ติดตาม
Alenka Copic
Alenka Copic
Group Leader, CNRS, Montpellier Cell Biology Research Center
ยืนยันอีเมลแล้วที่ crbm.cnrs.fr - หน้าแรก
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อ้างโดย
อ้างโดย
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Phosphatidylserine transport by ORP/Osh proteins is driven by phosphatidylinositol 4-phosphate
J Moser von Filseck, A Čopič, V Delfosse, S Vanni, CL Jackson, ...
Science 349 (6246), 432-436, 2015
3652015
Advances on the transfer of lipids by lipid transfer proteins
LH Wong, A Čopič, TP Levine
Trends in biochemical sciences 42 (7), 516-530, 2017
1912017
The many faces of amphipathic helices
M Giménez-Andrés, A Čopič, B Antonny
Biomolecules 8 (3), 45, 2018
1792018
ER cargo properties specify a requirement for COPII coat rigidity mediated by Sec13p
A Čopič, CF Latham, MA Horlbeck, JG D’Arcangelo, EA Miller
Science 335 (6074), 1359-1362, 2012
1612012
A combinatorial lipid code shapes the electrostatic landscape of plant endomembranes
MP Platre, LC Noack, M Doumane, V Bayle, MLA Simon, L Maneta-Peyret, ...
Developmental cell 45 (4), 465-480. e11, 2018
1592018
A giant amphipathic helix from a perilipin that is adapted for coating lipid droplets
A Čopič, S Antoine-Bally, M Giménez-Andrés, C La Torre Garay, ...
Nature communications 9 (1), 1332, 2018
1242018
Genomewide analysis reveals novel pathways affecting endoplasmic reticulum homeostasis, protein modification and quality control
A Cˇopic, M Dorrington, S Pagant, J Barry, MCS Lee, I Singh, ...
Genetics 182 (3), 757-769, 2009
812009
Ent3p and Ent5p Exhibit Cargo-specific Functions in Trafficking Proteins between the Trans-Golgi Network and the Endosomes in Yeast
A Čopič, TL Starr, R Schekman
Molecular biology of the cell 18 (5), 1803-1815, 2007
702007
A high affinity acceptor for phospholipase A2 with neurotoxic activity is a calmodulin
J Sˇribar, A Copic, A Pariš, NE Sherman, F Gubenšek, JW Fox, I Krizaj
Journal of Biological Chemistry 276 (16), 12493-12496, 2001
702001
Identification and purification of a novel receptor for secretory phospholipase A2 in porcine cerebral cortex
A Čopič, N Vučemilo, F Gubenšek, I Križaj
Journal of biological chemistry 274 (37), 26315-26320, 1999
631999
Membrane bending: the power of protein imbalance
J Derganc, B Antonny, A Čopič
Trends in biochemical sciences 38 (11), 576-584, 2013
592013
Membrane bending by protein crowding is affected by protein lateral confinement
J Derganc, A Čopič
Biochimica et Biophysica Acta (BBA)-Biomembranes 1858 (6), 1152-1159, 2016
492016
Osh6 requires Ist2 for localization to ER–PM contacts and efficient phosphatidylserine transport in budding yeast
JM d'Ambrosio, V Albanèse, NF Lipp, L Fleuriot, D Debayle, G Drin, ...
Journal of cell science 133 (11), jcs243733, 2020
452020
An electrostatic switching mechanism to control the lipid transfer activity of Osh6p
NF Lipp, R Gautier, M Magdeleine, M Renard, V Albanèse, A Čopič, ...
Nature communications 10 (1), 3926, 2019
402019
Traffic of p24 proteins and COPII coat composition mutually influence membrane scaffolding
JG D’Arcangelo, J Crissman, S Pagant, A Čopič, CF Latham, EL Snapp, ...
Current Biology 25 (10), 1296-1305, 2015
392015
Transport pathways that contribute to the cellular distribution of phosphatidylserine
G Lenoir, JM D’ambrosio, T Dieudonné, A Čopič
Frontiers in cell and developmental biology 9, 737907, 2021
342021
Identification of a new high-affinity binding protein for neurotoxic phospholipases A2
N Vučemilo, A Čopič, F Gubenšek, I Križaj
Biochemical and biophysical research communications 251 (1), 209-212, 1998
341998
New molecular mechanisms of inter-organelle lipid transport
G Drin, JM von Filseck, A Čopič
Biochemical Society Transactions 44 (2), 486-492, 2016
312016
The amino acid region 115–119 of ammodytoxins plays an important role in neurotoxicity
G Ivanovski, A Čopič, I Križaj, F Gubenšek, J Pungerčar
Biochemical and biophysical research communications 276 (3), 1229-1234, 2000
292000
Crotoxin acceptor protein isolated from Torpedo electric organ: binding properties to crotoxin by surface plasmon resonance
G Faure, A Čopič, S Le Porrier, F Gubenšek, C Bon, I Križaj
Toxicon 41 (4), 509-517, 2003
282003
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