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23S rRNA + H2O
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Substrates: cleavage of sarcin-ricin loop of 23S rRNA inhibits in vitro translation, slightly affects binding of elongation factor Tu ternary complex to the ribosome, inhibits elongation factor G binding, and consequently GTP hydrolysis and mRNA-tRNA translocation
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23S rRNA containing guanosine-adenosine pair + H2O
an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment]
Substrates: -
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28 S rRNA + H2O
alpha-fragment from the 3' end of 28S rRNA
70S ribosomes + H2O
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Substrates: -
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ApA + H2O
3'-AMP + adenosine
CpC + H2O
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Substrates: -
Products: -
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Escherichia coli 23S rRNA containing guanosine-adenosine pair + H2O
an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment]
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Substrates: -
Products: -
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Escherichia coli 28S rRNA containing guanosine-adenosine pair + H2O
an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment]
high-molecular-weight yeast RNA + H2O
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poly(A) + H2O
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Substrates: -
Products: -
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rabbit 28S rRNA containing guanosine-adenosine pair + H2O
an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment]
Substrates: -
Products: -
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rabbit reticulocyte 28S rRNA containing guanosine-adenosine pair + H2O
an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment]
Substrates: -
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rabbit ribosomes + H2O
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Substrates: ribosomes isolated from reticulocyte lysate
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Rattus norvegicus 28S rRNA containing guanosine-adenosine pair + H2O
an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment]
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Substrates: alpha-sarcin hydrolyzes a phosphodiester bond on the 3' side of a guanine residue 393 nucleotides from the 3' end. The alpha-sarcin domain is composed of a purine-rich sequence of 14 highly conserved nucleotides
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ribosomes + H2O
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Substrates: -
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Saccharomyces cerevisiae 28S rRNA containing guanosine-adenosine pair + H2O
an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment]
Saccharomyces cerevisiae rRNA containing guanosine-adenosine pair + H2O
an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment]
Substrates: -
Products: -
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sarcin ribosomal loop rRNA + H2O
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Substrates: alpha-sarcin shows specific ribonucleolytic activity against just one single rRNA phosphodiester bond, located at the sarcin-ricin loop (SRL) of the larger rRNA
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sarcin/ricin ribosomal loop RNA + H2O
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Substrates: -
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SRL + H2O
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Substrates: sarcin/ricin loop in ribosomal RNA
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supercoiled double-stranded DNA + H2O
nicked circular conformation of DNA
yeast 25S RNA + H2O
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-
Substrates: -
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yeast 26 S RNA + H2O
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Substrates: alpha-sarcin cleaves the phosphodiester bond between the guanine residue at position 3025 and the adenine residue at position 3026
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additional information
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28 S rRNA + H2O

alpha-fragment from the 3' end of 28S rRNA
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Substrates: rat liver 28S rRNA
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28 S rRNA + H2O
alpha-fragment from the 3' end of 28S rRNA
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Substrates: -
Products: -
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28 S rRNA + H2O
alpha-fragment from the 3' end of 28S rRNA
Substrates: -
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28 S rRNA + H2O
alpha-fragment from the 3' end of 28S rRNA
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Substrates: human rhabdomyosarcoma 28S rRNA
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28 S rRNA + H2O
alpha-fragment from the 3' end of 28S rRNA
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Substrates: mini-stem-loop RNA
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28 S rRNA + H2O
alpha-fragment from the 3' end of 28S rRNA
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Substrates: rat liver 28S rRNA
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28 S rRNA + H2O
alpha-fragment from the 3' end of 28S rRNA
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Substrates: -
Products: -
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28 S rRNA + H2O
alpha-fragment from the 3' end of 28S rRNA
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Substrates: rat liver 28S rRNA
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28 S rRNA + H2O
alpha-fragment from the 3' end of 28S rRNA
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Substrates: human rhabdomyosarcoma 28S rRNA
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ApA + H2O

3'-AMP + adenosine
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Substrates: -
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ApA + H2O
3'-AMP + adenosine
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Substrates: reaction of alpha-sarcin on ApA is composed of 2 steps, transphosphorylation adenosine + 2',3'-cyclic adenosine monophosphate are the reaction products, followed by hydrolysis of the cyclic mononucleotide, producing 3'-AMP
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ApA + H2O
3'-AMP + adenosine
Substrates: -
Products: -
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ApA + H2O
3'-AMP + adenosine
-
Substrates: -
Products: -
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Escherichia coli 28S rRNA containing guanosine-adenosine pair + H2O

an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment]
Substrates: -
Products: -
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Escherichia coli 28S rRNA containing guanosine-adenosine pair + H2O
an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment]
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Substrates: -
Products: -
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Escherichia coli 28S rRNA containing guanosine-adenosine pair + H2O
an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment]
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Substrates: -
Products: -
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GpA + H2O

3'-GMP
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Substrates: hydrolysis of the 3'-5' phosphodiester bond of the substrate yields 2',3'-cyclic adenosine mononucleotide, this intermediate is converted into the corresponding 3'-monophosphate derivative as the final product of the reaction
Products: -
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GpA + H2O
3'-GMP
