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helianthus/protease

הקישור נשמר בלוח
מאמריםניסויים קלינייםפטנטים
עמוד 1 מ 47 תוצאות

Evidence for the probable oil body association of a thiol-protease, leading to oleosin degradation in sunflower seedling cotyledons.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
The activity of a 65 kDa, cytosolic protease from sunflower seedling cotyledons coincides with the degradation of oleosins during seed germination. Further investigations carried out in this laboratory have demonstrated the probable association of a thiol-protease with oil bodies, leading to gradual
Matriptase, initially isolated from human breast cancer cells in culture, is a member of the emerging class of type II transmembrane serine proteases. Matriptase blockade could potentially modulate tumorigenesis and metastasis in vivo. Sunflower trypsin inhibitor-1 (1, SFTI-1), isolated from

Complete substitutional analysis of a sunflower trypsin inhibitor with different serine proteases.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
Here we present a method to simultaneously characterize and/or optimize both the binding loop towards the protease and a cysteine-stabilized scaffold. The small peptidic sunflower trypsin inhibitor (SFTI-1) was chosen as a model system for these experiments. The inhibitor was investigated for
Plant seed knottins, mainly from the Cucurbitacea family, and sunflower seed trypsin inhibitor (SFTI 1) are the most low-molecular canonical peptide inhibitors of serine proteases. High efficiency of inhibition of various serine proteases, structure rigidity together with the possibility of limited
Sunflower trypsin inhibitor-1 (SFTI-1), a natural 14-residue cyclic peptide, and some of its synthetic acyclic variants are potent protease inhibitors displaying peculiar inhibitory profiles. Here we describe the synthesis and use of affinity sorbents prepared by coupling SFTI-1 analogues to agarose
We report here the synthesis of a 14-amino acid long bicyclic peptide, previously isolated from sunflower seeds. This peptide, termed sunflower trypsin inhibitor (SFTI-1), is one of the most potent naturally occurring small-molecule trypsin inhibitors. In addition to inhibiting trypsin, the
The cross-linked enzyme aggregates (CLEAs) have numerous economic advantages in the industrial bio catalysis. In the present study, the multi CLEAs containing protease, catalase, and lipase from the sunflower seeds using starch as a cofeeder as well as bovine serum albumin (BSA) are designed and
Laskowski inhibitors regulate serine proteases by an intriguing mode of action that involves deceiving the protease into synthesizing a peptide bond. Studies exploring naturally occurring Laskowski inhibitors have uncovered several structural features that convey the inhibitor's resistance to

Two variants of the major serine protease inhibitor from the sea anemone Stichodactyla helianthus, expressed in Pichia pastoris.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
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 chymotrypsin, and human neutrophil elastase. We performed site-directed mutagenesis of ShPI-1 to produce two variants
The most potent known naturally occurring Bowman-Birk inhibitor, sunflower trypsin inhibitor-1 (SFTI-1), is a bicyclic 14-amino acid peptide from sunflower seeds comprising one disulfide bond and a cyclic backbone. At present, little is known about the cyclization mechanism of SFTI-1. We show here

Differential sensitivity of oleosins to proteolysis during oil body mobilization in sunflower seedlings.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
Until now, there has been no conclusive demonstration of any in vivo oleosin degradation at the early stages of oil body mobilization. The present work on sunflower (Helianthus annuus L.) has demonstrated limited oleosin degradation during seed germination. Seedling cotyledon homogenization in

Oil body mobilization in sunflower seedlings is potentially regulated by thioredoxin h.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
Thioredoxins are believed to mediate starch and protein mobilization in germinating cereals and dicotyledons. Nothing is known about redox regulation of lipid mobilization in plants. The possible redox regulation by thioredoxin h (Trx h) of a thiol-protease which degrades the oleosin coat of the oil

A new family of beta-hairpin mimetics based on a trypsin inhibitor from sunflower seeds.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
The ability of proteases to regulate many aspects of cell function and defense accounts for the considerable interest in the design of novel protease inhibitors. There are many naturally occurring proteinaceous serine protease inhibitors, one of which is a 14 amino acid cyclic peptide from sunflower

Engineering potent mesotrypsin inhibitors based on the plant-derived cyclic peptide, sunflower trypsin inhibitor-1.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
Plants produce a diverse range of peptides and proteins that inhibit the activity of different serine proteases. The value of these inhibitors not only stems from their native role(s) in planta, but they are also regarded as promising templates for inhibitor engineering. Interest in this field has

Highly Potent and Selective Plasmin Inhibitors Based on the Sunflower Trypsin Inhibitor-1 Scaffold Attenuate Fibrinolysis in Plasma.

רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
Antifibrinolytic drugs provide important pharmacological interventions to reduce morbidity and mortality from excessive bleeding during surgery and after trauma. Current drugs used for inhibiting the dissolution of fibrin, the main structural component of blood clots, are associated with adverse
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