Rapid topology probing using fluorescence spectroscopy in planar lipid bilayer: the pore-forming mechanism of the toxin Cry1Aa of Bacillus thuringiensis.
about
Acquiring snapshots of the orientation of trans-membrane protein domains using a hybrid FRET pair.The Human Sodium-Glucose Cotransporter (hSGLT1) Is a Disulfide-Bridged Homodimer with a Re-Entrant C-Terminal LoopStructure of anthrax lethal toxin prepore complex suggests a pathway for efficient cell entry.Single molecule fluorescence study of the Bacillus thuringiensis toxin Cry1Aa reveals tetramerization.Do lipids show state-dependent affinity to the voltage-gated potassium channel KvAP?Relative positioning of Kv11.1 (hERG) K channel cytoplasmic domain-located fluorescent tags toward the plasma membrane
P2860
Rapid topology probing using fluorescence spectroscopy in planar lipid bilayer: the pore-forming mechanism of the toxin Cry1Aa of Bacillus thuringiensis.
description
2010 nî lūn-bûn
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2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Rapid topology probing using f ...... 1Aa of Bacillus thuringiensis.
@en
Rapid topology probing using f ...... 1Aa of Bacillus thuringiensis.
@nl
type
label
Rapid topology probing using f ...... 1Aa of Bacillus thuringiensis.
@en
Rapid topology probing using f ...... 1Aa of Bacillus thuringiensis.
@nl
prefLabel
Rapid topology probing using f ...... 1Aa of Bacillus thuringiensis.
@en
Rapid topology probing using f ...... 1Aa of Bacillus thuringiensis.
@nl
P2860
P356
P1476
Rapid topology probing using f ...... 1Aa of Bacillus thuringiensis.
@en
P2093
Marc Juteau
Nicolas Groulx
P2860
P304
P356
10.1085/JGP.200910347
P577
2010-11-01T00:00:00Z