Advanced Search
Display options
Filter resources
Text Availability
Article type
Publication date
Species
Language
Sex
Age
Showing 25 to 36 of 101 entries
Sorted by: Best Match Show Resources per page
Solubilized proteins from carrot (Daucus carota L.) membranes bind calcium channel blockers and form calcium-permeable ion channels.

Proceedings of the National Academy of Sciences of the United States of America

Thuleau P, Graziana A, Ranjeva R, Schroeder JI.
PMID: 11607356
Proc Natl Acad Sci U S A. 1993 Jan 15;90(2):765-9. doi: 10.1073/pnas.90.2.765.

Calcium channels have been suggested to play a major role in the initiation of a large number of signal transduction processes in higher plant cells. However, molecular components of higher plant Ca2+ channels remain unidentified to date. Calcium channel...

Cite
Thuleau P, Graziana A, Ranjeva R, et al. Solubilized proteins from carrot (Daucus carota L.) membranes bind calcium channel blockers and form calcium-permeable ion channels. Proc Natl Acad Sci U S A. 1993;90(2):765-9doi: 10.1073/pnas.90.2.765.
Thuleau, P., Graziana, A., Ranjeva, R., & Schroeder, J. I. (1993). Solubilized proteins from carrot (Daucus carota L.) membranes bind calcium channel blockers and form calcium-permeable ion channels. Proceedings of the National Academy of Sciences of the United States of America, 90(2), 765-9. https://doi.org/10.1073/pnas.90.2.765
Thuleau, P, et al. "Solubilized proteins from carrot (Daucus carota L.) membranes bind calcium channel blockers and form calcium-permeable ion channels." Proceedings of the National Academy of Sciences of the United States of America vol. 90,2 (1993): 765-9. doi: https://doi.org/10.1073/pnas.90.2.765
Thuleau P, Graziana A, Ranjeva R, Schroeder JI. Solubilized proteins from carrot (Daucus carota L.) membranes bind calcium channel blockers and form calcium-permeable ion channels. Proc Natl Acad Sci U S A. 1993 Jan 15;90(2):765-9. doi: 10.1073/pnas.90.2.765. PMID: 11607356; PMCID: PMC45746.
Copy Download .nbib Format: NLM
K+-conducting ion channel of the chloroplast inner envelope: functional reconstitution into liposomes.

Proceedings of the National Academy of Sciences of the United States of America

Wang X, Berkowitz GA, Peters JS.
PMID: 11607404
Proc Natl Acad Sci U S A. 1993 Jun 01;90(11):4981-5. doi: 10.1073/pnas.90.11.4981.

Potassium flux between the chloroplast stroma and cytoplasm is known to be indirectly linked to H+ countertransport and, hence, stromal pH and photosynthetic capacity. The specific molecular mechanism that facilitates K+ flux across the chloroplast envelope is not known...

Cite
Wang X, Berkowitz GA, Peters JS. K+-conducting ion channel of the chloroplast inner envelope: functional reconstitution into liposomes. Proc Natl Acad Sci U S A. 1993;90(11):4981-5doi: 10.1073/pnas.90.11.4981.
Wang, X., Berkowitz, G. A., & Peters, J. S. (1993). K+-conducting ion channel of the chloroplast inner envelope: functional reconstitution into liposomes. Proceedings of the National Academy of Sciences of the United States of America, 90(11), 4981-5. https://doi.org/10.1073/pnas.90.11.4981
Wang, X, et al. "K+-conducting ion channel of the chloroplast inner envelope: functional reconstitution into liposomes." Proceedings of the National Academy of Sciences of the United States of America vol. 90,11 (1993): 4981-5. doi: https://doi.org/10.1073/pnas.90.11.4981
Wang X, Berkowitz GA, Peters JS. K+-conducting ion channel of the chloroplast inner envelope: functional reconstitution into liposomes. Proc Natl Acad Sci U S A. 1993 Jun 01;90(11):4981-5. doi: 10.1073/pnas.90.11.4981. PMID: 11607404; PMCID: PMC46637.
Copy Download .nbib Format: NLM
Photobleaching of Chlorophyll in Light-Harvesting Complex II Increases in Lipid Environment.

Frontiers in plant science

Lingvay M, Akhtar P, Sebők-Nagy K, Páli T, Lambrev PH.
PMID: 32670321
Front Plant Sci. 2020 Jun 24;11:849. doi: 10.3389/fpls.2020.00849. eCollection 2020.

