Results 71 to 80 of about 155,063 (214)

New Kunitz-Type HCRG Polypeptides from the Sea Anemone Heteractis crispa

open access: yesMarine Drugs, 2015
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.
Irina Gladkikh   +8 more
doaj   +1 more source

Chamber‐Specific Decellularized Extracellular Matrices Differentially Modulate Cardiomyocyte Subtypes to Drive Engineered Heart Tissue Development and Function

open access: yesAdvanced Healthcare Materials, EarlyView.
Chamber‐specific decellularized extracellular matrices (ECMs) were developed, preserving native proteomic profiles of ventricular and atrial myocardium. These innate biochemical cues differentially modulate cardiomyocyte subtypes to drive engineered heart tissue development and function, highlighting the importance of incorporating regional ECM cues in
Dong Gyu Hwang   +7 more
wiley   +1 more source

Coaxially Electrospun Myocardial dECM‐ Based Nanofibrous Scaffolds Demonstrate Enhanced Cardiomyocyte Biocompatibility

open access: yesAdvanced Healthcare Materials, EarlyView.
Our coaxial electrospinning system is capable of incorporating decellularized myocardial extracellular matrix in a core‐sheath configuration, creating nanofibrous scaffolds. These scaffolds, in turn, support the maintenance of functional cardiomyocytes adhered to the surface of these bioactive scaffolds.
Dhanusha N. Rajapakse   +9 more
wiley   +1 more source

Avaliação biológica de soja com baixas atividades de inibidores de tripsina e ausência do inibidor Kunitz

open access: yesArchivos Latinoamericanos de Nutrición, 2001
Cultivar de soja BR 36 com atividades de inibidores de tripsina convencional e linhagem BRM 95-5262, geneticamente modificadas para conter baixas atividades de inibidores de tripsina, contendo 40 e 20 e 30 e 20% de atividades residuais relativa de ...
Edna Mayumi Yuahasi Miura   +4 more
doaj  

Dietary wheat amylase trypsin inhibitors exacerbate CNS inflammation in experimental multiple sclerosis. [PDF]

open access: yesGut, 2023
Zevallos VF   +14 more
europepmc   +1 more source

Flash Assembloids: A Rapid Biofabrication of a Platform for Modeling Early Glioblastoma Invasion at the Glioblastoma–Brain Organoid Interfaces

open access: yesAdvanced Healthcare Materials, EarlyView.
This study presents a bioengineered assembloid (ASM) system combining glioblastoma (GBM) cells in oxidized alginate (OA) microgels with dorsal organoids (DOs). This model simulates brain tumor‐host interactions, revealing enhanced GBM invasion, altered gene expression, and aggressive infiltration patterns, demonstrating ASM as a valuable platform for ...
Chao Liang   +17 more
wiley   +1 more source

Crystal structure of Kunitz-type trypsin inhibitor: Entomotoxic effect of native and encapsulated protein targeting gut trypsin of Tribolium castaneum Herbst

open access: yesComputational and Structural Biotechnology Journal
Trypsin inhibitors are known to act against insect pests by inhibiting proteases of the digestive tract. In this study, we report structural and functional characterization of ∼ 19 kDa Albizia procera Kunitz-type trypsin inhibitor (ApKTI) protein with ...
Sohaib Mehmood   +11 more
doaj   +1 more source

Improving the understanding of plasma kallikrein contribution to arterial thrombus formation using two plant protease inhibitors

open access: yesPlatelets, 2019
The purpose of antithrombotic therapy is the prevention of thrombus formation and/or its extension with a minimum risk of bleeding. The inhibition of a variety of proteolytic processes, particularly those of the coagulation cascade, has been reported as ...
Bruno R Salu   +10 more
doaj   +1 more source

Protease Inhibitors from Marine Venomous Animals and Their Counterparts in Terrestrial Venomous Animals

open access: yesMarine Drugs, 2013
The Kunitz-type protease inhibitors are the best-characterized family of serine protease inhibitors, probably due to their abundance in several organisms.
Caroline B. F. Mourão   +1 more
doaj   +1 more source

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