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Substrates: hydrolysis of the 3'-5' phosphodiester bond of the substrate yields 2',3'-cyclic adenosine mononucleotide, this intermediate is converted into the corresponding 3'-monophosphate derivative as the final product of the reaction
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high-molecular-weight yeast RNA + H2O

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Substrates: -
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high-molecular-weight yeast RNA + H2O
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Substrates: ribonuclease activity
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high-molecular-weight yeast RNA + H2O
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Substrates: ribonuclease activity
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pUC18 plasmid + H2O

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Substrates: -
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pUC18 plasmid + H2O
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Substrates: nicking endonuclease activity
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pUC18 plasmid + H2O
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Substrates: nicking endonuclease activity
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RNA + H2O

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Substrates: -
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RNA + H2O
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Substrates: hydrolyzes naked RNA at purines in both single-and double-stranded regions
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RNA + H2O
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Substrates: hydrolyzes naked RNA at purines in both single-and double-stranded regions
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RNA + H2O
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Substrates: with total rRNA as substrate alpha-sarcin causes extensive progressive digestion of nucleic acids
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rRNA + H2O

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646298, 646299, 646300, 646301, 646302, 646303, 646304, 646305, 646306, 646307, 646308, 646309, 646310, 646311, 646312 Substrates: -
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rRNA + H2O
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Substrates: -
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rRNA + H2O
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-
Substrates: -
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rRNA + H2O
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Substrates: -
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rRNA + H2O
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-
Substrates: -
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rRNA + H2O
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-
Substrates: -
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rRNA + H2O
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Substrates: -
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Saccharomyces cerevisiae 28S rRNA containing guanosine-adenosine pair + H2O

an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment]
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Substrates: -
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Saccharomyces cerevisiae 28S rRNA containing guanosine-adenosine pair + H2O
an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment]
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Substrates: -
Products: -
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supercoiled double-stranded DNA + H2O

nicked circular conformation of DNA
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Substrates: no effect on linear DNA
Products: at low concentrations, further into a linear form at high concentrations
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supercoiled double-stranded DNA + H2O
nicked circular conformation of DNA
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Substrates: -
Products: -
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additional information

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Substrates: alpha-sarcin cleavage site lies between a guanosine and adenosine residue in the sequence AGUACGAG AGGAAG
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additional information
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Substrates: specific ribonuclease activity against ribosomal RNA causes ribosome disruption and subsequent protein biosynthesis inhibition
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additional information
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Substrates: major type II ribotoxin
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additional information
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Substrates: mechanism of action is hydrolysis of a phosphodiester bond between G-4325 and A-4326 of rat 28S ribosomal RNA producing an alpha-fragment from the 3' end of 28S rRNA
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additional information
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Substrates: alpha-sarcin modifies neighbouring sites in the sarcin/ricin loop of 28S rRNA, destroying the necessary dynamic flexibility of the ribosome, inhibiting the elongation factor assisted steps of the elongation cycle
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additional information
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Substrates: induction of cell death via apoptosis
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additional information
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Substrates: deletion mutant delta(7-22) exhibits activity against naked rRNA and synthetic substrates but lacks the specific ability of the wild-type protein to degrade rRNA in intact ribosomes
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additional information
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Substrates: arginine 121 is a crucial residue for the specific cytotoxic activity of alpha-sarcin
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additional information
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Substrates: acts as a cyclizing ribonuclease
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additional information
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Substrates: acts as a cyclizing ribonuclease
Products: -
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additional information
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Substrates: acts as a cyclizing ribonuclease
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additional information
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Substrates: alpha-sarcin site nucleotide sequence is identical in the large rRNAs of cytoplasmic ribosomes from a range of evolutionary diverse organisms, evolutionarily conserved in all eukaryotes and prokaryotes so far tested
Products: -
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additional information
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Substrates: alpha-sarcin site nucleotide sequence is identical in the large rRNAs of cytoplasmic ribosomes from a range of evolutionary diverse organisms, evolutionarily conserved in all eukaryotes and prokaryotes so far tested
Products: -
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additional information
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Substrates: alpha-sarcin site nucleotide sequence is identical in the large rRNAs of cytoplasmic ribosomes from a range of evolutionary diverse organisms, evolutionarily conserved in all eukaryotes and prokaryotes so far tested
Products: -
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additional information
?