Excess light causes damage to the photosynthetic apparatus of plants and algae primarily via reactive oxygen species. Singlet oxygen can be formed by interaction of chlorophyll (Chl) triplet states, especially in the Photosystem II reaction center, with oxygen. Whether...

Cite
Lingvay M, Akhtar P, Sebők-Nagy K, et al. Photobleaching of Chlorophyll in Light-Harvesting Complex II Increases in Lipid Environment. Front Plant Sci. 2020;11:849doi: 10.3389/fpls.2020.00849.
Lingvay, M., Akhtar, P., Sebők-Nagy, K., Páli, T., & Lambrev, P. H. (2020). Photobleaching of Chlorophyll in Light-Harvesting Complex II Increases in Lipid Environment. Frontiers in plant science, 11849. https://doi.org/10.3389/fpls.2020.00849
Lingvay, Mónika, et al. "Photobleaching of Chlorophyll in Light-Harvesting Complex II Increases in Lipid Environment." Frontiers in plant science vol. 11 (2020): 849. doi: https://doi.org/10.3389/fpls.2020.00849
Lingvay M, Akhtar P, Sebők-Nagy K, Páli T, Lambrev PH. Photobleaching of Chlorophyll in Light-Harvesting Complex II Increases in Lipid Environment. Front Plant Sci. 2020 Jun 24;11:849. doi: 10.3389/fpls.2020.00849. eCollection 2020. PMID: 32670321; PMCID: PMC7327537.
Copy Download .nbib Format: NLM
The Human SLC1A5 (ASCT2) Amino Acid Transporter: From Function to Structure and Role in Cell Biology.

Frontiers in cell and developmental biology

Scalise M, Pochini L, Console L, Losso MA, Indiveri C.
PMID: 30234109
Front Cell Dev Biol. 2018 Sep 04;6:96. doi: 10.3389/fcell.2018.00096. eCollection 2018.

SLC1A5, known as ASCT2, is a neutral amino acid transporter belonging to the SLC1 family and localized in the plasma membrane of several body districts. ASCT2 is an acronym standing for Alanine, Serine, Cysteine Transporter 2 even if the...

Cite
Scalise M, Pochini L, Console L, et al. The Human SLC1A5 (ASCT2) Amino Acid Transporter: From Function to Structure and Role in Cell Biology. Front Cell Dev Biol. 2018;6:96doi: 10.3389/fcell.2018.00096.
Scalise, M., Pochini, L., Console, L., Losso, M. A., & Indiveri, C. (2018). The Human SLC1A5 (ASCT2) Amino Acid Transporter: From Function to Structure and Role in Cell Biology. Frontiers in cell and developmental biology, 696. https://doi.org/10.3389/fcell.2018.00096
Scalise, Mariafrancesca, et al. "The Human SLC1A5 (ASCT2) Amino Acid Transporter: From Function to Structure and Role in Cell Biology." Frontiers in cell and developmental biology vol. 6 (2018): 96. doi: https://doi.org/10.3389/fcell.2018.00096
Scalise M, Pochini L, Console L, Losso MA, Indiveri C. The Human SLC1A5 (ASCT2) Amino Acid Transporter: From Function to Structure and Role in Cell Biology. Front Cell Dev Biol. 2018 Sep 04;6:96. doi: 10.3389/fcell.2018.00096. eCollection 2018. PMID: 30234109; PMCID: PMC6131531.
Copy Download .nbib Format: NLM
Characterization of a Novel Mitochondrial Ascorbate Transporter From Rat Liver and Potato Mitochondria.

Frontiers in molecular biosciences

Scalera V, Giangregorio N, De Leonardis S, Console L, Carulli ES, Tonazzi A.
PMID: 29998111
Front Mol Biosci. 2018 Jun 26;5:58. doi: 10.3389/fmolb.2018.00058. eCollection 2018.

The Mitochondrial Ascorbic Acid Transporter (MAT) from both rat liver and potato mitochondria has been reconstituted in proteoliposomes. The protein has a molecular mass in the range of 28-35 kDa and catalyzes saturable, temperature and pH dependent, unidirectional ascorbic...

