PS 34:1 (BioDeep_00000632607)

 

Secondary id: BioDeep_00000009639

LipidSearch


代谢物信息卡片


L-Serine, 3-[(1-oxohexadecyl)oxy]-2-[(1-oxo-9-octadecenyl)oxy]propyl hydrogen phosphate (ester), [R-(Z)]-

化学式: C40H76NO10P (761.5207)
中文名称:
谱图信息: 最多检出来源 Homo sapiens(lipidomics) 94.28%

分子结构信息

SMILES: C(O)(=O)[C@@]([H])(N)COP(OC[C@]([H])(OC(CCCCCCC/C=C\CCCC)=O)COC(CCCCCCCCCCCCCCCCCCC)=O)(=O)O
InChI: InChI=1S/C40H76NO10P/c1-3-5-7-9-11-13-14-15-16-17-18-19-20-21-22-24-25-27-29-31-38(42)48-33-36(34-49-52(46,47)50-35-37(41)40(44)45)51-39(43)32-30-28-26-23-12-10-8-6-4-2/h17-18,36-37H,3-16,19-35,41H2,1-2H3,(H,44,45)(H,46,47)/b18-17-/t36-,37+/m1/s1

描述信息

A 3-sn-phosphatidyl-L-serine compound with a palmitoyl group at the 1-position and an oleoyl group at the 2-position.

同义名列表

49 个代谢物同义名

L-Serine, 3-[(1-oxohexadecyl)oxy]-2-[(1-oxo-9-octadecenyl)oxy]propyl hydrogen phosphate (ester), [R-(Z)]-; {1-O-hexadecanoyl-2-O-[(Z)-octadec-9-enoyl]-sn-glycero-3-phospho}serine; 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoserine; 1-Palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylserine; PS(16:0/18:1(9Z)); PS(16:0_18:1); PS(16:0/18:1); PS(34:1); PS 34:1; POPS; 1-(9Z-octadecenoyl)-2-hexadecanoyl-glycero-3-phosphoserine; PS(18:1(9Z)/16:0); 1-octadecanoyl-2-(9Z-hexadecenoyl)-glycero-3-phosphoserine; PS(18:0/16:1(9Z)); PS(16:1_18:0); 1-(11Z-docosenoyl)-2-dodecanoyl-glycero-3-phosphoserine; PS(22:1(11Z)/12:0); PS(12:0_22:1); 1-(11Z-eicosenoyl)-2-tetradecanoyl-glycero-3-phosphoserine; PS(20:1(11Z)/14:0); PS(14:0_20:1); 1-eicosanoyl-2-(9Z-tetradecenoyl)-glycero-3-phosphoserine; PS(20:0/14:1(9Z)); PS(14:1_20:0); 1-(9Z-nonadecenoyl)-2-pentadecanoyl-glycero-3-phosphoserine; PS(19:1(9Z)/15:0); PS(15:0_19:1); 1-nonadecanoyl-2-(9Z-pentadecenoyl)-glycero-3-phosphoserine; PS(19:0/15:1(9Z)); PS(15:1_19:0); 1-(9Z-heptadecenoyl)-2-heptadecanoyl-glycero-3-phosphoserine; PS(17:1(9Z)/17:0); PS(17:0_17:1); 1-heptadecanoyl-2-(9Z-heptadecenoyl)-glycero-3-phosphoserine; PS(17:0/17:1(9Z)); 1-(9Z-hexadecenoyl)-2-octadecanoyl-glycero-3-phosphoserine; PS(16:1(9Z)/18:0); 1-(9Z-pentadecenoyl)-2-nonadecanoyl-glycero-3-phosphoserine; PS(15:1(9Z)/19:0); 1-pentadecanoyl-2-(9Z-nonadecenoyl)-glycero-3-phosphoserine; PS(15:0/19:1(9Z)); 1-(9Z-tetradecenoyl)-2-eicosanoyl-glycero-3-phosphoserine; PS(14:1(9Z)/20:0); 1-tetradecanoyl-2-(11Z-eicosenoyl)-glycero-3-phosphoserine; PS(14:0/20:1(11Z)); 1-dodecanoyl-2-(11Z-docosenoyl)-glycero-3-phosphoserine; PS(12:0/22:1(11Z)); 1-hexadecanoyl-2-(11Z-octadecenoyl)-sn-glycero-3-phosphoserine; PS(16:0/18:1(11Z))



数据库引用编号

51 个数据库交叉引用编号

分类词条

相关代谢途径

Reactome(0)

BioCyc(0)

PlantCyc(0)

代谢反应

6 个相关的代谢反应过程信息。

Reactome(0)

BioCyc(0)

WikiPathways(0)

Plant Reactome(0)

INOH(0)

PlantCyc(0)

COVID-19 Disease Map(0)

PathBank(6)

PharmGKB(0)

0 个相关的物种来源信息

在这里通过桑基图来展示出与当前的这个代谢物在我们的BioDeep知识库中具有相关联信息的其他代谢物。在这里进行关联的信息来源主要有:

  • PubMed: 来源于PubMed文献库中的文献信息,我们通过自然语言数据挖掘得到的在同一篇文献中被同时提及的相关代谢物列表,这个列表按照代谢物同时出现的文献数量降序排序,取前10个代谢物作为相关研究中关联性很高的代谢物集合展示在桑基图中。
  • NCBI Taxonomy: 通过文献数据挖掘,得到的代谢物物种来源信息关联。这个关联信息同样按照出现的次数降序排序,取前10个代谢物作为高关联度的代谢物集合展示在桑吉图上。
  • Chemical Taxonomy: 在物质分类上处于同一个分类集合中的其他代谢物
  • Chemical Reaction: 在化学反应过程中,存在为当前代谢物相关联的生化反应过程中的反应底物或者反应产物的关联代谢物信息。