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Substrates: alpha-sarcin site nucleotide sequence is identical in the large rRNAs of cytoplasmic ribosomes from a range of evolutionary diverse organisms, evolutionarily conserved in all eukaryotes and prokaryotes so far tested
Products: -
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additional information
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Substrates: with rat liver ribosomes or 60S ribosomal subunits as substrates alpha-sarcin cleaves a single oligonucleotide of about 488 residues, the alpha-fragment from the 3' end of 28 S rRNA, 40 S ribosomal subunits are not affected by the enzyme, hydrolysis of DNA requires large amounts of the toxin
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additional information
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Substrates: cytotoxic protein that inhibits eukaryotic elongation factor 1 catalyzed binding of aminoacyl-tRNA to ribosomes as a result of cleaving a fragment from the large RNA in the 60 S ribosomal subunit
Products: -
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additional information
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Substrates: cytotoxic protein that inhibits eukaryotic elongation factor 1 catalyzed binding of aminoacyl-tRNA to ribosomes as a result of cleaving a fragment from the large RNA in the 60 S ribosomal subunit
Products: -
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additional information
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Substrates: leucine 145 plays a key role for determining the specificity of the ribosome-inactivating activity of the protein
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additional information
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Substrates: the ribosome-inactivating proteins alpha-sarcin targets the ribosomal sarcin/ricin loop, specific recognition and cleavage. The eukaryotic ribosomal stalk directly interacts with several members of the N-glycosidase family, favoring their disruption of the sarcin/ricin loop, overview. alpha-Sarcin does not interact with the P1/P2 C-terminal peptide SDDDMGFGLFD
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additional information
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Substrates: the rate of cleavage is comparable both in presence and in absence of ribosomal proteins. More complete cleavage is observed in the absence of ribosomal proteins
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additional information
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Substrates: analysis of the RNase activity assay of purified recombinant engineered IMTXA33furalphaS using rabbit ribosomes as substrate compared to the specific RNase activity of recombinant alpha-sarcin
Products: -
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additional information
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Substrates: specific ribonuclease activity against ribosomal RNA causes ribosome disruption and subsequent protein biosynthesis inhibition
Products: -
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additional information
?
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Substrates: alpha-sarcin site nucleotide sequence is identical in the large rRNAs of cytoplasmic ribosomes from a range of evolutionary diverse organisms, evolutionarily conserved in all eukaryotes and prokaryotes so far tested
Products: -
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additional information
?
-
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Substrates: mechanism of action is hydrolysis of a phosphodiester bond between G-4325 and A-4326 of rat 28S ribosomal RNA producing an alpha-fragment from the 3' end of 28S rRNA
Products: -
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additional information
?
