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Entry ID	Original Release date	Data summary	Entry Title	Citation Title	Authors
34285	2019-05-17	Chemical Shifts: 1 set	Solution structure of the capsid domain from the activity-regulated cytoskeleton-associated protein, Arc	The Capsid Domain of Arc Changes Its Oligomerization Propensity through Direct Interaction with the NMDA Receptor	C P Pedersen, K Teilum, L D Nielsen, S Erlendsson
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