Advanced Search
Display options
Filter resources
Text Availability
Article type
Publication date
Species
Language
Sex
Age
Showing 1 to 12 of 101 entries
Sorted by: Best Match Show Resources per page
Catch me if you can: a biotinylated proteoliposome affinity assay for the investigation of assembly of the MexA-MexB-OprM efflux pump from Pseudomonas aeruginosa.

Frontiers in microbiology

Ntsogo Enguéné VY, Verchère A, Phan G, Broutin I, Picard M.
PMID: 26082762
Front Microbiol. 2015 Jun 02;6:541. doi: 10.3389/fmicb.2015.00541. eCollection 2015.

Efflux pumps are membrane transporters that actively extrude various substrates, leading to multidrug resistance (MDR). In this study, we have designed a new test that allows investigating the assembly of the MexA-MexB-OprM efflux pump from the Gram negative bacteria...

Cite
Ntsogo Enguéné VY, Verchère A, Phan G, et al. Catch me if you can: a biotinylated proteoliposome affinity assay for the investigation of assembly of the MexA-MexB-OprM efflux pump from Pseudomonas aeruginosa. Front Microbiol. 2015;6:541doi: 10.3389/fmicb.2015.00541.
Ntsogo Enguéné, V. Y., Verchère, A., Phan, G., Broutin, I., & Picard, M. (2015). Catch me if you can: a biotinylated proteoliposome affinity assay for the investigation of assembly of the MexA-MexB-OprM efflux pump from Pseudomonas aeruginosa. Frontiers in microbiology, 6541. https://doi.org/10.3389/fmicb.2015.00541
Ntsogo Enguéné, Véronique Yvette, et al. "Catch me if you can: a biotinylated proteoliposome affinity assay for the investigation of assembly of the MexA-MexB-OprM efflux pump from Pseudomonas aeruginosa." Frontiers in microbiology vol. 6 (2015): 541. doi: https://doi.org/10.3389/fmicb.2015.00541
Ntsogo Enguéné VY, Verchère A, Phan G, Broutin I, Picard M. Catch me if you can: a biotinylated proteoliposome affinity assay for the investigation of assembly of the MexA-MexB-OprM efflux pump from Pseudomonas aeruginosa. Front Microbiol. 2015 Jun 02;6:541. doi: 10.3389/fmicb.2015.00541. eCollection 2015. PMID: 26082762; PMCID: PMC4451422.
Copy Download .nbib Format: NLM
The Aquaporin Splice Variant NbXIP1;1α Is Permeable to Boric Acid and Is Phosphorylated in the N-terminal Domain.

Frontiers in plant science

Ampah-Korsah H, Anderberg HI, Engfors A, Kirscht A, Norden K, Kjellstrom S, Kjellbom P, Johanson U.
PMID: 27379142
Front Plant Sci. 2016 Jun 16;7:862. doi: 10.3389/fpls.2016.00862. eCollection 2016.

Aquaporins (AQPs) are membrane channel proteins that transport water and uncharged solutes across different membranes in organisms in all kingdoms of life. In plants, the AQPs can be divided into seven different subfamilies and five of these are present...

Cite
Ampah-Korsah H, Anderberg HI, Engfors A, et al. The Aquaporin Splice Variant NbXIP1;1α Is Permeable to Boric Acid and Is Phosphorylated in the N-terminal Domain. Front Plant Sci. 2016;7:862doi: 10.3389/fpls.2016.00862.
Ampah-Korsah, H., Anderberg, H. I., Engfors, A., Kirscht, A., Norden, K., Kjellstrom, S., Kjellbom, P., & Johanson, U. (2016). The Aquaporin Splice Variant NbXIP1;1α Is Permeable to Boric Acid and Is Phosphorylated in the N-terminal Domain. Frontiers in plant science, 7862. https://doi.org/10.3389/fpls.2016.00862
Ampah-Korsah, Henry, et al. "The Aquaporin Splice Variant NbXIP1;1α Is Permeable to Boric Acid and Is Phosphorylated in the N-terminal Domain." Frontiers in plant science vol. 7 (2016): 862. doi: https://doi.org/10.3389/fpls.2016.00862
Ampah-Korsah H, Anderberg HI, Engfors A, Kirscht A, Norden K, Kjellstrom S, Kjellbom P, Johanson U. The Aquaporin Splice Variant NbXIP1;1α Is Permeable to Boric Acid and Is Phosphorylated in the N-terminal Domain. Front Plant Sci. 2016 Jun 16;7:862. doi: 10.3389/fpls.2016.00862. eCollection 2016. PMID: 27379142; PMCID: PMC4909777.
Copy Download .nbib Format: NLM
Sterol Modulation of the Plasma Membrane H+-ATPase Activity from Corn Roots Reconstituted into Soybean Lipids.