-
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Substrates: acts as a cyclizing ribonuclease
Products: -
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additional information
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Substrates: acts as a cyclizing ribonuclease
Products: -
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additional information
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Substrates: induction of cell death via apoptosis
Products: -
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additional information
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Substrates: the rate of cleavage is comparable both in presence and in absence of ribosomal proteins. More complete cleavage is observed in the absence of ribosomal proteins
Products: -
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additional information
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Substrates: ageritin shows specific ribonucleolytic activity against the ribosomal sarcin-ricin loop in a rabbit reticulocytes assay
Products: -
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additional information
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Substrates: hybridization, pH 7.55, 350 mM of monovalent cations, 10 mM MgCl2, 37°C
Products: -
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additional information
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Substrates: cleaving a specific adenine from the highly conserved alpha-sarcin loop of the host 28S ribosomal RNA
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additional information
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Substrates: eryngitin proteins induce formation of the alpha-fragment from rabbit ribosomes
Products: -
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evolution
ribotoxin-like proteins (RL-Ps) represent a novel specific ribonuclease family found in edible mushrooms
malfunction
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mutations in alpha-sarcin, which impair alpha-sarcin's ability to inhibit protein synthesis, do not affect its cytotoxicity. The mutants are unable to activate Jun N-terminal kinase, thus the sarcin-ricin loop remains intact indicating that the alpha-sarcin mutants are catalytically inactive
physiological function

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both alpha-sarcin and ricin transfected cells demonstrate a dose-dependent decrease in viability at 48 hours, whereby ricin is more effective at low doses (50 ng) than alpha-sarcin. At concentrations greater than 250 ng, no further reduction in viability and approximately 20% of the cells remain viable. Direct cytoplasmic expression of alpha-sarcin and ricin in mammalian cells is cytotoxic: exogenous expression of both alpha-sarcin and ricin in HeLa cells results in decreased viability within 48 hours. Both alpha-sarcin and ricin induce cell death at similar rates, with ricin exhibiting slightly enhanced cytotoxicity. Direct expression of alpha-sarcin in Cos-7 cells also results in cytotoxicity. Although protein synthesis inhibition likely contributes to cell death, it is not required. alpha-Sarcin can promote cell death through a mechanism that is independent of rRNA cleavage and Jun N-terminal kinase activation
physiological function
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alpha-sarcin cleaves the large 23S rRNA at the universally conserved sarcin-ricin loop leading to complete inactivation of the ribosome and cellular death. alpha-Sarcin-treated ribosomes show no defects in mRNA and tRNA binding, peptide-bond formation and sparsomycin-dependent translocation, whereas activity of elongation factor G is strongly impaired
physiological function
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the fungal ribotoxin alpha-sarcin is one of the most potent and specific toxins known. It is small, protease-resistant, thermostable and highly efficient towards the inactivation of ribosomes
physiological function
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the inactivation exerted by alpha-sarcin is independent of the composition of the ribosomal stalk
physiological function
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alpha-sarcin is cytotoxic to many tumor cell lines as well as dividing and non-dividing cells, the cytotoxicity of the protein toxin is regulated by protein splicin. alpha-Sarcin splicing is dependent on rapamycin, is inducible with rapid kinetics, and triggers apoptosis in HeLa cells. Spliced alpha-sarcin inhibits protein synthesis
physiological function
purified ageritin is able to inhibit protein synthesis in a rabbit reticulocyte lysate, with an IC50 value of 133 pM
physiological function
ageritin heterologously expressed in Escherichia coli shows a strong toxicity against Aedes aegypti larvae yet not against nematodes. Entomotoxicity of ageritin is mediated by ribonucleolytic cleavage
