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Structure of the Integrin αIIb Transmembrane Segment

Lau, T., Dua, V., & Ulmer, T. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801748200 · Cited by 91

Cholesterol reduces pardaxin's dynamics—a barrel-stave mechanism of membrane disruption investigated by solid-state NMR

Ramamoorthy, A., Lee, D.-K., Narasimhaswamy, T., & Nanga, R. P. R. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2009.08.012 · Cited by 91

French Swimwear for Membrane Proteins

Sanders, C. R., Hoffmann, A. K., Gray, D. N., Keyes, M. H., & Ellis, C. D. (2004) · ChemBioChem · doi:10.1002/cbic.200300830 · Cited by 91

High resolution 1H nuclear magnetic resonance of a transmembrane peptide

Davis, J. H., Auger, M., & Hodges, R. S. (1995) · Biophysical Journal · doi:10.1016/s0006-3495(95)80062-7 · Cited by 90

Molecular Mechanism of Action of β-Hairpin Antimicrobial Peptide Arenicin: Oligomeric Structure in Dodecylphosphocholine Micelles and Pore Formation in Planar Lipid Bilayers

Shenkarev, Z. O., Баландин, С. В., Trunov, K. I., Paramonov, A. S., Sukhanov, S. V., Barsukov, L. I., Arseniev, A. S., & Ovchinnikova, T. V. (2011) · Biochemistry · doi:10.1021/bi200746t · Cited by 89

Tolerance to Changes in Membrane Lipid Composition as a Selected Trait of Membrane Proteins

Sanders, C. R., & Mittendorf, K. F. (2011) · Biochemistry · doi:10.1021/bi2011527 · Cited by 88

Membrane Alignment of the Pore-Forming Component TatAd of the Twin-Arginine Translocase from Bacillus subtilis Resolved by Solid-State NMR Spectroscopy

Walther, T. H., Grage, S. L., Roth, N., & Ulrich, A. S. (2010) · Journal of the American Chemical Society · doi:10.1021/ja106963s · Cited by 82

Opsin Stability and Folding: Modulation by Phospholipid Bicelles

McKibbin, C., Farmer, N. A., Jeans, C., Reeves, P. J., Khorana, H. G., Wallace, B. A., Edwards, P. C., Villa, C., & Booth, P. J. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.10.018 · Cited by 82

Monomeric structure of the cardioprotective chemokine SDF‐1/CXCL12

Veldkamp, C. T., Ziarek, J. J., Su, J., Basnet, H., Lennertz, R. C., Weiner, J. J., Peterson, F. C., Baker, J. E., & Volkman, B. F. (2009) · Protein Science · doi:10.1002/pro.167 · Cited by 81

Interactions of platelet integrin αΙΙb and β3 transmembrane domains in mammalian cell membranes and their role in integrin activation

Kim, C., Lau, T., Ulmer, T. S., & Ginsberg, M. H. (2009) · Blood · doi:10.1182/blood-2008-10-186551 · Cited by 76

Bicelles: Lipid Nanostructured Platforms with Potential Dermal Applications

Barbosa‐Barros, L., Rodríguez, G., Barba, C., Cócera, M., Rubio, L., Estelrich, J., López‐Iglesias, C., de la Maza, A., & Serrano, O. L. (2011) · Small · doi:10.1002/smll.201101545 · Cited by 76

Structure and Dynamics of the Membrane-Bound Form of Pf1 Coat Protein: Implications of Structural Rearrangement for Virus Assembly

Park, S., Marassi, F. M., Black, D., & Opella, S. J. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.06.009 · Cited by 75

Interaction of the Neuropeptide Met-Enkephalin with Zwitterionic and Negatively Charged Bicelles as Viewed by 31P and 2H Solid-State NMR

Marcotte, I., Dufourc, É. J., Ouellet, M., & Auger, M. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)74477-4 · Cited by 75

NMR of membrane proteins in solution

Tamm, L. K., & Liang, B. (2006) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2006.05.005 · Cited by 75

