ReviewProtein science : a publication of the Protein Society2012
Signal peptidase I: cleaving the way to mature proteins.
Review in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.
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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
100 citing papers in PubMed, 187 citations in OpenAlex.
- Mechanistic insights into the degradation of poly (3-hydroxybutyrate) and its copolymers by Nocardiopsis dassonvillei NCIM 5124.Molecular biology reports · 2026Article
- Review
- Genome-wide prediction of secretory proteins in Ceratocystis paradoxa and expression analysis of effectors during early infection.BMC microbiology · 2026Article
- Co-opting the bacterial lipoprotein pathway for the biosynthesis of lipidated macrocyclic peptides.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Native Mass Spectrometry-Based Proteomics Reveals the Mechanism of Hemophore Release by PathogenicbioRxiv : the preprint server for biology · 2026Article
- The Signal Peptidase MoSpc2 Orchestrates Fungal Development, Protein Secretion and Pathogenicity in Magnaporthe oryzae.Rice (New York, N.Y.) · 2025Article
- Molecular interplay between peptidoglycan integrity and outer membrane asymmetry in maintaining cell envelope homeostasis.Journal of bacteriology · 2025Article
- Protein Translocation Control inBiomolecules · 2025Article
- Dynamic nature of Staphylococcus aureus type I signal peptidases.Biophysical journal · 2025Article
- Mapping the ultrastructural topology of the corynebacterial cell surface.PLoS biology · 2025Article
- Tat-fimbriae ("tafi"): An unusual type of haloarchaeal surface structure depending on the twin-arginine translocation pathway.iScience · 2025Article
- OXA β-lactamases frommBio · 2025Article
- The Unique Capability of Endolysin to Tackle Antibiotic Resistance: Cracking the Barrier.Journal of xenobiotics · 2025Review
- Lipoprotein Signal Peptide as Adjuvants: Leveraging Lipobox-Driven TLR2 Activation in Modern Vaccine Design.Vaccines · 2025Review
- Heterologous protein exposure and secretion optimization in Mycoplasma pneumoniae.Microbial cell factories · 2024Article
- OXA β-lactamases frombioRxiv : the preprint server for biology · 2024Article
- The Salmonella enterica EnvE is an Outer Membrane Lipoprotein and Its Gene Expression Leads to Transcriptional Repression of the Virulence Gene msgA.Journal of microbiology (Seoul, Korea) · 2024Article
- Expression, purification, and characterization of diacylated Lipo-YcjN frombioRxiv : the preprint server for biology · 2024Article
- Membrane RRM2-positive cells represent a malignant population with cancer stem cell features in intrahepatic cholangiocarcinoma.Journal of experimental & clinical cancer research : CR · 2024Article
- The Freshwater CyanobacteriumPlants (Basel, Switzerland) · 2024Article
40 more citing papers are in PubMed but not listed here.
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
Signal peptidase I (SPase I) is critical for the release of translocated preproteins from the membrane as they are transported from a cytoplasmic site of synthesis to extracytoplasmic locations. These proteins are synthesized with an amino-terminal extension, the signal sequence, which directs the preprotein to the Sec- or Tat-translocation pathway. Recent evidence indicates that the SPase I cleaves preproteins as they emerge from either pathway, though the steps involved are unclear. Now that the structure of many translocation pathway components has been elucidated, it is critical to determine how these components work in concert to support protein translocation and cleavage. Molecular modeling and NMR studies have provided insight on how the preprotein docks on SPase I in preparation for cleavage. This is a key area for future work since SPase I enzymes in a variety of species have now been identified and the inhibition of these enzymes by antibiotics is being pursued. The eubacterial SPase I is essential for cell viability and belongs to a unique group of serine endoproteases which utilize a Ser-Lys catalytic dyad instead of the prototypical Ser-His-Asp triad used by eukaryotes. As such, SPase I is a desirable antimicrobial target. Advances in our understanding of how the preprotein interfaces with SPase I during the final stages of translocation will facilitate future development of inhibitors that display a high efficacy against SPase I function.
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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.