点击图上的相关代谢物的名称,可以跳转到相关代谢物的信息页面。

亚细胞结构定位 关联基因列表
Cytoplasm 10 ANXA1, ANXA2, FANCL, GLTP, HRAS, PRKCA, PRNP, PTH2, S100A10, SNCA
Golgi apparatus, trans-Golgi network membrane 1 AQP2
Peripheral membrane protein 2 ANXA1, PRKCA
Endosome membrane 1 ANXA1
Endoplasmic reticulum membrane 1 HRAS
Mitochondrion membrane 1 PRKCA
Nucleus 5 ANXA1, ANXA2, FANCL, PRKCA, SNCA
cytosol 11 ANXA1, ANXA2, APOA1, FANCL, GLTP, HRAS, PRKCA, PRKCQ, PRNP, PTH2, SNCA
dendrite 1 PRNP
mitochondrial membrane 1 PRKCA
nuclear body 1 FANCL
nucleoplasm 4 ANXA1, FANCL, HRAS, PRKCA
RNA polymerase II transcription regulator complex 2 ANXA2, S100A10
Cell membrane 6 ANXA1, AQP2, HRAS, KCNMA1, PRKCA, PRNP
Lipid-anchor 1 HRAS
Cytoplasmic side 1 HRAS
Cell projection, axon 1 SNCA
Early endosome membrane 1 ANXA1
Multi-pass membrane protein 4 AQP2, KCNA3, KCNMA1, PTH2R
Golgi apparatus membrane 1 HRAS
Synapse 1 SNCA
cell cortex 1 SNCA
cell surface 5 ANXA1, ANXA2, F3, PRNP, S100A10
glutamatergic synapse 2 HRAS, KCNA3
Golgi apparatus 4 AQP2, ATRN, HRAS, PRNP
Golgi membrane 1 HRAS
growth cone 1 SNCA
lysosomal membrane 1 ANXA2
neuronal cell body 2 IAPP, SNCA
postsynapse 2 PRNP, SNCA
presynaptic membrane 1 KCNA3
sarcolemma 2 ANXA1, ANXA2
Lysosome 1 SNCA
endosome 2 ANXA1, ANXA2
plasma membrane 15 ANXA1, ANXA2, APOA1, AQP2, ATRN, F3, HRAS, KCNA3, KCNMA1, PRKCA, PRKCQ, PRNP, PTH2R, S100A10, SNCA
synaptic vesicle membrane 1 SNCA
terminal bouton 1 PRNP
Membrane 14 ANXA1, ANXA2, AQP2, F3, FANCL, HRAS, KCNA3, KCNMA1, PRKCA, PRNP, PTH2, PTH2R, S100A10, SNCA
apical plasma membrane 3 ANXA1, AQP2, KCNMA1
axon 2 KCNA3, SNCA
basolateral plasma membrane 3 ANXA1, ANXA2, AQP2
caveola 1 KCNMA1
extracellular exosome 8 ANXA1, ANXA2, APOA1, AQP2, ATRN, PRKCA, PRNP, S100A10
endoplasmic reticulum 2 PRKCA, PRNP
extracellular space 9 ANXA1, ANXA2, APOA1, ATRN, DEFB103A, F3, IAPP, S100A10, SNCA
perinuclear region of cytoplasm 5 AQP2, HRAS, KCNA3, PRKCA, SNCA
adherens junction 2 ANXA1, ANXA2
mitochondrion 4 PRKCA, PRNP, PTH2, SNCA
protein-containing complex 1 SNCA
intracellular membrane-bounded organelle 2 FANCL, PRNP
postsynaptic density 2 PRNP, PTH2
Single-pass type I membrane protein 2 ATRN, F3
Secreted 4 ANXA1, APOA1, IAPP, SNCA
extracellular region 8 ANXA1, ANXA2, APOA1, DEFB103A, IAPP, PTH2, S100A10, SNCA
Mitochondrion outer membrane 2 PRNP, PTH2
Single-pass membrane protein 2 PRNP, PTH2
mitochondrial outer membrane 2 PRNP, PTH2
[Isoform 1]: Membrane 1 F3
[Isoform 2]: Secreted 2 ATRN, F3
Extracellular side 1 ANXA1
Cell projection, cilium 1 ANXA1
centriolar satellite 1 PRKCQ
motile cilium 1 ANXA1
nuclear membrane 1 PRNP
external side of plasma membrane 2 F3, PRNP
Extracellular vesicle 1 APOA1
chylomicron 1 APOA1
high-density lipoprotein particle 1 APOA1
low-density lipoprotein particle 1 APOA1
very-low-density lipoprotein particle 1 APOA1
actin cytoskeleton 1 SNCA
dendritic spine 1 PTH2
cytoplasmic vesicle 1 APOA1
midbody 1 ANXA2
Early endosome 3 ANXA1, ANXA2, APOA1
recycling endosome 1 AQP2
vesicle 2 ANXA1, ANXA2
postsynaptic membrane 2 KCNA3, KCNMA1
Apical cell membrane 2 ANXA1, AQP2
Membrane raft 2 KCNA3, PRNP
focal adhesion 1 ANXA1
basement membrane 1 ANXA2
Cell projection, dendritic spine 1 PTH2
Nucleus, PML body 1 PTH2
PML body 1 PTH2
collagen-containing extracellular matrix 5 ANXA1, ANXA2, APOA1, F3, S100A10
lateral plasma membrane 2 ANXA1, AQP2
ciliary basal body 1 PRKCA
cilium 1 ANXA1
chromatin 1 FANCL
Late endosome membrane 1 ANXA2
Cell projection, phagocytic cup 1 ANXA1
phagocytic cup 1 ANXA1
supramolecular fiber 1 SNCA
Secreted, extracellular space 1 ANXA1
plasma membrane protein complex 2 ANXA2, S100A10
blood microparticle 1 APOA1
Basolateral cell membrane 2 ANXA1, AQP2
Lipid-anchor, GPI-anchor 1 PRNP
[Isoform 2]: Cell membrane 1 KCNA3
[Isoform 3]: Secreted 1 ATRN
nuclear envelope 1 FANCL
Endomembrane system 1 HRAS
Lipid droplet 1 ANXA2
Cornified envelope 2 ANXA1, ANXA2
Fanconi anaemia nuclear complex 1 FANCL
Cytoplasmic vesicle membrane 2 ANXA1, AQP2
Melanosome 1 ANXA2
side of membrane 1 PRNP
voltage-gated potassium channel complex 2 KCNA3, KCNMA1
secretory granule lumen 1 APOA1
Golgi lumen 1 DEFB103A
endoplasmic reticulum lumen 1 APOA1
nuclear matrix 2 ANXA2, S100A10
axon terminus 1 SNCA
extrinsic component of membrane 1 PRNP
endocytic vesicle 1 APOA1
Schmidt-Lanterman incisure 1 ANXA2
Secreted, extracellular exosome 1 ANXA1
azurophil granule lumen 1 ANXA2
immunological synapse 1 PRKCQ
aggresome 1 PRKCQ
calyx of Held 1 KCNA3
vesicle membrane 2 ANXA1, ANXA2
Lateral cell membrane 1 ANXA1
[Isoform 1]: Cell membrane 2 ATRN, KCNA3
spherical high-density lipoprotein particle 1 APOA1
Secreted, extracellular space, extracellular matrix, basement membrane 1 ANXA2
endocytic vesicle lumen 1 APOA1
GTPase complex 1 HRAS
transport vesicle membrane 1 AQP2
Cytoplasmic vesicle, secretory vesicle lumen 1 ANXA1
inclusion body 2 PRNP, SNCA
alphav-beta3 integrin-PKCalpha complex 1 PRKCA
AnxA2-p11 complex 2 ANXA2, S100A10
myelin sheath adaxonal region 1 ANXA2
PCSK9-AnxA2 complex 1 ANXA2
serine-type peptidase complex 1 F3
[Isoform 3]: Cytoplasm, perinuclear region 1 KCNA3
lumenal side of membrane 1 AQP2


