Publications

See citations at Malene R. Jensen’s Google Scholar

(94)   K.K. Rasmussen, A. Palencia, A.K. Varming, H. El-Wali, E. Boeri Erba, M. Blackledge, K. Hammer, T. Herrmann, M. Kilstrup, L. Lo Leggio*, M.R. Jensen*. Proc. Natl. Acad. Sci. U.S.A. (2020) In press. “Revealing the mechanism of repressor inactivation during switching of a temperate bacteriophage”

(93)   A.R. Camacho-Zarco, S. Kalayil, D. Maurin, N. Salvi, E. Delaforge, S. Milles, M.R. Jensen, D.J. Hart, S. Cusack, M. Blackledge*. Nat. Commun. (2020) 11, 3656. “Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A”

(92)   S. Guseva, S. Milles, M.R. Jensen, G. Schoehn, R.W.H. Ruigrok*, M. Blackledge*. Curr. Opin. Virol. (2020) 41, 59-67. “Structure, dynamics and phase separation of measles virus RNA replication machinery”

(91)   M.R. Jensen, F. Yabukarski, G. Communie, E. Condamine, C. Mas, V. Volchkova, N. Tarbouriech, J.-M. Bourhis, V. Volchkov, M. Blackledge, M. Jamin*. Biophys. J. (2020) 118, 2470-2488. “Structural description of the Nipah virus phosphoprotein and its interaction with STAT1”

(90)   S. Guseva, S. MillesM.R. Jensen, N. Salvi, J.P. Kleman, D. Maurin, Rob. W. H. Ruigrok*, M. Blackledge*. Sci. Adv. (2020) 6, eaaz7095. “Measles virus nucleo- and phosphoproteins form liquid-like phase-separated compartments that promote nucleocapsid assembly”

(89)   W. Adamski, N. Salvi, D. Maurin, J. Magnat, S. Milles, M.R. Jensen, A. Abyzov, C. J. Moreau, M. Blackledge*. J. Am. Chem. Soc. (2019) 141, 17817-17829. “A unified description of intrinsically disordered protein dynamics under physiological conditions using NMR spectroscopy”

(88)   V. Kubán, P. Srb, H. Štégnerová, P. Padrta, M. Zachrdla, Z. Jasenáková, H. Šanderová, D. Vítovská, L. Krásny, T. Koval, J. Dohnálek, J. Ziemska-Legięcka, M. Grynberg, P. Jarnot, A. Gruca, M.R. Jensen, M. Blackledge*, L. Žídek*. J. Am. Chem. Soc. (2019) 141, 16817-16828. “Quantitative conformational analysis of functionally important electrostatic interactions in the intrinsically disordered region of delta subunit of bacterial RNA polymerase”

(87)   S. Panova, M.H. Cliff, P. Macek, M. Blackledge, M.R. Jensen, J.W.M. Nissink, K.J. Embrey, R. Davies, J.P. Waltho*. Structure (2019) 27, 1537-1546. “Mapping hidden residual structure within the Myc bHLH-LZ domain using chemical denaturant titration”

(86)   K. Melková, V. Zapletal, S. Narasimhan, S. Jansen, J. Hritz, R. Škrabana, M. Zweckstetter, M.R. Jensen, M. Blackledge, L. Žídek*. Biomolecules (2019) 9, E105. “Structure and functions of microtubule associated proteins Tau and MAP2c: Similarities and differences”

(85)   A. Desfosses, S. Milles, M.R. Jensen, S. Guseva, J.P. Colletier, D. Maurin, G. Schoehn, I. Gutsche, R.W.H. Ruigrok, M. Blackledge*. Proc. Natl. Acad. Sci. (2019) 116, 4256-4264. “Assembly and cryo-EM structures of RNA-specific measles virus nucleocapsids provide mechanistic insight into paramyxoviral replication”

(84)   R. Schneider, M. Blackledge, M.R. Jensen*. Curr. Opin. Struct. Biol. (2019) 54, 10-18. “Elucidating binding mechanisms and dynamics of intrinsically disordered protein complexes using NMR spectroscopy”

(83)   S. Milles, N. Salvi, M. Blackledge, M.R. Jensen*Prog. Nucl. Magn. Reson. Spectrosc. (2018) 109, 79-100. “Characterization of intrinsically disordered proteins and their dynamic complexes: From in vitro to cell-like environments”

