Activation mechanisms of transcriptional regulator CooA revealed by small-angle X-ray scattering.
暂无分享,去创建一个
[1] S. Aono. Biochemical and biophysical properties of the CO-sensing transcriptional activator CooA. , 2003, Accounts of chemical research.
[2] Y. Nishikawa,et al. Evaluation of three algorithms for ab initio determination of three-dimensional shape from one-dimensional solution scattering profiles , 2003 .
[3] Dmitri I. Svergun,et al. Uniqueness of ab initio shape determination in small-angle scattering , 2003 .
[4] Y. Izumi,et al. Solution X-ray scattering data show structural differences among chimeras of yeast and chicken calmodulin: implications for structure and function. , 2003, Biochemistry.
[5] R. Kerby,et al. Repositioning about the dimer interface of the transcription regulator CooA: a major signal transduction pathway between the effector and DNA-binding domains. , 2003, Journal of molecular biology.
[6] Dmitri I Svergun,et al. Addition of missing loops and domains to protein models by x-ray solution scattering. , 2002, Biophysical journal.
[7] Dmitri I Svergun,et al. Advances in structure analysis using small-angle scattering in solution. , 2002, Current opinion in structural biology.
[8] Pablo Chacón,et al. Using Situs for the registration of protein structures with low-resolution bead models from X-ray solution scattering , 2001 .
[9] G. Roberts,et al. Mapping CooA·RNA Polymerase Interactions , 2001, The Journal of Biological Chemistry.
[10] S. Takahashi,et al. Binding of CO at the Pro2 Side Is Crucial for the Activation of CO-sensing Transcriptional Activator CooA , 2001, The Journal of Biological Chemistry.
[11] G. Gilliland,et al. The Structure of the T127L/S128A Mutant of cAMP Receptor Protein Facilitates Promoter Site Binding* , 2001, The Journal of Biological Chemistry.
[12] H. Miyatake,et al. Redox Properties and Coordination Structure of the Heme in the CO-sensing Transcriptional Activator CooA* , 2001, The Journal of Biological Chemistry.
[13] G. Borgstahl,et al. Dynamic light-scattering analysis of full-length human RPA14/32 dimer: purification, crystallization and self-association. , 2001, Acta crystallographica. Section D, Biological crystallography.
[14] W. Lanzilotta,et al. Characterization of Variants Altered at the N-terminal Proline, a Novel Heme-Axial Ligand in CooA, the CO-sensing Transcriptional Activator* , 2000, The Journal of Biological Chemistry.
[15] M. Chan. CooA, CAP and allostery , 2000, Nature Structural Biology.
[16] D. J. Schuller,et al. Structure of the CO sensing transcription activator CooA , 2000, Nature Structural Biology.
[17] Y. Mizutani,et al. Identification of histidine 77 as the axial heme ligand of carbonmonoxy CooA by picosecond time-resolved resonance Raman spectroscopy. , 2000, Biochemistry.
[18] T. Uruga,et al. Small‐angle X‐ray scattering station at the SPring‐8 RIKEN beamline , 2000 .
[19] T. Matsuo,et al. Control of CooA activity by the mutation at the C-terminal end of the heme-binding domain. , 2000, Journal of inorganic biochemistry.
[20] N. Yagi,et al. The use of a Hamamatsu X-ray image intensifier with a cooled CCD as a solution X-ray scattering detector , 1999 .
[21] H. Nakajima,et al. Recognition of target DNA and transcription activation by the CO-sensing transcriptional activator CooA. , 1999, Biochemical and biophysical research communications.
[22] T. Donohue,et al. Transcription activation by CooA, the CO-sensing factor from Rhodospirillum rubrum. The interaction between CooA and the C-terminal domain of the alpha subunit of RNA polymerase. , 1999, The Journal of biological chemistry.
[23] K. Ohkubo,et al. Redox-controlled Ligand Exchange of the Heme in the CO-sensing Transcriptional Activator CooA* , 1998, The Journal of Biological Chemistry.
[24] J Brown,et al. Determination of the Conformations of cAMP Receptor Protein and Its T127L,S128A Mutant with and without cAMP from Small Angle Neutron Scattering Measurements* , 1998, The Journal of Biological Chemistry.
[25] D I Svergun,et al. Protein hydration in solution: experimental observation by x-ray and neutron scattering. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[26] T. Matsuo,et al. Single transduction in the transcriptional activator CooA containing a heme-based CO sensor: isolation of a dominant positive mutant which is active as the transcriptional activator even in the absence of CO. , 1997, Biochemical and biophysical research communications.
[27] R. Kerby,et al. CooA, a CO-sensing transcription factor from Rhodospirillum rubrum, is a CO-binding heme protein. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[28] H. Nakajima,et al. A novel heme protein that acts as a carbon monoxide-dependent transcriptional activator in Rhodospirillum rubrum. , 1996, Biochemical and biophysical research communications.
[29] M. Billeter,et al. MOLMOL: a program for display and analysis of macromolecular structures. , 1996, Journal of molecular graphics.
[30] K Schulten,et al. VMD: visual molecular dynamics. , 1996, Journal of molecular graphics.
[31] D. Svergun,et al. CRYSOL : a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates , 1995 .
[32] R. Kerby,et al. Carbon monoxide-induced activation of gene expression in Rhodospirillum rubrum requires the product of cooA, a member of the cyclic AMP receptor protein family of transcriptional regulators , 1995, Journal of bacteriology.
[33] R. Kerby,et al. Carbon monoxide-dependent growth of Rhodospirillum rubrum , 1995, Journal of bacteriology.
[34] D. Engelman,et al. Mutations can cause large changes in the conformation of a denatured protein. , 1993, Biochemistry.
[35] S. Adhya,et al. Allosteric changes in the cAMP receptor protein of Escherichia coli: hinge reorientation. , 1992, Proceedings of the National Academy of Sciences of the United States of America.
[36] Dmitri I. Svergun,et al. Determination of the regularization parameter in indirect-transform methods using perceptual criteria , 1992 .
[37] D. Svergun,et al. Mathematical methods in small-angle scattering data analysis , 1991 .
[38] T. Steitz,et al. Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees , 1991, Science.
[39] Thomas A. Steitz,et al. Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA , 1981, Nature.
[40] O. Glatter,et al. 19 – Small-Angle X-ray Scattering , 1973 .
[41] G. Fournet,et al. Small‐Angle Scattering of X‐Rays , 1956 .
[42] Bruno H. Zimm,et al. The Scattering of Light and the Radial Distribution Function of High Polymer Solutions , 1948 .