文献列表

  • Ruitao Jin, Sitong He, Katrina A Black, Oliver B Clarke, Di Wu, Jani R Bolla, Paul Johnson, Agalya Periasamy, Ahmad Wardak, Peter Czabotar, Peter M Colman, Carol V Robinson, Derek Laver, Brian J Smith, Jacqueline M Gulbis. Ion currents through Kir potassium channels are gated by anionic lipids. Nature communications. 2022 01; 13(1):490. doi: 10.1038/s41467-022-28148-4. [PMID: 35079013]
  • Sandra Rocha, Ranjeet Kumar, Bengt Nordén, Pernilla Wittung-Stafshede. Orientation of α-Synuclein at Negatively Charged Lipid Vesicles: Linear Dichroism Reveals Time-Dependent Changes in Helix Binding Mode. Journal of the American Chemical Society. 2021 11; 143(45):18899-18906. doi: 10.1021/jacs.1c05344. [PMID: 34748321]
  • Richelle D Björvang, Jasmin Hassan, Maria Stefopoulou, Kristina Gemzell-Danielsson, Matteo Pedrelli, Hannu Kiviranta, Panu Rantakokko, Päivi Ruokojärvi, Christian H Lindh, Ganesh Acharya, Pauliina Damdimopoulou. Persistent organic pollutants and the size of ovarian reserve in reproductive-aged women. Environment international. 2021 10; 155(?):106589. doi: 10.1016/j.envint.2021.106589. [PMID: 33945905]
  • Aml A Alnaas, Abena Watson-Siriboe, Sherleen Tran, Mikias Negussie, Jack A Henderson, J Ryan Osterberg, Nara L Chon, Beckston M Harrott, Julianna Oviedo, Tatyana Lyakhova, Cole Michel, Nichole Reisdorph, Richard Reisdorph, Colin T Shearn, Hai Lin, Jefferson D Knight. Multivalent lipid targeting by the calcium-independent C2A domain of synaptotagmin-like protein 4/granuphilin. The Journal of biological chemistry. 2021 Jan; 296(?):100159. doi: 10.1074/jbc.ra120.014618. [PMID: 33277360]
  • Samantha Schrecke, Yun Zhu, Jacob W McCabe, Mariah Bartz, Charles Packianathan, Minglei Zhao, Ming Zhou, David Russell, Arthur Laganowsky. Selective regulation of human TRAAK channels by biologically active phospholipids. Nature chemical biology. 2021 01; 17(1):89-95. doi: 10.1038/s41589-020-00659-5. [PMID: 32989299]
  • P Gehan, S Kulifaj, P Soule, J B Bodin, M Amoura, A Walrant, S Sagan, A R Thiam, K Ngo, V Vivier, S Cribier, N Rodriguez. Penetratin translocation mechanism through asymmetric droplet interface bilayers. Biochimica et biophysica acta. Biomembranes. 2020 11; 1862(11):183415. doi: 10.1016/j.bbamem.2020.183415. [PMID: 32710854]
  • Paulo Roberto Dores-Silva, David M Cauvi, Amanda L S Coto, Vanessa T R Kiraly, Júlio C Borges, Antonio De Maio. Interaction of HSPA5 (Grp78, BIP) with negatively charged phospholipid membranes via oligomerization involving the N-terminal end domain. Cell stress & chaperones. 2020 11; 25(6):979-991. doi: 10.1007/s12192-020-01134-9. [PMID: 32725381]
  • Xubo Lin, Alemayehu A Gorfe. Transmembrane potential of physiologically relevant model membranes: Effects of membrane asymmetry. The Journal of chemical physics. 2020 Sep; 153(10):105103. doi: 10.1063/5.0018303. [PMID: 32933265]
  • Lisanna Sinisalu, Partho Sen, Samira Salihović, Suvi M Virtanen, Heikki Hyöty, Jorma Ilonen, Jorma Toppari, Riitta Veijola, Matej Orešič, Mikael Knip, Tuulia Hyötyläinen. Early-life exposure to perfluorinated alkyl substances modulates lipid metabolism in progression to celiac disease. Environmental research. 2020 09; 188(?):109864. doi: 10.1016/j.envres.2020.109864. [PMID: 32846648]
  • Larissa Smulders, Amanda J Daniels, Caroline B Plescia, Devon Berger, Robert V Stahelin, Nikolas Nikolaidis. Characterization of the Relationship between the Chaperone and Lipid-Binding Functions of the 70-kDa Heat-Shock Protein, HspA1A. International journal of molecular sciences. 2020 Aug; 21(17):. doi: 10.3390/ijms21175995. [PMID: 32825419]
  • Maninder Singh, Vikash Kumar, Kamakshi Sikka, Ravi Thakur, Munesh Kumar Harioudh, Durga Prasad Mishra, Jimut Kanti Ghosh, Mohammad Imran Siddiqi. Computational Design of Biologically Active Anticancer Peptides and Their Interactions with Heterogeneous POPC/POPS Lipid Membranes. Journal of chemical information and modeling. 2020 01; 60(1):332-341. doi: 10.1021/acs.jcim.9b00348. [PMID: 31880450]
  • Josef Melcr, Tiago M Ferreira, Pavel Jungwirth, O H Samuli Ollila. Improved Cation Binding to Lipid Bilayers with Negatively Charged POPS by Effective Inclusion of Electronic Polarization. Journal of chemical theory and computation. 2020 Jan; 16(1):738-748. doi: 10.1021/acs.jctc.9b00824. [PMID: 31762275]
  • Alessandra Luchini, Frederik Grønbæk Tidemand, Nicolai Tidemand Johansen, Mario Campana, Javier Sotres, Michael Ploug, Marité Cárdenas, Lise Arleth. Peptide Disc Mediated Control of Membrane Protein Orientation in Supported Lipid Bilayers for Surface-Sensitive Investigations. Analytical chemistry. 2020 01; 92(1):1081-1088. doi: 10.1021/acs.analchem.9b04125. [PMID: 31769649]
  • Li-Ping Gao, Hai-Chao Chen, Ze-Lin Ma, An-Di Chen, Hong-Li Du, Jie Yin, Yu-Hong Jing. Fibrillation of human islet amyloid polypeptide and its toxicity to pancreatic β-cells under lipid environment. Biochimica et biophysica acta. General subjects. 2020 01; 1864(1):129422. doi: 10.1016/j.bbagen.2019.129422. [PMID: 31491457]
