NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles
about
Structures of rat and human islet amyloid polypeptide IAPP(1-19) in micelles by NMR spectroscopyStructure of the Na,K-ATPase regulatory protein FXYD1 in micellesMolecular dynamics simulations of biological membranes and membrane proteins using enhanced conformational sampling algorithmsNMR structures of membrane proteins in phospholipid bilayersSolution NMR studies on the orientation of membrane-bound peptides and proteins by paramagnetic probesAccurate Determination of Conformational Transitions in Oligomeric Membrane Proteins.Backbone structure of a small helical integral membrane protein: A unique structural characterizationStructure and topology of monomeric phospholamban in lipid membranes determined by a hybrid solution and solid-state NMR approachStructural and Functional Analysis of Transmembrane Segment VI of the NHE1 Isoform of the Na+/H+ ExchangerStructural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR methodStructures of the Excited States of Phospholamban and Shifts in Their Populations upon PhosphorylationStructure of an HIV-1-neutralizing antibody target, the lipid-bound gp41 envelope membrane proximal region trimerModeling Protein-Micelle Systems in Implicit Water.Strategies for dealing with conformational sampling in structural calculations of flexible or kinked transmembrane peptides.NMR of membrane proteins in micelles and bilayers: the FXYD family proteinsNuclear magnetic resonance structural studies of membrane proteins in micelles and bilayers.A refinement protocol to determine structure, topology, and depth of insertion of membrane proteins using hybrid solution and solid-state NMR restraints.Automated NMR Assignment and Protein Structure Determination using Sparse Dipolar Coupling Constraints.Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.The alpha-helical propensity of the cytoplasmic domain of phospholamban: a molecular dynamics simulation of the effect of phosphorylation and mutation.An allosteric mechanism inferred from molecular dynamics simulations on phospholamban pentamer in lipid membranesNMR structure of the cathelicidin-derived human antimicrobial peptide LL-37 in dodecylphosphocholine micelles.Effects of CMAP and electrostatic cutoffs on the dynamics of an integral membrane protein: the phospholamban study.Lipid interaction networks of peripheral membrane proteins revealed by data-driven micelle dockingEffect of membrane thickness on conformational sampling of phospholamban from computer simulations.Structural dynamics and conformational equilibria of SERCA regulatory proteins in membranes by solid-state NMR restrained simulations.The structure of phospholamban pentamer reveals a channel-like architecture in membranesMapping the interaction surface of a membrane protein: unveiling the conformational switch of phospholamban in calcium pump regulation.Phospholamban C-terminal residues are critical determinants of the structure and function of the calcium ATPase regulatory complex.(1)H/(15)N heteronuclear NMR spectroscopy shows four dynamic domains for phospholamban reconstituted in dodecylphosphocholine micelles.Comparison of the structure and function of phospholamban and the arginine-14 deficient mutant associated with dilated cardiomyopathy.Discovery and structural characterization of a phospholamban-binding cyclic peptide and design of novel inhibitors of phospholamban.Structure-function relation of phospholamban: modulation of channel activity as a potential regulator of SERCA activity.Lethal Arg9Cys phospholamban mutation hinders Ca2+-ATPase