HELEN DYSON

Summary

Affiliation: The Scripps Research Institute
Country: USA

Publications

  1. ncbi request reprint According to current textbooks, a well-defined three-dimensional structure is a prerequisite for the function of a protein. Is this correct?
    H Jane Dyson
    The Scripps Research Institute, La Jolla, California 92037, USA
    IUBMB Life 58:107-9. 2006
  2. pmc The client protein p53 adopts a molten globule-like state in the presence of Hsp90
    Sung Jean Park
    Department of Molecular Biology, The Scripps Research Institute, La Jolla, California, USA
    Nat Struct Mol Biol 18:537-41. 2011
  3. pmc Role of disorder in IκB-NFκB interaction
    H Jane Dyson
    Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA
    IUBMB Life 64:499-505. 2012
  4. pmc The role of hydrophobic interactions in initiation and propagation of protein folding
    H Jane Dyson
    Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Proc Natl Acad Sci U S A 103:13057-61. 2006
  5. ncbi request reprint Intrinsically unstructured proteins and their functions
    H Jane Dyson
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
    Nat Rev Mol Cell Biol 6:197-208. 2005
  6. ncbi request reprint Unfolded proteins and protein folding studied by NMR
    H Jane Dyson
    Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Chem Rev 104:3607-22. 2004
  7. pmc Hydrogen-deuterium exchange strategy for delineation of contact sites in protein complexes
    H Jane Dyson
    Department of Molecular Biology MB2, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States
    FEBS Lett 582:1495-500. 2008
  8. pmc Roles of intrinsic disorder in protein-nucleic acid interactions
    H Jane Dyson
    Department of Molecular Biology, The Scripps Research Institute, La Jolla, USA
    Mol Biosyst 8:97-104. 2012
  9. ncbi request reprint Coupling of folding and binding for unstructured proteins
    H Jane Dyson
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Curr Opin Struct Biol 12:54-60. 2002
  10. pmc Expanding the proteome: disordered and alternatively folded proteins
    H Jane Dyson
    Department of Molecular Biology MB2, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Q Rev Biophys 44:467-518. 2011

Research Grants

  1. NMR Studies of Chaperone-Client Protein Interactions
    HELEN JANE DYSON; Fiscal Year: 2010
  2. NMR Studies of Chaperone-Client Protein Interactions
    HELEN DYSON; Fiscal Year: 2009
  3. UNFOLDED STATES AND FOLDING PATHWAYS BY NMR
    HELEN DYSON; Fiscal Year: 2005
  4. UNFOLDED STATES AND FOLDING PATHWAYS BY NMR
    HELEN DYSON; Fiscal Year: 2004
  5. UNFOLDED STATES AND FOLDING PATHWAYS BY NMR
    HELEN DYSON; Fiscal Year: 2003
  6. UNFOLDED STATES AND FOLDING PATHWAYS BY NMR
    HELEN DYSON; Fiscal Year: 2002
  7. UNFOLDED STATES AND FOLDING PATHWAYS BY NMR
    HELEN DYSON; Fiscal Year: 2001
  8. UNFOLDED STATES AND FOLDING PATHWAYS BY NMR
    HELEN DYSON; Fiscal Year: 2000
  9. UNFOLDED STATES AND FOLDING PATHWAYS BY NMR
    HELEN DYSON; Fiscal Year: 1999