  • Shailendra S Rathore, Yinghui Liu, Haijia Yu, Chun Wan, MyeongSeon Lee, Qian Yin, Michael H B Stowell, Jingshi Shen. Intracellular Vesicle Fusion Requires a Membrane-Destabilizing Peptide Located at the Juxtamembrane Region of the v-SNARE. Cell reports. 2019 12; 29(13):4583-4592.e3. doi: 10.1016/j.celrep.2019.11.107. [PMID: 31875562]
  • Antti H Rantamäki, Wen Chen, Paulus Hyväri, Jussi Helminen, Gabriel Partl, Alistair W T King, Susanne K Wiedmer. Interactions of Ionic Liquids and Spirocyclic Compounds with Liposome Model Membranes. A Steady-State Fluorescence Anisotropy Study. Scientific reports. 2019 12; 9(1):18349. doi: 10.1038/s41598-019-53893-w. [PMID: 31797938]
  • Jianrong Sang, Ketav Kulkarni, Gabrielle M Watson, Xiuquan Ma, David J Craik, Sónia T Henriques, Aaron G Poth, Aurélie H Benfield, Jacqueline A Wilce. Evaluation of Cyclic Peptide Inhibitors of the Grb7 Breast Cancer Target: Small Change in Cargo Results in Large Change in Cellular Activity. Molecules (Basel, Switzerland). 2019 Oct; 24(20):. doi: 10.3390/molecules24203739. [PMID: 31627265]
  • Zhengjian Lv, Mohtadin Hashemi, Siddhartha Banerjee, Karen Zagorski, Jean-Christophe Rochet, Yuri L Lyubchenko. Assembly of α-synuclein aggregates on phospholipid bilayers. Biochimica et biophysica acta. Proteins and proteomics. 2019 09; 1867(9):802-812. doi: 10.1016/j.bbapap.2019.06.006. [PMID: 31226488]
  • Liang Xu, Shayon Bhattacharya, Damien Thompson. On the ubiquity of helical α-synuclein tetramers. Physical chemistry chemical physics : PCCP. 2019 Jun; 21(22):12036-12043. doi: 10.1039/c9cp02464f. [PMID: 31135803]
  • Caterina Ricci, Marco Maccarini, Peter Falus, Fabio Librizzi, Maria Rosalia Mangione, Oscar Moran, Maria Grazia Ortore, Ralf Schweins, Silvia Vilasi, Rita Carrotta. Amyloid β-Peptide Interaction with Membranes: Can Chaperones Change the Fate?. The journal of physical chemistry. B. 2019 01; 123(3):631-638. doi: 10.1021/acs.jpcb.8b11719. [PMID: 30569709]
  • José Carlos Bozelli, William Jennings, Stephanie Black, Yu Heng Hou, Darius Lameire, Preet Chatha, Tomohiro Kimura, Bob Berno, Adree Khondker, Maikel C Rheinstädter, Richard M Epand. Membrane curvature allosterically regulates the phosphatidylinositol cycle, controlling its rate and acyl-chain composition of its lipid intermediates. The Journal of biological chemistry. 2018 11; 293(46):17780-17791. doi: 10.1074/jbc.ra118.005293. [PMID: 30237168]
  • Chris Neale, Angel E García. Methionine 170 is an Environmentally Sensitive Membrane Anchor in the Disordered HVR of K-Ras4B. The journal of physical chemistry. B. 2018 11; 122(44):10086-10096. doi: 10.1021/acs.jpcb.8b07919. [PMID: 30351122]
  • Mason L Valentine, Alfredo E Cardenas, Ron Elber, Carlos R Baiz. Physiological Calcium Concentrations Slow Dynamics at the Lipid-Water Interface. Biophysical journal. 2018 10; 115(8):1541-1551. doi: 10.1016/j.bpj.2018.08.044. [PMID: 30269885]
  • Xubo Lin, Hongyin Wang, Zhichao Lou, Meng Cao, Zuoheng Zhang, Ning Gu. Roles of PIP2 in the membrane binding of MIM I-BAR: insights from molecular dynamics simulations. FEBS letters. 2018 08; 592(15):2533-2542. doi: 10.1002/1873-3468.13186. [PMID: 29995324]
  • Nicole Heitzig, Alexander Kühnl, David Grill, Katharina Ludewig, Sebastian Schloer, Hans-Joachim Galla, Thomas Grewal, Volker Gerke, Ursula Rescher. Cooperative binding promotes demand-driven recruitment of AnxA8 to cholesterol-containing membranes. Biochimica et biophysica acta. Molecular and cell biology of lipids. 2018 Apr; 1863(4):349-358. doi: 10.1016/j.bbalip.2018.01.001. [PMID: 29306076]
  • Tatsuro Goda, Yuji Miyahara. Specific binding of human C-reactive protein towards supported monolayers of binary and engineered phospholipids. Colloids and surfaces. B, Biointerfaces. 2018 Jan; 161(?):662-669. doi: 10.1016/j.colsurfb.2017.11.036. [PMID: 29172154]
  • Milka Doktorova, Frederick A Heberle, Richard L Kingston, George Khelashvili, Michel A Cuendet, Yi Wen, John Katsaras, Gerald W Feigenson, Volker M Vogt, Robert A Dick. Cholesterol Promotes Protein Binding by Affecting Membrane Electrostatics and Solvation Properties. Biophysical journal. 2017 Nov; 113(9):2004-2015. doi: 10.1016/j.bpj.2017.08.055. [PMID: 29117524]
  • Helen Y Fan, Heiko Heerklotz. Digitonin does not flip across cholesterol-poor membranes. Journal of colloid and interface science. 2017 Oct; 504(?):283-293. doi: 10.1016/j.jcis.2017.05.034. [PMID: 28551523]
  • Jeevan B Gc, Bernard S Gerstman, Prem P Chapagain. Membrane association and localization dynamics of the Ebola virus matrix protein VP40. Biochimica et biophysica acta. Biomembranes. 2017 Oct; 1859(10):2012-2020. doi: 10.1016/j.bbamem.2017.07.007. [PMID: 28711356]
  • Ellen M Muehl, Joshua M Gajsiewicz, Sara M Medfisch, Zachary S B Wiersma, James H Morrissey, Ryan C Bailey. Multiplexed silicon photonic sensor arrays enable facile characterization of coagulation protein binding to nanodiscs with variable lipid content. The Journal of biological chemistry. 2017 09; 292(39):16249-16256. doi: 10.1074/jbc.m117.800938. [PMID: 28801460]
  • Justine Wolf, Christopher Aisenbrey, Nicole Harmouche, Jesus Raya, Philippe Bertani, Natalia Voievoda, Regine Süss, Burkhard Bechinger. pH-Dependent Membrane Interactions of the Histidine-Rich Cell-Penetrating Peptide LAH4-L1. Biophysical journal. 2017 Sep; 113(6):1290-1300. doi: 10.1016/j.bpj.2017.06.053. [PMID: 28734478]