Plant physiology

Grandmougin-Ferjani A, Schuler-Muller I, Hartmann MA.
PMID: 12223599
Plant Physiol. 1997 Jan;113(1):163-174. doi: 10.1104/pp.113.1.163.

A partially purified H+-ATPase from the plasma membrane (PM) of corn (Zea mays L.) roots was inserted into vesicles prepared with soybean (Glycine max L.) phospholipids and various concentrations of individual sterols using either a freeze-thaw sonication or an...

Cite
Grandmougin-Ferjani A, Schuler-Muller I, Hartmann MA. Sterol Modulation of the Plasma Membrane H+-ATPase Activity from Corn Roots Reconstituted into Soybean Lipids. Plant Physiol. 1997;113(1):163-174doi: 10.1104/pp.113.1.163.
Grandmougin-Ferjani, A., Schuler-Muller, I., & Hartmann, M. A. (1997). Sterol Modulation of the Plasma Membrane H+-ATPase Activity from Corn Roots Reconstituted into Soybean Lipids. Plant physiology, 113(1), 163-174. https://doi.org/10.1104/pp.113.1.163
Grandmougin-Ferjani, A., et al. "Sterol Modulation of the Plasma Membrane H+-ATPase Activity from Corn Roots Reconstituted into Soybean Lipids." Plant physiology vol. 113,1 (1997): 163-174. doi: https://doi.org/10.1104/pp.113.1.163
Grandmougin-Ferjani A, Schuler-Muller I, Hartmann MA. Sterol Modulation of the Plasma Membrane H+-ATPase Activity from Corn Roots Reconstituted into Soybean Lipids. Plant Physiol. 1997 Jan;113(1):163-174. doi: 10.1104/pp.113.1.163. PMID: 12223599; PMCID: PMC158127.
Copy Download .nbib Format: NLM
Immunological Evidence for the Existence of a Carrier Protein for Sucrose Transport in Tonoplast Vesicles from Red Beet (Beta vulgaris L.) Root Storage Tissue.

Plant physiology

Getz HP, Grosclaude J, Kurkdjian A, Lelievre F, Maretzki A, Guern J.
PMID: 12231863
Plant Physiol. 1993 Jul;102(3):751-760. doi: 10.1104/pp.102.3.751.

Monoclonal antibodies were raised in mice against a highly purified tonoplast fraction from isolated red beet (Beta vulgaris L. ssp. conditiva) root vacuoles. Positive hybridoma clones and sub-clones were identified by prescreening using an enzyme-linked immunosorbent assay (ELISA) and...

