ArticleMarine drugs2015
New Kunitz-Type HCRG Polypeptides from the Sea Anemone Heteractis crispa.
Article in Marine drugs, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.
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
19 citing papers in PubMed, 1 synthesis or guideline pooled it, 34 citations in OpenAlex.
- Pooled it
- Cnidarian Venoms in the Omics Era: Toxin Discovery and Bioactive Potential.Marine drugs · 2026Review
- Insulin Resistance, Anti-inflammatory, and AntioxidantBiotechnology reports (Amsterdam, Netherlands) · 2026Article
- Anthozoan Chemical Defenses: Integrating Compounds, Enzymatic Activities, and Omics-Based Discoveries.International journal of molecular sciences · 2025Review
- Sea Anemone Kunitz Peptide HCIQ2c1 Reduces Histamine-, Lipopolysaccharide-, and Carrageenan-Induced Inflammation via the Suppression of Pro-Inflammatory Mediators.International journal of molecular sciences · 2025Article
- Sea Anemone Kunitz Peptide HCIQ2c1: Structure, Modulation of TRPA1 Channel, and Suppression of Nociceptive Reaction In Vivo.Marine drugs · 2024Article
- Diversity analysis of sea anemone peptide toxins in different tissues of Heteractis crispa based on transcriptomics.Scientific reports · 2024Article
- Spatial Distribution and Biochemical Characterization of Serine Peptidase Inhibitors in the Venom of the Brazilian Sea AnemoneMarine drugs · 2023Article
- Recombinant Analogs of Sea Anemone Kunitz-Type Peptides Influence P2X7 Receptor Activity in Neuro-2a Cells.Marine drugs · 2023Article
- First Anti-Inflammatory Peptide AnmTX Sco 9a-1 from the Swimming Sea AnemoneBiomolecules · 2022Article
- Molecular and Functional Characterization of a Novel Kunitz-Type Toxin-like Peptide in the Giant Triton SnailMarine drugs · 2022Article
- Deep-Sea Anemones Are Prospective Source of New Antimicrobial and Cytotoxic Compounds.Marine drugs · 2021Article
- Sea Anemone Kunitz-Type Peptides Demonstrate Neuroprotective Activity in the 6-Hydroxydopamine Induced Neurotoxicity Model.Biomedicines · 2021Article
- Kunitz-Type Peptides from the Sea AnemoneBiomedicines · 2020Article
- A Review of Toxins from Cnidaria.Marine drugs · 2020Review
- A new multigene HCIQ subfamily from the sea anemone Heteractis crispa encodes Kunitz-peptides exhibiting neuroprotective activity against 6-hydroxydopamine.Scientific reports · 2020Article
- Peripheral 5-HT3 Receptors Are Involved in the Antinociceptive Effect of Bunodosine 391.Toxins · 2017Article
- Kunitz-Type Peptide HCRG21 from the Sea Anemone Heteractis crispa Is a Full Antagonist of the TRPV1 Receptor.Marine drugs · 2016Article
- The Kunitz-Type Protein ShPI-1 Inhibits Serine Proteases and Voltage-Gated Potassium Channels.Toxins · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sea anemones are a rich source of Kunitz-type polypeptides that possess not only protease inhibitor activity, but also Kv channels toxicity, analgesic, antihistamine, and anti-inflammatory activities. Two Kunitz-type inhibitors belonging to a new Heteractis crispa RG (HCRG) polypeptide subfamily have been isolated from the sea anemone Heteractis crispa. The amino acid sequences of HCRG1 and HCRG2 identified using the Edman degradation method share up to 95% of their identity with the representatives of the HCGS polypeptide multigene subfamily derived from H. crispa cDNA. Polypeptides are characterized by positively charged Arg at the N-terminus as well as P1 Lys residue at their canonical binding loop, identical to those of bovine pancreatic trypsin inhibitor (BPTI). These polypeptides are shown by our current evidence to be more potent inhibitors of trypsin than the known representatives of the HCGS subfamily with P1Thr. The kinetic and thermodynamic characteristics of the intermolecular interactions between inhibitors and serine proteases were determined by the surface plasmon resonance (SPR) method. Residues functionally important for polypeptide binding to trypsin were revealed using molecular modeling methods. Furthermore, HCRG1 and HCRG2 possess anti-inflammatory activity, reducing tumor necrosis factor-α (TNF-α) and interleukin 6 (IL-6) secretions, as well as proIL-1β expression in lipopolysaccharide (LPS)-activated macrophages. However, there was no effect on nitric oxide (NO) generation.
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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.