  • Rafal Zdanowicz, Alex Kreutzberger, Binyong Liang, Volker Kiessling, Lukas K Tamm, David S Cafiso. Complexin Binding to Membranes and Acceptor t-SNAREs Explains Its Clamping Effect on Fusion. Biophysical journal. 2017 Sep; 113(6):1235-1250. doi: 10.1016/j.bpj.2017.04.002. [PMID: 28456331]
  • Antreas C Kalli, Tomasz Rog, Ilpo Vattulainen, Iain D Campbell, Mark S P Sansom. The Integrin Receptor in Biologically Relevant Bilayers: Insights from Molecular Dynamics Simulations. The Journal of membrane biology. 2017 08; 250(4):337-351. doi: 10.1007/s00232-016-9908-z. [PMID: 27465729]
  • Eileen Edler, Eric Schulze, Matthias Stein. Membrane localization and dynamics of geranylgeranylated Rab5 hypervariable region. Biochimica et biophysica acta. Biomembranes. 2017 Aug; 1859(8):1335-1349. doi: 10.1016/j.bbamem.2017.04.021. [PMID: 28455099]
  • Shruti Mukherjee, Rajiv K Kar, Ravi Prakash Reddy Nanga, Kamal H Mroue, Ayyalusamy Ramamoorthy, Anirban Bhunia. Accelerated molecular dynamics simulation analysis of MSI-594 in a lipid bilayer. Physical chemistry chemical physics : PCCP. 2017 Jul; 19(29):19289-19299. doi: 10.1039/c7cp01941f. [PMID: 28702543]
  • Elaheh Jamasbi, Frances Separovic, Mohammed Akhter Hossain, Giuseppe Donato Ciccotosto. Phosphorylation of a full length amyloid-β peptide modulates its amyloid aggregation, cell binding and neurotoxic properties. Molecular bioSystems. 2017 Jul; 13(8):1545-1551. doi: 10.1039/c7mb00249a. [PMID: 28642958]
  • Maria A Soria, Silvia A Cervantes, Thalia H Bajakian, Ansgar B Siemer. The Functional Amyloid Orb2A Binds to Lipid Membranes. Biophysical journal. 2017 Jul; 113(1):37-47. doi: 10.1016/j.bpj.2017.05.039. [PMID: 28700922]
  • Dayane S Alvares, João Ruggiero Neto, Ernesto E Ambroggio. Phosphatidylserine lipids and membrane order precisely regulate the activity of Polybia-MP1 peptide. Biochimica et biophysica acta. Biomembranes. 2017 Jun; 1859(6):1067-1074. doi: 10.1016/j.bbamem.2017.03.002. [PMID: 28274844]
  • Kaveesha J Wijesinghe, Sarah Urata, Nisha Bhattarai, Edgar E Kooijman, Bernard S Gerstman, Prem P Chapagain, Sheng Li, Robert V Stahelin. Detection of lipid-induced structural changes of the Marburg virus matrix protein VP40 using hydrogen/deuterium exchange-mass spectrometry. The Journal of biological chemistry. 2017 04; 292(15):6108-6122. doi: 10.1074/jbc.m116.758300. [PMID: 28167534]
  • Tao Ni, Antreas C Kalli, Fiona B Naughton, Luke A Yates, Omar Naneh, Mirijam Kozorog, Gregor Anderluh, Mark S P Sansom, Robert J C Gilbert. Structure and lipid-binding properties of the kindlin-3 pleckstrin homology domain. The Biochemical journal. 2017 02; 474(4):539-556. doi: 10.1042/bcj20160791. [PMID: 27974389]
  • Patrick Drücker, Andreas Rühling, David Grill, Da Wang, Annette Draeger, Volker Gerke, Frank Glorius, Hans-Joachim Galla. Imidazolium Salts Mimicking the Structure of Natural Lipids Exploit Remarkable Properties Forming Lamellar Phases and Giant Vesicles. Langmuir : the ACS journal of surfaces and colloids. 2017 02; 33(6):1333-1342. doi: 10.1021/acs.langmuir.6b03182. [PMID: 27935708]
  • Xiaoxue Zhang, Johnna R St Clair, Erwin London, Daniel P Raleigh. Islet Amyloid Polypeptide Membrane Interactions: Effects of Membrane Composition. Biochemistry. 2017 Jan; 56(2):376-390. doi: 10.1021/acs.biochem.6b01016. [PMID: 28054763]
  • Davit Hakobyan, Volker Gerke, Andreas Heuer. Modeling of annexin A2-Membrane interactions by molecular dynamics simulations. PloS one. 2017; 12(9):e0185440. doi: 10.1371/journal.pone.0185440. [PMID: 28937994]
  • Kari Kusler, Samuel O Odoh, Alexey Silakov, Matthew F Poyton, Saranya Pullanchery, Paul S Cremer, Laura Gagliardi. What Is the Preferred Conformation of Phosphatidylserine-Copper(II) Complexes? A Combined Theoretical and Experimental Investigation. The journal of physical chemistry. B. 2016 12; 120(50):12883-12889. doi: 10.1021/acs.jpcb.6b10675. [PMID: 27957849]
  • Himanshu Chaudhary, Aditya Iyer, Vinod Subramaniam, Mireille M A E Claessens. α-Synuclein Oligomers Stabilize Pre-Existing Defects in Supported Bilayers and Propagate Membrane Damage in a Fractal-Like Pattern. Langmuir : the ACS journal of surfaces and colloids. 2016 11; 32(45):11827-11836. doi: 10.1021/acs.langmuir.6b02572. [PMID: 27766878]
  • Jan K Marzinek, Daniel A Holdbrook, Roland G Huber, Chandra Verma, Peter J Bond. Pushing the Envelope: Dengue Viral Membrane Coaxed into Shape by Molecular Simulations. Structure (London, England : 1993). 2016 08; 24(8):1410-1420. doi: 10.1016/j.str.2016.05.014. [PMID: 27396828]
  • Ludovico Migliolo, Mário R Felício, Marlon H Cardoso, Osmar N Silva, Mary-Ann E Xavier, Diego O Nolasco, Adeliana Silva de Oliveira, Ignasi Roca-Subira, Jordi Vila Estape, Leandro D Teixeira, Sonia M Freitas, Anselmo J Otero-Gonzalez, Sónia Gonçalves, Nuno C Santos, Octavio L Franco. Structural and functional evaluation of the palindromic alanine-rich antimicrobial peptide Pa-MAP2. Biochimica et biophysica acta. 2016 Jul; 1858(7 Pt A):1488-98. doi: 10.1016/j.bbamem.2016.04.003. [PMID: 27063608]
