Oxford Index Search Results

You are looking at 1-10 of 27 items for:

��-sarcin x Biochemistry x clear all

α-sarcin

Overview page. Subjects: Chemistry.

A cytotoxin produced by Aspergillus giganteus. It has ribonuclease activity, specific for purines in both single‐stranded and double‐stranded RNA. It inhibits protein synthesis, cleaving a...

See overview in Oxford Index

Molecular dynamics simulations of sarcin–ricin rRNA motif

Nad'a Špačková and Jiří Šponer.

in Nucleic Acids Research

January 2006; p ublished online January 2006 .

Journal Article. Subjects: Chemistry; Biochemistry; Bioinformatics and Computational Biology; Genetics and Genomics; Molecular and Cell Biology. 9272 words.

Explicit solvent molecular dynamics (MD) simulations were carried out for sarcin–ricin domain (SRD) motifs from 23S (Escherichia coli) and 28S (rat) rRNAs. The SRD motif consists of GAGA...

Go to Oxford Journals »  full text: open access

α‐sarcin

Edited by Richard Cammack, Teresa Atwood, Peter Campbell, Howard Parish, Anthony Smith, Frank Vella and John Stirling.

in Oxford Dictionary of Biochemistry and Molecular Biology

January 2006; p ublished online January 2008 .

Reference Entry. Subjects: Biochemistry. 91 words.

a cytotoxin produced by Aspergillus giganteus. It has ribonuclease activity, specific for purines in both single‐stranded and double‐stranded RNA.

Go to Oxford Reference »  home page

A deimmunised form of the ribotoxin, α-sarcin, lacking CD4<sup>+</sup> T cell epitopes and its use as an immunotoxin warhead

Tim D. Jones, Arron R. Hearn, Robert G.E. Holgate, Dorota Kozub, Mark H. Fogg, Francis J. Carr, Matthew P. Baker, Javier Lacadena and Kurt R. Gehlsen.

in Protein Engineering, Design and Selection

November 2016; p ublished online October 2016 .

Journal Article. Subjects: Proteins. 7913 words.

Fungal ribotoxins that block protein synthesis can be useful warheads in the context of a targeted immunotoxin. α-Sarcin is a small (17 kDa) fungal ribonuclease produced by Aspergillus...

Go to Oxford Journals »  full text: open access

Production and characterization of a colon cancer-specific immunotoxin based on the fungal ribotoxin α-sarcin

Nelson Carreras-Sangrà, Jaime Tomé-Amat, Lucía García-Ortega, Carl A. Batt, Mercedes Oñaderra, Álvaro Martínez-del-Pozo, José G. Gavilanes and Javier Lacadena.

in Protein Engineering, Design and Selection

August 2012; p ublished online June 2012 .

Journal Article. Subjects: Proteins. 5898 words.

A single-chain fusion protein that directed the cytolytic activity of α-sarcin to A33 tumor antigen expressing cells was constructed and shown to effectively kill targeted cells....

Go to Oxford Journals »  abstract

Effects of Antisense DNA Against the α-Sarcin Stem-Loop Structure of the Ribosomal 23S rRNA

Hellmuth-Alexander Meyer, Francisco Triana-Alonso, Christian M. T. Spahn, Tomasz Twardowski, Andrzej Sobkiewicz and Knud H. Nierhaus.

in Nucleic Acids Research

October 1996; p ublished online October 1996 .

Journal Article. Subjects: Chemistry; Biochemistry; Bioinformatics and Computational Biology; Genetics and Genomics; Molecular and Cell Biology. 4598 words.

Antisense DNAs complementary against various sequences of the α-sarcin domain (C2646-G2674) of 23S rRNA from Escherichia coli were hybridized to naked 23S rRNA as well as to 70S ribosomes....

Go to Oxford Journals »  home page

Cleavage of the sarcin–ricin loop of 23S rRNA differentially affects EF-G and EF-Tu binding

Lucía García-Ortega, Elisa Álvarez-García, José G. Gavilanes, Álvaro Martínez-del-Pozo and Simpson Joseph.

in Nucleic Acids Research

July 2010; p ublished online March 2010 .

Journal Article. Subjects: Chemistry; Biochemistry; Bioinformatics and Computational Biology; Genetics and Genomics; Molecular and Cell Biology. 7930 words.

Ribotoxins are potent inhibitors of protein biosynthesis and inactivate ribosomes from a variety of organisms. The ribotoxin α-sarcin cleaves the large 23S ribosomal RNA (rRNA) at the...

Go to Oxford Journals »  full text: open access

Placement of the α-sarcin loop within the 50S subunit: Evidence derived using a photolabile oligodeoxynucleotide probe

Parimi Muralikrishna, Rebecca W. Alexander and Barry S. Cooperman.

in Nucleic Acids Research

November 1997; p ublished online November 1997 .

Journal Article. Subjects: Chemistry; Biochemistry; Bioinformatics and Computational Biology; Genetics and Genomics; Molecular and Cell Biology. 4915 words.

We report the synthesis of a radioactive, photolabile oligodeoxyribonucleotide probe and its exploitation in identifying 50S ribosomal subunit components neighboring the α-sarcin loop. The...

Go to Oxford Journals »  home page

The Influence of Base Identity and Base Pairing on the Function of the α-Sarcin Loop of 23S rRNA

Michael O'Connor and Albert E. Dahlberg.

in Nucleic Acids Research

July 1996; p ublished online July 1996 .

Journal Article. Subjects: Chemistry; Biochemistry; Bioinformatics and Computational Biology; Genetics and Genomics; Molecular and Cell Biology. 3049 words.

The α-sarcin loop of large subunit rRNAs is one of the sites of interaction of elongation factors with the ribosome, and the target of the cytotoxins α-sarcin and ricin. Using a genetic...

Go to Oxford Journals »  home page

Biochemical evidence of translational infidelity and decreased peptidyltransferase activity by a sarcin/ricin domain mutation of yeast 25S rRNA

Panagiotis Panopoulos, John Dresios and Dennis Synetos.

in Nucleic Acids Research

October 2004; p ublished online October 2004 .

Journal Article. Subjects: Chemistry; Biochemistry; Bioinformatics and Computational Biology; Genetics and Genomics; Molecular and Cell Biology. 9181 words.

A C→U mutation (rdn5) in the conserved sarcin/ricin domain of yeast 25S rRNA has been shown to cause translational suppression and paromomycin resistance. It also separates the killing from...

Go to Oxford Journals »  home page

Cinnamomin—a Versatile Type II Ribosome-inactivating Protein

Hong Xu and Wang-Yi Liu.

Edited by Guo-Rong Qi.

in Acta Biochimica et Biophysica Sinica

March 2004; p ublished online March 2004 .

Journal Article. Subjects: Biochemistry. 0 words.

Ribosome-inactivating proteins (RIPs) are a group of toxic proteins that can specifically act on the universally conserved sarcin/ricin domain (S/R domain) of the largest RNA in ribosome...

Go to Oxford Journals »  abstract