(82)   S. Milles, M.R. Jensen, C. Lazert, S. Guseva, S. Ivashchenko, G. Communie, D. Maurin, D. Gerlier, R.W.H. Ruigrok*, M. Blackledge*. Sci. Adv. (2018) 4, eaat7778. “An ultraweak interaction in the intrinsically disordered replication machinery is essential for measles virus function”

(81)   K. Melková, V. Zapletal, S. Jansen, E. Nomilner, M. Zachrdla, J. Hritz, J. Novácek, M. Zweckstetter, M.R. Jensen, M. Blackledge, L. Zidek. J. Biol. Chem. (2018) 293, 13297-13309. “Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics”

(80)   J. L. Ortega-Roldan, M. Blackledge, M.R. Jensen*. Methods Mol. Biol. (2018) 1764, 73-85. “Characterizing protein-protein interactions using solution NMR spectroscopy”

(79)   K.K. Rasmussen, A. K. Varming, S. N. Schmidt, K. E. H. Frandsen, P. W. Thulstrup, M.R. Jensen, L. L. Leggio*. FEBS Lett. (2018) 592, 1738-1750. “Structural basis of the TP901-1 CI repressor dimerization and interaction with DNA”

(78)   E. Delaforge, J. Kragelj, L. Tengo, A. Palencia, S. Milles, G. Bouvignies, N. Salvi, M. Blackledge, M.R. Jensen*. J. Am. Chem. Soc. (2018) 140, 1148-1158. “Deciphering the dynamic interaction profile of an intrinsically disordered protein by NMR exchange spectroscopy”

(77)   A. Labaronne, S. Milles, A. Donchet, M.R. Jensen, M. Blackledge, J.M. Bourhis, R. W. H. Ruigrok, Thibaut Crépin*. Sci. Rep. (2017) 7, 17164. “Structural analysis of the complex between influenza B nucleoprotein and human importin alpha”

(76)   G. Tesei*, M. Vazdar, M.R. Jensen, C. Cragnell, P.E. Mason, J. Heyda, M. Skepö, P. Jungwirth*, M. Lund*. Proc. Natl. Acad. Sci. U.S.A. (2017) 114, 11428-11433. “Self-association of a highly charged arginine-rich cell-penetrating peptide”

(75)   M. Bernetti, M. Masetti*, F. Pietrucci, M. Blackledge, M.R. Jensen, M. Recanatini, L. Mollica*, A. Cavalli*. J. Phys. Chem. B (2017) 121, 9572-9582. “Structural and kinetic characterization of the intrinsically disordered protein SeV NTAIL through enhanced sampling simulations”

(74)   J. Morgan, M.R. Jensen, V. Ozenne, M. Blackledge, E. J. Barbar*. Biochemistry (2017) 56, 4656-4666. “The LC8 recognition motif preferentially samples polyproline II structure in its free state”

(73)   D. C. Desravines, I. Serna Martin, R. Schneider*, P. J. Mas, N. Aleksandrova, M.R. Jensen, M. Blackledge, D. J. Hart*. Sci. Rep. (2017) 7, 3678. “Structural characterization of the SMRT corepressor interacting with histone deacetylase 7”

(72)   R. Sukackaite, D. Cornacchia, M.R. Jensen, P. J. Mas, M. Blackledge, E. Enervald, G. Duan, M. Koehn, D. J. Hart*, S. C. B. Buonomo*. Sci. Rep. (2017) 7, 2119. “Mouse Rif1 is a regulatory subunit of protein phosphatase 1 (PP1)”

(71)   M.J. Whitley, Z. Xi, J.C. Bartko, M.R. Jensen, M. Blackledge and A. M. Gronenborn*. Biophys. J. (2017) 112, 1135-1146. “A combined NMR and SAXS structural analysis of the partially folded cataract-associated V75D mutant of gD-crystallin”

(70)   E. Delaforge, S. Milles, J.-R. Huang, D. Bouvier, M.R. Jensen, D. Hart, M. Sattler, M. Blackledge*. Front. Mol. Biosci. (2016) 3, 54. “Investigating the role of large-scale domain dynamics in protein-protein interactions”

(69)   L. Mollica, L. M. Bessa, X. Hanoulle, M.R. Jensen, M. Blackledge, R. Schneider*. Front. Mol. Biosci. (2016), 3, 52. “Binding mechanisms of intrinsically disordered proteins: theory, simulation and experiment”