  • Victor Lopez, David M Cauvi, Nelson Arispe, Antonio De Maio. Bacterial Hsp70 (DnaK) and mammalian Hsp70 interact differently with lipid membranes. Cell stress & chaperones. 2016 07; 21(4):609-16. doi: 10.1007/s12192-016-0685-5. [PMID: 27075190]
  • Sung-Tae Yang, Volker Kiessling, Lukas K Tamm. Line tension at lipid phase boundaries as driving force for HIV fusion peptide-mediated fusion. Nature communications. 2016 Apr; 7(?):11401. doi: 10.1038/ncomms11401. [PMID: 27113279]
  • Fiona B Naughton, Antreas C Kalli, Mark S P Sansom. Association of Peripheral Membrane Proteins with Membranes: Free Energy of Binding of GRP1 PH Domain with Phosphatidylinositol Phosphate-Containing Model Bilayers. The journal of physical chemistry letters. 2016 Apr; 7(7):1219-24. doi: 10.1021/acs.jpclett.6b00153. [PMID: 26977543]
  • Rui Hu, Jiajie Diao, Ji Li, Zhipeng Tang, Xiaoqing Li, Jeremy Leitz, Jiangang Long, Jiankang Liu, Dapeng Yu, Qing Zhao. Intrinsic and membrane-facilitated α-synuclein oligomerization revealed by label-free detection through solid-state nanopores. Scientific reports. 2016 Feb; 6(?):20776. doi: 10.1038/srep20776. [PMID: 26865505]
  • Jumin Lee, Xi Cheng, Jason M Swails, Min Sun Yeom, Peter K Eastman, Justin A Lemkul, Shuai Wei, Joshua Buckner, Jong Cheol Jeong, Yifei Qi, Sunhwan Jo, Vijay S Pande, David A Case, Charles L Brooks, Alexander D MacKerell, Jeffery B Klauda, Wonpil Im. CHARMM-GUI Input Generator for NAMD, GROMACS, AMBER, OpenMM, and CHARMM/OpenMM Simulations Using the CHARMM36 Additive Force Field. Journal of chemical theory and computation. 2016 Jan; 12(1):405-13. doi: 10.1021/acs.jctc.5b00935. [PMID: 26631602]
  • Willy Nerdal, Torill Regine Sandvik Nilsen, Signe Steinkopf. CoenzymeQ10 localizations in model membranes. A Langmuir monolayer study. Biophysical chemistry. 2015 Dec; 207(?):74-81. doi: 10.1016/j.bpc.2015.09.003. [PMID: 26408828]
  • Xiao Cong, Matthew F Poyton, Alexis J Baxter, Saranya Pullanchery, Paul S Cremer. Unquenchable Surface Potential Dramatically Enhances Cu(2+) Binding to Phosphatidylserine Lipids. Journal of the American Chemical Society. 2015 Jun; 137(24):7785-92. doi: 10.1021/jacs.5b03313. [PMID: 26065920]
  • Gitte W Haxholm, Louise F Nikolajsen, Johan G Olsen, Jacob Fredsted, Flemming H Larsen, Vincent Goffin, Stine F Pedersen, Andrew J Brooks, Michael J Waters, Birthe B Kragelund. Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes. The Biochemical journal. 2015 Jun; 468(3):495-506. doi: 10.1042/bj20141243. [PMID: 25846210]
  • Drew Marquardt, Norbert Kučerka, John Katsaras, Thad A Harroun. α-Tocopherol's Location in Membranes Is Not Affected by Their Composition. Langmuir : the ACS journal of surfaces and colloids. 2015 Apr; 31(15):4464-72. doi: 10.1021/la502605c. [PMID: 25317847]
  • Thomas Schmidt, Jae-Eun Suk, Feng Ye, Alan J Situ, Parichita Mazumder, Mark H Ginsberg, Tobias S Ulmer. Annular anionic lipids stabilize the integrin αIIbβ3 transmembrane complex. The Journal of biological chemistry. 2015 Mar; 290(13):8283-93. doi: 10.1074/jbc.m114.623504. [PMID: 25632962]
  • Martin Göse, Paula Pescador, Uta Reibetanz. Design of a homogeneous multifunctional supported lipid membrane on layer-by-layer coated microcarriers. Biomacromolecules. 2015 Mar; 16(3):757-68. doi: 10.1021/bm5016688. [PMID: 25642843]
  • Joseph C Fogarty, Mihir Arjunwadkar, Sagar A Pandit, Jianjun Pan. Atomically detailed lipid bilayer models for the interpretation of small angle neutron and X-ray scattering data. Biochimica et biophysica acta. 2015 Feb; 1848(2):662-72. doi: 10.1016/j.bbamem.2014.10.041. [PMID: 25448879]
  • A Farrotti, G Bocchinfuso, A Palleschi, N Rosato, E S Salnikov, N Voievoda, B Bechinger, L Stella. Molecular dynamics methods to predict peptide locations in membranes: LAH4 as a stringent test case. Biochimica et biophysica acta. 2015 Feb; 1848(2):581-92. doi: 10.1016/j.bbamem.2014.11.002. [PMID: 25445672]
  • Sumit Garg, Francisco Castro-Roman, Lionel Porcar, Paul Butler, Pedro Jesus Bautista, Natalie Krzyzanowski, Ursula Perez-Salas. Cholesterol solubility limit in lipid membranes probed by small angle neutron scattering and MD simulations. Soft matter. 2014 Dec; 10(46):9313-7. doi: 10.1039/c4sm01219d. [PMID: 25338228]
  • Marianna Yanez Arteta, Marie-Louise Ainalem, Lionel Porcar, Anne Martel, Helena Coker, Dan Lundberg, Debby P Chang, Olaf Soltwedel, Robert Barker, Tommy Nylander. Interactions of PAMAM dendrimers with negatively charged model biomembranes. The journal of physical chemistry. B. 2014 Nov; 118(45):12892-906. doi: 10.1021/jp506510s. [PMID: 25310456]
  • Jianjun Pan, Xiaolin Cheng, Luca Monticelli, Frederick A Heberle, Norbert Kučerka, D Peter Tieleman, John Katsaras. The molecular structure of a phosphatidylserine bilayer determined by scattering and molecular dynamics simulations. Soft matter. 2014 Jun; 10(21):3716-25. doi: 10.1039/c4sm00066h. [PMID: 24807693]
  • Zhuxi Chen, Yanyan Mao, Jing Yang, Tao Zhang, Lifen Zhao, Kunqian Yu, Mingyue Zheng, Hualiang Jiang, Huaiyu Yang. Characterizing the binding of annexin V to a lipid bilayer using molecular dynamics simulations. Proteins. 2014 Feb; 82(2):312-22. doi: 10.1002/prot.24389. [PMID: 23934928]