Cite
Scalera V, Giangregorio N, De Leonardis S, et al. Characterization of a Novel Mitochondrial Ascorbate Transporter From Rat Liver and Potato Mitochondria. Front Mol Biosci. 2018;5:58doi: 10.3389/fmolb.2018.00058.
Scalera, V., Giangregorio, N., De Leonardis, S., Console, L., Carulli, E. S., & Tonazzi, A. (2018). Characterization of a Novel Mitochondrial Ascorbate Transporter From Rat Liver and Potato Mitochondria. Frontiers in molecular biosciences, 558. https://doi.org/10.3389/fmolb.2018.00058
Scalera, Vito, et al. "Characterization of a Novel Mitochondrial Ascorbate Transporter From Rat Liver and Potato Mitochondria." Frontiers in molecular biosciences vol. 5 (2018): 58. doi: https://doi.org/10.3389/fmolb.2018.00058
Scalera V, Giangregorio N, De Leonardis S, Console L, Carulli ES, Tonazzi A. Characterization of a Novel Mitochondrial Ascorbate Transporter From Rat Liver and Potato Mitochondria. Front Mol Biosci. 2018 Jun 26;5:58. doi: 10.3389/fmolb.2018.00058. eCollection 2018. PMID: 29998111; PMCID: PMC6028771.
Copy Download .nbib Format: NLM
Bacterial outer membrane vesicles and vaccine applications.

Frontiers in immunology

Acevedo R, Fernández S, Zayas C, Acosta A, Sarmiento ME, Ferro VA, Rosenqvist E, Campa C, Cardoso D, Garcia L, Perez JL.
PMID: 24715891
Front Immunol. 2014 Mar 24;5:121. doi: 10.3389/fimmu.2014.00121. eCollection 2014.

Vaccines based on outer membrane vesicles (OMV) were developed more than 20 years ago against Neisseria meningitidis serogroup B. These nano-sized structures exhibit remarkable potential for immunomodulation of immune responses and delivery of meningococcal antigens or unrelated antigens incorporated...

Cite
Acevedo R, Fernández S, Zayas C, et al. Bacterial outer membrane vesicles and vaccine applications. Front Immunol. 2014;5:121doi: 10.3389/fimmu.2014.00121.
Acevedo, R., Fernández, S., Zayas, C., Acosta, A., Sarmiento, M. E., Ferro, V. A., Rosenqvist, E., Campa, C., Cardoso, D., Garcia, L., & Perez, J. L. (2014). Bacterial outer membrane vesicles and vaccine applications. Frontiers in immunology, 5121. https://doi.org/10.3389/fimmu.2014.00121
Acevedo, Reinaldo, et al. "Bacterial outer membrane vesicles and vaccine applications." Frontiers in immunology vol. 5 (2014): 121. doi: https://doi.org/10.3389/fimmu.2014.00121
Acevedo R, Fernández S, Zayas C, Acosta A, Sarmiento ME, Ferro VA, Rosenqvist E, Campa C, Cardoso D, Garcia L, Perez JL. Bacterial outer membrane vesicles and vaccine applications. Front Immunol. 2014 Mar 24;5:121. doi: 10.3389/fimmu.2014.00121. eCollection 2014. PMID: 24715891; PMCID: PMC3970029.
Copy Download .nbib Format: NLM
Superior Efficacy and Safety of a Nonemulsive Variant of the NGcGM3/VSSP Vaccine in Advanced Breast Cancer Patients.

Breast cancer : basic and clinical research

de la Torre A, Pérez K, Vega AM, Santiesteban E, Ruiz R, Hernández L, Durrutí D, Viada CE, Sánchez L, Álvarez M, Durán Y, Moreno YG, Arencibia M, Cepeda M, Domecq M, Cabrera L, Sánchez JL, Hernández JJ, Valls AR, Fernández LE.
PMID: 26917965
Breast Cancer (Auckl). 2016 Feb 18;10:5-11. doi: 10.4137/BCBCR.S32785. eCollection 2016.

NGcGM3 ganglioside is a tumor-specific antigen expressed in human breast tumors. The NGcGM3/VSSP vaccine, consisting in very small-sized proteoliposomes (VSSP) obtained by the incorporation of NGcGM3 into the outer membrane protein complex of Neisseria meningitidis, has been previously tested...

