Entry ID |
Original Release date |
Data summary |
Entry Title |
Citation Title |
Authors |
52346 |
2024-09-05 |
Chemical Shifts: 1 set |
CPEB4 N-terminal domain isoform lacking microexon 4 |
kinetic stabilization of translation-repression condensates by a neuron-specific microexon
|
Andreea Balaceanu, Anna Bartomeu, Berta Duran-Arque, Carla Garcia-Cabau, Cesare De Pace, Giulio Tesei, Giuseppe Battaglia, Jesus Garcia, Jose J Lucas, Judit Martin, Julia Pose-Utrilla, Kai C Cheung, Kresten Lindorff-Larsen, Lorena Ruiz-Perez, Marcos Fernandez-Alfara, Raul Mendez, Ruben Hervas, Sara Pico, Xavier Salvatella |
52209 |
2024-01-06 |
Chemical Shifts: 1 set |
Chemical shifts of constitutively monomeric CXCL12 |
The acidic intrinsically disordered region of the inflammatory mediator HMGB1 mediates fuzzy interactions with CXCL12
|
Camilla Carmeno, Chiara Pastorello, Chiara Zucchelli, Federica De Leo, Francesca Caprioglio, Francesco De Marchis, Gabriele Giachin, Giacomo Quilici, Giovanna Musco, Liam Sean S Colley, Malisa Vittoria V Mantonico, Marco Emilio E Bianchi, Massimo Crippa, Michela Ghitti, Rosanna Mezzapelle, Stefano Ricagno, Tim Schulte |
51875 |
2024-09-05 |
Chemical Shifts: 1 set |
CPEB4 N-terminal domain |
kinetic stabilization of translation-repression condensates by a neuron-specific microexon
|
Andreea Balaceanu, Anna Bartomeu, Berta Duran-Arque, Carla Garcia-Cabau, Cesare De Pace, Giulio Tesei, Giuseppe Battaglia, Jesus Garcia, Judit Martin, Kresten Lindorff-Larsen, Lorena Ruiz-Perez, Marcos Fernandez-Alfara, Raul Mendez, Xavier Salvatella |
50507 |
2021-10-01 |
Chemical Shifts: 1 set |
1H, 15N and 13C NMR assignments of the N-terminal domain of HKU1-bCoV nucleoprotein. |
1H,15N and 13C resonance assignments of the N-terminal domain of the nucleocapsid protein from the endemic human coronavirus HKU1
|
Aline de Luna Marques, Fabio Ceneviva Lacerda Almeida, Gabriela Rocha R Araujo, Gisele Cardoso C Amorim, Icaro Putinhon P Caruso, Marcos Caique C Santana-Silva, Peter Reis R Bezerra |
50414 |
2020-08-11 |
Chemical Shifts: 1 set |
A10 nanobody protein backbone assignation |
Bacterial cytoplasm as an effective cell compartment for producing functional VHH-based affinity reagents and Camelidae IgG-like recombinant antibodies.
|
Anne Beugnet, Ario de Marco, Aurelie Schneider, Chiara Romani, Franck Perez, Klervi Even E Desrumeaux, Ronan Crepin, Sandrine Moutel, Selma Djender |
30495 |
2018-10-31 |
Chemical Shifts: 1 set |
Solution NMR structure of a de novo designed double-stranded beta-helix |
De novo design of a non-local beta-sheet protein with high stability and accuracy.