Cite
Getz HP, Grosclaude J, Kurkdjian A, et al. Immunological Evidence for the Existence of a Carrier Protein for Sucrose Transport in Tonoplast Vesicles from Red Beet (Beta vulgaris L.) Root Storage Tissue. Plant Physiol. 1993;102(3):751-760doi: 10.1104/pp.102.3.751.
Getz, H. P., Grosclaude, J., Kurkdjian, A., Lelievre, F., Maretzki, A., & Guern, J. (1993). Immunological Evidence for the Existence of a Carrier Protein for Sucrose Transport in Tonoplast Vesicles from Red Beet (Beta vulgaris L.) Root Storage Tissue. Plant physiology, 102(3), 751-760. https://doi.org/10.1104/pp.102.3.751
Getz, H. P., et al. "Immunological Evidence for the Existence of a Carrier Protein for Sucrose Transport in Tonoplast Vesicles from Red Beet (Beta vulgaris L.) Root Storage Tissue." Plant physiology vol. 102,3 (1993): 751-760. doi: https://doi.org/10.1104/pp.102.3.751
Getz HP, Grosclaude J, Kurkdjian A, Lelievre F, Maretzki A, Guern J. Immunological Evidence for the Existence of a Carrier Protein for Sucrose Transport in Tonoplast Vesicles from Red Beet (Beta vulgaris L.) Root Storage Tissue. Plant Physiol. 1993 Jul;102(3):751-760. doi: 10.1104/pp.102.3.751. PMID: 12231863; PMCID: PMC158844.
Copy Download .nbib Format: NLM
Purification and Characterization of a Glycerol-Resistant CF(0)-CF(1) and CF(1)-ATPase from the Halotolerant Alga Dunaliella bardawil.

Plant physiology

Finel M, Pick U, Selman-Reimer S, Selman BR.
PMID: 16663507
Plant Physiol. 1984 Apr;74(4):766-72. doi: 10.1104/pp.74.4.766.

The isolation of the chloroplast ATP synthase complex (CF(0)-CF(1)) and of CF(1) from Dunaliella bardawil is described. The subunit structure of the D. bardawil ATPase differs from that of the spinach in that the D. bardawil alpha subunit migrates...

Cite
Finel M, Pick U, Selman-Reimer S, et al. Purification and Characterization of a Glycerol-Resistant CF(0)-CF(1) and CF(1)-ATPase from the Halotolerant Alga Dunaliella bardawil. Plant Physiol. 1984;74(4):766-72doi: 10.1104/pp.74.4.766.
Finel, M., Pick, U., Selman-Reimer, S., & Selman, B. R. (1984). Purification and Characterization of a Glycerol-Resistant CF(0)-CF(1) and CF(1)-ATPase from the Halotolerant Alga Dunaliella bardawil. Plant physiology, 74(4), 766-72. https://doi.org/10.1104/pp.74.4.766
Finel, M, et al. "Purification and Characterization of a Glycerol-Resistant CF(0)-CF(1) and CF(1)-ATPase from the Halotolerant Alga Dunaliella bardawil." Plant physiology vol. 74,4 (1984): 766-72. doi: https://doi.org/10.1104/pp.74.4.766
Finel M, Pick U, Selman-Reimer S, Selman BR. Purification and Characterization of a Glycerol-Resistant CF(0)-CF(1) and CF(1)-ATPase from the Halotolerant Alga Dunaliella bardawil. Plant Physiol. 1984 Apr;74(4):766-72. doi: 10.1104/pp.74.4.766. PMID: 16663507; PMCID: PMC1066765.
Copy Download .nbib Format: NLM
Membrane transporters for the special amino acid glutamine: structure/function relationships and relevance to human health.

Frontiers in chemistry

Pochini L, Scalise M, Galluccio M, Indiveri C.
PMID: 25157349
Front Chem. 2014 Aug 11;2:61. doi: 10.3389/fchem.2014.00061. eCollection 2014.

Glutamine together with glucose is essential for body's homeostasis. It is the most abundant amino acid and is involved in many biosynthetic, regulatory and energy production processes. Several membrane transporters which differ in transport modes, ensure glutamine homeostasis by...

Cite
Pochini L, Scalise M, Galluccio M, et al. Membrane transporters for the special amino acid glutamine: structure/function relationships and relevance to human health. Front Chem. 2014;2:61doi: 10.3389/fchem.2014.00061.
Pochini, L., Scalise, M., Galluccio, M., & Indiveri, C. (2014). Membrane transporters for the special amino acid glutamine: structure/function relationships and relevance to human health. Frontiers in chemistry, 261. https://doi.org/10.3389/fchem.2014.00061
Pochini, Lorena, et al. "Membrane transporters for the special amino acid glutamine: structure/function relationships and relevance to human health." Frontiers in chemistry vol. 2 (2014): 61. doi: https://doi.org/10.3389/fchem.2014.00061
Pochini L, Scalise M, Galluccio M, Indiveri C. Membrane transporters for the special amino acid glutamine: structure/function relationships and relevance to human health. Front Chem. 2014 Aug 11;2:61. doi: 10.3389/fchem.2014.00061. eCollection 2014. PMID: 25157349; PMCID: PMC4127817.
Copy Download .nbib Format: NLM
Effect of vaccination with N-glycolyl GM3/VSSP vaccine by subcutaneous injection in patients with advanced cutaneous melanoma.

