross-linking interacting proteins with a genetically encoded benzophenone
resolves10.1128/JB.185.3.948-956.2003
A SecE Mutation That Modulates SecY-SecE Translocase Assembly, Identified as a Specific Suppressor of SecY Defects
resolves10.1002/j.1460-2075.1984.tb02133.x
Characterization of an amber mutation in the structural gene for ribosomal protein L15, which impairs the expression of the protein export gene, secY, in Escherichia coli.
resolves10.1111/j.1365-2958.1992.tb01559.x
SecY variants that interfere with <i>Escherichia coli</i> protein export in the presence of normal <i>secY</i>
resolves10.1074/jbc.C000550200
Two Independent Mechanisms Down-regulate the Intrinsic SecA ATPase Activity
The 2 references without a DOI — listed, not checked
no DOI — not checkedTJ Silhavy, ML Berman, LW Enquist Experiments with Gene Fusions (Cold Spring Harbor Lab Press, Cold Spring Harbor, NY, 1984).
no DOI — not checkedH Mori, K Ito J Biol Chem, in press. (2006).
What this badge says. CiteStamped means the CHECKABLE references of this
work were clean at the dated check: each resolved to a known work in a public registry, and none
carried a retraction notice at that time. It says nothing about the quality, findings,
or importance of the work itself, and nothing about references deposited without a DOI.
checked 2026-07-22 — re-checked daily as this page is visited; titles and statuses come from Crossref and DataCite and are not part of the signed record
Embed this badge
Both snippets point at the live badge image and link back to this page. The badge re-renders from the daily check, so an embed never goes stale by more than a day of visits.
<a href="https://citestamp.com/citestamped/10.1073/pnas.0606390103"><img src="https://citestamp.com/citestamped/10.1073/pnas.0606390103/badge.svg" alt="CiteStamped reference-health badge" width="460" height="64"></a>
[](https://citestamp.com/citestamped/10.1073/pnas.0606390103)