  • Poornima Budime Santhosh, Aljaž Velikonja, Šarka Perutkova, Ekaterina Gongadze, Mukta Kulkarni, Julia Genova, Kristina Eleršič, Aleš Iglič, Veronika Kralj-Iglič, Nataša Poklar Ulrih. Influence of nanoparticle-membrane electrostatic interactions on membrane fluidity and bending elasticity. Chemistry and physics of lipids. 2014 Feb; 178(?):52-62. doi: 10.1016/j.chemphyslip.2013.11.009. [PMID: 24309194]
  • Claudio Canale, Silvia Seghezza, Silvia Vilasi, Rita Carrotta, Donatella Bulone, Alberto Diaspro, Pier Luigi San Biagio, Silvia Dante. Different effects of Alzheimer's peptide Aβ(1-40) oligomers and fibrils on supported lipid membranes. Biophysical chemistry. 2013 Dec; 182(?):23-9. doi: 10.1016/j.bpc.2013.07.010. [PMID: 23998637]
  • Mario Vazdar, Erik Wernersson, Morteza Khabiri, Lukasz Cwiklik, Piotr Jurkiewicz, Martin Hof, Ella Mann, Sofiya Kolusheva, Raz Jelinek, Pavel Jungwirth. Aggregation of oligoarginines at phospholipid membranes: molecular dynamics simulations, time-dependent fluorescence shift, and biomimetic colorimetric assays. The journal of physical chemistry. B. 2013 Oct; 117(39):11530-40. doi: 10.1021/jp405451e. [PMID: 24020922]
  • Jonas Wietek, Ivan Haralampiev, Aouefa Amoussouvi, Andreas Herrmann, Martin Stöckl. Membrane bound α-synuclein is fully embedded in the lipid bilayer while segments with higher flexibility remain. FEBS letters. 2013 Aug; 587(16):2572-7. doi: 10.1016/j.febslet.2013.06.034. [PMID: 23831067]
  • Michael Mell, Lara H Moleiro, Yvonne Hertle, Peter Fouquet, Ralf Schweins, Iván López-Montero, Thomas Hellweg, Francisco Monroy. Bending stiffness of biological membranes: what can be measured by neutron spin echo?. The European physical journal. E, Soft matter. 2013 Jul; 36(7):75. doi: 10.1140/epje/i2013-13075-2. [PMID: 23852577]
  • Jobin Varkey, Naoko Mizuno, Balachandra G Hegde, Naiqian Cheng, Alasdair C Steven, Ralf Langen. α-Synuclein oligomers with broken helical conformation form lipoprotein nanoparticles. The Journal of biological chemistry. 2013 Jun; 288(24):17620-30. doi: 10.1074/jbc.m113.476697. [PMID: 23609437]
  • Masakazu Miyazaki, Yoko Tajima, Yasushi Ishihama, Tetsurou Handa, Minoru Nakano. Effect of phospholipid composition on discoidal HDL formation. Biochimica et biophysica acta. 2013 May; 1828(5):1340-6. doi: 10.1016/j.bbamem.2013.01.012. [PMID: 23357357]
  • Shih Lin Goh, Jonathan J Amazon, Gerald W Feigenson. Toward a better raft model: modulated phases in the four-component bilayer, DSPC/DOPC/POPC/CHOL. Biophysical journal. 2013 Feb; 104(4):853-62. doi: 10.1016/j.bpj.2013.01.003. [PMID: 23442964]
  • Volker Knecht, Benjamin Klasczyk. Specific binding of chloride ions to lipid vesicles and implications at molecular scale. Biophysical journal. 2013 Feb; 104(4):818-24. doi: 10.1016/j.bpj.2012.12.056. [PMID: 23442960]
  • Matthias Michalek, Evgeniy S Salnikov, Sebastiaan Werten, Burkhard Bechinger. Membrane interactions of the amphipathic amino terminus of huntingtin. Biochemistry. 2013 Feb; 52(5):847-58. doi: 10.1021/bi301325q. [PMID: 23305455]
  • Alexandre Therrien, Puttaswamy Manjunath, Michel Lafleur. Chemical and physical requirements for lipid extraction by bovine binder of sperm BSP1. Biochimica et biophysica acta. 2013 Feb; 1828(2):543-51. doi: 10.1016/j.bbamem.2012.08.020. [PMID: 22960042]
  • Michele F M Sciacca, Danilo Milardi, Grazia M L Messina, Giovanni Marletta, Jeffrey R Brender, Ayyalusamy Ramamoorthy, Carmelo La Rosa. Cations as switches of amyloid-mediated membrane disruption mechanisms: calcium and IAPP. Biophysical journal. 2013 Jan; 104(1):173-84. doi: 10.1016/j.bpj.2012.11.3811. [PMID: 23332070]
  • Angel Pérez-Lara, Antonio L Egea-Jiménez, Alessio Ausili, Senena Corbalán-García, Juan C Gómez-Fernández. The membrane binding kinetics of full-length PKCα is determined by membrane lipid composition. Biochimica et biophysica acta. 2012 Nov; 1821(11):1434-42. doi: 10.1016/j.bbalip.2012.06.012. [PMID: 22842589]
  • C J Lee, S Wu, L J Bartolotti, L G Pedersen. Molecular dynamic simulations of the binary complex of human tissue factor (TF(1-242) ) and factor VIIa (TF(1-242) /FVIIa) on a 4:1 POPC/POPS lipid bilayer. Journal of thrombosis and haemostasis : JTH. 2012 Nov; 10(11):2402-5. doi: 10.1111/j.1538-7836.2012.04920.x. [PMID: 22967237]
  • Signe Steinkopf, Linda Hanekam, Marit Schaathun, Adnan Budnjo, Bengt Erik Haug, Willy Nerdal. Interaction of local anaesthetic articaine enantiomers with brain lipids: a Langmuir monolayer study. European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences. 2012 Sep; 47(2):394-401. doi: 10.1016/j.ejps.2012.06.010. [PMID: 22750081]
  • Piotr Jurkiewicz, Lukasz Cwiklik, Alžběta Vojtíšková, Pavel Jungwirth, Martin Hof. Structure, dynamics, and hydration of POPC/POPS bilayers suspended in NaCl, KCl, and CsCl solutions. Biochimica et biophysica acta. 2012 Mar; 1818(3):609-16. doi: 10.1016/j.bbamem.2011.11.033. [PMID: 22155683]
