About us
Our group focuses on elucidating the role of intrinsically disordered proteins (IDPs) in cell signalling. In particular, we are interested in the mitogen-activated protein kinases (MAPKs) and how intrinsically disordered scaffold proteins regulate signaling specificity and MAPK activity. We use advanced NMR spectroscopy in combination with X-ray crystallography and biophysics to study these dynamic assemblies at atomic resolution.
Jensen group June 2026
Research
Publications
110.
L.F. Kjaer, F.S. Ielasi, T. Winbolt, E. Delaforge, M. Tengo, S. Nebl, G. Bouvignies, A. Palencia*, M.R. Jensen*.
J. Am. Chem. Soc. (2026) 148, 28401-28413.
Alternative splicing of a structured partner alters the folding-upon-binding trajectory of an intrinsically disordered protein
109.
L.F. Kjaer, F.S. Ielasi, T. Winbolt, E. Delaforge, M. Tengo, L.M. Bessa, L. Mariño Pérez, E. Boeri Erba, G. Bouvignies*, A. Palencia*, M.R. Jensen*.
Nat. Commun. (2025) 16, 11346.
Hierarchical folding-upon-binding of an intrinsically disordered protein
108.
T. Orand, E. Delaforge, M. Chenal, M. Tengo, T. Herrmann, J. Cortés, P. Bernadó, M.R. Jensen*.
Adv. Sci. (2025) 12, e03987.
Sequence- and docking-site-dependent contributions to multi-site phosphorylation of an intrinsically disordered MAPK substrate
107.
T. Orand, E. Delaforge, A. Lee, J. Kragelj, M. Tengo, L. Tengo, M. Blackledge, E. Boeri Erba, R.J. Davis, A. Palencia*, M.R. Jensen*.
Proc. Natl. Acad. Sci. U.S.A. (2025) 122, e2419915122.
Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1
106.
T. Orand, M.R. Jensen*.
Curr. Opin. Struct. Biol. (2024), 90, 102958.
Binding mechanisms of intrinsically disordered proteins: Insights from experimental studies and structural predictions
105.
L. Mariño Pérez, F.S. Ielasi, A. Lee, E. Delaforge, P. Juyoux, M. Tengo, R.J. Davis, A. Palencia*, M.R. Jensen*.
Structure (2024) 32, 1394-1403.
Structural basis of homodimerization of the JNK scaffold protein JIP2 and its heterodimerization with JIP1
104.
D. Seigneurin-Berny*, C. Karczewski, E. Delaforge, K. Yaacoub, C. G. Litholdo, J. J. Favory, M.R. Jensen, C. Bousquet-Antonelli*, A. Verdel*.
RNA Biol. (2024) 21, 1-13.
ECT2 peptide outside the YTH domain regulate its m6A-RNA binding
103.
G. Hoffmann, M. Lukarska, R.H. Clare, E.K.G Masters, K.L. Johnston, L. Ford, J.D. Turner, S.A. Ward, M.J. Taylor, M.R. Jensen, A. Palencia*.
Sci. Adv. (2024) 10, eado1453.
Targeting a microbiota Wolbachian aminoacyl-tRNA synthetase to block its pathogenic host
102.
G. Hoffmann, M. Le Gorrec, E. Mestdach, S. Cusack, L. Salmon, M.R. Jensen*, A. Palencia*.
J. Am. Chem. Soc. (2023) 145, 800-810.
Adenosine-dependent activation mechanism of prodrugs targeting an aminoacyl-tRNA synthetase
101.
A.R. Camacho-Zarco, V. Schnapka, S. Guseva, A. Abyzov, W. Adamski, S. Milles, M.R. Jensen, L. Zidek, N. Salvi, M. Blackledge*.
Chem. Rev. (2022) 122, 9331-9356.
NMR provides unique insight into the functional dynamics and interactions of intrinsically disordered proteins
100.
J.M. Bourhis, F. Yabukarski, G. Communie, R. Schneider, V.A. Volchkova, M. Frénéat, F.C. Gérard, C. Ducournau, C. Mas, N. Tarbouriech, M.R. Jensen, V.E. Volchkov, M. Blackledge, M. Jamin*.
J. Mol. Biol. (2022) 434, 167551.
Structural dynamics of the C-terminal X domain of Nipah and Hendra viruses controls the attachment to the C-terminal tail of the nucleocapsid protein
99.
L. Marino Perez, F. S. Ielasi, L.M. Bessa, D. Maurin, J. Kragelj, M. Blackledge, N. Salvi, G. Bouvignies, A. Palencia*, M.R. Jensen*.
