𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Interaction between dipalmitoylphosphatidylglycerol and phosphatidylcholine and calcium

✍ Scribed by K. Naga; N.H. Rich; K.M.W. Keough

Publisher
Elsevier Science
Year
1994
Tongue
English
Weight
410 KB
Volume
244
Category
Article
ISSN
0040-6090

No coin nor oath required. For personal study only.

πŸ“œ SIMILAR VOLUMES

Interaction between phosphatidylcholine
Interaction between phosphatidylcholine and cholesterol in benzene
✍ J.P.M. Janson; M. Kunst; A. Rip; P. Bordewijk πŸ“‚ Article πŸ“… 1973 πŸ› Elsevier Science 🌐 English βš– 506 KB

The interaction between phosphatidylcholine (PC) and cholesterol was studied in benzene with the help of vapour-pressure osmometry and static dielectric measurements. No indication for the occurrence of molecular complexes was found. Instead, our results can be explained by assuming PC aggregates (a

Investigation of the interaction between
Investigation of the interaction between melittin and dipalmitoylphosphatidylglycerol bilayers by vibrational spectroscopy
✍ Michel Lafleur; Isabelle Samson; Michel PΓ©zolet πŸ“‚ Article πŸ“… 1991 πŸ› Elsevier Science 🌐 English βš– 969 KB

Melittin is shown to affect the structure of the charged phospholipid dipalmitoylphosphatidylglycerol (DPPG). In the gel phase, the presence of melittin leads to (i) an increased lipid interchain vibrational coupling, (ii) a shift of the rectangular to hexagonal lipid packing transition toward low t

Phosphatidylcholine and cholesterol inte
Phosphatidylcholine and cholesterol interactions in model membranes
✍ W. Guyer; K. Bloch πŸ“‚ Article πŸ“… 1983 πŸ› Elsevier Science 🌐 English βš– 484 KB

Various phosphatidylcholines differing either in the stereochemistry around their chiral center or in the position of a cis double bond along the acyl chains were synthesized in order to study critical contact regions in the phospholipid molecule with adjacent cholesterol in model membranes. Microvi

Calcium- and FK506-independent interacti
Calcium- and FK506-independent interaction between the immunophilin FKBP51 and calcineurin
✍ Ta-Kai Li; Shairaz Baksh; Anthony D. Cristillo; Barbara E. Bierer πŸ“‚ Article πŸ“… 2002 πŸ› John Wiley and Sons 🌐 English βš– 216 KB

## Abstract FKBP51 is a member of the immunophilin family having intrinsic peptidyl‐prolyl cis‐trans‐isomerase (PPIase) activity. Its enzymatic activity is inhibited by binding either immunosuppressive agent FK506 or rapamycin. Similar to FKBP12, but at higher concentrations of FK506, FKBP51 has be