(68)   K. K. Rasmussen, K. Frandsen, E. Boeri-Erba, M. Pedersen, A. K. Varming, K. Hammer, M. Kilstrup, P. Thulstrup, M. Blackledge, M.R. Jensen*, L. Lo Leggio*. Sci. Rep. (2016) 6, 29574. “Structural and dynamics studies of a truncated variant of CI repressor from bacteriophage TP901-1”

(67)   S. MillesM.R. Jensen, G. Communie, D. Maurin, G. Schoehn, R.W.H. Ruigrok*, M. Blackledge*. Angew. Chem. (2016) 55, 9356-9360. “Self-assembly of measles virus nucleocapsid-like particles: Kinetics and RNA sequence dependence”

(66)   A. Abyzov, N. Salvi, R. Schneider, D. Maurin, R.W.H. Ruigrok, M.R. Jensen, M. Blackledge*. J. Am. Chem. Soc. (2016) 138, 6240-6251. “Identification of dynamic modes in an intrinsically disordered protein from temperature-dependent NMR relaxation”

(65)   F. Yabukarski, C. Leyrat, N. Martinez, G. Communie, I. Ivanov, E.A. Ribeiro, M. Buisson, F.C. Gerard, J. M. Bourhis,  M.R. Jensen, P. Bernadó, M. Blackledge, M. Jamin*. J. Mol. Biol. (2016) 428, 2671-2694. “Ensemble structure of the highly flexible complex formed between vesicular stomatitis virus unassembled nucleoprotein and its phosphoprotein chaperone”

(64)   S. Milles, D. Mercadante, I. V. AramburuM.R. Jensen, N. Banterle, C. Koehler, S. Tyagi, J. Clarke, S. Shammas, M. Blackledge*, F. Grater*, E.A. Lemke*. Cell (2015) 163, 734-745. “Plasticity of an ultrafast interaction between nucleoporins and nuclear transport receptors”

(63)   E. Delaforge, S. Milles, G. Bouvignies, D. Bouvier, S. Boivin, N. Salvi, D. Maurin, A. Martel, A. Round, E.A. Lemke, M.R. Jensen, D. Hart*, M. Blackledge*. J. Am. Chem. Soc. (2015) 137, 15122-15134. “Large scale conformational dynamics control H5N1 influenza polymerase PB2 binding to importin alpha”

(62)   J. Kragelj, A. Palencia, M. Nanao, D. Maurin, G. Bouvignies, M. Blackledge*, M.R. Jensen*. Proc. Natl. Acad. Sci. U.S.A. (2015) 112, 3409-3414. “Structure and dynamics of the MKK7-JNK signalling complex”

(61)   R. Schneider, D. Maurin, G. Communie, J. Kragelj, D.F. Hansen, R.W.H. Ruigrok, M.R. Jensen, M. Blackledge*. J. Am. Chem. Soc. (2015) 137, 1220-1229. “Visualizing the molecular recognition trajectory of an intrinsically disordered protein using multinuclear relaxation dispersion NMR”

(60)   M. Blanc, T. L. Coetzer, M. Blackledge, M. Haertlein, E.P. Mitchell, V. T. Forsyth, M.R. Jensen*. BBA Proteins and Proteomics (2014) 1844, 2306-2314. “Intrinsic disorder within the erythrocyte binding-like proteins from Plasmodium falciparum”

(59)   E. Barbet-Massin, M. Felletti, R. Schneider, S. Jehle, G. Communie, N. Martinez, M.R. Jensen, R.W.H. Ruigrok, L. Emsley, A. Lesage, M. Blackledge, G. Pintacuda*. Biophys. J. (2014) 107, 941-946. “Insights into the structure and dynamics of measles virus nucleocapsids by 1H-detected solid-state NMR”

(58)   F. Yabukarski, P. Lawrence, N. Tarbouriech, J.M. Bourhis, E. Delaforge, M.R. Jensen, R.W.H. Ruigrok, M. Blackledge, V. Volchkov, M. Jamin*. Nat. Struct. Mol. Biol. (2014) 21, 754-759. “Structure of Nipah virus unassembled nucleoprotein in complex with its viral chaperone”

