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luffin/vėžys

Nuoroda įrašoma į mainų sritį
StraipsniaiKlinikiniai tyrimaiPatentai
5 rezultatus

Differential response of human melanoma and Ehrlich ascites cells in vitro to the ribosome-inactivating protein luffin.

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The cytotoxicity and inhibitory effect on proliferation of the type 1 ribosome-inactivating protein luffin purified from the seeds of Luffa aegyptiaca were investigated both in human metastatic melanoma cells and in murine Ehrlich ascites tumour cells. Results indicate that luffin from the seeds of

Cloning and soluble expression of mature alpha-luffin from Luffa cylindrica and its antitumor activities in vitro.

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Luffin-a, a single-chain Type I ribosome-inactivating protein, which is known to be the most toxic of the luffin family and apparently possesses antitumor activity, was isolated from Luffa cylindrica seeds. In the present study, mature alpha-luffin was cloned from L. cylindrica and it was found that
A new ribosome-inactivating protein (RIP), sechiumin, was purified from the seeds of edible gourd, Sechium edule Swartz by gel-filtration and ion-exchange chromatography, with an apparent relative molecular mass of 27 kDa. It inhibits the protein synthesis of rabbit reticulocyte lysate strongly with

Synthesis and purification of a toxin-linked conjugate targeting epidermal growth factor receptor in Escherichia coli.

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Aberrant epidermal growth factor receptor (EGFR) signaling is a common feature of multiple tumor types, including glioblastoma (GBM). As such, EGFR has emerged as an attractive target for antitumor therapy. In the present study, we sought to develop an immunotoxin capable of specifically targeting
The aberrant signaling activation of vascular endothelial growth factor receptor (VEGFR) and urokinase plasminogen activator (uPA) is a common characteristic of many tumors, including lung cancer. Accordingly, VEGFR and uPA have emerged as attractive targets for tumor. KDR (Flk-1/VEGFR-2), a member
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