Insights from biophysical studies on the role of polyunsaturated fatty acids for function of G-protein coupled membrane receptors

Gawrisch, K., Soubias, O., & Mihailescu, M. (2008) · Prostaglandins Leukotrienes and Essential Fatty Acids · doi:10.1016/j.plefa.2008.09.002 · Cited by 73

Structure and dynamics of polyunsaturated hydrocarbon chains in lipid bilayers—significance for GPCR function

Gawrisch, K., & Soubias, O. (2008) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2008.02.016 · Cited by 71

Structure-Dependent Charge Density as a Determinant of Antimicrobial Activity of Peptide Analogues of Defensin

Bai, Y., Liu, S., Jiang, P., Zhou, L., Li, J., Tang, C., Verma, C. S., Mu, Y., Beuerman, R. W., & Pervushin, K. V. (2009) · Biochemistry · doi:10.1021/bi900670d · Cited by 70

Isotropic Bicelles Stabilize the Functional Form of a Small Multidrug-Resistance Pump for NMR Structural Studies

Poget, S. F., Cahill, S. M., & Girvin, M. E. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0679836 · Cited by 69

NMR solution structure and dynamics of motilin in isotropic phospholipid bicellar solution

Andersson, A., & Mäler, L. (2002) · Journal of Biomolecular NMR · doi:10.1023/a:1020902915969 · Cited by 67

Structural and thermodynamic insight into the process of “weak” dimerization of the ErbB4 transmembrane domain by solution NMR

Bocharov, E. V., Mineev, K. S., Goncharuk, M. V., & Arseniev, A. S. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2012.05.001 · Cited by 67

Fluorine—a new element in the design of membrane-active peptides

Marsh, E. N. G., Buer, B. C., & Ramamoorthy, A. (2009) · Molecular BioSystems · doi:10.1039/b909864j · Cited by 66

NMR Structure in a Membrane Environment Reveals Putative Amyloidogenic Regions of the SEVI Precursor Peptide PAP248−286

Nanga, R. P. R., Brender, J., Vivekanandan, S., Popovych, N., & Ramamoorthy, A. (2009) · Journal of the American Chemical Society · doi:10.1021/ja908170s · Cited by 65

Efficient solid-state NMR methods for measuring heteronuclear dipolar couplings in unoriented lipid membrane systems

Двинских, С. В., Castro, V., & Sandström, D. (2005) · Physical Chemistry Chemical Physics · doi:10.1039/b418131j · Cited by 63

NMR of Membrane-Associated Peptides and Proteins

Wang, G. (2008) · Current Protein and Peptide Science · doi:10.2174/138920308783565714 · Cited by 62

Interactions of Interleukin-8 with the Human Chemokine Receptor CXCR1 in Phospholipid Bilayers by NMR Spectroscopy

Park, S. H., Casagrande, F., Cho, L., Albrecht, L. V., & Opella, S. J. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.08.025 · Cited by 57

Uniting Polypeptides with Sequence-Designed Peptides: Synthesis and Assembly of Poly(γ-benzyl l -glutamate)-b-Coiled-Coil Peptide Copolymers

Marsden, H. R., Handgraaf, J., Nudelman, F., Sommerdijk, N. A. J. M., & Kros, A. (2010) · Journal of the American Chemical Society · doi:10.1021/ja909540a · Cited by 55

Orientation of the Escherichia coli Outer Membrane Protein OmpX in Phospholipid Bilayer Membranes Determined by Solid-State NMR

Mahalakshmi, R., & Marassi, F. M. (2008) · Biochemistry · doi:10.1021/bi800362b · Cited by 55

Broadband-PISEMA solid-state NMR spectroscopy

Yamamoto, K., Lee, D. K., & Ramamoorthy, A. (2005) · Chemical Physics Letters · doi:10.1016/j.cplett.2005.03.082 · Cited by 55

