Canonical protein inhibitors of serine proteases

D Krowarsch, T Cierpicki, F Jelen, J Otlewski - Cellular and molecular life …, 2003 - Springer
Serine proteases and their natural protein inhibitors are among the most intensively studied
protein complexes. About 20 structurally diverse inhibitor families have been identified …

The bovine basic pancreatic trypsin inhibitor (Kunitz inhibitor): a milestone protein

P Ascenzi, A Bocedi, M Bolognesi… - Current Protein and …, 2003 - ingentaconnect.com
The pancreatic Kunitz inhibitor, also known as aprotinin, bovine basic pancreatic trypsin
inhibitor (BPTI), and trypsin-kallikrein inhibitor, is one of the most extensively studied …

Predicting free energy changes using structural ensembles

A Benedix, CM Becker, BL de Groot, A Caflisch… - Nature …, 2009 - nature.com
To the Editor: Reliable and fast computation of protein free energy is crucial for protein-
structure analysis, structure-based protein design and protein docking. Rigorous treatments …

Structure and function of invertebrate Kunitz serine protease inhibitors

S Ranasinghe, DP McManus - Developmental & Comparative Immunology, 2013 - Elsevier
Kunitz type proteins are an important group of ubiquitous protease inhibitors found spanning
the evolutionary tree from microbes to mammals. These proteins can have single or multiple …

Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates

ES Radisky, JM Lee, CJK Lu… - Proceedings of the …, 2006 - National Acad Sciences
Atomic resolution structures of trypsin acyl-enzymes and a tetrahedral intermediate analog,
along with previously solved structures representing the Michaelis complex, are used to …

Antimicrobial peptides with stability toward tryptic degradation

J Svenson, W Stensen, BO Brandsdal, BE Haug… - Biochemistry, 2008 - ACS Publications
The inherent instability of peptides toward metabolic degradation is an obstacle on the way
toward bringing potential peptide drugs onto the market. Truncation can be one way to …

[HTML][HTML] Isolation, cloning and structural characterisation of boophilin, a multifunctional Kunitz-type proteinase inhibitor from the cattle tick

S Macedo-Ribeiro, C Almeida, BM Calisto, T Friedrich… - PLoS …, 2008 - journals.plos.org
Inhibitors of coagulation factors from blood-feeding animals display a wide variety of
structural motifs and inhibition mechanisms. We have isolated a novel inhibitor from the …

[HTML][HTML] Serine protease inhibitors in ticks: an overview of their role in tick biology and tick-borne pathogen transmission

AA Blisnick, T Foulon, SI Bonnet - Frontiers in Cellular and Infection …, 2017 - frontiersin.org
New tick and tick-borne pathogen control approaches that are both environmentally
sustainable and which provide broad protection are urgently needed. Their development …

The cathepsin-like cysteine peptidases of trematodes of the genus Fasciola

K Cwiklinski, S Donnelly, O Drysdale, H Jewhurst… - Advances in …, 2019 - Elsevier
Fasciolosis caused by trematode parasites of the genus Fasciola is a global disease of
livestock, particularly cattle, sheep, water buffalo and goats. It is also a major human …

Structure, function and biology of tissue factor pathway inhibitor-2

HS Chand, DC Foster, W Kisiel - Thrombosis and haemostasis, 2005 - thieme-connect.com
Tissue factor pathway inhibitor-2 (TFPI-2) is a 32 kDa matrix-associated Kunitz-type serine
proteinase inhibitor consisting of a short amino-terminal region, three tandem Kunitz-type …