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Journal Abstract Search
407 related items for PubMed ID: 17704143
1. Investigating the interaction of saposin C with POPS and POPC phospholipids: a solid-state NMR spectroscopic study. Abu-Baker S, Qi X, Lorigan GA. Biophys J; 2007 Nov 15; 93(10):3480-90. PubMed ID: 17704143 [Abstract] [Full Text] [Related]
3. PMP1 18-38, a yeast plasma membrane protein fragment, binds phosphatidylserine from bilayer mixtures with phosphatidylcholine: a (2)H-NMR study. Roux M, Beswick V, Coïc YM, Huynh-Dinh T, Sanson A, Neumann JM. Biophys J; 2000 Nov 15; 79(5):2624-31. PubMed ID: 11053135 [Abstract] [Full Text] [Related]
4. pH-Dependent Membrane Interactions of the Histidine-Rich Cell-Penetrating Peptide LAH4-L1. Wolf J, Aisenbrey C, Harmouche N, Raya J, Bertani P, Voievoda N, Süss R, Bechinger B. Biophys J; 2017 Sep 19; 113(6):1290-1300. PubMed ID: 28734478 [Abstract] [Full Text] [Related]
6. Investigating the interaction between peptides of the amphipathic helix of Hcf106 and the phospholipid bilayer by solid-state NMR spectroscopy. Zhang L, Liu L, Maltsev S, Lorigan GA, Dabney-Smith C. Biochim Biophys Acta; 2014 Jan 19; 1838(1 Pt B):413-8. PubMed ID: 24144541 [Abstract] [Full Text] [Related]
7. Solid-state nuclear magnetic resonance relaxation studies of the interaction mechanism of antimicrobial peptides with phospholipid bilayer membranes. Lu JX, Damodaran K, Blazyk J, Lorigan GA. Biochemistry; 2005 Aug 02; 44(30):10208-17. PubMed ID: 16042398 [Abstract] [Full Text] [Related]
14. Investigating structural changes in the lipid bilayer upon insertion of the transmembrane domain of the membrane-bound protein phospholamban utilizing 31P and 2H solid-state NMR spectroscopy. Dave PC, Tiburu EK, Damodaran K, Lorigan GA. Biophys J; 2004 Mar 14; 86(3):1564-73. PubMed ID: 14990483 [Abstract] [Full Text] [Related]
17. Interaction of Human β Defensin Type 3 (hBD-3) with Different PIP2-Containing Membranes, a Molecular Dynamics Simulation Study. Zhang L. J Chem Inf Model; 2021 Sep 27; 61(9):4670-4686. PubMed ID: 34473496 [Abstract] [Full Text] [Related]