Evolutionary aspects of the structural convergence and functional diversification of Kunitz-domain inhibitors
M Mishra - Journal of Molecular Evolution, 2020 - Springer
Kunitz-type domains are ubiquitously found in natural systems as serine protease inhibitors
or animal toxins in venomous animals. Kunitz motif is a cysteine-rich peptide chain of~ 60 …
or animal toxins in venomous animals. Kunitz motif is a cysteine-rich peptide chain of~ 60 …
The Kunitz-type protein ShPI-1 inhibits serine proteases and voltage-gated potassium channels
The bovine pancreatic trypsin inhibitor (BPTI)-Kunitz-type protein ShPI-1 (UniProt: P31713)
is the major protease inhibitor from the sea anemone Stichodactyla helianthus. This …
is the major protease inhibitor from the sea anemone Stichodactyla helianthus. This …
Diversity analysis of sea anemone peptide toxins in different tissues of Heteractis crispa based on transcriptomics
Q Guo, J Fu, L Yuan, Y Liao, M Li, X Li, B Yi, J Zhang… - Scientific Reports, 2024 - nature.com
Peptide toxins found in sea anemones venom have diverse properties that make them
important research subjects in the fields of pharmacology, neuroscience and biotechnology …
important research subjects in the fields of pharmacology, neuroscience and biotechnology …
Structural and functional characterization of complex formation between two Kunitz-type serine protease inhibitors from Russell's Viper venom
Snake venom Kunitz-type serine protease inhibitors (KSPIs) exhibit various biological
functions including anticoagulant activity. This study elucidates the occurrence and subunit …
functions including anticoagulant activity. This study elucidates the occurrence and subunit …
Structure–Activity Relationship and Molecular Docking of a Kunitz-Like Trypsin Inhibitor, Kunitzin-AH, from the Skin Secretion of Amolops hainanensis
Y Chen, X Xi, C Ma, M Zhou, X Chen, Z Ye, L Ge, Q Wu… - Pharmaceutics, 2021 - mdpi.com
Kunitz-like trypsin inhibitors are one of the most noteworthy research objects owing to their
significance in pharmacological studies, including anticarcinogenic activity, obesity …
significance in pharmacological studies, including anticarcinogenic activity, obesity …
The structural universe of disulfide-rich venom peptides
Animal venoms are heterogenous composite secretions designed for predatory and
defensive purposes. Their function is to disrupt homeostasis in target organisms following …
defensive purposes. Their function is to disrupt homeostasis in target organisms following …
Structural features of cysteine-rich polypeptides from sea anemone venoms
At present, the discovery of drugs based on animal venoms undergoes its rebirth:
pharmaceutical companies start to accept gradually the potential of animal venoms as …
pharmaceutical companies start to accept gradually the potential of animal venoms as …
Therapeutic applications of spider-venom peptides
As a result of competition between species, a multitude of physical adaptations have
emerged that confer an evolutionary bene t to the animals that possess them. One …
emerged that confer an evolutionary bene t to the animals that possess them. One …
Three-dimensional Structure of a Kunitz-type Inhibitor in Complex with an Elastase-like Enzyme
R García-Fernández, M Perbandt, D Rehders… - Journal of Biological …, 2015 - ASBMB
Elastase-like enzymes are involved in important diseases such as acute pancreatitis,
chronic inflammatory lung diseases, and cancer. Structural insights into their interaction with …
chronic inflammatory lung diseases, and cancer. Structural insights into their interaction with …
Two variants of the major serine protease inhibitor from the sea anemone Stichodactyla helianthus, expressed in Pichia pastoris
R García-Fernández, P Ziegelmüller, L González… - Protein Expression and …, 2016 - Elsevier
The major protease inhibitor from the sea anemone Stichodactyla helianthus (ShPI-1) is a
non-specific inhibitor that binds trypsin and other trypsin-like enzymes, as well as …
non-specific inhibitor that binds trypsin and other trypsin-like enzymes, as well as …