Fuzzy Interactions Form and Shape the Histone Transport Complex
暂无分享,去创建一个
Franz Herzog | Victor Solis-Mezarino | F. Herzog | M. Halić | S. Bilokapic | Nives Ivic | Mia Potočnjak | Victor Solis-Mezarino | Mario Halic | Silvija Bilokapic | Nives Ivic | Mia Potocnjak | Franz Herzog
[1] Yuh Min Chook,et al. Recognition of nuclear targeting signals by Karyopherin-β proteins. , 2010, Current opinion in structural biology.
[2] Nikolaus Grigorieff,et al. Measuring the optimal exposure for single particle cryo-EM using a 2.6 Å reconstruction of rotavirus VP6 , 2015, eLife.
[3] D. Cowburn,et al. Deciphering the "Fuzzy" Interaction of FG Nucleoporins and Transport Factors Using Small-Angle Neutron Scattering. , 2017, Structure.
[4] Alfred Wittinghofer,et al. Structural View of the Ran–Importin β Interaction at 2.3 Å Resolution , 1999, Cell.
[5] M. Radermacher,et al. Three-dimensional reconstruction of single particles from random and nonrandom tilt series. , 1988, Journal of electron microscopy technique.
[6] Conrad C. Huang,et al. UCSF Chimera—A visualization system for exploratory research and analysis , 2004, J. Comput. Chem..
[7] Chiung-wen Chang,et al. Structural Biology and Regulation of Protein Import into the Nucleus. , 2016, Journal of molecular biology.
[8] N. Grigorieff,et al. CTFFIND4: Fast and accurate defocus estimation from electron micrographs , 2015, bioRxiv.
[9] E. Hurt,et al. Analysis of the yeast nucleoporin Nup188 reveals a conserved S-like structure with similarity to karyopherins. , 2012, Journal of structural biology.
[10] C. Müller,et al. Structure of importin-β bound to the IBB domain of importin-α , 1999, Nature.
[11] Richard Bayliss,et al. Structural Basis for the Interaction between FxFG Nucleoporin Repeats and Importin-β in Nuclear Trafficking , 2000, Cell.
[12] P. Bork,et al. A Novel Class of RanGTP Binding Proteins , 1997, The Journal of cell biology.
[13] R. L. Adams,et al. Uncovering Nuclear Pore Complexity with Innovation , 2013, Cell.
[14] E. Hartmann,et al. Distinct functions for the two importin subunits in nuclear protein import , 1995, Nature.
[15] W. Albig,et al. Core histones and linker histones are imported into the nucleus by different pathways. , 2001, European journal of cell biology.
[16] M. Beck,et al. The nuclear pore complex: understanding its function through structural insight , 2016, Nature Reviews Molecular Cell Biology.
[17] Friedrich Förster,et al. False discovery rate estimation for cross-linked peptides identified by mass spectrometry , 2012, Nature Methods.
[18] R. Ficner,et al. Thermodynamic Analysis of H1 Nuclear Import , 2007, Journal of Biological Chemistry.
[19] T. Schwartz,et al. Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex , 2012, Proceedings of the National Academy of Sciences.
[20] Yawen Bai,et al. Emerging roles of linker histones in regulating chromatin structure and function , 2017, Nature Reviews Molecular Cell Biology.
[21] T. Schwartz,et al. Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors , 2013, eLife.
[22] M. Blackledge,et al. Plasticity of an Ultrafast Interaction between Nucleoporins and Nuclear Transport Receptors , 2015, Cell.
[23] F. Bischoff,et al. Identification of different roles for RanGDP and RanGTP in nuclear protein import. , 1996, The EMBO journal.
[24] E. Hurt,et al. Evidence for an evolutionary relationship between the large adaptor nucleoporin Nup192 and karyopherins , 2014, Proceedings of the National Academy of Sciences.
[25] Amos Bairoch,et al. ScanProsite: detection of PROSITE signature matches and ProRule-associated functional and structural residues in proteins , 2006, Nucleic Acids Res..
[26] C. Müller,et al. Structure of importin-beta bound to the IBB domain of importin-alpha. , 1999, Nature.
[27] Aurelia Cassany,et al. Reconstitution of nuclear import in permeabilized cells. , 2009, Methods in molecular biology.
[28] P. Schwarzmaier,et al. Importins fulfil a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains , 2002, The EMBO journal.
[29] M. Stewart,et al. Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-beta homologue, Kap95p. , 2005, Journal of molecular biology.
[30] M. Rout,et al. The nuclear pore complex core scaffold and permeability barrier: variations of a common theme. , 2017, Current opinion in cell biology.
[31] M. Stewart. Molecular mechanism of the nuclear protein import cycle , 2007, Nature Reviews Molecular Cell Biology.
[32] C. Müller,et al. Nuclear import factors importin alpha and importin beta undergo mutually induced conformational changes upon association. , 2000, FEBS letters.
[33] M. Sotomayor,et al. Using thermal scanning assays to test protein-protein interactions of inner-ear cadherins , 2017, PloS one.
[34] Ben M. Webb,et al. Comparative Protein Structure Modeling Using MODELLER , 2016, Current protocols in bioinformatics.
[35] A. Goryachev,et al. System analysis shows distinct mechanisms and common principles of nuclear envelope protein dynamics , 2011, The Journal of cell biology.