Collaborators

Detail Information

Publications66

  1. ncbi request reprint According to current textbooks, a well-defined three-dimensional structure is a prerequisite for the function of a protein. Is this correct?
    H Jane Dyson
    The Scripps Research Institute, La Jolla, California 92037, USA
    IUBMB Life 58:107-9. 2006
  2. pmc The client protein p53 adopts a molten globule-like state in the presence of Hsp90
    Sung Jean Park
    Department of Molecular Biology, The Scripps Research Institute, La Jolla, California, USA
    Nat Struct Mol Biol 18:537-41. 2011
    ..We propose that Hsp90 interacts with p53 by multiple transient interactions, forming a dynamic heterogeneous manifold of conformational states that resembles a molten globule...
  3. pmc Role of disorder in IκB-NFκB interaction
    H Jane Dyson
    Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA
    IUBMB Life 64:499-505. 2012
    ....
  4. pmc The role of hydrophobic interactions in initiation and propagation of protein folding
    H Jane Dyson
    Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Proc Natl Acad Sci U S A 103:13057-61. 2006
    ..These results provide a putative mechanism for the control of protein-folding initiation and growth by polar/nonpolar sequence propensity alone...
  5. ncbi request reprint Intrinsically unstructured proteins and their functions
    H Jane Dyson
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
    Nat Rev Mol Cell Biol 6:197-208. 2005
    ..Many disordered segments fold on binding to their biological targets (coupled folding and binding), whereas others constitute flexible linkers that have a role in the assembly of macromolecular arrays...
  6. ncbi request reprint Unfolded proteins and protein folding studied by NMR
    H Jane Dyson
    Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Chem Rev 104:3607-22. 2004
  7. pmc Hydrogen-deuterium exchange strategy for delineation of contact sites in protein complexes
    H Jane Dyson
    Department of Molecular Biology MB2, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States
    FEBS Lett 582:1495-500. 2008
    ..This method can potentially provide data for complexes with unknown structure and for large or dynamic complexes inaccessible via NMR and X-ray methods...
  8. pmc Roles of intrinsic disorder in protein-nucleic acid interactions
    H Jane Dyson
    Department of Molecular Biology, The Scripps Research Institute, La Jolla, USA
    Mol Biosyst 8:97-104. 2012
    ....
  9. ncbi request reprint Coupling of folding and binding for unstructured proteins
    H Jane Dyson
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Curr Opin Struct Biol 12:54-60. 2002
    ..Many new examples of coupled folding and binding events have been reported recently, providing new insights into mechanisms of molecular recognition...
  10. pmc Expanding the proteome: disordered and alternatively folded proteins
    H Jane Dyson
    Department of Molecular Biology MB2, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Q Rev Biophys 44:467-518. 2011
    ....
  11. ncbi request reprint Solution structure of the KIX domain of CBP bound to the transactivation domain of c-Myb
    Tsaffrir Zor
    Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 N Torrey Pines Road, La Jolla, CA 92037, USA
    J Mol Biol 337:521-34. 2004
    ..These results explain the structural and thermodynamic basis for the observed constitutive versus inducible activation properties of c-Myb and CREB...
  12. ncbi request reprint Sequence determinants of a protein folding pathway
    Chiaki Nishimura
    Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    J Mol Biol 351:383-92. 2005
    ....
  13. ncbi request reprint CBP/p300 TAZ1 domain forms a structured scaffold for ligand binding
    Roberto N De Guzman
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
    Biochemistry 44:490-7. 2005
    ..The structure of the free TAZ1 domain suggests that this difference is an inherent feature that determines binding specificity and facilitates discrimination between different subsets of transcription factors by the two TAZ domains...
  14. pmc Enhanced picture of protein-folding intermediates using organic solvents in H/D exchange and quench-flow experiments
    Chiaki Nishimura
    Department of Molecular Biology and The Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Proc Natl Acad Sci U S A 102:4765-70. 2005
    ..the kinetic experiment (pH 6) and the change in the status of the stabilizing hydrogen bond between the side chains of His-24 and His-119...
  15. pmc Energetic frustration of apomyoglobin folding: role of the B helix
    Chiaki Nishimura
    Department of Molecular Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    J Mol Biol 396:1319-28. 2010
    ..We conclude that instability at the N-terminus of the B helix of apomyoglobin contributes to the energetic frustration of folding by preventing docking and stabilization of the E helix...
  16. ncbi request reprint Cooperativity in transcription factor binding to the coactivator CREB-binding protein (CBP). The mixed lineage leukemia protein (MLL) activation domain binds to an allosteric site on the KIX domain
    Natalie K Goto
    Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA
    J Biol Chem 277:43168-74. 2002
    ..In the case of MLL and c-Myb, both proteins are involved in proliferation of hematopoietic cells and leukemogenesis, and synergistic interactions mediated by CBP may play a functional role...
  17. ncbi request reprint Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites
    Roberto N De Guzman
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA
    J Biol Chem 279:3042-9. 2004
