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1 ity seeds)--the natural sources of ricin and abrin.
2 toxication operated by type 2 RIPs ricin and abrin.
4 whose B chains are believed to either have (abrin-a and abrin-d) or lack (abrin-b and abrin-c) the a
7 ant protein that occurs in several isoforms (abrin-a, abrin-b, abrin-c and abrin-d), whose B chains a
8 od and clinical matrices for the isoforms of abrin and also the closely related, less toxic Abrus pre
11 resistant to the Gal-binding lectins ricin, abrin, and modeccin and hypersensitive to the toxicity o
13 tivating proteins (RIPs) family (e.g. ricin, abrin) are potent cytotoxins showing a strong lethal act
15 in that occurs in several isoforms (abrin-a, abrin-b, abrin-c and abrin-d), whose B chains are believ
16 ccurs in several isoforms (abrin-a, abrin-b, abrin-c and abrin-d), whose B chains are believed to eit
18 preproabrin cDNA, tentatively identified as abrin-c, which was predicted to lack lectin activity, an
19 resulted in a dramatic increase of ricin or abrin cytotoxicity compared with control mock-treated ce
20 ins are believed to either have (abrin-a and abrin-d) or lack (abrin-b and abrin-c) the ability to bi
21 eral isoforms (abrin-a, abrin-b, abrin-c and abrin-d), whose B chains are believed to either have (ab
24 t enhanced the activities of ricin, RCA, and abrin II to different extents, thus improving the diagno
29 for targeted MS imaging of the toxic protein abrin, showing the presence of abrin-a in all compartmen
30 ted with magnetic beads coated with multiple abrin-specific antibodies, thereby concentrating and ext
32 -II family of plant proteins, such as ricin, abrin, viscumin, and volkensin was based on their affini