Cancer management and research

Osorio M, Gracia E, Reigosa E, Hernandez J, de la Torre A, Saurez G, Perez K, Viada C, Cepeda M, Carr A, Avila Y, Rodríguez M, Fernandez LE.
PMID: 23055778
Cancer Manag Res. 2012;4:341-5. doi: 10.2147/CMAR.S22617. Epub 2012 Oct 05.

NeuGc-containing gangliosides have been described in melanoma cells and are an attractive target for cancer immunotherapy because they are minimally or not expressed in normal human tissues. Melanoma patients treated with a vaccine based on N-glycolyl gangliosides have shown...

Cite
Osorio M, Gracia E, Reigosa E, et al. Effect of vaccination with N-glycolyl GM3/VSSP vaccine by subcutaneous injection in patients with advanced cutaneous melanoma. Cancer Manag Res. 2012;4:341-5doi: 10.2147/CMAR.S22617.
Osorio, M., Gracia, E., Reigosa, E., Hernandez, J., de la Torre, A., Saurez, G., Perez, K., Viada, C., Cepeda, M., Carr, A., Avila, Y., Rodríguez, M., & Fernandez, L. E. (2012). Effect of vaccination with N-glycolyl GM3/VSSP vaccine by subcutaneous injection in patients with advanced cutaneous melanoma. Cancer management and research, 4341-5. https://doi.org/10.2147/CMAR.S22617
Osorio, Marta, et al. "Effect of vaccination with N-glycolyl GM3/VSSP vaccine by subcutaneous injection in patients with advanced cutaneous melanoma." Cancer management and research vol. 4 (2012): 341-5. doi: https://doi.org/10.2147/CMAR.S22617
Osorio M, Gracia E, Reigosa E, Hernandez J, de la Torre A, Saurez G, Perez K, Viada C, Cepeda M, Carr A, Avila Y, Rodríguez M, Fernandez LE. Effect of vaccination with N-glycolyl GM3/VSSP vaccine by subcutaneous injection in patients with advanced cutaneous melanoma. Cancer Manag Res. 2012;4:341-5. doi: 10.2147/CMAR.S22617. Epub 2012 Oct 05. PMID: 23055778; PMCID: PMC3468021.
Copy Download .nbib Format: NLM
Design and assembly of a chemically switchable and fluorescently traceable light-driven proton pump system for bionanotechnological applications.

Scientific reports

Hirschi S, Fischer N, Kalbermatter D, Laskowski PR, Ucurum Z, Müller DJ, Fotiadis D.
PMID: 30705382
Sci Rep. 2019 Jan 31;9(1):1046. doi: 10.1038/s41598-018-37260-9.

Energy-supplying modules are essential building blocks for the assembly of functional multicomponent nanoreactors in synthetic biology. Proteorhodopsin, a light-driven proton pump, is an ideal candidate to provide the required energy in form of an electrochemical proton gradient. Here we...

