Research Topics
Genomes and Genes
| Elizabeth J GoldsmithSummaryAffiliation: University of Texas Southwestern Medical Center Country: USA Publications
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Detail Information
Publications
Three-dimensional docking in the MAPK p38αElizabeth J Goldsmith
Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas, Dallas, TX 75390 8816, USA
Sci Signal 4:pe47. 2011..This structure offers insights into the action of MKP5 and other MKPs...- Structural studies of MAP Kinase cascade componentsElizabeth J Goldsmith
Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, Dallas, TX, USA
Methods Mol Biol 661:223-37. 2010..Here, we describe the preparation of MAP2K MEK6 and MAP3K TAO2 substituted with selenomethionine (SeMet) for de novo phasing. TAO2 and SeMet TAO2 were expressed in insect cells... 
Substrate and docking interactions in serine/threonine protein kinasesElizabeth J Goldsmith
Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, Texas 75390-8816, USA
Chem Rev 107:5065-81. 2007- WNK1: analysis of protein kinase structure, downstream targets, and potential roles in hypertensionBing E Xu
Department of Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd, Dallas, TX, USA
Cell Res 15:6-10. 2005..The WNK kinases may be able to influence ion homeostasis through its effects on synaptotagmin function... - The structure of the MAP2K MEK6 reveals an autoinhibitory dimerXiaoshan Min
Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, TX 75390 8816, USA
Structure 17:96-104. 2009..The autoinhibited structure likely confers specificity on active MAP2Ks. The dimer may also serve the function in unphosphorylated MEK6 of preventing activation loop phosphorylation by inappropriate kinases... - Properties of WNK1 and implications for other family membersLisa Y Lenertz
Department of Pharmacology, The University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75390, USA
J Biol Chem 280:26653-8. 2005..However, WNK1 phosphorylated both WNK4 and WNK2. In addition, the WNK1 autoinhibitory domain inhibited the catalytic activity of these WNKs. These findings suggest potential mechanisms for interconnected regulation of WNK family members... 
Evolution of substrate specificity within a diverse family of beta/alpha-barrel-fold basic amino acid decarboxylases: X-ray structure determination of enzymes with specificity for L-arginine and carboxynorspermidineXiaoyi Deng
Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas 75390 9041, USA
J Biol Chem 285:25708-19. 2010..These studies provide insight into the structural basis for the evolution of novel function within a common structural-fold...- Crystal structure of the TAO2 kinase domain: activation and specificity of a Ste20p MAP3KTianjun Zhou
Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA
Structure 12:1891-900. 2004..Finally, active TAO2 displays unusual interactions with ATP, involving, in part, a subgroup-specific C-terminal extension of TAO2. The observed interactions may be useful in making specific inhibitors of TAO kinases... - Unique MAP Kinase binding sitesRadha Akella
Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, Dallas, TX 75390 8816, USA
Biochim Biophys Acta 1784:48-55. 2008..Crystallographic evidence of these latter two binding sites is presented... - Structural plasticity of malaria dihydroorotate dehydrogenase allows selective binding of diverse chemical scaffoldsXiaoyi Deng
Department of Pharmacology, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75390 9041, USA
J Biol Chem 284:26999-7009. 2009..Together, these studies will directly impact efforts to exploit PfDHODH for the development of anti-malarial chemotherapy... - Crystallization of MAP kinasesSeung-Jae Lee
Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, TX 75390-8816, USA
Methods 40:224-33. 2006..Further, some success has been gained in crystallizing the MAP kinase activators MAP2Ks and MAP3K kinase domains. This review describes the key methods that have been utilized to crystallize MAP kinases and MAP kinase pathway components... - WNK1 phosphorylates synaptotagmin 2 and modulates its membrane bindingByung Hoon Lee
Department of Pharmacology, The University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA
Mol Cell 15:741-51. 2004..These findings provide a biochemical mechanism that could lead to the retention or insertion of proteins in the plasma membrane. Interruption of this regulatory pathway may disturb membrane events that regulate ion balance... - Crystal structure of the MAP3K TAO2 kinase domain bound by an inhibitor staurosporineTian Jun Zhou
Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas, Dallas, TX 75390 9038, USA
Acta Biochim Biophys Sin (Shanghai) 38:385-92. 2006..The structure presented here should aid in the design of inhibitors specific to TAO2 and related kinases... - Docking interactions induce exposure of activation loop in the MAP kinase ERK2Tianjun Zhou
Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, Texas 75390, USA
Structure 14:1011-9. 2006..However, the binding interactions and conformational changes are unique to each, thus contributing to specificity among MAP kinases... - Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylationSohini Mukherjee
Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA
Science 312:1211-4. 2006..The acetylation on MAPKK6 directly competed with phosphorylation, preventing activation of the modified protein. This covalent modification may be used as a general regulatory mechanism in biological signaling... - Crystal structure of domain-swapped STE20 OSR1 kinase domainSeung Jae Lee
Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, 75390 9041, USA
