Single-molecule FRET reveals the native-state dynamics of the IκBα ankyrin repeat domain.
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Taekjip Ha | Elizabeth A. Komives | Hajin Kim | E. Komives | T. Ha | Hajin Kim | Jorge A. Lamboy | Holly Dembinski | Holly E. Dembinski
[1] E. Rhoades,et al. Identification of an aggregation-prone structure of tau. , 2012, Journal of the American Chemical Society.
[2] Alessandro Borgia,et al. Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy , 2012, Proceedings of the National Academy of Sciences.
[3] Peer Bork,et al. SMART 7: recent updates to the protein domain annotation resource , 2011, Nucleic Acids Res..
[4] Monika Fuxreiter,et al. Fuzzy complexes: a more stochastic view of protein function. , 2012, Advances in experimental medicine and biology.
[5] Edward A Lemke,et al. Single molecule study of the intrinsically disordered FG-repeat nucleoporin 153. , 2011, Biophysical journal.
[6] Shifeng Xiao,et al. Effect of Src Kinase Phosphorylation on Disordered C-terminal Domain of N-Methyl-d-aspartic Acid (NMDA) Receptor Subunit GluN2B Protein* , 2011, The Journal of Biological Chemistry.
[7] E. Komives,et al. Visualization of the nanospring dynamics of the IκBα ankyrin repeat domain in real time , 2011, Proceedings of the National Academy of Sciences.
[8] Elizabeth A Komives,et al. Folding kinetics of the cooperatively folded subdomain of the IκBα ankyrin repeat domain. , 2011, Journal of molecular biology.
[9] K. Weninger,et al. Beyond the random coil: stochastic conformational switching in intrinsically disordered proteins. , 2011, Structure.
[10] Adam J. Trexler,et al. Single molecule characterization of α-synuclein in aggregation-prone states. , 2010, Biophysical journal.
[11] L. Reymond,et al. Charge interactions can dominate the dimensions of intrinsically disordered proteins , 2010, Proceedings of the National Academy of Sciences.
[12] M. Tsai,et al. Contributions of conserved TPLH tetrapeptides to the conformational stability of ankyrin repeat proteins. , 2010, Journal of molecular biology.
[13] Elizabeth A Komives,et al. Molecular mechanisms of system control of NF-kappaB signaling by IkappaBalpha. , 2010, Biochemistry.
[14] Elizabeth A. Komives,et al. Kinetic enhancement of NF-κB·DNA dissociation by IκBα , 2009, Proceedings of the National Academy of Sciences.
[15] J. Mccammon,et al. Functional Dynamics of the Folded Ankyrin Repeats of IκBα Revealed by Nuclear Magnetic Resonance† , 2009, Biochemistry.
[16] E. Lemke,et al. Interplay of α-synuclein binding and conformational switching probed by single-molecule fluorescence , 2009, Proceedings of the National Academy of Sciences.
[17] K. Misra. Single - molecule fluorescence resonance energy transfer: A diagnostic tool in gene therapy , 2009 .
[18] H. Dyson,et al. Transfer of flexibility between ankyrin repeats in IkappaB* upon formation of the NF-kappaB complex. , 2008, Journal of molecular biology.
[19] Elizabeth A Komives,et al. Pre-folding IkappaBalpha alters control of NF-kappaB signaling. , 2008, Journal of molecular biology.
[20] Rahul Roy,et al. A practical guide to single-molecule FRET , 2008, Nature Methods.
[21] Elizabeth A Komives,et al. Folding landscapes of ankyrin repeat proteins: experiments meet theory. , 2008, Current opinion in structural biology.
[22] Andre Levchenko,et al. A homeostatic model of IκB metabolism to control constitutive NF-κB activity , 2007, Molecular systems biology.
[23] Peter G. Wolynes,et al. Stabilizing IκBα by “Consensus” Design , 2007 .
[24] Peter G Wolynes,et al. Stabilizing IkappaBalpha by "consensus" design. , 2007, Journal of molecular biology.
[25] Elizabeth A. Komives,et al. Regions of IκBα that are critical for its inhibition of NF-κB·DNA interaction fold upon binding to NF-κB , 2006, Proceedings of the National Academy of Sciences.