Cite
Hirschi S, Fischer N, Kalbermatter D, et al. Design and assembly of a chemically switchable and fluorescently traceable light-driven proton pump system for bionanotechnological applications. Sci Rep. 2019;9(1):1046doi: 10.1038/s41598-018-37260-9.
Hirschi, S., Fischer, N., Kalbermatter, D., Laskowski, P. R., Ucurum, Z., Müller, D. J., & Fotiadis, D. (2019). Design and assembly of a chemically switchable and fluorescently traceable light-driven proton pump system for bionanotechnological applications. Scientific reports, 9(1), 1046. https://doi.org/10.1038/s41598-018-37260-9
Hirschi, S, et al. "Design and assembly of a chemically switchable and fluorescently traceable light-driven proton pump system for bionanotechnological applications." Scientific reports vol. 9,1 (2019): 1046. doi: https://doi.org/10.1038/s41598-018-37260-9
Hirschi S, Fischer N, Kalbermatter D, Laskowski PR, Ucurum Z, Müller DJ, Fotiadis D. Design and assembly of a chemically switchable and fluorescently traceable light-driven proton pump system for bionanotechnological applications. Sci Rep. 2019 Jan 31;9(1):1046. doi: 10.1038/s41598-018-37260-9. PMID: 30705382; PMCID: PMC6355921.
Copy Download .nbib Format: NLM
Properties of Omp2a-Based Supported Lipid Bilayers: Comparison with Polymeric Bioinspired Membranes.

ACS omega

Puiggalí-Jou A, Pawlowski J, Del Valle LJ, Michaux C, Perpète EA, Sek S, Alemán C.
PMID: 31459033
ACS Omega. 2018 Aug 13;3(8):9003-9019. doi: 10.1021/acsomega.8b00913. eCollection 2018 Aug 31.

Omp2a β-barrel outer membrane protein has been reconstituted into supported lipid bilayers (SLBs) to compare the nanomechanical properties (elastic modulus, adhesion forces, and deformation) and functionality of the resulting bioinspired system with those of Omp2a-based polymeric nanomembranes (NMs). Protein...

Cite
Puiggalí-Jou A, Pawlowski J, Del Valle LJ, et al. Properties of Omp2a-Based Supported Lipid Bilayers: Comparison with Polymeric Bioinspired Membranes. ACS Omega. 2018;3(8):9003-9019doi: 10.1021/acsomega.8b00913.
Puiggalí-Jou, A., Pawlowski, J., Del Valle, L. J., Michaux, C., Perpète, E. A., Sek, S., & Alemán, C. (2018). Properties of Omp2a-Based Supported Lipid Bilayers: Comparison with Polymeric Bioinspired Membranes. ACS omega, 3(8), 9003-9019. https://doi.org/10.1021/acsomega.8b00913
Puiggalí-Jou, Anna, et al. "Properties of Omp2a-Based Supported Lipid Bilayers: Comparison with Polymeric Bioinspired Membranes." ACS omega vol. 3,8 (2018): 9003-9019. doi: https://doi.org/10.1021/acsomega.8b00913
Puiggalí-Jou A, Pawlowski J, Del Valle LJ, Michaux C, Perpète EA, Sek S, Alemán C. Properties of Omp2a-Based Supported Lipid Bilayers: Comparison with Polymeric Bioinspired Membranes. ACS Omega. 2018 Aug 13;3(8):9003-9019. doi: 10.1021/acsomega.8b00913. eCollection 2018 Aug 31. PMID: 31459033; PMCID: PMC6645002.
Copy Download .nbib Format: NLM
Functional Reconstitution of Membrane Proteins Derived From Eukaryotic Cell-Free Systems.

Frontiers in pharmacology

Dondapati SK, Lübberding H, Zemella A, Thoring L, Wüstenhagen DA, Kubick S.
PMID: 31543813
Front Pharmacol. 2019 Aug 30;10:917. doi: 10.3389/fphar.2019.00917. eCollection 2019.

Cell-free protein synthesis (CFPS) based on eukaryotic

Cite
Dondapati SK, Lübberding H, Zemella A, et al. Functional Reconstitution of Membrane Proteins Derived From Eukaryotic Cell-Free Systems. Front Pharmacol. 2019;10:917doi: 10.3389/fphar.2019.00917.
Dondapati, S. K., Lübberding, H., Zemella, A., Thoring, L., Wüstenhagen, D. A., & Kubick, S. (2019). Functional Reconstitution of Membrane Proteins Derived From Eukaryotic Cell-Free Systems. Frontiers in pharmacology, 10917. https://doi.org/10.3389/fphar.2019.00917
Dondapati, Srujan Kumar, et al. "Functional Reconstitution of Membrane Proteins Derived From Eukaryotic Cell-Free Systems." Frontiers in pharmacology vol. 10 (2019): 917. doi: https://doi.org/10.3389/fphar.2019.00917
Dondapati SK, Lübberding H, Zemella A, Thoring L, Wüstenhagen DA, Kubick S. Functional Reconstitution of Membrane Proteins Derived From Eukaryotic Cell-Free Systems. Front Pharmacol. 2019 Aug 30;10:917. doi: 10.3389/fphar.2019.00917. eCollection 2019. PMID: 31543813; PMCID: PMC6728924.
Copy Download .nbib Format: NLM
A native cell membrane nanoparticles system allows for high-quality functional proteoliposome reconstitution.

