ReviewBiopolymers2008
Use of synthetic signal sequences to explore the protein export machinery.
Review in Biopolymers, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
12 citing papers in PubMed, 32 citations in OpenAlex.
- The signal peptide of BmNPV GP64 activates the ERAD pathway to regulate heterogeneous secretory protein expression.Microbial cell factories · 2024Article
- Genomic evidence for the widespread presence of GH45 cellulases among soil invertebrates.Molecular ecology · 2024Article
- The Bombyx mori Nucleopolyhedrovirus GP64 Retains the Transmembrane Helix of Signal Peptide to Contribute to Secretion across the Cytomembrane.Microbiology spectrum · 2022Article
- Molecular Modeling of Signal Peptide Recognition by Eukaryotic Sec Complexes.International journal of molecular sciences · 2021Review
- "Multiple partial recognitions in dynamic equilibrium" in the binding sites of proteins form the molecular basis of promiscuous recognition of structurally diverse ligands.Biophysical reviews · 2018Review
- Positive charge in the n-region of the signal peptide contributes to efficient post-translational translocation of small secretory preproteins.The Journal of biological chemistry · 2018Article
- Site-saturation mutagenesis of mutant L-asparaginase II signal peptide hydrophobic region for improved excretion of cyclodextrin glucanotransferase.Journal of industrial microbiology & biotechnology · 2017Article
- Glucagon-Like Peptide-1 and Its Class B G Protein-Coupled Receptors: A Long March to Therapeutic Successes.Pharmacological reviews · 2016Review
- Chimeras taking shape: potential functions of proteins encoded by chimeric RNA transcripts.Genome research · 2012Article
- A career pathway in protein folding: from model peptides to postreductionist protein science.Protein science : a publication of the Protein Society · 2011Review
- Engineering anti-vascular endothelial growth factor single chain disulfide-stabilized antibody variable fragments (sc-dsFv) with phage-displayed sc-dsFv libraries.The Journal of biological chemistry · 2010Article
- Exploring the interactions between signal sequences and E. coli SRP by two distinct and complementary crosslinking methods.Biopolymers · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The information for correct localization of newly synthesized proteins in both prokaryotes and eukaryotes resides in self-contained, often transportable targeting sequences. Of these, signal sequences specify that a protein should be secreted from a cell or incorporated into the cytoplasmic membrane. A central puzzle is presented by the lack of primary structural homology among signal sequences, although they share common features in their sequences. Synthetic signal peptides have enabled a wide range of studies of how these "zipcodes" for protein secretion are decoded and used to target proteins to the protein machinery that facilitates their translocation across and integration into membranes. We review research on how the information in signal sequences enables their passenger proteins to be correctly and efficiently localized. Synthetic signal peptides have made possible binding and crosslinking studies to explore how selectivity is achieved in recognition by the signal sequence-binding receptors, signal recognition particle, or SRP, which functions in all organisms, and SecA, which functions in prokaryotes and some organelles of prokaryotic origins. While progress has been made, the absence of atomic resolution structures for complexes of signal peptides and their receptors has definitely left many questions to be answered in the future.
Indexed as
Identifiers
What OpenQuestion holds
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.