(57)   H. Johansson, M.R. Jensen, H. Gesmar, S. Meier, J.M. Vinther, C. Keeler, M.E. Hodsdon, J.J. Led*. J. Am. Chem. Soc. (2014) 136, 10277-10286. “Non-specific interactions in ultra-weak protein-protein associations revealed by solvent paramagnetic relaxation enhancements”

(56)   N. Krishnan, D. Koveal, D.H. Miller, B. Xue, S.D. Akshinthala, J. Kragelj, M.R. Jensen, C.-M. Gauss, R. Page, M. Blackledge, S.K. Muthuswamy, W. Peti, N.K. Tonks*. Nat. Chem. Biol. (2014) 10, 558-566. “Targeting the disordered C-terminus of PTP1B with an allosteric inhibitor”

(55)   Y.G.J. Sterckx, A.N. Volkov, W.F. Vranken, J. Kragelj, M.R. Jensen, L. Buts, A. Garcia-Pino, T. Jové, L. Van Melderen, M. Blackledge, N.A.J. van Nuland*, R. Loris*. Structure (2014) 22, 854-865. “Small angle X-ray scattering and nuclear magnetic resonance-derived conformational ensemble of the highly flexible antitoxin PaaA2”

(54)   M.R. Jensen, M. Zweckstetter, J.R. Huang, M. Blackledge*. Chem. Rev. (2014) 114, 6632-6660. “Exploring the free-energy landscapes of intrinsically disordered proteins at atomic resolution using NMR spectroscopy”

(53)   M.R. Jensen, M. Blackledge*. Proc. Natl. Acad. Sci. U.S.A. (2014) 111, E1557-E1558. “Testing the validity of ensemble descriptions of intrinsically disordered proteins”

(52)   G. Communie, R.W.H. Ruigrok, M.R. Jensen, M. Blackledge*. Curr. Opin. Virol. (2014) 5, 72-81. “Intrinsically disordered proteins implicated in paramyxoviral replication machinery”

(51)   R. Sukackaite, M.R. Jensen, P.J. Mas, M. Blackledge, S.B. Buonomo, D.J. Hart*. J. Biol. Chem. (2014) 289, 13903-13911. “Structural and biophysical characterization of murine Rif1 C terminus reveals high specificity for DNA cruciform structures”

(50)   M. Schwalbe, V. Ozenne, S. Bibow, M. Jaremko, L. Jaremko, M. Gajda, M.R. Jensen, J. Biernat, S. Becker, E. Mandelkow, M. Zweckstetter*, M. Blackledge*. Structure (2014) 22, 238-249. “Predictive atomic resolution descriptions of intrinsically disordered hTau40 and α-synuclein in solution from NMR and small angle scattering

(49)   V. Ozenne, J.K. Noel, P.O. Heidarsson, S. Brander, F.M. Poulsen, M.R. Jensen, B.B. Kragelund, M. Blackledge, J. Danielsson*. J. Mol. Biol. (2014) 426, 722-734. “Exploring the minimally frustrated energy landscape of unfolded ACBP

(48)   M. Schwalbe, J. Biernat, S. Bibow, V. Ozenne, M.R. Jensen, H. Kadavath, M. Blackledge, E. Mandelkow, M. Zweckstetter*. Biochemistry (2013) 52, 9068-9079. “Phosphorylation of human Tau protein by microtubule affinity-regulating kinase 2” 

(47)    K.H. Frandsen, K.K. Rasmussen, M.R. Jensen, K. Hammer, M. Pedersen, J.C. Poulsen, L. Arleth,  L. Lo Leggio*. Biochemistry (2013) 52, 6892-6904. “Binding of the N-terminal domain of the Lactococcal Bacteriophage TP901-1 CI repressor to its target DNA: A crystallography, small angle scattering and nuclear magnetic resonance study 

(46)    G. Communie, J. Habchi, F. Yabukarski, D. Blocquel, R. Schneider, N. Tarbouriech, N. Papageorgiou, R.W.H. Ruigrok, M. Jamin, M.R. Jensen*, S. Longhi*, M. Blackledge. PLoS Pathog. (2013) 9, e1003631. “Atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virus” 

(45)    J.L. Ortega-Roldan, S. Casares, M.R. Jensen, N. Cardenes, J. Bravo, M. Blackledge, A.I. Azuaga*, N.A.J. van Nuland*. PLoS One (2013) 8, e73018. “Distinct ubiquitin binding modes exhibited by SH3 domains: Molecular determinants and functional implications