physiological function
ageritin displayed antibacterial activity against Micrococcus lysodeikticus, activity against the tobacco mosaic virus RNA, endonuclease activity against a supercoiled plasmid, nuclease activity against genomic DNA, cytotoxicity to COLO 320, HeLa, and Raji cells by promoting apoptosis, and antifungal activity against the green mold Penicillium digitatum
physiological function
immunotoxins are chimeric molecules that combine the specificity of an antibody to recognize and bind tumor antigens with the potency of the enzymatic activity of a toxin, thus, promoting the death of target cells. Due to their high cytotoxicity, specificity, and effectivity, immunotoxins have arisen as potent and promising antitumor agents. These chimeric proteins are composed of a target domain that specifically targets a tumor marker, fused to a toxic domain, responsible for the cytotoxicity. Their mechanism of action involves, in a first step, high affinity binding to the tumor antigen by the targeting domain, followed by the internalization of the complex by endocytosis, and finally the release of the toxic domain promoting the death of target cells. High specificity of the ribonucleolytic activity of alpha-sarcin against ribosomes. Alpha-sarcin shows specific ribonucleolytic activity against just one single rRNA phosphodiester bond, located at the sarcin-ricin loop (SRL) of the larger rRNA, causing protein biosynthesis inhibition and apoptosis
physiological function
ribotoxin-like proteins (RL-Ps) found in edible mushrooms are able to inhibit protein synthesis. Four RL-Ps, named eryngitins, are identified and isolated from fruiting bodies of the king oyster mushroom (Pleurotus eryngii). The two 15 kDa eryngitins (3 and 4) are considerably more thermostable than the 21 kDa ones (1 and 2), while their overall structural features, as determined by far-UV CD spectrometry, are similar. Complete in vitro digestibility by pepsin-trypsin, and lack of cytotoxicity towards human HUVEC cells suggest low toxicity of eryngitins, if ingested. But eryngitins exhibit cytotoxic action against insect Sf9 cells. This cytotoxicity is not enhanced in the presence of cytolytic protein complexes based on aegerolysin proteins from Pleurotus mushrooms
physiological function
-
edulitin 1 shows a slight cytotoxic activity on HeLa cells. Edulitin 2 is more cytotoxic than edulitin 1
physiological function
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HeLa cells viability decreases in a concentration dependent manner with edulitin 2 (IC50 values 0.0061 mM and 0.0004 mM at 24 and 48 h, respectively). The same trend for the protein is observed on HepG2 cells, nevertheless only after an incubation of 48 h it is possible to calculate for edulitin 2 an IC50 of 0.0058 mM. Edulitin 2 is more cytotoxic than edulitin 1
physiological function
ageritin is a specific ribonuclease with major rRNA as target
physiological function
the ribotoxin ostreatin is a specific ribonuclease releasing alpha-fragment when incubated with yeast or rabbit ribosomes. Ostreatin shows an IC50 of 234 pM in rabbit reticulocyte lysate, and metal-dependent endonuclease activity. Ostreatin was able to inactivate ribosomes
physiological function
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ageritin is a specific ribonuclease, isolated from the basidiomycete fungus Agrocybe aegerita, that cleaves ribosomal RNA resulting in an irreversibly block of protein synthesis. The extreme specificity of ageritin for rRNA is due to the cleavage of a single phosphodiester bond in a highly conserved region, known as sarcin-ricin loop (SRL), evolutionarily conserved from bacteria to mammalians, and involved in the binding of elongation factors. The SRL sequence is also the target of ribotoxins, specific extracellular ribonucleases, produced by several fungal ascomycetes species, such as Aspergillus giganteus, from which has been isolated alpha-sarcin, the prototype of this enzyme family. Ageritin and other ribotoxins are able to inhibit protein synthesis by releasing a small rRNA fragment known as alpha-fragment, when incubated with several eukaryotic and prokaryotic ribosomes. Analysis of the cytotoxicity of argeritin against simian-virus-40-transformed mouse fibroblasts (SVT2 cells) and the parental non-transformed BALB/c 3T3 cell lines. Ageritin shows selective cytotoxic activity. Internalization of ageritin in BALB/c 3T3 and SVT2 cells. Selective antitumor activity of ageritin. Interaction analysis of argeritin with model membranes shows that increasing ageritin concentrations lead to a progressive decrease of enthalpy change of the pre-transition peak, indicating a strong perturbation of the lipids head groups of the bilayer upon protein interaction
physiological function
Asp f I is an allergenic ribotoxin
physiological function
-
