Reference health

The surprising complexity of signal sequences

https://doi.org/10.1016/j.tibs.2006.08.004
CiteStamped reference-health badge
1 of 79 checkable references need attention · checked 2026-07-22

At the dated check, the references listed below either did not resolve in Crossref or DataCite, or carried a retraction notice. Each one is shown with the registry record that put it there.

References needing attention

marked retracted — notice via Crossref, record curated by Retraction Watch10.1038/sj.embor.7400551
L25 functions as a conserved ribosomal docking site shared by nascent chain‐associated complex and signal‐recognition particle
The 78 checked references that resolve
resolves10.1083/jcb.67.3.835
Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma.
resolves10.1016/0022-2836(85)90046-4
Signal sequences
resolves10.1021/bi00429a001
Signal sequences
resolves10.1073/pnas.77.6.3369
Eukaryotic signal sequence transports insulin antigen in Escherichia coli.
resolves10.1016/S0021-9258(18)33642-1
A bacterial secretory protein requires signal recognition particle for translocation across mammalian endoplasmic reticulum.
resolves10.1126/science.3541205
Many Random Sequences Functionally Replace the Secretion Signal Sequence of Yeast Invertase
resolves10.1002/j.1460-2075.1985.tb04164.x
Analysis of signals for secretion in the staphylococcal protein A gene.
resolves10.1093/protein/2.7.531
The structure of signal peptides from bacterial lipoproteins
resolves10.1073/pnas.77.12.7112
Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum.
resolves10.1083/jcb.102.5.1543
Secretory protein translocation in a yeast cell-free system can occur posttranslationally and requires ATP hydrolysis.
resolves10.1016/0092-8674(83)90352-5
Translocation of domains of nascent periplasmic proteins across the cytoplasmic membrane is independent of elongation
resolves10.1126/science.1701272
An <i>E. coli</i> Ribonucleoprotein Containing 4.5 <i>S</i> RNA Resembles Mammalian Signal Recognition Particle
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
resolves10.1016/S0092-8674(00)81418-X
Crystal Structure of the Signal Sequence Binding Subunit of the Signal Recognition Particle
resolves10.1126/science.287.5456.1232
Crystal Structure of the Ribonucleoprotein Core of the Signal Recognition Particle
resolves10.1074/jbc.M309082200
Basic Amino Acids in a Distinct Subset of Signal Peptides Promote Interaction with the Signal Recognition Particle
resolves10.1083/jcb.134.2.269
Signal sequences specify the targeting route to the endoplasmic reticulum membrane.
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.051484198
The targeting pathway of <i>Escherichia coli</i> presecretory and integral membrane proteins is specified by the hydrophobicity of the targeting signal
resolves10.1074/jbc.M205950200
Trigger Factor Retards Protein Export in Escherichia coli
resolves10.1038/sj.embor.embor921
The ribosome and YidC
resolves10.1128/JB.187.9.2983-2991.2005
Use of Thioredoxin as a Reporter To Identify a Subset of <i>Escherichia coli</i> Signal Sequences That Promote Signal Recognition Particle-Dependent Translocation
resolves10.1083/jcb.200407082
N-myristoylation determines dual targeting of mammalian NADH-cytochrome b(5) reductase to ER and mitochondrial outer membranes by a mechanism of kinetic partitioning
resolves10.1093/emboj/18.20.5494
Dual targeting of cytochrome P4502B1 to endoplasmic reticulum and mitochondria involves a novel signal activation by cyclic AMP‐dependent phosphorylation at Ser128
resolves10.1016/0092-8674(95)90313-5
A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane
resolves10.1016/S0092-8674(00)81738-9
Signal Sequence Recognition in Posttranslational Protein Transport across the Yeast ER Membrane
resolves10.1038/nature03821
A substrate-specific inhibitor of protein translocation into the endoplasmic reticulum
resolves10.1038/nature03670
Selective inhibition of cotranslational translocation of vascular cell adhesion molecule 1
resolves10.1038/nature02218
X-ray structure of a protein-conducting channel
resolves10.1083/jcb.134.1.25
Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum membrane.
resolves10.1083/jcb.200210095
Substrate-specific function of the translocon-associated protein complex during translocation across the ER membrane
resolves10.1016/S0092-8674(00)81861-9
Binding of Secretory Precursor Polypeptides to a Translocon Subcomplex Is Regulated by BiP
resolves10.1091/mbc.10.2.329
Detection of Transient In Vivo Interactions between Substrate and Transporter during Protein Translocation into the Endoplasmic Reticulum
resolves10.1016/S1534-5807(01)00120-4
Signal Sequences Control Gating of the Protein Translocation Channel in a Substrate-Specific Manner
resolves10.1016/S1357-2725(97)00153-2
Calreticulin
resolves10.1016/j.devcel.2005.09.001
Regulation of Protein Compartmentalization Expands the Diversity of Protein Function
resolves10.1083/jcb.106.4.1093
Targeting of the hepatitis B virus precore protein to the endoplasmic reticulum membrane: after signal peptide cleavage translocation can be aborted and the product released into the cytoplasm.
resolves10.1128/JVI.63.12.5238-5243.1989
Transport of hepatitis B virus precore protein into the nucleus after cleavage of its signal peptide
resolves10.1128/JVI.71.1.345-353.1997
