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Structure and evolution of mammalian ribosomal proteins.

• Ira G. Wool, Y L Chan, Anton Glück
• Biochemistry and cell biology = Biochimie et…
• 1995

Mammalian (rat) ribosomes have 80 proteins; the sequence of amino acids in 75 have been determined. What has been learned of the structure of the rat ribosomal proteins is reviewed with particular… (More)

Ribotoxin recognition of ribosomal RNA and a proposal for the mechanism of translocation.

• Ira G. Wool, Anton Glück, Yaeta Endo
• Trends in biochemical sciences
• 1992

The ribotoxins alpha-sarcin and ricin catalyse covalent modifications in adjacent nucleotides in 28S rRNA, yet the elements of nucleic acid structure that they recognize are not only different but… (More)

Ribosomal RNA identity elements for ricin A-chain recognition and catalysis.

• Yaeta Endo, Anton Glück, Ira G. Wool
• Journal of molecular biology
• 1991

Ricin is a cytotoxic protein that inactivates ribosomes by hydrolyzing the N-glycosidic bond between the base and the ribose at position A4324 in eukaryotic 28 S rRNA. The requirements for the… (More)

The primary structure of rat ribosomal proteins P0, P1, and P2 and a proposal for a uniform nomenclature for mammalian and yeast ribosomal proteins.

• Ira G. Wool, Y L Chan, Anton Glück, Koji Suzuki
• Biochimie
• 1991

The covalent structures of rat ribosomal proteins P0, P1, and P2 were deduced from the sequences of nucleotides in recombinant cDNAs. P0 contains 316 amino acids and has a molecular weight of 34,178;… (More)

Determination of the 28 S ribosomal RNA identity element (G4319) for alpha-sarcin and the relationship of recognition to the selection of the catalytic site.

• Anton Glück, Ira G. Wool
• Journal of molecular biology
• 1996

Ricin A-chin and alpha-sarcin are ribotoxins that inactivate eukaryotic ribosomes by modifying 28 S rRNA; ricin A-chain is an RNA N-glycosidase that depurinates the adenosine at position 4324 and… (More)

Ribosomal RNA identity elements for ricin A-chain recognition and catalysis. Analysis with tetraloop mutants.

• Anton Glück, Yaeta Endo, Ira G. Wool
• Journal of molecular biology
• 1992

Ricin is a cytotoxic protein that inactivates ribosomes by hydrolyzing the N-glycosidic bond between the base and the ribose of the adenosine at position 4324 in eukaryotic 28 S rRNA. Ricin A-chain… (More)

The ribosomal RNA identity elements for ricin and for alpha-sarcin: mutations in the putative CG pair that closes a GAGA tetraloop.

• Anton Glück, Yaeta Endo, Ira G. Wool
• Nucleic acids research
• 1994

alpha-Sarcin is a ribonuclease that cleaves the phosphodiester bond on the 3' side of G4325 in 28S rRNA; ricin A-chain is a RNA N-glycosidase that depurinates the 5' adjacent A4324. These single… (More)

Analysis by systematic deletion of amino acids of the action of the ribotoxin restrictocin.

• Anton Glück, Ira G. Wool
• Biochimica et biophysica acta
• 2002

A series of contiguous deletions were made in a cDNA encoding the ribonuclease restrictocin with the purpose of identifying the amino acids that are essential for the cleavage of the phosphodiester… (More)

RNA-protein interaction. An analysis with RNA oligonucleotides of the recognition by alpha-sarcin of a ribosomal domain critical for function.

• Yaeta Endo, Anton Glück, Y L Chan, Kunio Tsurugi, Ira G. Wool
• The Journal of biological chemistry
• 1990

alpha-Sarcin is a cytotoxic protein that inactivates ribosomes by hydrolyzing a single phosphodiester bond on the 3' side of G-4325 in eukaryotic 28 S rRNA. We have examined the requirements for the… (More)

Dependence of depurination of oligoribonucleotides by ricin A-chain on divalent cations and chelating agents.

• Anton Glück, Ira G. Wool
• Biochemistry and molecular biology international
• 1996

Ricin A-chain is a cytotoxic RNA N-glycosidase that inactivates eukaryotic ribosomes by depurinating the adenosine at position 4324 in 28S rRNA. The enzyme retains its specificity when a synthetic… (More)

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