Entry ID |
Original Release date |
Data summary |
Entry Title |
Citation Title |
Authors |
28062 |
2021-07-16 |
Chemical Shifts: 1 set |
Backbone 1H, 13C, and 15N Chemical Shift Assignments for RPT1 of hSNF5 and SWIRM of BAF155 |
A Coil-to-Helix Transition Serves as a Binding Motif for hSNF5 and BAF155 Interaction
|
Gye-Young Y Park, Iktae Kim, Jae-Hyun H Park, Jeongmin Han, Jeong-Yong Y Suh, Ji-Hye H Yun, Jooyoung Lee, Keehyoung Joo, Kenji Mizutani, Kyoung-Seok S Ryu, Rho Hyun H Seong, Sam-Young Y Park, Taehee Kim, Weontae Lee, Yoon-Joo J Ko |
28063 |
2021-07-16 |
Chemical Shifts: 1 set |
Backbone 1H, 13C, and 15N Chemical shift Assignments for SWIRM domain of BAF155 and RPT1 of hSNF5 |
A Coil-to-Helix Transition Serves as a Binding Motif for hSNF5 and BAF155 Interaction
|
Gye-Young Y Park, Iktae Kim, Jae-Hyun H Park, Jeongmin Han, Jeong-Yong Y Suh, Ji-Hye H Yun, Jooyoung Lee, Keehyoung Joo, Kenji Mizutani, Kyoung-Seok S Ryu, Rho Hyun H Seong, Sam-Young Y Park, Taehee Kim, Weontae Lee, Yoon-Joo J Ko |
28064 |
2021-07-16 |
Chemical Shifts: 1 set |
Solution structure of hSNF5 RPT1 domain |
A Coil-to-Helix Transition Serves as a Binding Motif for hSNF5 and BAF155 Interaction
|
Gye-Young Y Park, Iktae Kim, Jae-Hyun H Park, Jeongmin Han, Jeong-Yong Y Suh, Ji-Hye H Yun, Jooyoung Lee, Keehyoung Joo, Kenji Mizutani, Kyoung-Seok S Ryu, Rho Hyun H Seong, Sam-Young Y Park, Taehee Kim, Weontae Lee, Yoon-Joo J Ko |
4595 |
2000-12-04 |
Chemical Shifts: 1 set |
Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation -- P25 |
Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation
|
A S Mildvan, M A Massiah, P L Pedersen, Y H Ko |
4596 |
2000-12-04 |
Chemical Shifts: 1 set |
Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation -- P26 |
Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation -- P26
|
A S Mildvan, M A Massiah, P L Pedersen, Y H Ko |
4597 |
2000-12-04 |
Chemical Shifts: 1 set |
Cystic Fibrosis Transmembrane Conductance Regulator: Solution Structures of Peptides Based on the Phe508 Region, the Most Common Site of Disease-Causing DeltaF508 Mutation |
Cystic Fibrosis Transmembrane Conductance Regulator: Solution Structures of Peptides Based on the Phe508 Region, the Most Common Site of Disease-Causing DeltaF508 Mutation
|
A S Mildvan, M A Massiah, P L Pedersen, Y H Ko |
4598 |
2000-12-04 |
Chemical Shifts: 1 set |
Cystic Fibrosis Transmembrane Conductance Regulator: Solution Structures of Peptides Based on the Phe508 Region, the Most Common Site of Disease-Causing DeltaF508 Mutation |
Cystic Fibrosis Transmembrane Conductance Regulator: Solution Structures of Peptides Based on the Phe508 Region, the Most Common Site of Disease-Causing DeltaF508 Mutation
|
A S Mildvan, M A Massiah, P L Pedersen, Y H Ko |