Posttranscriptional regulation of hepatitis B virus replication by the precore protein
resolves10.1126/science.1073725
Neurotoxicity and Neurodegeneration When PrP Accumulates in the Cytosol
resolves10.1126/science.279.5352.827
A Transmembrane Form of the Prion Protein in Neurodegenerative Disease
resolves10.1091/mbc.E02-05-0293
Cotranslational Partitioning of Nascent Prion Protein into Multiple Populations at the Translocation Channel
resolves10.1038/sj.emboj.7600462
Protection from cytosolic prion protein toxicity by modulation of protein translocation
resolves10.1073/pnas.0406055102
An unusual signal peptide facilitates late steps in the biogenesis of a bacterial autotransporter
resolves10.1074/jbc.M302117200
Signal Sequences Initiate the Pathway of Maturation in the Endoplasmic Reticulum Lumen
resolves10.1021/bi049156s
Signal Sequences Influence Membrane Integration of the Prion Protein
resolves10.1093/emboj/20.7.1573
Signal peptide cleavage of a type I membrane protein, HCMV US11, is dependent on its membrane anchor
resolves10.1074/jbc.M007723200
Signal Peptidase and Oligosaccharyltransferase Interact in a Sequential and Dependent Manner within the Endoplasmic Reticulum
resolves10.1073/pnas.93.18.9606
Effects of inefficient cleavage of the signal sequence of HIV-1 gp 120 on its association with calnexin, folding, and intracellular transport.
resolves10.1074/jbc.M002373200
The Long Signal Peptide Isoform and Its Alternative Processing Direct the Intracellular Trafficking of Interleukin-15
resolves10.1128/JB.185.9.2910-2919.2003
The YSIRK-G/S Motif of Staphylococcal Protein A and Its Role in Efficiency of Signal Peptide Processing
resolves10.1016/S0021-9258(18)33964-4
Prolipoprotein signal peptidase in Escherichia coli is distinct from the M13 procoat protein signal peptidase.
resolves10.1073/pnas.88.8.3281
Product of the Pseudomonas aeruginosa gene pilD is a prepilin leader peptidase.
resolves10.1126/science.1070925
Identification of Signal Peptide Peptidase, a Presenilin-Type Aspartic Protease
resolves10.1016/S1097-2765(02)00655-X
Requirements for Signal Peptide Peptidase-Catalyzed Intramembrane Proteolysis
resolves10.1002/eji.1830270517
The human major histocompatibility complex class Ib molecule HLA‐E binds signal sequence‐derived peptides with primary anchor residues at positions 2 and 9
resolves10.1084/jem.187.5.813
Recognition of Human Histocompatibility Leukocyte Antigen (HLA)-E Complexed with HLA Class I Signal Sequence–derived Peptides by CD94/NKG2 Confers Protection from Natural Killer Cell–mediated Lysis
resolves10.1038/35869
HLA-E binds to natural killer cell receptors CD94/NKG2A, B and C
resolves10.1126/science.287.5455.1031
Surface Expression of HLA-E, an Inhibitor of Natural Killer Cells, Enhanced by Human Cytomegalovirus gpUL40
resolves10.4049/jimmunol.164.10.5019
Cutting Edge: The Human Cytomegalovirus <i>UL40</i> Gene Product Contains a Ligand for HLA-E and Prevents NK Cell-Mediated Lysis
resolves10.1093/emboj/16.22.6636
Signal peptide fragments of preprolactin and HIV‐1 p‐gp160 interact with calmodulin
resolves10.1128/JVI.75.13.5762-5771.2001
A Particle-Associated Glycoprotein Signal Peptide Essential for Virus Maturation and Infectivity
resolves10.1074/jbc.M302343200
Long-lived Signal Peptide of Lymphocytic Choriomeningitis Virus Glycoprotein pGP-C
resolves10.1038/sj.embor.7400002
Identification of Lassa virus glycoprotein signal peptide as a trans‐acting maturation factor
resolves10.1016/S1097-2765(02)00692-5
Targeting and Beyond
resolves10.1091/mbc.E04-06-0508
The Efficiency of Protein Compartmentalization into the Secretory Pathway
resolves10.1016/0092-8674(95)90077-2
Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p
resolves10.1002/j.1460-2075.1996.tb00492.x
A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae.
resolves10.1091/mbc.01-10-0518
Recognition of a Subset of Signal Sequences by Ssh1p, a Sec61p-related Protein in the Membrane of Endoplasmic Reticulum of Yeast<i>Saccharomyces cerevisiae</i>
resolves10.1093/glycob/cwj026
Two oligosaccharyl transferase complexes exist in yeast and associate with two different translocons
resolves10.1146/annurev.cellbio.15.1.799
The Translocon: A Dynamic Gateway at the ER Membrane
resolves10.1073/pnas.97.13.7214
Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant proteins in dog pancreas microsomes
resolves10.1074/jbc.275.19.14550
Mammalian Sec61 Is Associated with Sec62 and Sec63
resolves10.1093/emboj/16.10.2756
Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme
resolves10.1046/j.1365-2958.2003.03346.x
Versatility of inner membrane protein biogenesis in <i>Escherichia coli</i>
resolves10.1046/j.1365-2958.2002.02972.x
SecDFyajC forms a heterotetrameric complex with YidC
resolves10.1111/j.1365-2958.2005.04919.x
Determinants of the streptococcal surface glycoprotein GspB that facilitate export by the accessory Sec system
resolves10.1074/jbc.M411716200
Secretion of Cartilage Oligomeric Matrix Protein Is Affected by the Signal Peptide
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/10.1016/j.tibs.2006.08.004"><img src="https://citestamp.com/citestamped/10.1016/j.tibs.2006.08.004/badge.svg" alt="CiteStamped reference-health badge" width="460" height="64"></a>
[![CiteStamped reference-health badge](https://citestamp.com/citestamped/10.1016/j.tibs.2006.08.004/badge.svg)](https://citestamp.com/citestamped/10.1016/j.tibs.2006.08.004)