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Erwin London
Erwin London
distinguished professor of biochemistry and cell biology
Bestätigte E-Mail-Adresse bei stonybrook.edu
Titel
Zitiert von
Zitiert von
Jahr
Functions of lipid rafts in biological membranes
DA Brown, E London
Annual review of cell and developmental biology 14, 111-136, 1998
39571998
Structure and function of sphingolipid-and cholesterol-rich membrane rafts
DA Brown, E London
Journal of Biological Chemistry 275 (23), 17221-17224, 2000
30472000
Structure and origin of ordered lipid domains in biological membranes
DA Brown, E London
The Journal of membrane biology 164, 103-114, 1998
11811998
Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes …
R Schroeder, E London, D Brown
Proceedings of the National Academy of Sciences 91 (25), 12130-12134, 1994
9141994
On the origin of sphingolipid/cholesterol-rich detergent-insoluble cell membranes: physiological concentrations of cholesterol and sphingolipid induce formation of a detergent …
SN Ahmed, DA Brown, E London
Biochemistry 36 (36), 10944-10953, 1997
8801997
Insolubility of lipids in triton X-100: physical origin and relationship to sphingolipid/cholesterol membrane domains (rafts)
E London, DA Brown
Biochimica et Biophysica Acta (BBA)-Biomembranes 1508 (1-2), 182-195, 2000
8592000
Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids
A Chattopadhyay, E London
Biochemistry 26 (1), 39-45, 1987
7671987
Structure of Detergent-Resistant Membrane Domains: Does Phase Separation Occur in Biological Membranes?
DA Brown, E London
Biochemical and biophysical research communications 240, 1-7, 1997
664*1997
Effect of the structure of natural sterols and sphingolipids on the formation of ordered sphingolipid/sterol domains (rafts)
X Xu, R Bittman, G Duportail, D Heissler, C Vilcheze, E London
Journal of Biological Chemistry 276 (36), 33540-33546, 2001
6302001
The effect of sterol structure on membrane lipid domains reveals how cholesterol can induce lipid domain formation
X Xu, E London
Biochemistry 39 (5), 843-849, 2000
6262000
Cholesterol and sphingolipid enhance the Triton X-100 insolubility of glycosylphosphatidylinositol-anchored proteins by promoting the formation of detergent-insoluble ordered …
RJ Schroeder, SN Ahmed, Y Zhu, E London, DA Brown
Journal of Biological Chemistry 273 (2), 1150-1157, 1998
5231998
Fluorimetric determination of critical micelle concentration avoiding interference from detergent charge
A Chattopadhyay, E London
Analytical biochemistry 139 (2), 408-412, 1984
5061984
Refolding of an integral membrane protein. Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments.
KS Huang, H Bayley, MJ Liao, E London, HG Khorana
Journal of Biological Chemistry 256 (8), 3802-3809, 1981
4421981
Location of diphenylhexatriene (DPH) and its derivatives within membranes: comparison of different fluorescence quenching analyses of membrane depth
RD Kaiser, E London
Biochemistry 37 (22), 8180-8190, 1998
4201998
Ceramide selectively displaces cholesterol from ordered lipid domains (rafts) implications for lipid raft structure and function
Megha, E London
Journal of Biological Chemistry 279 (11), 9997-10004, 2004
4132004
Insights into lipid raft structure and formation from experiments in model membranes
E London
Current opinion in structural biology 12 (4), 480-486, 2002
3352002
How principles of domain formation in model membranes may explain ambiguities concerning lipid raft formation in cells
E London
Biochimica et Biophysica Acta (BBA)-Molecular Cell Research 1746 (3), 203-220, 2005
3072005
Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures.
E London, HG Khorana
Journal of Biological Chemistry 257 (12), 7003-7011, 1982
3061982
Extension of the parallax analysis of membrane penetration depth to the polar region of model membranes: use of fluorescence quenching by a spin-label attached to the …
FS Abrams, E London
Biochemistry 32 (40), 10826-10831, 1993
2461993
Transmembrane orientation of hydrophobic α-helices is regulated both by the relationship of helix length to bilayer thickness and by the cholesterol concentration
J Ren, S Lew, Z Wang, E London
Biochemistry 36 (33), 10213-10220, 1997
2431997
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