|
Andrew C McShan, Audrey Davis, David Baker, Enrique Marcos, Gustav Oberdorfer, Konstantinos Tripsianes, Lauren Carter, Lucas G Nivon, Nikolaos G Sgourakis, Santrupti Nerli, Tamuka M Chidyausiku, Thomas Evangelidis |
30320 |
2017-09-28 |
Chemical Shifts: 1 set |
De Novo Design of Covalently Constrained Meso-size Protein Scaffolds with Unique Tertiary Structures |
De novo design of covalently constrained mesosize protein scaffolds with unique tertiary structures
|
Alexander Ford, Bobo Dang, Daniel-Adriano A Silva, David Baker, Haifan Wu, Marco Mravic, Thomas Lemmin, Vikram Khipple K Mulligan, William F DeGrado, Yibing Wu |
30319 |
2017-09-28 |
Chemical Shifts: 1 set |
De Novo Design of Covalently Constrained Meso-size Protein Scaffolds with Unique Tertiary Structures |
De novo design of covalently constrained mesosize protein scaffolds with unique tertiary structures
|
Alexander Ford, Bobo Dang, Daniel-Adriano A Silva, David Baker, Haifan Wu, Marco Mravic, Thomas Lemmin, Vikram Khipple K Mulligan, William F DeGrado, Yibing Wu |
30267 |
2017-09-25 |
Chemical Shifts: 1 set |
De Novo Design of Novel Covalent Constrained Meso-size Peptide Scaffolds with Unique Tertiary Structures |
De novo design of covalently constrained mesosize protein scaffolds with unique tertiary structures
|
Alexander Ford, Bobo Dang, Daniel-Adriano A Silva, David Baker, Haifan Wu, Marco Mravic, Thomas Lemmin, Vikram Khipple K Mulligan, William F DeGrado, Yibing Wu |
17472 |
2011-05-19 |
Chemical Shifts: 1 set |
TRPV5 C-terminal peptide |
Molecular Mechanisms of Calmodulin Action on TRPV5 and Modulation by Parathyroid Hormone.
|
Eline AE van der Hagen, Geerten W Vuister, Joost G Hoenderop, Marco Felici, Nadezda V Kovalevskaya, Nathalie Schilderink, Rene JM Bindels, Sjoerd Verkaart, Theun de Groot |
11004 |
2008-06-25 |
Chemical Shifts: 1 set |
NMR Structure of Ebola fusion peptide in SDS micelles at pH 7 |
Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts
|
Ana Paula Valente, Fabio Ceneviva Almeida, Jerson Lima Silva, Lenize Fernandes Maia, Leo Degreve, Luciane Pinto Gaspar, Luzineide Wanderley Tinoco, Marcius Silva Almeida, Marcos Lorenzoni, Monica Santos de Freitas |
15149 |
2007-06-05 |
Chemical Shifts: 1 set |
HMGB1 Full Length backbone assignment |
Glycyrrhizin binds to high-mobility group box 1 protein and inhibits its cytokine activities
|
Alessandra Agresti, Andrea Spitaleri, Corrado Dallacosta, Francesco De Marchis, Giovanna Musco, Lisa Trisciuoglio, Luca Mollica, Marco E Bianchi, Moreno Zamai |
15148 |
2007-06-05 |
Chemical Shifts: 1 set |
HMGB1 AB boxes + basic tail backbone assignment |
Glycyrrhizin binds to high-mobility group box 1 protein and inhibits its cytokine activities
|
Alessandra Agresti, Andrea Spitaleri, Corrado Dallacosta, D Pennacchini, Francesco De Marchis, Giovanna Musco, Lisa Trisciuoglio, Luca Mollica, Marco E Bianchi, Moreno Zamai |
4752 |
2000-09-27 |
Chemical Shifts: 1 set |
1H,13C,15N chemical shift assignments for the DNA binding domain of gpNu1 |
Letter to the Editor: Assignment of the 1H, 13C, and 15N resonances of the DNA binding domain of gpNu1, a genome packaging protein from bacteriophage l
|
Carlos E Catalano, Marcos Ortega, Michael Overduin, Nancy Berton, Qin Yang, Tonny de Beer |
415 |
1995-07-31 |
Chemical Shifts: 1 set |
The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor |
The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor
|
A De Marco, Gerhard Wagner, Kurt Wuthrich, Larry R Brown, Rene Richarz |
416 |
1995-07-31 |
Chemical Shifts: 1 set |
The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor |
The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor
|
A De Marco, Gerhard Wagner, Kurt Wuthrich, Larry R Brown, Rene Richarz |
1096 |
1999-06-14 |
Chemical Shifts: 1 set |
The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor |
The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor
|
A De Marco, Gerhard Wagner, Kurt Wuthrich, Larry R Brown, Rene Richarz |
90 |
1995-07-31 |
Chemical Shifts: 1 set |