Bicelle‐Enabled Structural Studies on a Membrane‐Associated Cytochrome b5 by Solid‐State MAS NMR Spectroscopy

Xu, J., Dürr, U., Im, S., Gan, Z., Waskell, L. A., & Ramamoorthy, A. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200801338 · Cited by 55

Diffusion and dynamics of penetratin in different membrane mimicking media

Andersson, A., Almqvist, J., Hagn, F., & Mäler, L. (2003) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2003.11.014 · Cited by 54

Bicellar systems for in vitro percutaneous absorption of diclofenac

Rubio, L., Alonso, C., Rodríguez, G., Barbosa‐Barros, L., Coderch, L., de la Maza, A., Parra, J. L., & Serrano, O. L. (2009) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2009.11.004 · Cited by 53

Lipid dynamics in fast-tumbling bicelles with varying bilayer thickness: Effect of model transmembrane peptides

Lind, J., Nordin, J., & Mäler, L. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.07.010 · Cited by 52

NMR Solution Structure of the Mitochondrial F1β Presequence from Nicotiana plumbaginifolia

Moberg, P., Nilsson, S., Ståhl, A.-L., Eriksson, A., Glaser, E. G., & Mäler, L. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.01.006 · Cited by 52

Simultaneous Definition of High Resolution Protein Structure and Backbone Conformational Dynamics using NMR Residual Dipolar Couplings

Bouvignies, G., Markwick, P. R. L., & Blackledge, M. J. (2007) · ChemPhysChem · doi:10.1002/cphc.200700353 · Cited by 51

Disordered Proteins: Biological Membranes as Two-Dimensional Aggregation Matrices

Byström, R., Aisenbrey, C., Borowik, T., Bokvist, M., Lindström, F., Sani, M., Olofsson, A., & Gröbner, G. (2008) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-008-9033-4 · Cited by 50

Location of the Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) Effector Domain in Negatively Charged Phospholipid Bicelles

Ellena, J. F., Burnitz, M. C., & Cafiso, D. S. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)74667-0 · Cited by 48

Pardaxin Permeabilizes Vesicles More Efficiently by Pore Formation than by Disruption

Vad, B. S., Bertelsen, K., Johansen, C., Pedersen, J. M., Skrydstrup, T., Nielsen, N. C., & Otzen, D. E. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2009.08.063 · Cited by 46

Solid-State NMR Spectroscopy of Membrane-Associated Myelin Basic Protein—Conformation and Dynamics of an Immunodominant Epitope

Ahmed, M. A. M., Bamm, V. V., Harauz, G., & Ladizhansky, V. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.06.022 · Cited by 45

NMR evidence of GM1-induced conformational change of Substance P using isotropic bicelles

Gayen, A., Goswami, S. K., & Mukhopadhyay, C. (2010) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.09.023 · Cited by 43

PITANSEMA-MAS, a solid-state NMR method to measure heteronuclear dipolar couplings under MAS

Yamamoto, K., Ermakov, V. L., Lee, D. K., & Ramamoorthy, A. (2005) · Chemical Physics Letters · doi:10.1016/j.cplett.2005.04.017 · Cited by 42

Lipid Domains in Bicelles Containing Unsaturated Lipids and Cholesterol

Cho, H. S., Dominick, J. L., & Spence, M. M. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp100276u · Cited by 41

Biphenyl phosphatidylcholine: A promoter of liposome deformation and bicelle collective orientation by magnetic fields

Loudet, C., Diller, A., Grélard, A., Oda, R., & Dufourc, É. J. (2010) · Progress in Lipid Research · doi:10.1016/j.plipres.2010.02.002 · Cited by 41

The role of the length and sequence of the linker domain of cytochrome b5 in stimulating cytochrome P450 2B4 catalysis.

