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Peptide inhibitors of mammalian ribonucleotide reductase

✍ Scribed by Barry S. Cooperman; Ying Gao; Chiheng Tan; Ossama B. Kashlan; Jaskiran Kaur

Book ID
113418871
Publisher
Elsevier Science
Year
2005
Tongue
English
Weight
420 KB
Volume
45
Category
Article
ISSN
0065-2571

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πŸ“œ SIMILAR VOLUMES

Mechanisms of action of peptide inhibito
Mechanisms of action of peptide inhibitors of mammalian ribonucleotide reductase targeting quaternary structure
✍ Ying Gao; Ossama B. Kashlan; Jaskiran Kaur; Chiheng Tan; Barry S. Cooperman πŸ“‚ Article πŸ“… 2005 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 203 KB

Mammalian ribonucleotide reductase (mRR) is a chemotherapeutic target. The enzyme is composed of 2 subunits (mR1 and mR2) and is inhibited by Ac-FTLDADF (denoted P7), corresponding to the C-terminus of mR2, which competes with mR2 for binding to mR1. mRR has 2 physiologically important active forms,

Sequencing cyclic peptide inhibitors of
Sequencing cyclic peptide inhibitors of mammalian ribonucleotide reductase by electrospray ionization mass spectrometry
✍ Shanhua Lin; Sebastian Liehr; Barry S. Cooperman; Robert J. Cotter πŸ“‚ Article πŸ“… 2001 πŸ› John Wiley and Sons 🌐 English βš– 138 KB

## Abstract Mammalian ribonucleotide reductase (mRR) is a potential target for cancer intervention. A series of lactam‐bridged cyclic peptide inhibitors (1–9) of mRR have been synthesized and tested in previous work. These inhibitors consist of cyclic and linear regions, causing their mass spectral