Analysis of the Methyl 1H-NMR Spectrum of Crambin, a Hydrophobic Protein |
Analysis of the Methyl 1H-NMR Spectrum of Crambin, a Hydrophobic Protein
|
A De Marco, Juliette TJ Lecomte, M Llinas |
1097 |
1999-06-14 |
Chemical Shifts: 1 set |
The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor |
The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor
|
A De Marco, Gerhard Wagner, Kurt Wuthrich, Larry R Brown, Rene Richarz |
1098 |
1999-06-14 |
Chemical Shifts: 1 set |
The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor |
The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor
|
A De Marco, Gerhard Wagner, Kurt Wuthrich, Larry R Brown, Rene Richarz |
1541 |
1995-07-31 |
Chemical Shifts: 1 set |
Analysis of the Methyl 1H-NMR Spectrum of Crambin, a Hydrophobic Protein |
Analysis of the Methyl 1H-NMR Spectrum of Crambin, a Hydrophobic Protein
|
A De Marco, Juliette TJ Lecomte, M Llinas |
1542 |
1995-07-31 |
Chemical Shifts: 1 set |
Analysis of the Methyl 1H-NMR Spectrum of Crambin, a Hydrophobic Protein |
Analysis of the Methyl 1H-NMR Spectrum of Crambin, a Hydrophobic Protein
|
A De Marco, Juliette TJ Lecomte, M Llinas |
1562 |
1995-07-31 |
Chemical Shifts: 1 set |
Opioid Peptides in Micellar Systems: Conformational Analysis by CD and by One-Dimensional and Two-Dimensional 1H-NMR Spectroscopy |
Opioid Peptides in Micellar Systems: Conformational Analysis by CD and by One-Dimensional and Two-Dimensional 1H-NMR Spectroscopy
|
A De Marco, Ernesto Manera, Giuseppe Vecchio, Lucia Zetta, Renato Longhi, Roberto Consonni |
2455 |
1999-06-14 |
Chemical Shifts: 1 set |
pH and Temperature Effects on the Molecular Conformation of the Porcine Pancreatic Secretory Trypsin Inhibitor As Detected by Hydrogen-1 Nuclear Magnetic Resonance |
pH and Temperature Effects on the Molecular Conformation of the Porcine Pancreatic Secretory Trypsin Inhibitor As Detected by Hydrogen-1 Nuclear Magnetic Resonance
|
A De Marco, Enea Menegatti, Mario Guarneri |
2473 |
1995-07-31 |
Chemical Shifts: 1 set |
Ligand-binding effects on the kringle 4 domain from human plasminogen: a study by laser photo-CIDNP 1H-NMR spectroscopy |
Ligand-binding effects on the kringle 4 domain from human plasminogen: a study by laser photo-CIDNP 1H-NMR spectroscopy
|
A De Marco, Andrew M Petros, M Llinas, Robert Kaptein, Rolf Boelens |
2474 |
1995-07-31 |
Chemical Shifts: 1 set |
Ligand-binding effects on the kringle 4 domain from human plasminogen: a study by laser photo-CIDNP 1H-NMR spectroscopy |
Ligand-binding effects on the kringle 4 domain from human plasminogen: a study by laser photo-CIDNP 1H-NMR spectroscopy
|
A De Marco, Andrew M Petros, M Llinas, Robert Kaptein, Rolf Boelens |
2475 |
1995-07-31 |
Chemical Shifts: 1 set |
Ligand-binding effects on the kringle 4 domain from human plasminogen: a study by laser photo-CIDNP 1H-NMR spectroscopy |
Ligand-binding effects on the kringle 4 domain from human plasminogen: a study by laser photo-CIDNP 1H-NMR spectroscopy
|
A De Marco, Andrew M Petros, M Llinas, Robert Kaptein, Rolf Boelens |
411 |
1995-07-31 |
Chemical Shifts: 1 set |
The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor |
The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor
|
A De Marco, Gerhard Wagner, Kurt Wuthrich, Larry R Brown, Rene Richarz |
412 |
1995-07-31 |
Chemical Shifts: 1 set |
The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor |
The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor
|
A De Marco, Gerhard Wagner, Kurt Wuthrich, Larry R Brown, Rene Richarz |
413 |
1995-07-31 |
Chemical Shifts: 1 set |
The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor |
The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor
|
A De Marco, Gerhard Wagner, Kurt Wuthrich, Larry R Brown, Rene Richarz |
414 |
1995-07-31 |
Chemical Shifts: 1 set |
The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor |
The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor
|
A De Marco, Gerhard Wagner, Kurt Wuthrich, Larry R Brown, Rene Richarz |