Clarke, T. A., Im, S., Bidwai, A. K., & Waskell, L. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406055200 · Cited by 41

Templated growth of platinum nanowheels using the inhomogeneous reaction environment of bicelles

Garcia, R. M., Song, Y., Dorin, R. M., Wang, H., Moreno, A. M., Jiang, Y., Tian, Y., Qiu, Y. J., Medforth, C. J., Coker, E. N., et al. (2010) · Physical Chemistry Chemical Physics · doi:10.1039/c0cp01930e · Cited by 40

In the cauldron of cell-free synthesis of membrane proteins: playing with new surfactants

Park, K.-H. P., Billon-Denis, E., Dahmane, T., Lebaupain, F., Pucci, B., Breyton, C., & Zito, F. (2010) · New Biotechnology · doi:10.1016/j.nbt.2010.08.008 · Cited by 40

Kinetic Folding Mechanism of an Integral Membrane Protein Examined by Pulsed Oxidative Labeling and Mass Spectrometry

Pan, Y. H., Brown, L. S., & Konermann, L. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.04.074 · Cited by 40

Fuzzy complexes of myelin basic protein: NMR spectroscopic investigations of a polymorphic organizational linker of the central nervous systemThis paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process.

Libich, D. S., Ahmed, M. A. M., Zhong, L., Bamm, V. V., Ladizhansky, V., & Harauz, G. (2010) · Biochemistry and Cell Biology · doi:10.1139/o09-123 · Cited by 39

Membrane Lipid Polymorphism

Epand, R. M. (2007) · Methods in molecular biology · doi:10.1007/978-1-59745-519-0_2 · Cited by 39

Manipulation of the Director in Bicellar Mesophases by Sample Spinning: A New Tool for NMR Spectroscopy

Zandomeneghi, G., Tomaselli, M., van Beek, J. D., & Meier, B. H. (2001) · Journal of the American Chemical Society · doi:10.1021/ja0019326 · Cited by 38

Membrane Mimetic Environments Alter the Conformation of the Outer Membrane Protein BtuB

Fanucci, G. E., Lee, J., & Cafiso, D. S. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0376442 · Cited by 37

Proton-Evolved Local-Field Solid-State NMR Studies of Cytochrome b5 Embedded in Bicelles, Revealing both Structural and Dynamical Information

Soong, R., Smith, P. E. S., Xu, J., Yamamoto, K., Im, S., Waskell, L. A., & Ramamoorthy, A. (2010) · Journal of the American Chemical Society · doi:10.1021/ja910807e · Cited by 37

Role of Membrane Lipids for the Activity of Pore Forming Peptides and Proteins

Fuertes, G., Giménez, D., Esteban-Martín, S., Sáez, A. J. G., Sánchez, O. A., & Salgado, J. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-6327-7_4 · Cited by 36

Structure elucidation of dimeric transmembrane domains of bitopic proteins

Bocharov, E. V., Volynsky, P. E., Pavlov, K. V., Efremov, R. G., & Arseniev, A. S. (2010) · Cell Adhesion & Migration · doi:10.4161/cam.4.2.11930 · Cited by 36

Membrane Interactions of Dynorphins,

Lind, J., Gräslund, A., & Mäler, L. (2006) · Biochemistry · doi:10.1021/bi061199g · Cited by 35

Two-dimensional homonuclear chemical shift correlation established by the cross-relaxation driven spin diffusion in solids

Xu, J., Struppe, J. O., & Ramamoorthy, A. (2008) · The Journal of Chemical Physics · doi:10.1063/1.2826323 · Cited by 35

A reconstitution protocol for the in vitro folded human G protein-coupled Y2 receptor into lipid environment

Schmidt, P. M., Berger, C., Scheidt, H. A., Berndt, S., Bunge, A., Beck‐Sickinger, A. G., & Huster, D. (2010) · Biophysical Chemistry · doi:10.1016/j.bpc.2010.02.019 · Cited by 33

Theoretical framework for NMR residual dipolar couplings in unfolded proteins

Obolensky, O. I., Schlepckow, K., Schwalbe, H., & Solov’yov, A. V. (2007) · Journal of Biomolecular NMR · doi:10.1007/s10858-007-9169-3 · Cited by 32