the fungal ribotoxin alpha-sarcin is one of the most potent and specific toxins known. It is small, protease-resistant, thermostable and highly efficient towards the inactivation of ribosomes
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physiological function
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the ribotoxin ostreatin is a specific ribonuclease releasing alpha-fragment when incubated with yeast or rabbit ribosomes. Ostreatin shows an IC50 of 234 pM in rabbit reticulocyte lysate, and metal-dependent endonuclease activity. Ostreatin was able to inactivate ribosomes
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additional information

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the recombinant fusion enzyme scFvA33alphasarcin shows high specific toxicity against GPA33-positive tumoral colon carcinoma cell lines, cellular binding and internalization of recombinant enzyme fusion construct scFvA33alphasarcin, overview
additional information
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the P1/P2 C-terminal peptide SDDDMGFGLFD does not interact with alpha-sarcin
additional information
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selective reduction and S-pyridylethylation of edulitin 2, binding of S-pyridyethyl to a cisteinyl residue
additional information
structure homology modeling reveals that ostreatin and ageritin share a similar fold in which the common catalytic triad is conserved, they shares 38.8% amino acid sequence identity. Selective reduction and S-pyridylethylation of ostreatin, binding of S-pyridyethyl to a cisteinyl residue
additional information
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ageritin is a basic protein of 135 amino acid residues, with a single free cysteinyl residue in contrast to canonical ribotoxins that have two disulphide bridges
additional information
development of an immunological detection method for the enzyme from patient urine using an monoclonal antibody derived from mitogillin by hybridoma technique. Method development for detection of ribotoxin Asp f I in patients with aspergillosis, and further influenza-associated pulmonary aspergillosis (IAPA) and COVID-19 ICU patients with COVID-19-associated pulmonary aspergillosis (CAPA). The murine IgG1 mAb raised against the Aspergillus fumigatus ribotoxin mitogillin binds to an epitope conserved amongst the Aspergillus ribotoxins mitogillin, Asp f I, restrictocin, and alpha-sarcin
additional information
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the recombinant fusion enzyme scFvA33alphasarcin shows high specific toxicity against GPA33-positive tumoral colon carcinoma cell lines, cellular binding and internalization of recombinant enzyme fusion construct scFvA33alphasarcin, overview
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additional information
-
structure homology modeling reveals that ostreatin and ageritin share a similar fold in which the common catalytic triad is conserved, they shares 38.8% amino acid sequence identity. Selective reduction and S-pyridylethylation of ostreatin, binding of S-pyridyethyl to a cisteinyl residue
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Endo, Y.; Wool, I.G.
The site of action of alpha-sarcin on eukaryotic ribosomes. The sequence at the alpha-sarcin cleavage site in 28 S ribosomal ribonucleic acid
J. Biol. Chem.
257
9054-9060
1982
Aspergillus giganteus
brenda
Endo, Y.; Huber, P.W.; Wool, I.G.
The ribonuclease activity of the cytotoxin alpha-sarcin. The characteristics of the enzymatic activity of alpha-sarcin with ribosomes and ribonucleic acids as substrates
J. Biol. Chem.
258
2662-2667
1983
Aspergillus giganteus
brenda
Wool, I.G.
The mechanism of the action of the cytotoxic nuclease alpha-sarcin and its use to analyze ribosome structure
Trends Biochem. Sci.
9
14-17
1984
Aspergillus giganteus
-
brenda
Stirpe, F.; Bailey, S.; Miller, S.P.; Bodley, J.W.
Modification of ribosomal RNA by ribosome-inactivating proteins from plants
Nucleic Acids Res.
16
1349-1357
1988
Aspergillus giganteus
brenda
Ling, J.; Liu, W.; Wang, T.P.
Cleavage of supercoiled double-stranded DNA by several ribosome-inactivating proteins in vitro
FEBS Lett.
345
143-146
1994
Aspergillus giganteus
brenda
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Thermal unfolding of the cytotoxin alpha-sarcin: phospholipid binding induces destabilization of the protein structure
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1995
Aspergillus giganteus, Aspergillus giganteus MDH 18894
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Lacadena, J.; Mancheno, J.M.; Martinez-Ruiz, A.; Martinez del Pozo, A.; Gasset, M.; Onaderra, M.; Gavilanes, J.G.
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Aspergillus giganteus, Aspergillus giganteus MDH 18894
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Campos-Olivas, R.; Bruix, M.; Santoro, J.; Martinez del Pozo, A.; Lacadena, J.; Gavilanes, J.G.; Rico, M.
