.
. Protein–Protein Interactions: A Molecular Cloning Manual, Second EditionCSHL Press .
. . . . .
.
.
.
. .
 
.
. . .
.  FIRST VISIT?
 TRY THESE LINKS
.
. . .
.
.   Enroll for Updates
  Privacy Policy
  Purchase the book
.
.
 
 
.
. . .
.  BOOK COVER .
. . .
.
. Protein–Protein Interactions: A Molecular Cloning Manual, Second Edition cover .
.
CLICK TO ENLARGE
 
Buy the Book
 
   
 

Chapter 24: Using Genetically Engineered Kinases to Screen for Novel Protein Kinase Substrates—References

Chaudhary A., Brugge J.S., and Cooper J.A. 2002. Direct phosphorylation of focal adhesion kinase by c-src: Evidence using a modified nucleotide pocket kinase and ATP analog. Biochem. Biophys. Res. Commun. 294: 293–300.

Eblen S.T., Kumar N.V., Shah K., Henderson M.J., Watts C.K.W., Shokat K.M., and Weber M.J. 2003. Identification of novel ERK2 substrates through use of an engineered kinase and ATP analogs. J. Biol. Chem. 278: 14926–14935.

Habelhah H., Shah K., Huang L., Burlingame A.L., Shokat K.M., and Ronai Z. 2001. Identification of new JNK substrate using ATP pocket mutant JNK and a corresponding ATP analogue. J. Biol. Chem. 276: 18090–18095.

Harlow E.H. and Lane D.L. 1999. Using antibodies: A laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.

Liu Y., Kung C., Fishburn J., Ansari A.Z., Shokat K.M., and Hahn S. 2004. Two cyclin-dependent kinases promote RNA polymerase II transcription and formation of the scaffold complex. Mol. Cell Biol. 24: 1721–1735.

Mortz E., Krogh T.N., Vorum H., and Gorg A. 2001. Improved silver staining protocols for high sensitivity protein identification using matrix-assisted laser desorption/ionization-time of flight analysis. Proteomics 1: 1359–1363.

Shah K. and Shokat K.M. 2002. A chemical genetic screen for direct v-Src substrates reveals ordered assembly of a retrograde signaling pathway. Chem. Biol. 9: 35–47.

Shah K., Liu Y., Deirmengian C., and Shokat K.M. 1997. Engineering unnatural nucleotide specificity for Rous sarcoma virus tyrosine kinase to uniquely label its direct substrates. Proc. Natl. Acad. Sci. 94: 3565–3570.

Tanoue T., Adachi M., Moriguchi T., and Nishida E. 2000. A conserved docking motif in MAP kinases common to substrates, activators and regulators. Nat. Cell Biol. 2: 110–116.

Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K., Shokat K.M., and Morgan D.O. 2003. Targets of the cyclin-dependent kinase Cdk1. Nature 425: 859–864.

Ulrich S.M., Sallee N.A., and Shokat K.M. 2002. Conformational restraint is a critical determinant of unnatural nucleotide recognition by protein kinases. Bioorg. Med. Chem. Lett. 12: 3223–3227.

van der Geer P. and Hunter T. 1994. Phosphopeptide mapping and phosphoamino acid analysis by electrophoresis and chromatography on thin-layer cellulose plates. Electrophoresis 15: 544–554.

Weber M.J. and Edlin G. 1971. Phosphate transport, nucleotide pools, and ribonucleic acid synthesis in growing and in density-inhibited 3T3 cells. J. Biol. Chem. 246: 1828–1833.

Wessel D. and Flugge U.I. 1984. A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem. 138: 141–143.

Zhang F., Strand A., Robbins D., Cobb M.H., and Goldsmith E.J. 1994. Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution. Nature 367: 704–711.

<<< Chapter 23 References            Chapter 25 References >>>

 
 
 

 
   
. .