(44)    J. Kragelj, V. Ozenne, M. Blackledge, M.R. Jensen*. ChemPhysChem (2013) 14, 3034-3045. “Conformational propensities of intrinsically disordered proteins from NMR chemical shifts

(43)    V. Iesmantavicius, M.R. Jensen, V. Ozenne, M. Blackledge, F.M. Poulsen, M. Kjaergaard*. J. Am. Chem. Soc. (2013) 135, 10155-10163. “Modulation of the intrinsic helix propensity of an intrinsically disordered protein reveals long-range helix-helix interactions

(42)    G. Communie, T. Crepin, D. Maurin, M.R. Jensen, M. Blackledge, R.W.H. Ruigrok*. J. Virol. (2013) 87, 7166-7169. “Structure of the tetramerization domain of measles virus phosphoprotein

(41)    M.R. Jensen, R.W.H. Ruigrok, M. Blackledge*. Curr. Opin. Struct. Biol. (2013) 23, 426-435. “Describing intrinsically disordered proteins at atomic resolution by NMR

(40)    J.R. Huang, V. Ozenne, M.R. Jensen, M. Blackledge*. Angew. Chem. (2013) 52, 687-690. “Direct prediction of NMR residual dipolar couplings from the primary sequence of unfolded proteins

(39)    L. Salmon, M.R. Jensen, M. Blackledge*. Methods Mol. Biol. (2012) 895, 115-125. “Measurement and analysis of NMR residual dipolar couplings for the study of intrinsically disordered proteins”

(38)    V. Ozenne, R. Schneider, M. Yao, J.R. Huang, L. Salmon, M. Zweckstetter, M.R. Jensen, M. Blackledge*. J. Am. Chem. Soc. (2012) 134, 15138-15148. “Mapping the potential energy landscape of intrinsically disordered proteins at amino acid resolution

(37)    C. Leyrat, R. Schneider, E.A. Ribeiro, F. Yabukarski, M. Yao, F.C. Gerard, M.R. Jensen, R.W.H. Ruigrok, M. Blackledge, M. Jamin*. J. Mol. Biol. (2012) 423, 182-197. “Ensemble structure of the modular and flexible full-length vesicular stomatitis virus phosphoprotein

(36)    L. Salmon, L. Pierce, A. Grimm, J.-L. Ortega-Roldan, L. Mollica, M.R. Jensen, N. van Nuland, P.R.L. Markwick, J. A. McCammon, M. Blackledge*. Angew. Chem. (2012) 51, 6103-6106. “Multi-timescale conformational dynamics of the SH3 domain of CD2-associated protein using NMR spectroscopy and accelerated molecular dynamics

(35)    V. Ozenne, F. Bauer, L. Salmon, J.-R. Huang, M.R. Jensen, S. Segard, P. Bernado, C. Charavay, M. Blackledge*. Bioinformatics (2012) 28, 1463-1470. “Flexible-Meccano: A tool for the generation of explicit ensemble descriptions of intrinsically disordered proteins and their associated experimental observables

(34)    F. Sziegat, R. Silvers, M. Hähnke, M.R. Jensen, M. Blackledge, J. Wirmer-Bartoschek, H. Schwalbe*. Biochemistry (2012) 51, 3361-3372. “Disentangling the coil: Modulation of conformational and dynamic properties by site-directed mutation in the non-native state of hen egg white lysozyme

(33)    J.-R. Huang, F. Gabel, M.R. Jensen, S. Grzesiek, M. Blackledge*. J. Am. Chem. Soc. (2012) 134, 4429-4436. “Sequence-specific mapping of the interaction between urea and unfolded ubiquitin from ensemble analysis of NMR and small angle scattering data

(32)   R. Schneider, J.-R. Huang, M. Yao, G. Communie, V. Ozenne, L. Mollica, L. Salmon, M.R. Jensen, M. Blackledge*. Mol. Biosyst. (2012) 8, 58-68. “Towards a robust description of intrinsic protein disorder using nuclear magnetic resonance spectroscopy”

(31)   T. Tosi, N. N. Nickerson, L. Mollica, M.R. Jensen, M. Blackledge, B. Baron, P. England, A. P. Pugsley and A. Dessen*. Mol. Microbiol. (2011) 82, 1422-1432. “Pilotin-secretin recognition in the type II secretion system of Klebsiella oxytoca