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Aspergillus giganteus
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Aspergillus giganteus
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Aspergillus giganteus
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Hao, J.J.; Xu, Y-z.; Geng, C.d.; Liu, W.Y.; Wang, E.d; Gong, Z.z.; Ulbrich, N.
Purification of alpha-sarcin and an antifungal protein from Aspergillus giganteus by blue sepharose CL-6B affinity chromatography
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Aspergillus giganteus, Aspergillus giganteus MDH 18894
brenda
Lacadena, J.; Martinez del Pozo, A.; Lacadena, V.; Martinez-Ruiz, A.; Mancheno, J.M.; Onaderra, M.; Gavilanes, J.G.
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Aspergillus giganteus, Aspergillus giganteus MDH 18894
brenda
Perez-Canadillas, J.M.; Campos-Olivas, R.; Lacadena, J.; Martinez del Pozo, A.; Gavilanes, J.G.; Santoro, J.; Rico, M.; Bruix, M.
Characterization of pKa values and titration shifts in the cytotoxic ribonuclease alpha-sarcin by NMR. Relationship between electrostatic interactions, structure, and catalytic function
Biochemistry
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Aspergillus giganteus
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Lacadena, J.; Martinez del Pozo, A.; Martinez-Ruiz, A.; Perez-Canadillas, J.M.; Bruix, M.; Mancheno, J.M.; Onaderra, M.; Gavilanes, J.G.
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Aspergillus giganteus, Aspergillus giganteus MDH 18894
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The action mode of the ribosome-inactivating protein alpha-sarcin
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Aspergillus giganteus
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The highly refined solution structure of the cytotoxic ribonuclease alpha-sarcin reveals the structural requirements for substrate recognition and ribonucleolytic activity
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Aspergillus giganteus (P00655)
brenda
Xu, Y.Z.; Liu, W.Y.
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Aspergillus giganteus
brenda
Masip, M.; Lacadena, J.; Mancheno, J.M.; Onaderra, M.; Martinez-Ruiz, A.; Martinez del Pozo, A.; Gavilanes, J.G.
Arginine 121 is a crucial residue for the specific cytotoxic activity of the ribotoxin alpha-sarcin
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Aspergillus giganteus
brenda
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Aspergillus giganteus, Aspergillus giganteus MDH 18894
brenda
Garcia-Ortega, L.; Masip, M.; Mancheno, J.M.; Onaderra, M.; Lizarbe, M.A.; Garcia-Mayoral, M.F.; Bruix, M.; Martinez del Pozo, A.; Gavilanes, J.G.
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Aspergillus giganteus (P00655)
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Larsson, S.L.; Sloma, M.S.; Nygard, O.
Conformational changes in the structure of domains II and V of 28S rRNA in ribosomes treated with the translational inhibitors ricin or alpha-sarcin
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Aspergillus giganteus
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Purification of alpha-sarcin and an antifungal protein from mold (Aspergillus giganteus) by chitin affinity chromatography
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2002
Aspergillus giganteus, Aspergillus giganteus MDH 18894
brenda
Masip, M.; Garcia-Ortega, L.; Olmo, N.; Garcia-Mayoral, M.F.; Perez-Canadillas, J.M.; Bruix, M.; Onaderra, M.; Martinez del Pozo, A.; Gavilanes, J.G.
Leucine 145 of the ribotoxin alpha-sarcin plays a key role for determining the specificity of the ribosome-inactivating activity of the protein
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2003
Aspergillus giganteus
brenda
Perez-Canadilllas, J.M.; Garcia-Mayoral, M.F.; Laurents, D.V.; Martinez del Pozo, A.; Gavilanes, J.G.; Rico, M.; Bruix, M.
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Aspergillus giganteus
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Aspergillus giganteus
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Aspergillus restrictus
brenda
Petyuk, V.A.; Serikov, R.N.; Vlassov, V.V.; Zenkova, M.A.
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Escherichia coli
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Escherichia coli
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Aspergillus giganteus (P00655)
brenda
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Lactococcus lactis, Lactococcus lactis MG1363
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Herrero-Galan, E.; Lacadena, J.; Martinez Del Pozo, A.; Boucias, D.G.; Olmo, N.; Onaderra, M.; Gavilanes, J.G.