Cite
de la Torre A, Pérez K, Vega AM, et al. Superior Efficacy and Safety of a Nonemulsive Variant of the NGcGM3/VSSP Vaccine in Advanced Breast Cancer Patients. Breast Cancer (Auckl). 2016;10:5-11doi: 10.4137/BCBCR.S32785.
de la Torre, A., Pérez, K., Vega, A. M., Santiesteban, E., Ruiz, R., Hernández, L., Durrutí, D., Viada, C. E., Sánchez, L., Álvarez, M., Durán, Y., Moreno, Y. G., Arencibia, M., Cepeda, M., Domecq, M., Cabrera, L., Sánchez, J. L., Hernández, J. J., Valls, A. R., & Fernández, L. E. (2016). Superior Efficacy and Safety of a Nonemulsive Variant of the NGcGM3/VSSP Vaccine in Advanced Breast Cancer Patients. Breast cancer : basic and clinical research, 105-11. https://doi.org/10.4137/BCBCR.S32785
de la Torre, Ana, et al. "Superior Efficacy and Safety of a Nonemulsive Variant of the NGcGM3/VSSP Vaccine in Advanced Breast Cancer Patients." Breast cancer : basic and clinical research vol. 10 (2016): 5-11. doi: https://doi.org/10.4137/BCBCR.S32785
de la Torre A, Pérez K, Vega AM, Santiesteban E, Ruiz R, Hernández L, Durrutí D, Viada CE, Sánchez L, Álvarez M, Durán Y, Moreno YG, Arencibia M, Cepeda M, Domecq M, Cabrera L, Sánchez JL, Hernández JJ, Valls AR, Fernández LE. Superior Efficacy and Safety of a Nonemulsive Variant of the NGcGM3/VSSP Vaccine in Advanced Breast Cancer Patients. Breast Cancer (Auckl). 2016 Feb 18;10:5-11. doi: 10.4137/BCBCR.S32785. eCollection 2016. PMID: 26917965; PMCID: PMC4760670.
Copy Download .nbib Format: NLM
Isolation and characterization of the tricarboxylate transporter from pea mitochondria.

Plant physiology

McIntosh CA, Oliver DJ.
PMID: 16653235
Plant Physiol. 1992 Dec;100(4):2030-4. doi: 10.1104/pp.100.4.2030.

The tricarboxylate transporter was solubilized from pea (Pisum sativum) mitochondria with Triton X-114, partially purified over a hydroxylapatite column, and reconstituted in phospholipid vesicles. The proteoliposomes exchanged external [(14)C]citrate for internal citrate or malate but not for preloaded d,l-isocitrate....

Cite
McIntosh CA, Oliver DJ. Isolation and characterization of the tricarboxylate transporter from pea mitochondria. Plant Physiol. 1992;100(4):2030-4doi: 10.1104/pp.100.4.2030.
McIntosh, C. A., & Oliver, D. J. (1992). Isolation and characterization of the tricarboxylate transporter from pea mitochondria. Plant physiology, 100(4), 2030-4. https://doi.org/10.1104/pp.100.4.2030
McIntosh, C A, and Oliver, D J. "Isolation and characterization of the tricarboxylate transporter from pea mitochondria." Plant physiology vol. 100,4 (1992): 2030-4. doi: https://doi.org/10.1104/pp.100.4.2030
McIntosh CA, Oliver DJ. Isolation and characterization of the tricarboxylate transporter from pea mitochondria. Plant Physiol. 1992 Dec;100(4):2030-4. doi: 10.1104/pp.100.4.2030. PMID: 16653235; PMCID: PMC1075902.
Copy Download .nbib Format: NLM
Bactericidal mode of action of plantaricin C.

Applied and environmental microbiology

Gonzalez B, Glaasker E, Kunji E, Driessen A, Suarez JE, Konings WN.
PMID: 16535371
Appl Environ Microbiol. 1996 Aug;62(8):2701-9. doi: 10.1128/aem.62.8.2701-2709.1996.

Plantaricin C is a bacteriocin produced by Lactobacillus plantarum LL441 that kills sensitive cells by acting on the cytoplasmic membrane. In contrast to its lack of impact on immune cells, plantaricin C dissipates the proton motive force and inhibits...

Cite
Gonzalez B, Glaasker E, Kunji E, et al. Bactericidal mode of action of plantaricin C. Appl Environ Microbiol. 1996;62(8):2701-9doi: 10.1128/aem.62.8.2701-2709.1996.
Gonzalez, B., Glaasker, E., Kunji, E., Driessen, A., Suarez, J. E., & Konings, W. N. (1996). Bactericidal mode of action of plantaricin C. Applied and environmental microbiology, 62(8), 2701-9. https://doi.org/10.1128/aem.62.8.2701-2709.1996
Gonzalez, B, et al. "Bactericidal mode of action of plantaricin C." Applied and environmental microbiology vol. 62,8 (1996): 2701-9. doi: https://doi.org/10.1128/aem.62.8.2701-2709.1996
Gonzalez B, Glaasker E, Kunji E, Driessen A, Suarez JE, Konings WN. Bactericidal mode of action of plantaricin C. Appl Environ Microbiol. 1996 Aug;62(8):2701-9. doi: 10.1128/aem.62.8.2701-2709.1996. PMID: 16535371; PMCID: PMC1388909.
Copy Download .nbib Format: NLM
Vesicle fusion with bilayer lipid membrane controlled by electrostatic interaction.

