Year |
Citation |
Score |
2006 |
Golebiewska U, Gambhir A, Hangyás-Mihályné G, Zaitseva I, Rädler J, McLaughlin S. Membrane-bound basic peptides sequester multivalent (PIP2), but not monovalent (PS), acidic lipids. Biophysical Journal. 91: 588-99. PMID 16648167 DOI: 10.1529/Biophysj.106.081562 |
0.72 |
|
2004 |
Rusu L, Gambhir A, McLaughlin S, Rädler J. Fluorescence correlation spectroscopy studies of Peptide and protein binding to phospholipid vesicles. Biophysical Journal. 87: 1044-53. PMID 15298909 DOI: 10.1529/Biophysj.104.039958 |
0.727 |
|
2004 |
Gambhir A, Hangyás-Mihályné G, Zaitseva I, Cafiso DS, Wang J, Murray D, Pentyala SN, Smith SO, McLaughlin S. Electrostatic sequestration of PIP2 on phospholipid membranes by basic/aromatic regions of proteins. Biophysical Journal. 86: 2188-207. PMID 15041659 DOI: 10.1016/S0006-3495(04)74278-2 |
0.76 |
|
2004 |
Wang J, Gambhir A, McLaughlin S, Murray D. A computational model for the electrostatic sequestration of PI(4,5)P2 by membrane-adsorbed basic peptides. Biophysical Journal. 86: 1969-86. PMID 15041641 DOI: 10.1016/S0006-3495(04)74260-5 |
0.74 |
|
2002 |
Wang J, Gambhir A, Hangyás-Mihályné G, Murray D, Golebiewska U, McLaughlin S. Lateral sequestration of phosphatidylinositol 4,5-bisphosphate by the basic effector domain of myristoylated alanine-rich C kinase substrate is due to nonspecific electrostatic interactions. The Journal of Biological Chemistry. 277: 34401-12. PMID 12097325 DOI: 10.1074/Jbc.M203954200 |
0.681 |
|
2002 |
McLaughlin S, Wang J, Gambhir A, Murray D. PIP(2) and proteins: interactions, organization, and information flow. Annual Review of Biophysics and Biomolecular Structure. 31: 151-75. PMID 11988466 DOI: 10.1146/Annurev.Biophys.31.082901.134259 |
0.717 |
|
1999 |
Murray D, Arbuzova A, Hangyás-Mihályné G, Gambhir A, Ben-Tal N, Honig B, McLaughlin S. Electrostatic properties of membranes containing acidic lipids and adsorbed basic peptides: theory and experiment. Biophysical Journal. 77: 3176-88. PMID 10585939 DOI: 10.1016/S0006-3495(99)77148-1 |
0.712 |
|
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