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S. Skinner, R. Fogh, W. Boucher, T. Ragan, Luca Mureddu, G. Vuister (2016)
CcpNmr AnalysisAssign: a flexible platform for integrated NMR analysisJournal of Biomolecular Nmr, 66
M Sattler, J Schleucher, C Griesinger (1999)
Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradientsProg NMR Magn Reson Spectrosc, 34
S. Hymowitz, H. Christinger, G. Fuh, M. Ultsch, M. O'connell, R. Kelley, A. Ashkenazi, A. Vos (1999)
Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex with death receptor 5.Molecular cell, 4 4
V. Pavet, J. Beyrath, C. Pardin, Alexandre Morizot, Marie-Charlotte Lechner, J. Briand, M. Wendland, W. Maison, S. Fournel, O. Micheau, G. Guichard, H. Gronemeyer (2010)
Multivalent DR5 peptides activate the TRAIL death pathway and exert tumoricidal activity.Cancer research, 70 3
D. Wishart, C. Bigam, Jian Yao, F. Abildgaard, H. Dyson, E. Oldfield, J. Markley, B. Sykes (1995)
1H, 13C and 15N chemical shift referencing in biomolecular NMRJournal of Biomolecular NMR, 6
H. Walczak, M. Degli-Esposti, Richard Johnson, P. Smolak, Jennifer Waugh, N. Boiani, Martin Timour, M. Gerhart, K. Schooley, Craig Smith, R. Goodwin, C. Rauch (1997)
TRAIL‐R2: a novel apoptosis‐mediating receptor for TRAILThe EMBO Journal, 16
T. Tamada, Daisuke Shinmi, M. Ikeda, Y. Yonezawa, S. Kataoka, R. Kuroki, Eiji Mori, K. Motoki (2015)
TRAIL-R2 Superoligomerization Induced by Human Monoclonal Agonistic Antibody KMTR2Scientific Reports, 5
J. Beyrath, Neila Chekkat, C. Smulski, C. Lombardo, Marie-Charlotte Lechner, C. Seguin, M. Decossas, M. Spanedda, B. Frisch, G. Guichard, S. Fournel (2016)
Synthetic ligands of death receptor 5 display a cell-selective agonistic effect at different oligomerization levelsOncotarget, 7
A. Ashkenazi, V. Dixit (1998)
Death receptors: signaling and modulation.Science, 281 5381
F. Delaglio, S. Grzesiek, G. Vuister, G. Zhu, John Pfeifer, A. Bax (1995)
NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 6
J. Mongkolsapaya, J. Grimes, N. Chen, Xiao-ning Xu, D. Stuart, E. Jones, G. Screaton (1999)
Structure of the TRAIL–DR5 complex reveals mechanisms conferring specificity in apoptotic initiationNature Structural Biology, 6
Kazuyoshi Takeda, K. Takeda, J. Stagg, H. Yagita, K. Okumura, M. Smyth (2007)
Targeting death-inducing receptors in cancer therapyOncogene, 26
S. Cha, B. Sung, Young-A Kim, Young-Lan Song, Hyun-Ju Kim, Sunshin Kim, Myung-Shik Lee, B. Oh (2000)
Crystal Structure of TRAIL-DR5 Complex Identifies a Critical Role of the Unique Frame Insertion in Conferring Recognition Specificity*The Journal of Biological Chemistry, 275
Bing Li, S. Russell, D. Compaan, K. Totpal, S. Marsters, A. Ashkenazi, A. Cochran, S. Hymowitz, S. Sidhu (2006)
Activation of the proapoptotic death receptor DR5 by oligomeric peptide and antibody agonists.Journal of molecular biology, 361 3
M. Sattler, J. Schleucher, C. Griesinger (1999)
Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradientsProgress in Nuclear Magnetic Resonance Spectroscopy, 34
T. Newsom-Davis, Silvia Prieske, H. Walczak (2009)
Is TRAIL the holy grail of cancer therapy?Apoptosis, 14
D. Merino, N. Lalaoui, Alexandre Morizot, E. Solary, O. Micheau (2007)
TRAIL in cancer therapy: present and future challengesExpert Opinion on Therapeutic Targets, 11
J. Graves, J. Kordich, Tzu-Hsuan Huang, J. Piasecki, T. Bush, T. Sullivan, I. Foltz, Wesley Chang, Heather Douangpanya, Thu Dang, J. O'neill, R. Mallari, Xiaoning Zhao, D. Branstetter, J. Rossi, A. Long, Xin Huang, P. Holland (2014)
Apo2L/TRAIL and the death receptor 5 agonist antibody AMG 655 cooperate to promote receptor clustering and antitumor activity.Cancer cell, 26 2
I. Nemčovičová, C. Benedict, D. Zajonc (2013)
Structure of Human Cytomegalovirus UL141 Binding to TRAIL-R2 Reveals Novel, Non-canonical Death Receptor InteractionsPLoS Pathogens, 9
Frederic Fellouse, Bing Li, D. Compaan, A. Peden, S. Hymowitz, S. Sidhu (2005)
Molecular recognition by a binary code.Journal of molecular biology, 348 5
Yunjun Wang, O. Jardetzky (2002)
Probability‐based protein secondary structure identification using combined NMR chemical‐shift dataProtein Science, 11
M. MacFarlane, Manzoor Ahmad, S. Srinivasula, T. Fernandes‐Alnemri, G. Cohen, E. Alnemri (1997)
Identification and Molecular Cloning of Two Novel Receptors for the Cytotoxic Ligand TRAIL*The Journal of Biological Chemistry, 272
C. Adams, K. Totpal, David Lawrence, S. Marsters, R. Pitti, S. Yee, S. Ross, L. Deforge, H. Koeppen, M. Sagolla, D. Compaan, H. Lowman, S. Hymowitz, A. Ashkenazi (2008)
Structural and functional analysis of the interaction between the agonistic monoclonal antibody Apomab and the proapoptotic receptor DR5Cell Death and Differentiation, 15
Yang Shen, A. Bax (2013)
Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networksJournal of Biomolecular NMR, 56
Karolina Pułka-Ziach, V. Pavet, Neila Chekkat, K. Estieu-Gionnet, R. Rohac, Marie-Charlotte Lechner, Cristian Smulski, G. Zeder‐Lutz, D. Altschuh, H. Gronemeyer, S. Fournel, B. Odaert, G. Guichard (2015)
Thioether Analogues of Disulfide‐Bridged Cyclic Peptides Targeting Death Receptor 5: Conformational Analysis, Dimerisation and Consequences for Receptor ActivationChemBioChem, 16
Death receptors (DR) selectively drive cancer cells to apoptosis upon binding to the Tumor necrosis factor-a-Related Apoptosis-Inducing Ligand (TRAIL). Complex formation induces the oligomerization of the death receptors DR4 (TRAIL-R1) and DR5 (TRAIL-R2) and transduces the apoptogenic signal to their respective death domains, leading to Death Inducing Signaling Complex (DISC) formation, caspase activation and ultimately cell death. Several crystal structures of the ExtraCellular Domain from Death Receptor 5 (DR5-ECD) have been reported in complex with the TRAIL ligand or anti-DR5 antibodies, but none for the isolated protein. In order to fill this gap and to perform binding experiments with TRAIL peptidomimetics, we have produced isotopically labelled DR5-ECD and started a conformational analysis by using high-field 3D NMR spectroscopy. Herein, we present the first resonance assignment of a TRAIL receptor in solution and the determination of its secondary structure from NMR chemical shifts.
Biomolecular NMR Assignments – Springer Journals
Published: Jun 5, 2018
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