Highly efficient solid-phase phosphopeptide synthesis using bis-(polyfluorophenyl) chlorophosphates: Preparation of serine-threonine protein phosphatase substrates
- 4 November 1996
- journal article
- Published by Elsevier in Tetrahedron Letters
- Vol. 37 (45) , 8227-8230
- https://doi.org/10.1016/0040-4039(96)01874-6
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- Crystal Structure of the Catalytic Subunit of Human Protein Phosphatase 1 and its Complex with TungstateJournal of Molecular Biology, 1995
- Phospho-serine and phospho-threonine building blocks for the synthesis of phosphorylated peptides by the Fmoc solid phase strategyBioorganic & Medicinal Chemistry Letters, 1995
- Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1Nature, 1995
- Protein kinases and phosphatases: The Yin and Yang of protein phosphorylation and signalingCell, 1995
- Synthesis and properties of mechanism-based inhibitors and probes for inositol monophosphatase derived from 6-O-(2′-hydroxyethyl)-(1R,2R,4R,6R)-cyclohexane-1,2,4,6-tetraolJournal of the Chemical Society, Chemical Communications, 1995
- Protein serine/threonine phosphatases; an expanding familyFEBS Letters, 1990
- Synthesis of oligophosphoseryl sequences occurring in caseinInternational Journal of Peptide and Protein Research, 1990
- An investigation of the substrate specificity of protein phosphatase 2C using synthetic peptide substrates; comparison with protein phosphatase 2ABiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1990
- Solid‐phase synthesis of phosphopeptidesInternational Journal of Peptide and Protein Research, 1989
- THE STRUCTURE AND REGULATION OF PROTEIN PHOSPHATASESAnnual Review of Biochemistry, 1989