(30)    M.R. Jensen, J.L. Ortega-Roldan, L. Salmon, N. van Nuland, M. Blackledge*. Eur. Biophys. J. (2011) 40, 1371-1381. ”Characterizing weak protein-protein complexes by NMR residual dipolar couplings”

(29)    F. Dupeux, J. Santiago, K. Betz, J. Twycross, S.-Y. Park, L. Rodriguez, M. Gonzales-Guzman, M.R. Jensen, N. Krasnogor, M. Blackledge, M. Holdsworth, S.R. Cutler, P.L. Rodriguez, J.A. Márquez*. EMBO J. (2011) 30, 4171-4184. “A thermodynamic switch modulates abscisic acid receptor sensitivity”

(28)    C. Leyrat, F. Yabukarski, N. Tarbouriech, E.A. Ribeiro Jr, M.R. Jensen, M. Blackledge, R.W.H. Ruigrok, M. Jamin*. PLoS Pathog. (2011) 7, e1002248. “Structure of the vesicular stomatitis virus N0-P complex”

(27)    M.R. Jensen, G. Communie, E.A. Ribeiro Jr, N. Martinez, A. Desfosses, L. Salmon, L. Mollica, F. Gabel, M. Jamin, S. Longhi, R.W.H. Ruigrok, M. Blackledge*. Proc. Natl. Acad. Sci. U.S.A. (2011) 108, 9839-9844. “Intrinsic disorder in measles virus nucleocapsids” 

(26)    L. Salmon, J.L. Ortega-Roldan, E. Lescop, A. Licinio, N. van Nuland, M.R. Jensen*, M. Blackledge*. Angew. Chem. (2011) 50, 3755-3759. “Structure, dynamics, and kinetics of weak protein-protein complexes from NMR spin relaxation measurements of titrated solutions” 

(25)    J. Habchi, S. Blangy, L. Mamelli, M.R. Jensen, M. Blackledge, H. Darbon, M. Oglesbee, Y. Shu, S. Longhi*. J. Biol. Chem. (2011) 286, 13583-13602. “Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus” 

(24)    C. Leyrat, M.R. Jensen, E.A. Ribeiro Jr, F.C. Gerard, R.W.H. Ruigrok, M. Blackledge, M. Jamin*. Protein Sci. (2011) 20, 542-556. “The N(0)-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient a-helices” 

(23)   L. Salmon, G. Nodet, V. Ozenne, M.R. Jensen, M. Zweckstetter, M. Blackledge*. J. Am. Chem. Soc. (2010) 132, 8407-8418 “NMR characterization of long-range order in intrinsically disordered proteins” 

(22)    M.R. Jensen, P. Bernado, K. Houben, L. Blanchard, D. Marion, R. W. H. Ruigrok, M. Blackledge*. Protein and Pept. Lett. (2010) 17, 952-960. “Structural disorder within Sendai virus nucleoprotein and phosphoprotein: Insight into the structural basis of molecular recognition”

(21)    M.R. Jensen*, L. Salmon, G. Nodet, M. Blackledge*. J. Am. Chem. Soc. (2010) 132, 1270-1272. “Defining conformational ensembles of intrinsically disordered and partially folded proteins directly from chemical shifts”

(20)    S. Gely, D.F. Lowry, C. Bernard, M.R. Jensen, M. Blackledge, S. Costanzo, J.-M. Bourhis, H. Darbon, G. Daughdrill*, S. Longhi*. J. Mol. Recog. (2010) 23, 435-447. “Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoprotein”

(19)    G. Nodet, L. Salmon, V. Ozenne, S. Meier, M.R. Jensen, M. Blackledge*. J. Am. Chem. Soc. (2009) 131, 17908-17918. “Quantitative description of backbone conformational sampling of unfolded proteins at amino acid specific resolution from NMR residual dipolar couplings”

(18)    M.R. Jensen, P. Markwick, S. Meier, C. Griesinger, M. Zweckstetter, S. Grzesiek, P. Bernado, M. Blackledge*. Structure (2009) 17, 1169-1185. “Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings”

(17)    M.-K. Cho, G. Nodet, H.-Y. Kim, M.R. Jensen, P. Bernado, C.O. Fernandez, S. Becker, M. Blackledge, M. Zweckstetter*. Protein Sci. (2009) 18, 1840-1846. “Structural characterization of alpha-synuclein in an aggregation prone state”