The insecticidal protein hirsutellin A from the mite fungal pathogen Hirsutella thompsonii is a ribotoxin
Proteins
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Aspergillus giganteus (P00655)
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Alford, S.; Pearson, J.; Carette, A.; Ingham, R.; Howard, P.
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Aspergillus giganteus
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Aspergillus giganteus
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Aspergillus giganteus
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Carreras-Sangra, N.; Tome-Amat, J.; Garcia-Ortega, L.; Batt, C.A.; Onaderra, M.; Martinez-del-Pozo, A.; Gavilanes, J.G.; Lacadena, J.
Production and characterization of a colon cancer-specific immunotoxin based on the fungal ribotoxin alpha-sarcin
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Aspergillus giganteus, Aspergillus giganteus MDH18894
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Aspergillus giganteus
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Cyclocybe aegerita (C0HLG3)
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Cyclocybe aegerita (C0HLG3)
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Aspergillus giganteus, Aspergillus giganteus MH18894
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Structural and enzymatic properties of Ageritin, a novel metal-dependent ribotoxin-like protein with antitumor activity
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Cyclocybe aegerita (C0HLG3)
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Conformational study of the antitumor protein alpha-sarcin
Biochim. Biophys. Acta
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1988
Aspergillus giganteus
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Aspergillus giganteus (P00655)
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Wawrzynczak, E.J.; Henry, R.V.; Cumber, A.J.; Parnell, G.D.; Derbyshire, E.J.; Ulbrich, N.
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1991
Aspergillus giganteus (P00655), Aspergillus giganteus
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Mutational studies on the alpha-sarcin loop of Escherichia coli 23S ribosomal RNA
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Aspergillus giganteus
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Cyclocybe aegerita (C0HLG3)
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Aspergillus giganteus
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Aspergillus giganteus (P00655)
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Yang, X.; Moffat, K.
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1996
Aspergillus restrictus (P67876), Aspergillus restrictus
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Endo, Y.; Oka, T.; Tsurugi, K.; Natori, Y.
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Aspergillus giganteus (P00655), Aspergillus giganteus
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Aspergillus giganteus (P00655), Aspergillus giganteus
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Landi, N.; Ragucci, S.; Culurciello, R.; Russo, R.; Valletta, M.; Pedone, P.V.; Pizzo, E.; Di Maro, A.
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Pleurotus eryngii (P84525)
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Landi, N.; Ragucci, S.; Russo, R.; Valletta, M.; Pizzo, E.; Ferreras, J.M.; Di Maro, A.
The ribotoxin-like protein Ostreatin from Pleurotus ostreatus fruiting bodies Confirmation of a novel ribonuclease family expressed in basidiomycetes
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Pleurotus ostreatus (A0A067NAU1), Pleurotus ostreatus PC15 (A0A067NAU1)
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Lampitella, E.; Landi, N.; Oliva, R.; Ragucci, S.; Petraccone, L.; Berisio, R.; Di Maro, A.; Del Vecchio, P.
Conformational stability of ageritin, a metal binding ribotoxin-like protein of fungal origin
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Cyclocybe aegerita (C0HLG3)
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Lampitella, E.; Landi, N.; Oliva, R.; Gaglione, R.; Bosso, A.; De Lise, F.; Ragucci, S.; Arciello, A.; Petraccone, L.; Pizzo, E.; Del Vecchio, P.; Di Maro, A.
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Cyclocybe aegerita
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Davies, G.; Singh, O.; Prattes, J.; Hoenigl, M.; Sheppard, P.W.; Thornton, C.R.
Aspergillus fumigatus and its allergenic ribotoxin Asp f I old enemies but new opportunities for urine-based detection of invasive pulmonary aspergillosis using lateral-flow technology
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Aspergillus fumigatus (O60023)
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Ruiz-de-la-Herran, J.; Tome-Amat, J.; Lazaro-Gorines, R.; Gavilanes, J.G.; Lacadena, J.
Inclusion of a furin cleavage site enhances antitumor efficacy against colorectal cancer cells of ribotoxin alpha-sarcin- or RNase T1-based immunotoxins
Toxins
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Aspergillus giganteus (P00655)
brenda