Nature (2022) 602, 695-700.
Visualizing protein breathing motions associated with aromatic ring flipping
98.
L.M. Bessa‡, S. Guseva‡, A.R. Camacho-Zarco‡, N. Salvi‡, D. Maurin, L. Marino Perez, M. Botova, A. Malki, M. Nanano, M.R. Jensen, R.W.H. Ruigrok, M. Blackledge*.
Sci. Adv. (2022) 8, eabm4034.
Structure of SARS-CoV-2 nucleoprotein in dynamic complex with its viral partner nsp3a
97.
S. Naudi-Fabra, M. Tengo, M.R. Jensen, M. Blackledge, S. Milles*.
J. Am. Chem. Soc. (2021) 143, 20109-20121.
Quantitative description of intrinsically disordered proteins using single-molecule FRET, NMR, and SAXS
96.
Jaka Kragelj‡, T. Orand‡, E. Delaforge, L. Tengo, M. Blackledge, A. Palencia, M.R. Jensen*.
Biomolecules. (2021) 11, 1204.
Enthalpy–entropy compensation in the promiscuous interaction of an intrinsically disordered protein with homologous protein partners
95.
T. Lazar, E. Martínez-Pérez, F. Quaglia, A. Hatos, L.B. Chemes, J.A. Iserte, N.A. Méndez, N.A. Garrone, T.E. Saldaño, J. Marchetti, A.J.V. Rueda, P. Bernadó, M. Blackledge, T.N. Cordeiro, E. Fagerberg, J.D. Forman-Kay, M.S. Fornasara, T.J. Gibson, G.W. Gomes, C.C. Gradinaru, T. Head-Gordon, M.R. Jensen, E.A. Lemke, S. Longhi, C. Marino-Buslje, G. Minervini, T. Mittag, A.M. Monzon, R.V. Pappu, G. Parisi, S. Richard-Blum, K.M. Ruff, E. Salladini, M. Skepö, D. Svergun, S.D. Vallet, M. Varadi, P. Tompa, S.C.E. Tosatto, D. Piovesan.
Nucleic Acids Res. (2021) 49, D404-D411.
PED in 2021: a major update of the protein ensemble database for intrinsically disordered proteins
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) 117, 20576-20585.
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. Milles‡, M.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. Milles‡, M.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. Aramburu, M.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
Group members
Malene R. Jensen, Ph.D., HDR 
Principal Investigator
Research Director (CNRS DR1)
Ph.D. University of Copenhagen, Denmark (2006)
Torsten Herrmann, Ph.D. 
Research Director (CNRS DR2)
Ph.D. ETH Zürich, Switzerland (2002)
Elise Delaforge, Ph.D.
Researcher (CNRS CRCN)
Ph.D. University Grenoble Alpes, France (2015)
Nihar Khandave, Ph.D. 
Postdoctoral fellow (CNRS, ANR)
Ph.D. TIFR Hyderabad, India (2025)
Michal Buša, Ph.D. 
Postdoctoral fellow (CNRS, Impulscience)
Ph.D. Charles University Prague, Czech Republic (2023)
Stefan Nebl, Ph.D. 
Postdoctoral fellow (CNRS, Impulscience)
Ph.D. Monash University, Australia (2023)
Thomas Winbolt, M.Sc. 
Ph.D. student (CNRS, Marie Skłodowska-Curie IDPro)
M.Sc. University of Edinburgh, Scotland (2022)
Lorenzo Attanasio, M.Sc. 
Ph.D. student (CEA, CEA fellowship)
M.Sc. University of Florence, Italy (2025)
Marion Chenal, M.Sc.
Ph.D. student (CNRS, Impulscience)
M.Sc. University of Lorraine, France (2023)
Maud Tengo, B.Sc.
Research technician (CNRS, Impulscience)
B.Sc. University of Grenoble Alpes, France (2017)
Join us
If you are interested in joining our group, please send a CV and a letter of motivation to Malene R. Jensen. We always welcome applications from master's students, Ph.D. students and postdoctoral fellows.
Contact us
@CEA/D. Morel
We are located at the Institut de Biologie Structurale on the EPN science campus in Grenoble together with the European Molecular Biology Laboratory Grenoble (EMBL), the Institut Laue-Langevin (ILL) and the European Synchrotron Radiation Facility (ESRF)
Mailing address:
Dr. Malene R. Jensen
Institut de Biologie Structurale
71, avenue des Martyrs
CS 10090
38044 Grenoble CEDEX 9
France