(16)    F. Gabel*, M.R. Jensen, G. Zaccai, M. Blackledge*. J. Am. Chem. Soc. (2009) 131, 8769-8771. “Quantitative model-free analysis of urea binding to unfolded ubiquitin using a combination of small angle X-ray and neutron scattering”  

(15)    J.-L. Ortega-Roldan, M.R. Jensen*, B. Brutscher, A. I. Azuaga, M. Blackledge*, N.A.J. van Nuland. Nucleic Acids Res. (2009) 37, e70. “Accurate characterization of weak macromolecular interactions by titration of NMR residual dipolar couplings. Application to the CD2AP SH3-C:Ubiquitin complex”  

(14)    E.E. Büllesbach*, M.A.S. Hass, M.R. Jensen, D.F. Hansen, S.M. Kristensen, C. Schwabe, J.J. Led. Biochemistry (2008) 47, 13308-13317. “Solution structure of a conformationally restricted fully active derivative of the human relaxin-like factor” 

(13)   M.R. Jensen, M. Blackledge*. J. Am. Chem. Soc. (2008) 130, 11266-11267. “On the origin of NMR dipolar waves in transient helical elements of partially folded proteins” 

(12)   M.R. Jensen, K. Houben, E. Lescop, L. Blanchard, R.W.H. Ruigrok, M. Blackledge*. J. Am. Chem. Soc. (2008) 130, 8055-8061. “Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: Applications to the molecular recognition element of Sendai virus nucleoprotein” 

(11)    M.R. Jensen, S.M. Kristensen, C. Keeler, H.E.M. Christensen, M.E. Hodsdon, J.J. Led*. Proteins: Structure, Function and Bioinformatics (2008), 73, 161-172.  “Weak self-association of human growth hormone investigated by nitrogen-15 NMR relaxation” 

(10)    M. Wells, H. Tidow, T.J. Rutherford, P. Markwick, M.R. Jensen, E. Mylonas, D.I. Svergun, M. Blackledge*, A.R. Fersht*. Proc. Natl. Acad. Sci. U.S.A. (2008) 105, 5762-5767. “Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain”  

(9)     M.A.S. Hass, M.R. Jensen, J.J. Led*. Proteins: Structure, Function and Bioinformatics (2008) 72, 333-343. “Probing electric fields in proteins in solution using NMR spectroscopy”  

(8)     M.R. Jensen, M.A.S. Hass, D.F. Hansen, J.J. Led*. Cell. Mol. Life Sci. (2007) 64, 1085-1104. “Investigating metal binding in proteins by nuclear magnetic resonance”  

(7)     M.R. Jensen, S.M. Kristensen, J.J. Led*. Magn. Reson. Chem. (2007) 45, 257-261. “Elimination of spin diffusion effects in saturation transfer experiments: Application to hydrogen exchange in proteins”

(6)     M.R. Jensen, J.J. Led*Biochemistry (2006) 45, 8782-8787. “Metal-protein interactions: Structure information from Ni2+ induced pseudocontact shifts in a native non-metalloprotein”

(5)     M.R. Jensen, D.F. Hansen, U. Ayna, R. Dagil, M.A.S. Hass, H.E.M. Christensen, J.J. Led*. Magn. Reson. Chem. (2006) 44, 294-301. “On the use of pseudocontact shifts in the structure determination of metallo-proteins”

(4)     M.R. Jensen, G. Petersen, C. Lauritzen, J. Pedersen, J.J. Led*. Biochemistry (2005) 44, 11014-11023. “Metal binding sites in proteins: Identification and characterization by paramagnetic NMR relaxation”  

(3)     M.R. Jensen, J.J. Led*J. Magn. Res. (2004) 167, 169-177. “Determination of the electron relaxation rates in paramagnetic metal complexes: Applicability of available NMR methods”  

(2)     M.R. Jensen, C. Lauritzen, S.W. Dahl, J. Pedersen, J.J. Led*. J. Biomol. NMR (2004) 29, 175-185. “Binding ability of a HHP-tagged protein towards Ni2+ studied by paramagnetic NMR relaxation: The possibility of obtaining long-range structure information”  

(1)     M.R. Jensen, D.F. Hansen, J.J. Led*. J. Am. Chem. Soc. (2002) 124, 4093-4096. “A general method for determining the electron self-exchange rates of blue copper proteins by longitudinal NMR relaxation”