Protein Sci 18:304-13. 2009..The OSR1 kinase domain has now been added to a growing list of domain-swapped protein kinases recently reported, suggesting that the domain-swapping event provides an additional layer of complexity in regulating protein kinase activity... - Crystal structure of the kinase domain of WNK1, a kinase that causes a hereditary form of hypertensionXiaoshan Min
Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA
Structure 12:1303-11. 2004..The structure of the WNK1 catalytic domain, with its unique active site, may help in the design of therapeutic reagents for the treatment of hypertension... - The third conformation of p38α MAP kinase observed in phosphorylated p38α and in solutionRadha Akella
Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, TX 75390 8816, USA
Structure 18:1571-8. 2010..The structure supports the idea that MAP kinases adopt three distinct conformations: unphosphorylated, phosphorylated, and a docking peptide-induced form... - Mutations in ERK2 binding sites affect nuclear entryMustafa N Yazicioglu
Departments of Pharmacology, The University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75390 9041, USA
J Biol Chem 282:28759-67. 2007..These results further support the idea that direct interactions with nucleoporins are involved in ERK2 nuclear entry and that multiple events contribute to the ligand-dependent relocalization of these protein kinases... - X-ray structure of Paramecium bursaria Chlorella virus arginine decarboxylase: insight into the structural basis for substrate specificityRahul Shah
Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas 75390 9041, USA
Biochemistry 46:2831-41. 2007..In conjunction with prior structural studies these data predict that this loop adopts different conformations throughout the catalytic cycle, and that loop movement may be kinetically linked to the rate-limiting step of product release... - Characterization of mitogen-activated protein kinase (MAPK) dimersJulie L Wilsbacher
Department of Pharmacology, University of Texas Southwestern Medical Center, 6001 Forest Park Road, Dallas, Texas 75390-9041, USA
Biochemistry 45:13175-82. 2006.... - Multiple active site conformations revealed by distant site mutation in ornithine decarboxylaseLaurie K Jackson
Department of Pharmacology, The University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, Texas 75390-9041, USA
Biochemistry 43:12990-9. 2004..These data also suggest that the structure is less constrained in the mutant enzyme. The observation of a gem-diamine intermediate provides insight into the conformational changes that occur during the ODC catalytic cycle... - Phylogenetic diversity and the structural basis of substrate specificity in the beta/alpha-barrel fold basic amino acid decarboxylasesJeongmi Lee
Departments of Pharmacology and Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390 9041, USA
J Biol Chem 282:27115-25. 2007..Our data demonstrate that there is greater structural and functional diversity in bacterial polyamine biosynthetic decarboxylases than previously suspected... - Structure of MAPKsElizabeth J Goldsmith
Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, Dallas, TX, USA
Methods Mol Biol 250:127-44. 2004 - X-ray structure determination of Trypanosoma brucei ornithine decarboxylase bound to D-ornithine and to G418: insights into substrate binding and ODC conformational flexibilityLaurie K Jackson
Department of Pharmacology, The University of Texas Southwestern Medical Center, Dallas, 5323 Harry Hines Boulevard, TX 75390-9041, USA
J Biol Chem 278:22037-43. 2003..The disordering of residues in the active site provides a potential mechanism for inhibition by G418 and suggests that allosteric inhibition from this site is feasible... - Natural language query in the biochemistry and molecular biology domains based on cognition search™Elizabeth J Goldsmith
Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, Texas 75390 8816
Summit on Translat Bioinforma 2009:32-7. 2009..Thus, the CSIR has the right architecture to form the basis for a scientific search engine... - Another twist in helix C and a missing pocketElizabeth J Goldsmith
Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, 75390, USA
Structure 10:888-9. 2002..PKB/Akt reveals a major role for helix C in the regulation of activity in the first structure of an AGC family protein kinase in its low-activity form... - Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3bChung I Chang
Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA
Mol Cell 9:1241-9. 2002..The peptides also induce unexpected and different conformational changes in the active site, as well as structural disorder in the phosphorylation lip... - Determinants that control the specific interactions between TAB1 and p38alphaHuamin Zhou
The Key Laboratory of the Ministry of Education for Cell Biology and Tumor Cell Engineering, School of Life Sciences, Xiamen University, Fujian, China
Mol Cell Biol 26:3824-34. 2006..This suggests that TAB1-induced autophosphorylation of p38alpha results from conformational changes that are similar but unique to those seen in p38alpha interactions with its substrates and activating kinases... - Regulation of WNK1 by an autoinhibitory domain and autophosphorylationBing E Xu
Department of Pharmacology, The University of Texas Southwestern Medical Center, Dallas 75390 9041, USA
J Biol Chem 277:48456-62. 2002..We also found that WNK1 expressed in bacteria is autophosphorylated; autophosphorylation on serine 382 in the activation loop is required for its activity... - Docking motif interactions in MAP kinases revealed by hydrogen exchange mass spectrometryThomas Lee
Department of Chemistry and Biochemistry, University of Colorado at Boulder, Boulder, CO 80309, USA
Mol Cell 14:43-55. 2004..In vitro assays confirm the dependence of Elk1 and nucleoporin binding on ERK2 phosphorylation, and provide a structural basis for preferential involvement of active ERK in substrate binding and nuclear pore protein interactions...