  • Svetlana V Oard. Deciphering a mechanism of membrane permeabilization by α-hordothionin peptide. Biochimica et biophysica acta. 2011 Jun; 1808(6):1737-45. doi: 10.1016/j.bbamem.2011.02.003. [PMID: 21315063]
  • Veronica Beswick, Adriana Isvoran, Pierre Nédellec, Alain Sanson, Nadège Jamin. Membrane interface composition drives the structure and the tilt of the single transmembrane helix protein PMP1: MD studies. Biophysical journal. 2011 Apr; 100(7):1660-7. doi: 10.1016/j.bpj.2011.02.002. [PMID: 21463579]
  • Chen Wan, Volker Kiessling, David S Cafiso, Lukas K Tamm. Partitioning of synaptotagmin I C2 domains between liquid-ordered and liquid-disordered inner leaflet lipid phases. Biochemistry. 2011 Apr; 50(13):2478-85. doi: 10.1021/bi101864k. [PMID: 21322640]
  • Marija Raguz, Laxman Mainali, Justyna Widomska, Witold K Subczynski. The immiscible cholesterol bilayer domain exists as an integral part of phospholipid bilayer membranes. Biochimica et biophysica acta. 2011 Apr; 1808(4):1072-80. doi: 10.1016/j.bbamem.2010.12.019. [PMID: 21192917]
  • Shoshannah L Roth, Gary R Whittaker. Promotion of vesicular stomatitis virus fusion by the endosome-specific phospholipid bis(monoacylglycero)phosphate (BMP). FEBS letters. 2011 Mar; 585(6):865-9. doi: 10.1016/j.febslet.2011.02.015. [PMID: 21333650]
  • Alessio Ausili, Senena Corbalán-García, Juan C Gómez-Fernández, Derek Marsh. Membrane docking of the C2 domain from protein kinase Cα as seen by polarized ATR-IR. The role of PIP₂. Biochimica et biophysica acta. 2011 Mar; 1808(3):684-95. doi: 10.1016/j.bbamem.2010.11.035. [PMID: 21144818]
  • Chunbo Yuan, Maohui Chen, Douglas F Covey, Linda J Johnston, Steven N Treistman. Cholesterol tuning of BK ethanol response is enantioselective, and is a function of accompanying lipids. PloS one. 2011; 6(11):e27572. doi: 10.1371/journal.pone.0027572. [PMID: 22140451]
  • Janice Lin, John Szymanski, Peter C Searson, Kalina Hristova. Electrically addressable, biologically relevant surface-supported bilayers. Langmuir : the ACS journal of surfaces and colloids. 2010 Jul; 26(14):12054-9. doi: 10.1021/la101084b. [PMID: 20446710]
  • Arnaud Marquette, Bernard Lorber, Burkhard Bechinger. Reversible liposome association induced by LAH4: a peptide with potent antimicrobial and nucleic acid transfection activities. Biophysical journal. 2010 Jun; 98(11):2544-53. doi: 10.1016/j.bpj.2010.02.042. [PMID: 20513398]
  • Philip J Robinson, Teresa J T Pinheiro. Phospholipid composition of membranes directs prions down alternative aggregation pathways. Biophysical journal. 2010 Apr; 98(8):1520-8. doi: 10.1016/j.bpj.2009.12.4304. [PMID: 20409471]
  • Kanika Vats, Kristofer Knutson, Anne Hinderliter, Erin D Sheets. Peripheral protein organization and its influence on lipid diffusion in biomimetic membranes. ACS chemical biology. 2010 Apr; 5(4):393-403. doi: 10.1021/cb900303s. [PMID: 20175560]
  • Magnus Jensen, Morten Bjerring, Niels Chr Nielsen, Willy Nerdal. Cisplatin interaction with phosphatidylserine bilayer studied by solid-state NMR spectroscopy. Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 2010 Feb; 15(2):213-23. doi: 10.1007/s00775-009-0586-5. [PMID: 19768472]
  • Sunhwan Jo, Joseph B Lim, Jeffery B Klauda, Wonpil Im. CHARMM-GUI Membrane Builder for mixed bilayers and its application to yeast membranes. Biophysical journal. 2009 Jul; 97(1):50-8. doi: 10.1016/j.bpj.2009.04.013. [PMID: 19580743]
  • Parijat Sengupta, Eran Bosis, Esther Nachliel, Menachem Gutman, Steven O Smith, Gyöngyi Mihályné, Irina Zaitseva, Stuart McLaughlin. EGFR juxtamembrane domain, membranes, and calmodulin: kinetics of their interaction. Biophysical journal. 2009 Jun; 96(12):4887-95. doi: 10.1016/j.bpj.2009.03.027. [PMID: 19527647]
  • Robert Vácha, Max L Berkowitz, Pavel Jungwirth. Molecular model of a cell plasma membrane with an asymmetric multicomponent composition: water permeation and ion effects. Biophysical journal. 2009 Jun; 96(11):4493-501. doi: 10.1016/j.bpj.2009.03.010. [PMID: 19486672]
  • Sonia Sánchez-Bautista, Senena Corbalán-García, Angel Pérez-Lara, Juan C Gómez-Fernández. A comparison of the membrane binding properties of C1B domains of PKCgamma, PKCdelta, and PKCepsilon. Biophysical journal. 2009 May; 96(9):3638-47. doi: 10.1016/j.bpj.2009.02.021. [PMID: 19413969]
  • A P Dabkowska, G Fragneto, A V Hughes, P J Quinn, M J Lawrence. Specular neutron reflectivity studies of the interaction of cytochrome c with supported phosphatidylcholine bilayers doped with phosphatidylserine. Langmuir : the ACS journal of surfaces and colloids. 2009 Apr; 25(7):4203-10. doi: 10.1021/la802926k. [PMID: 19714900]
  • Weiwei Kuo, Dawn Z Herrick, Jeffrey F Ellena, David S Cafiso. The calcium-dependent and calcium-independent membrane binding of synaptotagmin 1: two modes of C2B binding. Journal of molecular biology. 2009 Mar; 387(2):284-94. doi: 10.1016/j.jmb.2009.01.064. [PMID: 19302798]
  • Kévin Carvalho, Laurence Ramos, Christian Roy, Catherine Picart. Giant unilamellar vesicles containing phosphatidylinositol(4,5)bisphosphate: characterization and functionality. Biophysical journal. 2008 Nov; 95(9):4348-60. doi: 10.1529/biophysj.107.126912. [PMID: 18502807]