Entry ID |
Data summary |
Entry Title |
Citation Title |
Authors |
34541 |
Chemical Shifts: 1 set |
TFIIS N-terminal domain (TND) from human IWS1 |
A ubiquitous disordered protein interaction module orchestrates transcription elongation
|
Eric A Smith, H Courtney C Hodges, Jan De Rijck, Jonas Demeulemeester, Karen Adelman, Katerina Cermakova, Magdalena Horejsi, Marcela Madlikova, Milan Fabry, Monika Nedomova, Pavel Srb, Rozalie Hexnerova, Seth R Goldman, Vaclav Veverka, Vanda Lux, Zeger Debyser |
34535 |
Chemical Shifts: 1 set |
Human TFIIS N-terminal domain (TND) |
A ubiquitous disordered protein interaction module orchestrates transcription elongation
|
Eric A Smith, H Courtney C Hodges, Jan De Rijck, Jonas Demeulemeester, Karen Adelman, Katerina Cermakova, Magdalena Horejsi, Marcela Madlikova, Milan Fabry, Monika Nedomova, Pavel Srb, Rozalie Hexnerova, Seth R Goldman, Vaclav Veverka, Vanda Lux, Zeger Debyser |
34536 |
Chemical Shifts: 1 set |
TFIIS N-terminal domain (TND) from human Elongin-A |
A ubiquitous disordered protein interaction module orchestrates transcription elongation
|
Eric A Smith, H Courtney C Hodges, Jan De Rijck, Jonas Demeulemeester, Karen Adelman, Katerina Cermakova, Magdalena Horejsi, Marcela Madlikova, Milan Fabry, Monika Nedomova, Pavel Srb, Rozalie Hexnerova, Seth R Goldman, Vaclav Veverka, Vanda Lux, Zeger Debyser |
34537 |
Chemical Shifts: 1 set |
TFIIS N-terminal domain (TND) from human LEDGF/p75 |
A ubiquitous disordered protein interaction module orchestrates transcription elongation
|
Eric A Smith, H Courtney C Hodges, Jan De Rijck, Jonas Demeulemeester, Karen Adelman, Katerina Cermakova, Magdalena Horejsi, Marcela Madlikova, Milan Fabry, Monika Nedomova, Pavel Srb, Rozalie Hexnerova, Seth R Goldman, Vaclav Veverka, Vanda Lux, Zeger Debyser |
34538 |
Chemical Shifts: 1 set |
TFIIS N-terminal domain (TND) from human IWS1 |
A ubiquitous disordered protein interaction module orchestrates transcription elongation
|
Eric A Smith, H Courtney C Hodges, Jan De Rijck, Jonas Demeulemeester, Karen Adelman, Katerina Cermakova, Magdalena Horejsi, Marcela Madlikova, Milan Fabry, Monika Nedomova, Pavel Srb, Rozalie Hexnerova, Seth R Goldman, Vaclav Veverka, Vanda Lux, Zeger Debyser |
34539 |
Chemical Shifts: 1 set |
TFIIS N-terminal domain (TND) from human PPP1R10 |
A ubiquitous disordered protein interaction module orchestrates transcription elongation
|
Eric A Smith, H Courtney C Hodges, Jan De Rijck, Jonas Demeulemeester, Karen Adelman, Katerina Cermakova, Magdalena Horejsi, Marcela Madlikova, Milan Fabry, Monika Nedomova, Pavel Srb, Rozalie Hexnerova, Seth R Goldman, Vaclav Veverka, Vanda Lux, Zeger Debyser |
34540 |
Chemical Shifts: 1 set |
TFIIS N-terminal domain (TND) from human MED26 |
A ubiquitous disordered protein interaction module orchestrates transcription elongation
|
Eric A Smith, H Courtney C Hodges, Jan De Rijck, Jonas Demeulemeester, Karen Adelman, Katerina Cermakova, Magdalena Horejsi, Marcela Madlikova, Milan Fabry, Monika Nedomova, Pavel Srb, Rozalie Hexnerova, Seth R Goldman, Vaclav Veverka, Vanda Lux, Zeger Debyser |
34442 |
Chemical Shifts: 1 set |
Solution structure of the HRP2 IBD |
Unlike Its Paralog LEDGF/p75, HRP-2 Is Dispensable for MLL-R Leukemogenesis but Important for Leukemic Cell Survival
|
Alessandro Canella, Courtney H Hodges, Filip Matthijssens, Frauke Christ, Jan De Rijck, Katerina Cermakova, Pieter Van Vlierberghe, Sara El Ashkar, Siska Van Belle, Steven Goossens, Vaclav Veverka, Zeger Debyser |
6260 |
Chemical Shifts: 2 sets |
NMR solution Structure of a Highly Stable de novo Heterodimeric Coiled-Coil |
NMR solution Structure of a Highly Stable de novo Heterodimeric Coiled-Coil
|
Brian D Sykes, Darrin A Lindhout, Jennifer R Litowski, Pascal Mercier, Robert S Hodges |
4200 |
Chemical Shifts: 2 sets |
NMR Solution Structure of the c-Myc-Max Heterodimeric Leucine Zipper |
Insights into the Mechanism of Heterodimerization from the 1H-NMR Solution Structure of the c-Myc-Max Heterodimeric Leucine Zipper
|
B D Sykes, C M Kay, M P Crump, P Lavigne, R S Hodges, S M Gagne |