Martin Blackledge

发表

What’s in a name? Why these proteins are intrinsically disordered

Sonia Longhi, Burkhard Rost, Zoran Obradovic, 2013, Intrinsically disordered proteins.

ProtSA: a web application for calculating sequence specific protein solvent accessibilities in the unfolded ensemble

Javier Sancho, Pau Bernadó, Martin Blackledge, 2009, BMC Bioinformatics.

Flexible-meccano: a tool for the generation of explicit ensemble descriptions of intrinsically disordered proteins and their associated experimental observables

Céline Charavay, Pau Bernadó, Martin Blackledge, 2012, Bioinform..

Characterization of the Interactions between the Nucleoprotein and the Phosphoprotein of Henipavirus*

Sonia Longhi, Martin Blackledge, Malene Ringkjøbing Jensen, 2011, The Journal of Biological Chemistry.

Direct structure determination using residual dipolar couplings: reaction-site conformation of methionine sulfoxide reductase in solution.

Frédéric Barras, Martin Blackledge, Bernhard Brutscher, 2002, Journal of the American Chemical Society.

Intrinsic disorder within the erythrocyte binding-like proteins from Plasmodium falciparum.

Martin Blackledge, Michael Haertlein, Malene Ringkjøbing Jensen, 2014, Biochimica et biophysica acta.

Mouse Rif1 is a regulatory subunit of protein phosphatase 1 (PP1)

Darren J Hart, Martin Blackledge, Elin Enervald, 2017, Scientific Reports.

Conformational distributions of unfolded polypeptides from novel NMR techniques.

Martin Blackledge, S. Grzesiek, M. Blackledge, 2008, The Journal of chemical physics.

Intrinsically disordered proteins implicated in paramyxoviral replication machinery.

Martin Blackledge, Malene Ringkjøbing Jensen, M. Blackledge, 2014, Current opinion in virology.

The N0‐binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient α‐helices

Martin Blackledge, Malene Ringkjøbing Jensen, M. Blackledge, 2011, Protein science : a publication of the Protein Society.

Sequence-specific mapping of the interaction between urea and unfolded ubiquitin from ensemble analysis of NMR and small angle scattering data.

Martin Blackledge, Jie-rong Huang, Malene Ringkjøbing Jensen, 2012, Journal of the American Chemical Society.

Quantitative description of backbone conformational sampling of unfolded proteins at amino acid resolution from NMR residual dipolar couplings.

Martin Blackledge, Loïc Salmon, M. Blackledge, 2009, Journal of the American Chemical Society.

Domain conformation of tau protein studied by solution small-angle X-ray scattering.

Dmitri I Svergun, Pau Bernadó, Martin Blackledge, 2008, Biochemistry.

Multi-Timescale Conformational Dynamics of the SH3 Domain of CD2-Associated Protein using NMR Spectroscopy and Accelerated Molecular Dynamics**

Levi C. T. Pierce, J Andrew McCammon, Luca Mollica, 2012, Angewandte Chemie.

Mapping the conformational landscape of urea-denatured ubiquitin using residual dipolar couplings.

Martin Blackledge, S. Grzesiek, M. Blackledge, 2007, Journal of the American Chemical Society.

Testing the validity of ensemble descriptions of intrinsically disordered proteins

Martin Blackledge, Malene Ringkjøbing Jensen, M. Blackledge, 2014, Proceedings of the National Academy of Sciences.

Sequence-specific solvent accessibilities of protein residues in unfolded protein ensembles.

Pau Bernadó, Martin Blackledge, Javier Sancho, 2006, Biophysical journal.

Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: application to the molecular recognition element of Sendai virus nucleoprotein.

Martin Blackledge, Laurence Blanchard, Malene Ringkjøbing Jensen, 2008, Journal of the American Chemical Society.

Mapping the potential energy landscape of intrinsically disordered proteins at amino acid resolution.

Martin Blackledge, Valéry Ozenne, Robert Schneider, 2012, Journal of the American Chemical Society.

Anisotropic small amplitude Peptide plane dynamics in proteins from residual dipolar couplings.

Pau Bernadó, Martin Blackledge, M. Blackledge, 2004, Journal of the American Chemical Society.

A self-consistent description of the conformational behavior of chemically denatured proteins from NMR and small angle scattering.

Pau Bernadó, Martin Blackledge, M. Blackledge, 2009, Biophysical journal.

Intrinsic disorder in measles virus nucleocapsids

Sonia Longhi, Luca Mollica, Martin Blackledge, 2011, Proceedings of the National Academy of Sciences.

Atomic Resolution Description of the Interaction between the Nucleoprotein and Phosphoprotein of Hendra Virus

Sonia Longhi, Martin Blackledge, Robert Schneider, 2013, PLoS pathogens.

A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering.