regulation and phosphorylation by protein kinase A.Interactions between Ca2+-ATPase and the pentameric form of phospholamban in two-dimensional co-crystalsStructure and orientation of pardaxin determined by NMR experiments in model membranes.Phosphorylation and mutation of phospholamban alter physical interactions with the sarcoplasmic reticulum calcium pumpPhospholamban phosphorylation, mutation, and structural dynamics: a biophysical approach to understanding and treating cardiomyopathy.Paramagnetic-based NMR restraints lift residual dipolar coupling degeneracy in multidomain detergent-solubilized membrane proteins.Spectroscopic validation of the pentameric structure of phospholamban
P2860
Q24633016-4C33C2E4-FD5C-4C12-B756-C18B565CCA37Q24656151-65226C18-F121-459C-9B79-3420173E5C42Q26772040-A7FBD757-6CC9-4996-B114-1F45B8659634Q27006900-322030E6-1920-4537-B91E-7AFF859B0472Q27024724-8C1CF74B-B1D8-4CAA-9AFE-4AB42F28C456Q27332169-3DE0FFCB-1F4A-432D-A434-167C867D8EE9Q27653592-7970008E-44F6-41BA-9A72-597893B4CB78Q27655848-3C890736-F665-47A2-B194-16313A010B14Q27664496-7C7E77DF-55B8-4C49-8B1C-9A74529B2C8EQ27667869-D72B9D12-854B-46AE-94F4-46690BA14527Q27679786-606DA084-E9EE-443A-976E-202E68BB6E15Q27681501-D994A301-F827-4BAB-8A4D-0817773750ABQ30152916-DF391559-30B1-4AC8-81F8-FF0D6A92816BQ30359168-4CA89E58-ACEE-4EEB-846D-00B206190613Q30360510-FEFB79EC-B073-4BD2-8126-E5F2B12B56C5Q30365322-09A3A7BA-129F-4BCB-ABE6-47FB438E1E92Q30378910-34EE94D9-6F4F-44BB-82A3-B4E0500F0957Q30385726-609648E3-44B7-484F-B8C3-DF692D2E2F56Q30405936-A008D95E-0FF9-4F3E-81D9-05D07557BFE0Q30984765-C91260F4-DD8A-4B05-875A-82D7C3685EACQ31007659-DCA07E63-A372-4D5E-BB91-7E25A23153CEQ31153718-21F690DE-9BCE-46BE-938F-CDD64E9ABF57Q31158106-7807C533-CADD-43A2-AD6D-C1F663A6CC50Q33300056-F6902A30-4C41-44FB-8BD8-927315CE6736Q33696035-6472068B-4509-4DD3-A1D4-BD6783EDC36FQ33803663-AE22865D-5AA7-4045-87B7-DD81CCBA13C2Q33911608-075C3C7D-F842-426A-8958-C6A26B921558Q33935080-AEC3E1BC-23D5-4DA6-BF3A-007839287725Q34170810-512DF451-535B-4A3C-BD70-DAEE6C2D3645Q34186620-85DAC583-6A09-48C4-B33E-BC587230F7A2Q34194634-3606B624-179F-4FC1-A0BA-54A69254D04DQ34266350-5EA21DB6-E1EE-4172-AEE3-24BC896AC6EBQ34544548-00FCE46B-7D4A-4BA3-B254-56ECE11EA2AAQ34582867-62A5D3C2-F6EB-461F-BB65-3A3F3048FE9EQ34600845-DC3B6C0E-3D81-44AE-8F00-6CF228FFDDE9Q34803793-62C6D2AC-BF2A-4D37-949A-933DA78B8407Q35063543-B42748CA-35ED-482E-A5DB-499EAAFFBB18Q35169578-FD06137C-9577-4F1D-8E35-746438C4742CQ35894280-0C15938B-8906-47F3-AC79-F2B11A3ACAADQ35990215-553BC059-0537-4BEA-B108-F9D7BB723686
P2860
NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles
description
2003 nî lūn-bûn
@nan
2003 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
name
NMR Solution Structure and Top ...... Dodecylphosphocholine Micelles
@nl
NMR solution structure and top ...... dodecylphosphocholine micelles
@ast
NMR solution structure and top ...... dodecylphosphocholine micelles
@en
type
label
NMR Solution Structure and Top ...... Dodecylphosphocholine Micelles
@nl
NMR solution structure and top ...... dodecylphosphocholine micelles
@ast
NMR solution structure and top ...... dodecylphosphocholine micelles
@en
prefLabel
NMR Solution Structure and Top ...... Dodecylphosphocholine Micelles
@nl
NMR solution structure and top ...... dodecylphosphocholine micelles
@ast
NMR solution structure and top ...... dodecylphosphocholine micelles
@en
P2093
P2860
P1433
P1476
NMR solution structure and top ...... dodecylphosphocholine micelles
@en
P2093
Alessandro Mascioni
Gianluigi Veglia
Jamillah Zamoon
P2860
P304
P356
10.1016/S0006-3495(03)74681-5
P407
P577
2003-10-01T00:00:00Z