A variety of compounds that show promise in cancer chemotherapy and chemoprevention have been identified as farnesyltransferase inhibitors. These can be classified into mainly two different types of inhibitors, farnesyl diphosphate competitors and CAAX peptidomimetics. The former type acts by compet
✦ LIBER ✦
Interplay of Isoprenoid and Peptide Substrate Specificity in Protein Farnesyltransferase †
✍ Scribed by Reigard, Sarah A.; Zahn, Todd J.; Haworth, Kellie B.; Hicks, Katherine A.; Fierke, Carol A.; Gibbs, Richard A.
- Book ID
- 126829313
- Publisher
- American Chemical Society
- Year
- 2005
- Tongue
- English
- Weight
- 244 KB
- Volume
- 44
- Category
- Article
- ISSN
- 0006-2960
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
Advances in the development of farnesylt
✍
Wenli Yang; Keith Del Villar; Jun Urano; Hiroshi Mitsuzawa; Fuyuhiko Tamanoi
📂
Article
📅
1997
🏛
John Wiley and Sons
🌐
English
⚖ 92 KB
👁 1 views
Cloning, heterologous expression, and su
✍
Frederick S Buckner; Richard T Eastman; José L Nepomuceno-Silva; Emily C Speelmo
📂
Article
📅
2002
🏛
Elsevier Science
🌐
English
⚖ 363 KB
Protein Tyrosine Phosphatase Substrate S
✍
Zhang, Zhong Yin; Maclean, Derek; McNamara, Dennis J.; Sawyer, Tomi K.; Dixon, J
📂
Article
📅
1994
🏛
American Chemical Society
🌐
English
⚖ 762 KB
Substrate specificity of peptide permeas
✍
Sławomir Milewski; Ryszard Andruszkiewicz; Edward Borowski
📂
Article
📅
1988
🏛
John Wiley and Sons
🌐
English
⚖ 375 KB
Role of the Carboxyterminal Residue in P
✍
Robert Roskoski Jr.; Patricia Ritchie
📂
Article
📅
1998
🏛
Elsevier Science
🌐
English
⚖ 125 KB
Comparison of Substrate Specificities of
✍
M. Loog; M. Eller; P. Ekman; L. Engstrom; S. Eriksson; J. Jarv; U. Ragnarsson; R
📂
Article
📅
1994
🏛
Elsevier Science
🌐
English
⚖ 430 KB
Peptides, obtained by gradual removal of amino acids from both ends of pEKRPSQRSKYL, and stereoisomeric nonapeptides KRPSQRAKY with one D-amino acid residue successively in each position, were tested as substrates for protein kinase A. All these compounds were phosphorylated but at quite different r