Pau Bernadó, Dominique Marion, Martin Blackledge, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Structural characterization of α‐synuclein in an aggregation prone state

Martin Blackledge, Stefan Becker, Pau Bernado, 2009, Protein science : a publication of the Protein Society.

Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings.

Rafael Brüschweiler, Pau Bernadó, Martin Blackledge, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Structural biology: Proteins in dynamic equilibrium

Pau Bernadó, Martin Blackledge, 2010, Nature.

Transient electrostatic interactions dominate the conformational equilibrium sampled by multidomain splicing factor U2AF65: a combined NMR and SAXS study.

Michael Sattler, Martin Blackledge, Cameron D Mackereth, 2014, Journal of the American Chemical Society.

Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: quantitative and absolute determination of backbone motion in ubiquitin.

Rafael Brüschweiler, Christian Griesinger, Martin Blackledge, 2009, Angewandte Chemie.

Direct prediction of NMR residual dipolar couplings from the primary sequence of unfolded proteins.

Martin Blackledge, Valéry Ozenne, Jie-rong Huang, 2013, Angewandte Chemie.

Residual dipolar couplings in short peptides reveal systematic conformational preferences of individual amino acids.

Martin Blackledge, Pau Bernado, S. Grzesiek, 2006, Journal of the American Chemical Society.

Mapping the Native Conformational Ensemble of Proteins from a Combination of Simulations and Experiments: New Insight into the src-SH3 Domain.

Fabio Pietrucci, Luca Mollica, Martin Blackledge, 2013, The journal of physical chemistry letters.

Highly populated turn conformations in natively unfolded tau protein identified from residual dipolar couplings and molecular simulation.

Martin von Bergen, Christian Griesinger, Pau Bernadó, 2007, Journal of the American Chemical Society.

Long-range correlated dynamics in intrinsically disordered proteins.

Christian Griesinger, Andrea Giachetti, Martin Blackledge, 2014, Journal of the American Chemical Society.

NMR characterization of long-range order in intrinsically disordered proteins.

Martin Blackledge, Valéry Ozenne, Markus Zweckstetter, 2010, Journal of the American Chemical Society.

Predictive atomic resolution descriptions of intrinsically disordered hTau40 and α-synuclein in solution from NMR and small angle scattering.

Mariusz Jaremko, Martin Blackledge, Stefan Becker, 2014, Structure.

A thermodynamic switch modulates abscisic acid receptor sensitivity

Natalio Krasnogor, Jamie Twycross, Martin Blackledge, 2011, The EMBO journal.

Towards a robust description of intrinsic protein disorder using nuclear magnetic resonance spectroscopy.

Luca Mollica, Martin Blackledge, Valéry Ozenne, 2012, Molecular bioSystems.

Structural and Biophysical Characterization of Murine Rif1 C Terminus Reveals High Specificity for DNA Cruciform Structures*

Martin Blackledge, Malene Ringkjøbing Jensen, M. Blackledge, 2014, The Journal of Biological Chemistry.

Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings.

Christian Griesinger, Pau Bernadó, Martin Blackledge, 2009, Structure.

Small-angle X-ray scattering- and nuclear magnetic resonance-derived conformational ensemble of the highly flexible antitoxin PaaA2.

Wim F Vranken, Remy Loris, Martin Blackledge, 2014, Structure.

Anisotropic collective motion contributes to nuclear spin relaxation in crystalline proteins.

Martin Blackledge, Lyndon Emsley, M. Blackledge, 2010, Journal of the American Chemical Society.

Characterization of intrinsically disordered proteins and their dynamic complexes: From in vitro to cell-like environments.

Martin Blackledge, Malene Ringkjøbing Jensen, M. Blackledge, 2018, Progress in nuclear magnetic resonance spectroscopy.

Charge-induced molecular alignment of intrinsically disordered proteins.

Martin Blackledge, Stefan Becker, Markus Zweckstetter, 2006, Angewandte Chemie.

Structural disorder within sendai virus nucleoprotein and phosphoprotein: insight into the structural basis of molecular recognition.

Pau Bernadó, Martin Blackledge, Laurence Blanchard, 2010, Protein and peptide letters.

Intrinsically Disordered Proteins: From Sequence and Conformational Properties toward Drug Discovery

Martin Blackledge, Markus Zweckstetter, M. Blackledge, 2012, Chembiochem : a European journal of chemical biology.

Amino acid bulkiness defines the local conformations and dynamics of natively unfolded alpha-synuclein and tau.

Martin Blackledge, Pau Bernado, Markus Zweckstetter, 2007, Journal of the American Chemical Society.

Structure and dynamics of the MKK7–JNK signaling complex

Martin Blackledge, Max H Nanao, Guillaume Bouvignies, 2015, Proceedings of the National Academy of Sciences.

Defining conformational ensembles of intrinsically disordered and partially folded proteins directly from chemical shifts.

Martin Blackledge, Malene Ringkjøbing Jensen, Loïc Salmon, 2010, Journal of the American Chemical Society.