Results 1 to 10 of about 1,627 (114)

Canonical or noncanonical? Structural plasticity of serine protease-binding loops in Kunitz-STI protease inhibitors. [PDF]

Protein Sci, 2023
AbstractThe Kunitz‐Soybean Trypsin Inhibitor (Kunitz‐STI) family is a large family of proteins with most of its members being protease inhibitors. The versatility of the inhibitory profile and the structural plasticity of these proteins, make this family a promising scaffold for designing new multifunctional proteins.
Guerra Y, Armijos-Jaramillo V, Pons T, Tejera E, Berry C.   +4 more
europepmc   +6 more sources

Structures of a bi-functional Kunitz-type STI family inhibitor of serine and aspartic proteases: Could the aspartic protease inhibition have evolved from a canonical serine protease-binding loop? [PDF]

Journal of Structural Biology, 2016
Bi-functional inhibitors from the Kunitz-type soybean trypsin inhibitor (STI) family are glycosylated proteins able to inhibit serine and aspartic proteases. Here we report six crystal structures of the wild-type and a non-glycosylated mutant of the bifunctional inhibitor E3Ad obtained at different pH values and space groups.
Yasel Guerra, Pedro A. Valiente, Tirso Pons, Colin Berry, E. Rudiño-Piñera   +4 more
openalex   +5 more sources

Crystal Structure of Crataeva tapia Bark Protein (CrataBL) and Its Effect in Human Prostate Cancer Cell Lines. [PDF]

PLoS One, 2013
A protein isolated from the bark of Crataeva tapia (CrataBL) is both a Kunitz-type plant protease inhibitor and a lectin. We have determined the amino acid sequence and three-dimensional structure of CrataBL, as well as characterized its selected ...
Ferreira Rda S, Zhou D, Ferreira JG, Silva MC, Silva-Lucca RA, Mentele R, Paredes-Gamero EJ, Bertolin TC, Dos Santos Correia MT, Paiva PM, Gustchina A, Wlodawer A, Oliva ML.   +12 more
europepmc   +2 more sources

A Kunitz-type peptide from Dendroaspis polylepis venom as a simultaneous inhibitor of serine and cysteine proteases

Journal of Venomous Animals and Toxins including Tropical Diseases, 2020
Background: Proteases play an important role for the proper physiological functions of the most diverse organisms. When unregulated, they are associated with several pathologies.
R. Kodama, A. K. Kuniyoshi, Cristiane Castilho Fernandes da Silva, Daniela Cajado-Carvalho, Bruno Duzzi, D. C. Mariano, Daniel Carvalho Pimenta, R. Borges, Wilmar Dias da Silva, F. Portaro   +9 more
semanticscholar   +1 more source

Serine protease inhibitor kunitz-type 2 is downregulated in myelodysplastic syndromes and modulates cell-cell adhesion.

Stem Cells and Development, 2014
Myelodysplastic syndromes (MDS) are clonal disorders involving hematopoietic stem cells (HSC) characterized by ineffective hematopoiesis. In addition to HSC defects, a defective hematopoiesis supporting capacity of mesenchymal stromal cells (MSCs) in the
F. M. Roversi, M. Lopes, J. Machado-Neto, A. L. Longhini, A. Duarte, M. O. Baratti, Bruna Palodetto, Flávia Adolfo Corrocher, F. Pericole, P. M. Campos, P. Favaro, F. Traina, S. Saad   +12 more
semanticscholar   +1 more source

The Immunomodulatory Effect of IrSPI, a Tick Salivary Gland Serine Protease Inhibitor Involved in Ixodes ricinus Tick Feeding

bioRxiv, 2019
Ticks are strict hematophagous arthropods and are the most important vectors of pathogens affecting both domestic and wild animals worldwide. Moreover, they are second only to mosquitoes as vectors of human pathogens.
Adrien A Blisnick, Ladislav Šimo, C. Grillon, F. Fasani, Sébastien Brûlé, B. L. Le Bonniec, É. Prina, M. Marsot, A. Relmy, S. Blaise-Boisseau, J. Richardson, S. Bonnet   +11 more
semanticscholar   +1 more source

Inhibition of an active zymogen protease: The zymogen form of matriptase is regulated by HAI‑1 and HAI‑2.

Biochemical Journal, 2020
The membrane-bound serine protease matriptase belongs to a rare subset of serine proteases that display significant activity in the zymogen form. Matriptase is critically involved in epithelial differentiation and homeostasis, and insufficient regulation
Signe Skovbjerg, Lasse Holt-Danborg, Annika W Nonboe, Z. Hong, Ásdís K Frost, C. Schar, Cecilia C Thomas, L. Vitved, J. Jensen, L. K. Vogel   +9 more
semanticscholar   +1 more source

Structure of the recombinant BPTI/Kunitz-type inhibitor rShPI-1A from the marine invertebrate Stichodactyla helianthus.

Acta Crystallographica. Section F : Structural Biology and Crystallization Communications, 2012
The BPTI/Kunitz-type inhibitor family includes several extremely potent serine protease inhibitors. To date, the inhibitory mechanisms have only been studied for mammalian inhibitors. Here, the first crystal structure of a BPTI/Kunitz-type inhibitor from
R. García-Fernández, T. Pons, A. Meyer, M. Perbandt, Yamile González-González, D. Gil, M. de los Angeles Chávez, C. Betzel, L. Redecke   +8 more
semanticscholar   +1 more source

Fusion proteins comprising annexin V and Kunitz protease inhibitors are highly potent thrombogenic site-directed anticoagulants.

Blood, 2005
The anionic phospholipid, phosphatidyl-L-serine (PS), is sequestered in the inner layer of the plasma membrane in normal cells. Upon injury, activation, and apoptosis, PS becomes exposed on the surfaces of cells and sheds microparticles, which are ...
Hsiu‐Hui Chen, C. Vicente, Li He, D. Tollefsen, T. Wun   +4 more
semanticscholar   +1 more source

Adenovirus-mediated expression of tissue factor pathway inhibitor-2 inhibits endothelial cell migration and angiogenesis.

Arteriosclerosis, Thrombosis and Vascular Biology, 2006
OBJECTIVE Extracellular matrix (ECM) remodeling during angiogenesis is accomplished through plasmin-dependent pericellular proteolysis and through the action of matrix metalloproteinases (MMPs).
L. Ivanciu, R. Gerard, Haiwang Tang, F. Lupu, C. Lupu   +4 more
semanticscholar   +2 more sources