Coupling Efficiency of Rhodopsin and Transducin in Bicelles

Kaya, A. İ., Thaker, T. M., Preininger, A. M., Iverson, T. M., & Hamm, H. E. (2011) · Biochemistry · doi:10.1021/bi200037j · Cited by 32

Domain-elongation NMR spectroscopy yields new insights into RNA dynamics and adaptive recognition

Zhang, Q., & Al‐Hashimi, H. M. (2009) · RNA · doi:10.1261/rna.1806909 · Cited by 30

Residual dipolar couplings: Synergy between NMR and structural genomics

Al‐Hashimi, H. M., & Patel, D. J. (2002) · Journal of Biomolecular NMR · doi:10.1023/a:1013801714041 · Cited by 29

INEPT-Based Separated-Local-Field NMR Spectroscopy: A Unique Approach To Elucidate Side-Chain Dynamics of Membrane-Associated Proteins

Xu, J., Soong, R., Im, S., Waskell, L. A., & Ramamoorthy, A. (2010) · Journal of the American Chemical Society · doi:10.1021/ja103983f · Cited by 27

Whole-Body Rocking Motion of a Fusion Peptide in Lipid Bilayers from Size-Dispersed 15N NMR Relaxation

Lorieau, J. L., Louis, J. M., & Bax, A. (2011) · Journal of the American Chemical Society · doi:10.1021/ja2045309 · Cited by 27

The FKBP–Rapamycin Binding Domain of Human TOR Undergoes Strong Conformational Changes in the Presence of Membrane Mimetics with and without the Regulator Phosphatidic Acid

Camargo, D. C. R., Link, N. M., & Dames, S. A. (2012) · Biochemistry · doi:10.1021/bi3002133 · Cited by 27

Solution NMR of SNAREs, complexin and α-synuclein in association with membrane-mimetics

Liang, B., & Tamm, L. K. (2018) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2018.02.001 · Cited by 26

Contemporary Methods in Structure Determination of Membrane Proteins by Solution NMR

Qureshi, T., & Goto, N. K. (2011) · Topics in current chemistry · doi:10.1007/128_2011_306 · Cited by 25

Estimation of Interdomain Flexibility of N-Terminus of Factor H Using Residual Dipolar Couplings

Maciejewski, M., Tjandra, N., & Barlow, P. N. (2011) · Biochemistry · doi:10.1021/bi200575b · Cited by 24

Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy

Gruene, T., Cho, M., Karyagina, I., Kim, H., Grosse, C., Giller, K., Zweckstetter, M., & Becker, S. (2011) · Journal of Biomolecular NMR · doi:10.1007/s10858-011-9471-y · Cited by 22

Anesthetic effects on the structure and dynamics of the second transmembrane domains of nAChR α4β2

Cui, T., Canlas, C. G., Xu, Y., & Tang, P. S. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2009.08.009 · Cited by 21

NMR methods for studying the structure and dynamics of oncogenic and antihistaminic peptides in biomembranes

Sizun, C., Aussenac, F., Grélard, A., et al. (2004) · Magnetic Resonance in Chemistry · doi:10.1002/mrc.1336 · Cited by 21

Efficient cross-polarization using a composite 0° pulse for NMR studies on static solids

Fukuchi, M., Ramamoorthy, A., & Takegoshi, K. (2008) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2008.10.013 · Cited by 21

Human Cannabinoid 1 GPCR C-Terminal Domain Interacts with Bilayer Phospholipids to Modulate the Structure of its Membrane Environment

Tiburu, E. K., Tyukhtenko, S. I., Zhou, H., Janero, D. R., Struppe, J. O., & Makriyannis, A. (2011) · The AAPS Journal · doi:10.1208/s12248-010-9244-7 · Cited by 20

Insights into the effect of detergents on the full-length rhomboid protease from Pseudomonas aeruginosa and its cytosolic domain

