ReviewEuropean biophysics journal : EBJ2013
Structure-function correlations of pulmonary surfactant protein SP-B and the saposin-like family of proteins.
Review in European biophysics journal : EBJ, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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.
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Who cites it
29 citing papers in PubMed, 82 citations in OpenAlex.
- Surfactant protein SP-B: one ring to rule the molecular and biophysical mechanisms of the pulmonary surfactant system.Biophysical reviews · 2025Review
- The proteotranscriptomic characterization of venom in the white seafanOpen biology · 2025Article
- Bacterial expression, purification and folding of exceptionally hydrophobic and essential protein: Surfactant Protein-B (SP-B).PloS one · 2025Article
- Effect of Nk-lysin peptides on bacterial growth, MIC, antimicrobial resistance, and viral activities.Animal biotechnology · 2024Article
- Immature Surfactant Protein B Increases in the Serum of Patients with Calcific Severe Aortic Stenosis.International journal of molecular sciences · 2024Article
- Phospholipase activity of acyloxyacyl hydrolase induces IL-22-producing CD1a-autoreactive T cells in individuals with psoriasis.European journal of immunology · 2022Article
- Pulmonary surfactant as a versatile biomaterial to fight COVID-19.Journal of controlled release : official journal of the Controlled Release Society · 2022Review
- Emulation of the structure of the Saposin protein fold by a lung surfactant peptide construct of surfactant Protein B.PloS one · 2022Article
- Expression and biological functions of Ancylostoma ceylanicum saposin-like protein.Parasitology research · 2021Article
- Pulmonary siRNA delivery for lung disease: Review of recent progress and challenges.Journal of controlled release : official journal of the Controlled Release Society · 2021Review
- Characterization of transcription profile and structural properties of avian NK-lysin.Poultry science · 2020Article
- All-Atom Molecular Dynamics Simulations of Dimeric Lung Surfactant Protein B in Lipid Multilayers.International journal of molecular sciences · 2019Article
- Functional Reconstitution of HlyB, a Type I Secretion ABC Transporter, in Saposin-A Nanoparticles.Scientific reports · 2019Article
- Antiviral Activity of a Turbot (Marine drugs · 2019Article
- Review
- Role of lipid transfer proteins in loading CD1 antigen-presenting molecules.Journal of lipid research · 2018Review
- Homo- and hetero-oligomerization of hydrophobic pulmonary surfactant proteins SP-B and SP-C in surfactant phospholipid membranes.The Journal of biological chemistry · 2018Article
- Structural basis for the activation of acid ceramidase.Nature communications · 2018Article
- Crystal structure of the mammalian lipopolysaccharide detoxifier.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- How α-Helical Motifs Form Functionally Diverse Lipid-Binding Compartments.Annual review of biochemistry · 2017Review
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
No grant is acknowledged in the PubMed record.
Abstract
Pulmonary surfactant is a lipid-protein complex secreted by the respiratory epithelium of mammalian lungs, which plays an essential role in stabilising the alveolar surface and so reducing the work of breathing. The surfactant protein SP-B is part of this complex, and is strictly required for the assembly of pulmonary surfactant and its extracellular development to form stable surface-active films at the air-liquid alveolar interface, making the lack of SP-B incompatible with life. In spite of its physiological importance, a model for the structure and the mechanism of action of SP-B is still needed. The sequence of SP-B is homologous to that of the saposin-like family of proteins, which are membrane-interacting polypeptides with apparently diverging activities, from the co-lipase action of saposins to facilitate the degradation of sphingolipids in the lysosomes to the cytolytic actions of some antibiotic proteins, such as NK-lysin and granulysin or the amoebapore of Entamoeba histolytica. Numerous studies on the interactions of these proteins with membranes have still not explained how a similar sequence and a potentially related fold can sustain such apparently different activities. In the present review, we have summarised the most relevant features of the structure, lipid-protein and protein-protein interactions of SP-B and the saposin-like family of proteins, as a basis to propose an integrated model and a common mechanistic framework of the apparent functional versatility of the saposin fold.
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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.