Phosphorylation and activation of a transducible recombinant form of human HSP20 in Escherichia coli.

[1]  J. Kuriyan,et al.  High yield bacterial expression of active c‐Abl and c‐Src tyrosine kinases , 2005, Protein science : a publication of the Protein Society.

[2]  C. Brophy,et al.  Role of the small heat shock proteins in regulating vascular smooth muscle tone. , 2005, Journal of the American College of Surgeons.

[3]  C. Flynn,et al.  Transduction of phosphorylated heat shock-related protein 20, HSP20, prevents vasospasm of human umbilical artery smooth muscle. , 2005, Journal of applied physiology.

[4]  G. Fan,et al.  Novel Cardioprotective Role of a Small Heat-Shock Protein, Hsp20, Against Ischemia/Reperfusion Injury , 2005, Circulation.

[5]  Yuejun Zhen,et al.  Transducible heat shock protein 20 (HSP20) phosphopeptide alters cytoskeletal dynamics , 2005, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[6]  C. Flynn,et al.  Transducible recombinant small heat shock-related protein, HSP20, inhibits vasospasm and platelet aggregation. , 2004, Surgery.

[7]  C. Brophy,et al.  Transduction of peptide analogs of the small heat shock-related protein HSP20 inhibits intimal hyperplasia. , 2004, Journal of vascular surgery.

[8]  O. Jensen.  Modification-specific proteomics: characterization of post-translational modifications by mass spectrometry. , 2004, Current opinion in chemical biology.

[9]  W. Blessing,et al.  Blockade of excitatory amino acid receptors in the ventrolateral medulla does not abolish the cardiovascular actions of l-glutamate , 2004, Naunyn-Schmiedeberg's Archives of Pharmacology.

[10]  C. Flynn,et al.  Transduction of biologically active motifs of the small heat shock‐related protein, HSP20, leads to relaxation of vascular smooth muscle , 2003, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[11]  C. Brophy,et al.  The small heat shock protein (HSP) 20 is dynamically associated with the actin cross-linking protein actinin. , 2003, The Journal of surgical research.

[12]  C. Brophy,et al.  Phosphorylation of the heat shock-related protein, HSP20, mediates cyclic nucleotide-dependent relaxation. , 2003, Journal of vascular surgery.

[13]  Hanno Steen,et al.  Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome. , 2002, Trends in biotechnology.

[14]  T. Date,et al.  Expression of unphosphorylated form of human double-stranded RNA-activated protein kinase in Escherichia coli. , 2001, Biochemical and biophysical research communications.

[15]  G. Waksman,et al.  Synthetic protein transduction domains: enhanced transduction potential in vitro and in vivo. , 2001, Cancer research.

[16]  C. Rembold,et al.  cGMP‐mediated phosphorylation of heat shock protein 20 may cause smooth muscle relaxation without myosin light chain dephosphorylation in swine carotid artery , 2000, The Journal of physiology.

[17]  H. Rasmussen,et al.  Phosphorylation events associated with cyclic nucleotidedependent inhibition of smooth muscle contraction. , 1999, American journal of physiology. Heart and circulatory physiology.

[18]  H. Rasmussen,et al.  The Small Heat Shock-related Protein, HSP20, Is Phosphorylated on Serine 16 during Cyclic Nucleotide-dependent Relaxation* , 1999, The Journal of Biological Chemistry.

[19]  G. Ramakers,et al.  Regulation of astrocyte morphology by RhoA and lysophosphatidic acid. , 1998, Experimental cell research.

[20]  H. Rasmussen,et al.  Cyclic Nucleotide-dependent Vasorelaxation Is Associated with the Phosphorylation of a Small Heat Shock-related Protein* , 1997, The Journal of Biological Chemistry.

[21]  D. Bossemeyer,et al.  In vivo activation of recombinant cAPK catalytic subunit active site mutants by coexpression of the wild‐type enzyme, evidence for intermolecular cotranslational phosphorylation , 1996, FEBS letters.

[22]  F. Hofmann,et al.  Expression of a chimeric, cGMP‐sensitive regulatory subunit of the cAMP‐depedent protein kinase type Iα , 1995 .

[23]  Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27. , 1995, Molecular and cellular biology.

[24]  T. Lincoln,et al.  cGMP signaling through cAMP- and cGMP-dependent protein kinases. , 1995, Advances in pharmacology.

[25]  K. Kato,et al.  Purification and characterization of a 20-kDa protein that is highly homologous to alpha B crystallin. , 1994, The Journal of biological chemistry.

[26]  T. Lincoln,et al.  Expression of the catalytic domain of cyclic GMP‐dependent protein kinase in a baculovirus system , 1994, FEBS letters.

[27]  E. Brown,et al.  Expression of recombinant human casein kinase II and recombinant heat shock protein 90 in Escherichia coli and characterization of their interactions. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[28]  F. Hofmann,et al.  Expression of cGMP-dependent protein kinase in Escherichia coli , 1993 .

[29]  R. Fleischmann,et al.  Expression of Chinese hamster cAMP-dependent protein kinase in Escherichia coli results in growth inhibition of bacterial cells: a model system for the rapid screening of mutant type I regulatory subunits. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[30]  S. Taylor,et al.  Expression of the catalytic subunit of cAMP-dependent protein kinase in Escherichia coli: multiple isozymes reflect different phosphorylation states. , 1993, Protein engineering.

[31]  K. Murray,et al.  Cyclic AMP and mechanisms of vasolidation , 1990 .

[32]  S. Taylor,et al.  Expression of the catalytic subunit of cAMP-dependent protein kinase in Escherichia coli. , 1989, The Journal of biological chemistry.

[33]  A. Means,et al.  Myosin light chain kinase structure function analysis using bacterial expression. , 1989, The Journal of biological chemistry.

[34]  Maurice Green,et al.  Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein , 1988, Cell.

[35]  Carl O. Pabo,et al.  Cellular uptake of the tat protein from human immunodeficiency virus , 1988, Cell.

[36]  F. Hofmann,et al.  A catalytically active fragment of cGMP-dependent protein kinase. Occupation of its cGMP-binding sites does not affect its phosphotransferase activity. , 1987, European journal of biochemistry.