Sherratt, A. R., Braganza, M. V., Nguyen, E., Ducat, T., & Goto, N. K. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2009.09.003 · Cited by 20

Structure, Dynamics, Lipid Binding, and Physiological Relevance of the Putative GTPase-binding Domain of Dictyostelium Formin C

Dames, S. A., Junemann, A., Sass, H. J., Schönichen, A., Stopschinski, B. E., Grzesiek, S., Faix, J., & Geyer, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.225052 · Cited by 20

Functional Reconstitution of Rhodopsin into Tubular Lipid Bilayers Supported by Nanoporous Media

Soubias, O., Polozov, I. V., Teague, W. E., Yeliseev, A., & Gawrisch, K. (2006) · Biochemistry · doi:10.1021/bi061416d · Cited by 20

Urea Unfolding of Opsin in Phospholipid Bicelles†

McKibbin, C., Farmer, N. A., Edwards, P. C., Villa, C., & Booth, P. J. (2009) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.2008.00503.x · Cited by 19

Potential role of the membrane in hERG channel functioning and drug-induced long QT syndrome

Chartrand, É., Arnold, A. A., Gravel, A. E., et al. (2010) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.05.019 · Cited by 17

Preparation of an Activated Rhodopsin/Transducin Complex Using a Constitutively Active Mutant of Rhodopsin

Xie, G., D’Antona, A. M., Edwards, P. C., Fransen, M. P., Standfuss, J., Schertler, G. F. X., & Oprian, D. D. (2011) · Biochemistry · doi:10.1021/bi201126r · Cited by 17

Ligand Binding and Membrane Insertion Compete with Oligomerization of the BclXL Apoptotic Repressor

Bhat, V. S., McDonald, C. B., Mikles, D. C., Deegan, B. J., Seldeen, K. L., Bates, M. L., & Farooq, A. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.12.015 · Cited by 17

Investigating the structural and dynamic properties of n-doxylstearic acid in magnetically-aligned phospholipid bilayers by X-band EPR spectroscopy

Nusair, N. A., & Lorigan, G. A. (2004) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2004.09.019 · Cited by 16

Structural characterization of AS1–membrane interactions from a subset of HAMP domains

Unnerståle, S., Mäler, L., & Draheim, R. R. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.06.018 · Cited by 16

Construction of Covalent Membrane Protein Complexes and High-Throughput Selection of Membrane Mimics

Suk, J.-E., Situ, A. J., & Ulmer, T. S. (2012) · Journal of the American Chemical Society · doi:10.1021/ja304247f · Cited by 15

Interactions of Tyrosine in Leu-Enkephalin at a Membrane−Water Interface: An Ultrafast Two-Dimensional Infrared Study Combined with Density Functional Calculations and Molecular Dynamics Simulations

Sul, S., Feng, Y., Le, U., Tobias, D. J., & Ge, N. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp9105844 · Cited by 12

Membrane interactions and dynamics of a 21-mer cytotoxic peptide: A solid-state NMR study

Ouellet, M., Voyer, N., & Auger, M. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2009.07.029 · Cited by 10

Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies

Wang, X., Gill, R. L., Zhu, Q., & Tian, F. (2011) · Protein Expression and Purification · doi:10.1016/j.pep.2011.02.004 · Cited by 10

Mimicking the Cell: Bio-Inspired Functions of Supramolecular Assemblies

Tu, Y., Peng, F., Adawy, A., Men, Y., Abdelmohsen, L. K. E. A., & Wilson, D. A. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00344 · Cited by 316

Conformational analysis of membrane-proximal segments of GDAP1 in a lipidic environment using synchrotron radiation suggests a mode of assembly at the mitochondrial outer membrane

Sutinen, A., Jones, N. C., Hoffmann, S. V., Ruskamo, S., & Kursula, P. (2023) · Biophysical Chemistry · doi:10.1016/j.bpc.2023.107113 · Cited by 3