BBA advances

Yang L, Catalano C, Xu Y, Qiu W, Zhang D, McDermott A, Guo Y, Blount P.
PMID: 34296205
BBA Adv. 2021;1. doi: 10.1016/j.bbadva.2021.100011. Epub 2021 Apr 05.

Proteoliposomes mimic the cell membrane environment allowing for structural and functional membrane protein analyses as well as antigen presenting and drug delivery devices. To make proteoliposomes, purified functional membrane proteins are required. Detergents have traditionally been used for the...

Cite
Yang L, Catalano C, Xu Y, et al. A native cell membrane nanoparticles system allows for high-quality functional proteoliposome reconstitution. BBA Adv. 2021;1doi: 10.1016/j.bbadva.2021.100011.
Yang, L., Catalano, C., Xu, Y., Qiu, W., Zhang, D., McDermott, A., Guo, Y., & Blount, P. (2021). A native cell membrane nanoparticles system allows for high-quality functional proteoliposome reconstitution. BBA advances, 1. https://doi.org/10.1016/j.bbadva.2021.100011
Yang, Limin, et al. "A native cell membrane nanoparticles system allows for high-quality functional proteoliposome reconstitution." BBA advances vol. 1 (2021). doi: https://doi.org/10.1016/j.bbadva.2021.100011
Yang L, Catalano C, Xu Y, Qiu W, Zhang D, McDermott A, Guo Y, Blount P. A native cell membrane nanoparticles system allows for high-quality functional proteoliposome reconstitution. BBA Adv. 2021;1. doi: 10.1016/j.bbadva.2021.100011. Epub 2021 Apr 05. PMID: 34296205; PMCID: PMC8294337.
Copy Download .nbib Format: NLM
Reconstitution of Bam Complex-Mediated Assembly of a Trimeric Porin into Proteoliposomes.

mBio

Hussain S, Peterson JH, Bernstein HD.
PMID: 34399610
mBio. 2021 Aug 31;12(4):e0169621. doi: 10.1128/mBio.01696-21. Epub 2021 Aug 17.

Many integral membrane proteins form oligomeric complexes, but the assembly of these structures is poorly understood. Here, we show that the assembly of OmpC, a trimeric porin that resides in the Escherichia coli outer membrane (OM), can be reconstituted

Cite
Hussain S, Peterson JH, Bernstein HD. Reconstitution of Bam Complex-Mediated Assembly of a Trimeric Porin into Proteoliposomes. mBio. 2021;12(4):e0169621doi: 10.1128/mBio.01696-21.
Hussain, S., Peterson, J. H., & Bernstein, H. D. (2021). Reconstitution of Bam Complex-Mediated Assembly of a Trimeric Porin into Proteoliposomes. mBio, 12(4), e0169621. https://doi.org/10.1128/mBio.01696-21
Hussain, Sunyia, et al. "Reconstitution of Bam Complex-Mediated Assembly of a Trimeric Porin into Proteoliposomes." mBio vol. 12,4 (2021): e0169621. doi: https://doi.org/10.1128/mBio.01696-21
Hussain S, Peterson JH, Bernstein HD. Reconstitution of Bam Complex-Mediated Assembly of a Trimeric Porin into Proteoliposomes. mBio. 2021 Aug 31;12(4):e0169621. doi: 10.1128/mBio.01696-21. Epub 2021 Aug 17. PMID: 34399610; PMCID: PMC8406188.
Copy Download .nbib Format: NLM
Showing 1 to 12 of 101 entries