    ....
  18. ncbi request reprint Molecular hinges in protein folding: the urea-denatured state of apomyoglobin
    Stephan Schwarzinger
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA
    Biochemistry 41:12681-6. 2002
    ..The model derived from the behavior of apoMb in urea depends only on the most fundamental properties of the local amino acid sequence, and thus provides a feasible paradigm for the initiation of folding...
  19. ncbi request reprint Identification of native and non-native structure in kinetic folding intermediates of apomyoglobin
    Chiaki Nishimura
    Department of Molecular Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    J Mol Biol 355:139-56. 2006
    ....
  20. ncbi request reprint The apomyoglobin folding pathway revisited: structural heterogeneity in the kinetic burst phase intermediate
    Chiaki Nishimura
    Department of Molecular Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, 92037, La Jolla, CA, USA
    J Mol Biol 322:483-9. 2002
    ..These sites include, besides the E helix, the ends of the A and B helices and part of the C helix. Our results give significant support to the hypothesis that the kinetic molten globule intermediate of apoMb is native-like...
  21. ncbi request reprint Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings
    Ronaldo Mohana-Borges
    Department of Molecular Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Pines Road, La Jolla, CA 92037, USA
    J Mol Biol 340:1131-42. 2004
    ....
  22. pmc Embryonic neural inducing factor churchill is not a DNA-binding zinc finger protein: solution structure reveals a solvent-exposed beta-sheet and zinc binuclear cluster
    Brian M Lee
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    J Mol Biol 371:1274-89. 2007
    ..Since Churchill does not appear to bind DNA, we suggest that it may function in embryogenesis as a protein-interaction factor...
  23. ncbi request reprint The dynamic energy landscape of dihydrofolate reductase catalysis
    David D Boehr
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Science 313:1638-42. 2006
    ..Thus, the modulation of the energy landscape by the bound ligands funnels the enzyme through its reaction cycle along a preferred kinetic path...
  24. pmc The kinetic and equilibrium molten globule intermediates of apoleghemoglobin differ in structure
    Chiaki Nishimura
    Department of Molecular Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    J Mol Biol 378:715-25. 2008
    ....
  25. pmc Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response
    Sonja A Dames
    Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Proc Natl Acad Sci U S A 99:5271-6. 2002
    ..The structure of this complex provides new insights into the mechanism through which Hif-1 alpha recruits CBP/p300 in response to hypoxia...
  26. ncbi request reprint Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance
    H Jane Dyson
    Department of Molecular Biology, Scripps Research Institute, La Jolla, California 92037, USA
    Adv Protein Chem 62:311-40. 2002
  27. pmc Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysis
    David D Boehr
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
    Biochemistry 47:9227-33. 2008
    ....
  28. ncbi request reprint The reduced, denatured somatomedin B domain of vitronectin refolds into a stable, biologically active molecule
    Yuichi Kamikubo
    Department of Cell Biology, Division of Vascular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
    Biochemistry 45:3297-306. 2006
    ..2004) Biochemistry 43, 6519] and that it binds specifically to mAb 153 via an interface that includes the three aromatic side chains previously implicated in binding to PAI-1...
  29. ncbi request reprint Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase
    Jason R Schnell
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
    Biochemistry 43:374-83. 2004
    ..Conformational fluctuations of these side chains may play a role in transition state stabilization; the observed line broadening for Ile14 suggests motions on a microsecond/millisecond time scale...
  30. pmc The CBP/p300 TAZ1 domain in its native state is not a binding partner of MDM2
    Theresia Matt
    Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Biochem J 381:685-91. 2004
    ..Rather, unfolded TAZ1 and HDM2 proteins have a high tendency to aggregate, and non-specific protein complexes are formed under certain conditions...
  31. pmc Transfer of flexibility between ankyrin repeats in IkappaB* upon formation of the NF-kappaB complex
    Shih Che Sue
    Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    J Mol Biol 380:917-31. 2008
    ....
  32. pmc Structural characterization of partially folded intermediates of apomyoglobin H64F
    Stephan Schwarzinger
    Department of Molecular Biology, The Scripps Research Institute and Skaggs Institute for Chemical Biology, La Jolla, California 92037, USA
    Protein Sci 17:313-21. 2008
    ....
  33. pmc Cooperative regulation of p53 by modulation of ternary complex formation with CBP/p300 and HDM2
    Josephine C Ferreon
    Department of Molecular Biology, The Scripps Research Institute, 10550 N Torrey Pines Road, La Jolla, CA 92037, USA
    Proc Natl Acad Sci U S A 106:6591-6. 2009
    ..After cellular stress and DNA damage, p53 becomes phosphorylated at T18 and other residues in the AD1 region, releases HDM2 and binds preferentially to CBP/p300, leading to stabilization and activation of p53...
  34. pmc Functional dynamics of the folded ankyrin repeats of I kappa B alpha revealed by nuclear magnetic resonance
    Carla F Cervantes
    Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Dr, La Jolla, CA 92093 0378, USA
    Biochemistry 48:8023-31. 2009
    ..The regions showing micro- to millisecond motions in the free protein are the ends of the beta-hairpins that directly interact with NF-kappaB in the complex...
  35. pmc Modeling transient collapsed states of an unfolded protein to provide insights into early folding events
    Daniel J Felitsky
    Department of Molecular Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Proc Natl Acad Sci U S A 105:6278-83. 2008
    ....
  36. pmc Linking folding and binding
    Peter E Wright
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States
    Curr Opin Struct Biol 19:31-8. 2009
    ....
  37. ncbi request reprint Localization of sites of interaction between p23 and Hsp90 in solution
    Maria A Martinez-Yamout
    Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA
    J Biol Chem 281:14457-64. 2006
    ..We conclude that p23 forms a specific complex with Hsp90 primarily through binding to its middle domain...
  38. ncbi request reprint The LEF-1 high-mobility group domain undergoes a disorder-to-order transition upon formation of a complex with cognate DNA
    John J Love
    Department of Molecular Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
    Biochemistry 43:8725-34. 2004
    ..Upon complex formation, the protein domain undergoes a cooperative folding transition with DNA to a highly ordered and well-folded state...
  39. ncbi request reprint Disulfide bonding arrangements in active forms of the somatomedin B domain of human vitronectin
    Yuichi Kamikubo
    Department of Cell Biology, Division of Vascular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
    Biochemistry 43:6519-34. 2004
    ..These results suggest that active forms of the SMB domain may have a number of allowed disulfide bond arrangements as long as the Cys(25)-Cys(31) disulfide bond is preserved...
  40. pmc Packing, specificity, and mutability at the binding interface between the p160 coactivator and CREB-binding protein
    Stephen J Demarest
    Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA
    Protein Sci 13:203-10. 2004
    ..These results suggest a mechanism for formation of the complex where the unfolded ACTR domain interacts with the partly folded CBP domain in a rapid and specific manner to form the final stable complex...
  41. ncbi request reprint Structure of the nuclear factor ALY: insights into post-transcriptional regulatory and mRNA nuclear export processes
    Gabriela C Pérez-Alvarado
    Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
    Biochemistry 42:7348-57. 2003
    ..The structure of the conserved RBD of ALY provides insight into the nature of interactions involving this multifunctional protein...
  42. pmc Diagnostic chemical shift markers for loop conformation and substrate and cofactor binding in dihydrofolate reductase complexes
    Michael J Osborne
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA
    Protein Sci 12:2230-8. 2003
    ..coli DHFR are populated in solution...
  43. ncbi request reprint Solution structure of the N-terminal zinc fingers of the Xenopus laevis double-stranded RNA-binding protein ZFa
    Heiko M Möller
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    J Mol Biol 351:718-30. 2005
    ..We conclude that the ZFa zinc fingers represent a new motif for the binding of double-stranded RNA...
  44. ncbi request reprint ZZ domain of CBP: an unusual zinc finger fold in a protein interaction module
    Glen B Legge
    Department of Molecular Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    J Mol Biol 343:1081-93. 2004
    ..These homologies suggest that the ZZ domain is involved in ligand binding or molecular scaffolding, with specificity provided by the variability of the sequence that contains the helix in the murine CPB ZZ domain structure...
  45. ncbi request reprint Roles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activators
    Tsaffrir Zor
    Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA
    J Biol Chem 277:42241-8. 2002
    ..After induction by phosphorylation, CREB is able to compete effectively with other transcriptional activators for binding to CBP...
  46. ncbi request reprint Recognition of the mRNA AU-rich element by the zinc finger domain of TIS11d
    Brian P Hudson
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
    Nat Struct Mol Biol 11:257-64. 2004
    ..The TIS11d structure provides insights into the RNA-binding functions of this large family of CCCH zinc finger proteins...
  47. ncbi request reprint Monomeric complex of human orphan estrogen related receptor-2 with DNA: a pseudo-dimer interface mediates extended half-site recognition
    Micah D Gearhart
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    J Mol Biol 327:819-32. 2003
    ..This pseudo-dimer interface provides a basis for the expansion of DNA recognition and suggests a mechanism through which dimerization may have evolved from an ancestral monomeric receptor...
  48. pmc Structural basis for subversion of cellular control mechanisms by the adenoviral E1A oncoprotein
    Josephine C Ferreon
    Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Proc Natl Acad Sci U S A 106:13260-5. 2009
    ..These observations reveal the molecular basis by which E1A inhibits p53-mediated transcriptional activation and provide a rationale for the efficiency of cellular transformation by the adenoviral E1A oncoprotein...
  49. pmc Role of a solvent-exposed tryptophan in the recognition and binding of antibiotic substrates for a metallo-beta-lactamase
    James J A Huntley
    Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Protein Sci 12:1368-75. 2003