[36] Katrine Bugge,et al. Extreme disorder in an ultrahigh-affinity protein complex , 2018, Nature.
[37] Hemant D. Tagare,et al. The Local Resolution of Cryo-EM Density Maps , 2013, Nature Methods.
[38] L. Pemberton,et al. Modulation of Histone Deposition by the Karyopherin Kap114 , 2005, Molecular and Cellular Biology.
[39] Ben M. Webb,et al. Comparative Protein Structure Modeling Using MODELLER , 2007, Current protocols in protein science.
[40] T. Littlewood,et al. GLFG and FxFG Nucleoporins Bind to Overlapping Sites on Importin-β* , 2002, The Journal of Biological Chemistry.
[41] M. Halić,et al. Preparative two-step purification of recombinant H1.0 linker histone and its domains , 2017, PloS one.
[42] F. Bischoff,et al. The importin β/importin 7 heterodimer is a functional nuclear import receptor for histone H1 , 1999, The EMBO journal.
[43] Randy J. Read,et al. Acta Crystallographica Section D Biological , 2003 .
[44] Y. Chook,et al. Importin 8 mediates m7G cap-sensitive nuclear import of the eukaryotic translation initiation factor eIF4E , 2016, Proceedings of the National Academy of Sciences.
[45] D. Cowburn,et al. The molecular mechanism of nuclear transport revealed by atomic-scale measurements , 2015, eLife.
[46] Sjors H.W. Scheres,et al. RELION: Implementation of a Bayesian approach to cryo-EM structure determination , 2012, Journal of structural biology.
[47] I R Vetter,et al. Structural view of the Ran-Importin beta interaction at 2.3 A resolution. , 1999, Cell.
[48] A. Sali,et al. Slide-and-exchange mechanism for rapid and selective transport through the nuclear pore complex , 2016, Proceedings of the National Academy of Sciences.
[49] Seung Joong Kim,et al. Simple rules for passive diffusion through the nuclear pore complex , 2016, The Journal of cell biology.
[50] D. Görlich,et al. A physical model describing the interaction of nuclear transport receptors with FG nucleoporin domain assemblies , 2016, eLife.
[51] Johannes Söding,et al. The HHpred interactive server for protein homology detection and structure prediction , 2005, Nucleic Acids Res..
[52] M. Halić,et al. Structural rearrangements of the histone octamer translocate DNA , 2018, Nature Communications.
[53] P. Emsley,et al. Features and development of Coot , 2010, Acta crystallographica. Section D, Biological crystallography.
[54] J. Shabanowitz,et al. Pathways Mediating the Nuclear Import of Histones H3 and H4 in Yeast* , 2002, The Journal of Biological Chemistry.
[55] Ian F. Harrison,et al. Nuclear import of HIV‐1 intracellular reverse transcription complexes is mediated by importin 7 , 2003, The EMBO journal.
[56] José María Carazo,et al. Image processing for electron microscopy single-particle analysis using XMIPP , 2008, Nature Protocols.
[57] T. Misteli,et al. The linker histone H1.0 generates epigenetic and functional intratumor heterogeneity , 2016, Science.
[58] D. Doenecke,et al. Importin 13 Mediates Nuclear Import of Histone Fold-containing Chromatin Accessibility Complex Heterodimers* , 2009, Journal of Biological Chemistry.
[59] M. Halić,et al. Histone octamer rearranges to adapt to DNA unwrapping , 2017, Nature Structural & Molecular Biology.
[60] T. Schwartz,et al. Exponential Megapriming PCR (EMP) Cloning—Seamless DNA Insertion into Any Target Plasmid without Sequence Constraints , 2012, PloS one.
[61] E. Yamashita,et al. Structural basis for the selective nuclear import of the C2H2 zinc-finger protein Snail by importin β. , 2014, Acta crystallographica. Section D, Biological crystallography.
[62] U. Kutay,et al. Multiple pathways contribute to nuclear import of core histones , 2001, EMBO reports.
[63] Wen Jiang,et al. EMAN2: an extensible image processing suite for electron microscopy. , 2007, Journal of structural biology.
[64] C. Müller,et al. Nuclear import factors importin α and importin β undergo mutually induced conformational changes upon association , 2000 .
[65] David S. Booth,et al. The export receptor Crm1 forms a dimer to promote nuclear export of HIV RNA , 2014, eLife.
[66] R. Aebersold,et al. Structural Probing of a Protein Phosphatase 2A Network by Chemical Cross-Linking and Mass Spectrometry , 2012, Science.
[67] W. Albig,et al. The Requirement of H1 Histones for a Heterodimeric Nuclear Import Receptor* , 2002, The Journal of Biological Chemistry.
[68] C. Müller,et al. Karyopherin flexibility in nucleocytoplasmic transport. , 2006, Current opinion in structural biology.
[69] L. Pemberton,et al. Histone chaperones link histone nuclear import and chromatin assembly. , 2012, Biochimica et biophysica acta.
[70] D. Shechter,et al. Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches. , 2017, Journal of molecular biology.
[71] R. Schneider,et al. The H1 linker histones: multifunctional proteins beyond the nucleosomal core particle , 2015, EMBO reports.
[72] R. Aebersold,et al. Chemical cross-linking/mass spectrometry targeting acidic residues in proteins and protein complexes , 2014, Proceedings of the National Academy of Sciences.