[26] M. Tsai,et al. Ankyrin repeat: a unique motif mediating protein-protein interactions. , 2006, Biochemistry.
[27] E. Komives,et al. Thermodynamics Reveal that Helix Four in the NLS of NF-κB p65 Anchors IκBα, Forming a Very Stable Complex , 2006 .
[28] E. Komives,et al. Thermodynamics reveal that helix four in the NLS of NF-kappaB p65 anchors IkappaBalpha, forming a very stable complex. , 2006, Journal of molecular biology.
[29] Elizabeth A Komives,et al. Regions of IkappaBalpha that are critical for its inhibition of NF-kappaB.DNA interaction fold upon binding to NF-kappaB. , 2006, Proceedings of the National Academy of Sciences of the United States of America.
[30] E. Komives,et al. Biophysical characterization of the free IκBα ankyrin repeat domain in solution , 2004 .
[31] Bharat B. Aggarwal,et al. Nuclear factor-κB: its role in health and disease , 2004, Journal of Molecular Medicine.
[32] Daniel C. Desrosiers,et al. The ankyrin repeat as molecular architecture for protein recognition , 2004, Protein science : a publication of the Protein Society.
[33] E. Komives,et al. Biophysical characterization of the free IkappaBalpha ankyrin repeat domain in solution. , 2004, Protein science : a publication of the Protein Society.
[34] B. Aggarwal,et al. Nuclear factor-kappaB: its role in health and disease. , 2004, Journal of molecular medicine.
[35] Andreas Plückthun,et al. Designing repeat proteins: well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. , 2003, Journal of molecular biology.
[36] A. Plückthun,et al. Designed to be stable: Crystal structure of a consensus ankyrin repeat protein , 2003, Proceedings of the National Academy of Sciences of the United States of America.
[37] Z. Peng,et al. Consensus-derived structural determinants of the ankyrin repeat motif , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[38] A. Hoffmann,et al. The I (cid:1) B –NF-(cid:1) B Signaling Module: Temporal Control and Selective Gene Activation , 2022 .
[39] A. Hoffmann,et al. The IkappaB-NF-kappaB signaling module: temporal control and selective gene activation. , 2002, Science.
[40] T. Ha,et al. Single-molecule fluorescence resonance energy transfer. , 2001, Methods.
[41] G. Ghosh,et al. IKAPPABALPHA/NF-KAPPAB COMPLEX , 1999 .
[42] G. Ghosh,et al. Structure and mechanism in NF-kappa B/I kappa B signaling. , 1999, Cold Spring Harbor symposia on quantitative biology.
[43] G. Ghosh,et al. The Crystal Structure of the IκBα/NF-κB Complex Reveals Mechanisms of NF-κB Inactivation , 1998, Cell.
[44] S. Harrison,et al. Structure of an IκBα/NF-κB Complex , 1998, Cell.
[45] J Schultz,et al. SMART, a simple modular architecture research tool: identification of signaling domains. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[46] S. Harrison,et al. Structure of an IkappaBalpha/NF-kappaB complex. , 1998, Cell.
[47] G. Ghosh,et al. The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation. , 1998, Cell.
[48] D. F. Ogletree,et al. Probing the interaction between single molecules: fluorescence resonance energy transfer between a single donor and a single acceptor , 1996, Summaries of Papers Presented at the Quantum Electronics and Laser Science Conference.
[49] D. Thomas,et al. Identification of lysine residues required for signal-induced ubiquitination and degradation of I kappa B-alpha in vivo. , 1996, Oncogene.
[50] M. Karin,et al. Mapping of the inducible IkappaB phosphorylation sites that signal its ubiquitination and degradation , 1996, Molecular and cellular biology.
[51] L. Baldi,et al. Critical Role for Lysines 21 and 22 in Signal-induced, Ubiquitin-mediated Proteolysis of IB- (*) , 1996, The Journal of Biological Chemistry.
[52] T. Maniatis,et al. Signal-induced degradation of I kappa B alpha requires site-specific ubiquitination. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[53] D. Baltimore,et al. I kappa B: a specific inhibitor of the NF-kappa B transcription factor. , 1988, Science.