    ..Rather, a more productive approach may be to design therapeutics directed towards this solvent-exposed tryptophan residue...
  50. ncbi request reprint Structure of the Escherichia coli quorum sensing protein SdiA: activation of the folding switch by acyl homoserine lactones
    Yong Yao
    Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    J Mol Biol 355:262-73. 2006
    ....
  51. pmc Millisecond timescale fluctuations in dihydrofolate reductase are exquisitely sensitive to the bound ligands
    David D Boehr
    Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines, La Jolla, CA 92037, USA
    Proc Natl Acad Sci U S A 107:1373-8. 2010
    ....
  52. pmc Leu628 of the KIX domain of CBP is a key residue for the interaction with the MLL transactivation domain
    Munehito Arai
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    FEBS Lett 584:4500-4. 2010
    ..Unexpectedly, MLL also binds to the c-Myb/phosphorylated kinase-inducible domain of CREB (pKID) site of KIX, highlighting the complex nature of interactions involving intrinsically disordered transcriptional activators...
  53. ncbi request reprint Folding of a beta-sheet protein monitored by real-time NMR spectroscopy
    Mineyuki Mizuguchi
    Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    J Mol Biol 328:1161-71. 2003
    ..Our results show that the local and long-range interactions in the native apoplastocyanin are formed simultaneously, consistent with highly cooperative formation of the native structure...
  54. pmc Evaluating beta-turn mimics as beta-sheet folding nucleators
    Amelia A Fuller
    Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Proc Natl Acad Sci U S A 106:11067-72. 2009
    ..These beta-turn mimics can now be used to interrogate protein folding transition state structures and the 2 kinetic analyses presented can be used to assess the nucleation capacity of other beta-turn mimics...
  55. pmc Prediction of the rotational tumbling time for proteins with disordered segments
    Sung Hun Bae
    Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA
    J Am Chem Soc 131:6814-21. 2009
    ....
  56. ncbi request reprint Role of the B helix in early folding events in apomyoglobin: evidence from site-directed mutagenesis for native-like long range interactions
    Chiaki Nishimura
    Department of Molecular Biology, Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    J Mol Biol 334:293-307. 2003
    ....
  57. ncbi request reprint An NMR perspective on enzyme dynamics
    David D Boehr
    Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
    Chem Rev 106:3055-79. 2006
  58. ncbi request reprint Mechanism of coupled folding and binding of an intrinsically disordered protein
    Kenji Sugase
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
    Nature 447:1021-5. 2007
    ..Future applications of our method will provide new understanding of the molecular mechanisms by which intrinsically disordered proteins perform their diverse biological functions...
  59. pmc Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis
    Dan McElheny
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Proc Natl Acad Sci U S A 102:5032-7. 2005
    ....
  60. doi request reprint NMR relaxation study of the complex formed between CBP and the activation domain of the nuclear hormone receptor coactivator ACTR
    Marc Olivier Ebert
    Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
    Biochemistry 47:1299-308. 2008
    ....
  61. ncbi request reprint Generation of native-like protein structures from limited NMR data, modern force fields and advanced conformational sampling
    Jianhan Chen
    Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, LaJolla, CA 92037, USA
    J Biomol NMR 31:59-64. 2005
    ....
  62. ncbi request reprint Structure, dynamics, and catalytic function of dihydrofolate reductase
    Jason R Schnell
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
    Annu Rev Biophys Biomol Struct 33:119-40. 2004
    ..These studies provide a detailed map of changes in conformation and dynamics throughout the catalytic cycle of DHFR and give new insights into the role of protein motions in the catalytic activity of this enzyme...
  63. ncbi request reprint Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators
    Stephen J Demarest
    Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
    Nature 415:549-53. 2002
    ..Our study uncovers a unique mechanism, called 'synergistic folding', through which p160 coactivators recruit CBP/p300 to allow transmission of the hormonal signal to the transcriptional machinery...
  64. pmc Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains
    Jonathan M Wojciak
    Department of Molecular Biology, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA
    EMBO J 28:948-58. 2009
    ..Because the different STAT TADs recognize different regions of CBP/p300, there is a potential for multivalent binding by STAT heterodimers that could enhance the recruitment of the coactivators to promoters...
  65. pmc Mapping the interactions of the p53 transactivation domain with the KIX domain of CBP
    Chul Won Lee
    Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
    Biochemistry 48:2115-24. 2009
    ..The p53 TAD simultaneously occupies the two distinct sites that have been identified on the CBP KIX domain and efficiently competes for these sites with other known KIX-binding transcription factors...
  66. pmc Prion proteins with pathogenic and protective mutations show similar structure and dynamics
    Sung Hun Bae
    Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 90237, USA
    Biochemistry 48:8120-8. 2009
    ....

