christer larsson
christer larsson
Department of Biochemistry and Structural Biology, Lund University, Sweden
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TitleCited byYear
Water transport activity of the plasma membrane aquaporin PM28A is regulated by phosphorylation
I Johansson, M Karlsson, VK Shukla, MJ Chrispeels, C Larsson, ...
The Plant Cell 10 (3), 451-459, 1998
[52] Preparation of high-purity plasma membranes
C Larsson, S Widell, P Kjellbom
Methods in Enzymology 148, 558-568, 1987
The role of aquaporins in cellular and whole plant water balance
I Johansson, M Karlsson, U Johanson, C Larsson, P Kjellbom
Biochimica et Biophysica Acta (BBA)-Biomembranes 1465 (1-2), 324-342, 2000
The major integral proteins of spinach leaf plasma membranes are putative aquaporins and are phosphorylated in response to Ca2+ and apoplastic water potential.
I Johansson, C Larsson, B Ek, P Kjellbom
The Plant Cell 8 (7), 1181-1191, 1996
Preparation and polypeptide composition of chlorophyll‐free plasma membranes from leaves of light‐grown spinach and barley
P Kjellbom, C Larsson
Physiologia Plantarum 62 (4), 501-509, 1984
Arabidopsis plasma membrane proteomics identifies components of transport, signal transduction and membrane trafficking
E Alexandersson, G Saalbach, C Larsson, P Kjellbom
Plant and Cell Physiology 45 (11), 1543-1556, 2004
Isolation of highly purified plant plasma membranes and separation of inside-out and right-side-out vesicles.
C Larsson
Methods Enzymol. 228, 451-469, 1994
Phosphorylation of Thr-948 at the C terminus of the plasma membrane H+-ATPase creates a binding site for the regulatory 14-3-3 protein
F Svennelid, A Olsson, M Piotrowski, M Rosenquist, C Ottman, C Larsson, ...
The Plant Cell 11 (12), 2379-2391, 1999
The 14-3-3 protein interacts directly with the C-terminal region of the plant plasma membrane H (+)-ATPase.
T Jahn, AT Fuglsang, A Olsson, IM Brüntrup, DB Collinge, D Volkmann, ...
The Plant Cell 9 (10), 1805-1814, 1997
Evolution of the 14-3-3 protein family: does the large number of isoforms in multicellular organisms reflect functional specificity?
M Rosenquist, P Sehnke, RJ Ferl, M Sommarin, C Larsson
Journal of molecular evolution 51 (5), 446-458, 2000
Aquaporins and water homeostasis in plants
P Kjellbom, C Larsson, I Johansson, M Karlsson, U Johanson
Trends in plant science 4 (8), 308-314, 1999
Sealed inside-out and right-side-out plasma membrane vesicles: optimal conditions for formation and separation
MG Palmgren, P Askerlund, K Fredrikson, S Widell, M Sommarin, ...
Plant Physiology 92 (4), 871-880, 1990
Phase partition—a method for purification and analysis of cell organelles and membrane vesicles
PÅ Albertsson, B Andersson, C Larsson, HE Åkerlund
Methods of biochemical analysis 28, 115-150, 1982
Data mining the Arabidopsis genome reveals fifteen 14-3-3 genes. Expression is demonstrated for two out of five novel genes
M Rosenquist, M Alsterfjord, C Larsson, M Sommarin
Plant physiology 127 (1), 142-149, 2001
Salinity and hyperosmotic stress induce rapid increases in phosphatidylinositol 4, 5-bisphosphate, diacylglycerol pyrophosphate, and phosphatidylcholine in Arabidopsis thaliana …
C Pical, T Westergren, SK Dove, C Larsson, M Sommarin
Journal of Biological Chemistry 274 (53), 38232-38240, 1999
Brij 58, a polyoxyethylene acyl ether, creates membrane vesicles of uniform sidedness. A new tool to obtain inside‐out (cytoplasmic side‐out) plasma membrane vesicles
F Johansson, M Olbe, M Sommarin, C Larsson
The Plant Journal 7 (1), 165-173, 1995
Fusicoccin activates the plasma membrane H+-ATPase by a mechanism involving the C-terminal inhibitory domain.
F Johansson, M Sommarin, C Larsson
The Plant Cell 5 (3), 321-327, 1993
Plasma membranes from oats prepared by partition in an aqueous polymer two-phase system: On the use of light-induced cytochrome b reduction as a marker for the plasma membrane
S Widell, T Lundborg, C Larsson
Plant physiology 70 (5), 1429-1435, 1982
Sidedness of plant plasma membrane vesicles purified by partitioning in aqueous two‐phase systems
C Larsson, P Kjellbom, S Widell, T Lundborg
FEBS letters 171 (2), 271-276, 1984
Proteolytic activation of the plant plasma membrane H (+)-ATPase by removal of a terminal segment.
MG Palmgren, C Larsson, M Sommarin
Journal of Biological Chemistry 265 (23), 13423-13426, 1990
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