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Saporin / ˈ s æ p ə r ɪ n / is a protein that is useful in biological research applications, especially studies of behavior. Saporins are so-called ribosome inactivating proteins (RIPs), due to its N-glycosidase activity, from the seeds of Saponaria officinalis (common name: soapwort).
A ribosome-inactivating protein (RIP) is a protein synthesis inhibitor that acts at the eukaryotic ribosome. [2] This protein family describes a large family of such proteins that work by acting as rRNA N-glycosylase (EC 3.2.2.22).
Cellular thermal shift assay (CETSA ®) [29] is a biophysical technique applicable on living cells as well as tissue biopsies. CETSA ® is based on the discovery that protein melting curves can also be generated in intact cells and that drug binding leads to very significant thermal stabilization of proteins. Upon denaturation, proteins are ...
CEllular Thermal Shift Assay (CETSA ®) is a patented label free chemoproteomics method that has enabled measurements of compound target engagement in intact cells and tissue, without modifications to the target protein. This is accomplished by comparing the measured cellular thermal stability of the protein in the presence and absence of the ...
Upon binding to a ligand, a protein's thermal stability is expected to increase, so ligand-bound proteins will be more resistant to thermal denaturation. After heating, the amount of non-denatured protein remaining is analyzed using quantitative proteomics and stability curves are generated.
Shiga toxins act to inhibit protein synthesis within target cells by a mechanism similar to that of the infamous plant toxin ricin. [ 19 ] [ 20 ] After entering a cell via a macropinosome , [ 21 ] the payload (A subunit) cleaves a specific adenine nucleobase from the 28S RNA of the 60S subunit of the ribosome , thereby halting protein synthesis ...
A ribosome-inactivating protein produced by the mold Aspergillus giganteus, alpha-sarcin cleaves the portion of ribosomal RNA that forms the small ribosomal substrate. The high specificity of alpha-sarcin and its efficiency of cleavage are point of study and also account for this protein's very high toxicity level. [2]
Ricin is the best known representative of the ribosomal inactivating protein (RIP) family. [22] RIPs are also highly specialized toxic proteins produced by plants and fungi that inactivate ribosomes acting as N-glycosidases. Its target is found in the same singular structure of the rRNA that is attacked by ribotoxins.