Research Grants11

  1. NMR Studies of Chaperone-Client Protein Interactions
    HELEN JANE DYSON; Fiscal Year: 2010
    ..Our studies will elucidate the structural and dynamic nature of these complexes in solution, as a guide for future drug design efforts. ..
  2. NMR Studies of Chaperone-Client Protein Interactions
    HELEN DYSON; Fiscal Year: 2009
    ..Our studies will elucidate the structural and dynamic nature of these complexes in solution, as a guide for future drug design efforts. ..
  3. UNFOLDED STATES AND FOLDING PATHWAYS BY NMR
    HELEN DYSON; Fiscal Year: 2005
    ..abstract_text> ..
  4. UNFOLDED STATES AND FOLDING PATHWAYS BY NMR
    HELEN DYSON; Fiscal Year: 2004
    ..abstract_text> ..
  5. UNFOLDED STATES AND FOLDING PATHWAYS BY NMR
    HELEN DYSON; Fiscal Year: 2003
    ..abstract_text> ..
  6. UNFOLDED STATES AND FOLDING PATHWAYS BY NMR
    HELEN DYSON; Fiscal Year: 2002
    ..abstract_text> ..
  7. UNFOLDED STATES AND FOLDING PATHWAYS BY NMR
    HELEN DYSON; Fiscal Year: 2001
    ..This surprising result typifies the new information that is constantly being uncovered in the protein folding and assembly a continual source of new and important information. ..
  8. UNFOLDED STATES AND FOLDING PATHWAYS BY NMR
    HELEN DYSON; Fiscal Year: 2000
    ..This surprising result typifies the new information that is constantly being uncovered in the protein folding and assembly a continual source of new and important information. ..
  9. UNFOLDED STATES AND FOLDING PATHWAYS BY NMR
    HELEN DYSON; Fiscal Year: 1999
    ..This surprising result typifies the new information that is constantly being uncovered in the protein folding and assembly a continual source of new and important information. ..