Biochemistry and biophysics reports

Oshima A, Sumitomo K.
PMID: 28955768
Biochem Biophys Rep. 2017 Jun 19;11:58-63. doi: 10.1016/j.bbrep.2017.06.003. eCollection 2017 Sep.

The fusion of proteoliposomes is a promising approach for incorporating membrane proteins in artificial lipid membranes. In this study, we employed an electrostatic interaction between vesicles and supported bilayer lipid membranes (s-BLMs) to control the fusion process. We combined...

Cite
Oshima A, Sumitomo K. Vesicle fusion with bilayer lipid membrane controlled by electrostatic interaction. Biochem Biophys Rep. 2017;11:58-63doi: 10.1016/j.bbrep.2017.06.003.
Oshima, A., & Sumitomo, K. (2017). Vesicle fusion with bilayer lipid membrane controlled by electrostatic interaction. Biochemistry and biophysics reports, 1158-63. https://doi.org/10.1016/j.bbrep.2017.06.003
Oshima, Azusa, and Sumitomo, Koji. "Vesicle fusion with bilayer lipid membrane controlled by electrostatic interaction." Biochemistry and biophysics reports vol. 11 (2017): 58-63. doi: https://doi.org/10.1016/j.bbrep.2017.06.003
Oshima A, Sumitomo K. Vesicle fusion with bilayer lipid membrane controlled by electrostatic interaction. Biochem Biophys Rep. 2017 Jun 19;11:58-63. doi: 10.1016/j.bbrep.2017.06.003. eCollection 2017 Sep. PMID: 28955768; PMCID: PMC5614691.
Copy Download .nbib Format: NLM
A polarly localized transporter for efficient manganese uptake in rice.

Nature plants

Ueno D, Sasaki A, Yamaji N, Miyaji T, Fujii Y, Takemoto Y, Moriyama S, Che J, Moriyama Y, Iwasaki K, Ma JF.
PMID: 27251715
Nat Plants. 2015 Nov 09;1:15170. doi: 10.1038/nplants.2015.170.

Manganese is an essential metal for plant growth. A number of transporters involved in the uptake of manganese from soils, and its translocation to the shoot, have been identified in Arabidopsis and rice. However, the transporter responsible for the...

Cite
Ueno D, Sasaki A, Yamaji N, et al. A polarly localized transporter for efficient manganese uptake in rice. Nat Plants. 2015;1:15170doi: 10.1038/nplants.2015.170.
Ueno, D., Sasaki, A., Yamaji, N., Miyaji, T., Fujii, Y., Takemoto, Y., Moriyama, S., Che, J., Moriyama, Y., Iwasaki, K., & Ma, J. F. (2015). A polarly localized transporter for efficient manganese uptake in rice. Nature plants, 115170. https://doi.org/10.1038/nplants.2015.170
Ueno, Daisei, et al. "A polarly localized transporter for efficient manganese uptake in rice." Nature plants vol. 1 (2015): 15170. doi: https://doi.org/10.1038/nplants.2015.170
Ueno D, Sasaki A, Yamaji N, Miyaji T, Fujii Y, Takemoto Y, Moriyama S, Che J, Moriyama Y, Iwasaki K, Ma JF. A polarly localized transporter for efficient manganese uptake in rice. Nat Plants. 2015 Nov 09;1:15170. doi: 10.1038/nplants.2015.170. PMID: 27251715.
Copy Download .nbib Format: NLM
Tuning RGD Motif and Hyaluronan Density to Study Integrin Binding.

Frontiers in physiology

Zapp C, Minsky BB, Boehm H.
PMID: 30131707
Front Physiol. 2018 Aug 07;9:1022. doi: 10.3389/fphys.2018.01022. eCollection 2018.

Well-controlled surfaces with immobilized substrates enable novel approaches to investigate specific aspects of biological processes related to cell adhesion or motility. A subset of integrins, cellular transmembrane glycoproteins, recognize the evolutionarily conserved tripeptide sequence RGD, and anchor cells to...

Cite
Zapp C, Minsky BB, Boehm H. Tuning RGD Motif and Hyaluronan Density to Study Integrin Binding. Front Physiol. 2018;9:1022doi: 10.3389/fphys.2018.01022.
Zapp, C., Minsky, B. B., & Boehm, H. (2018). Tuning RGD Motif and Hyaluronan Density to Study Integrin Binding. Frontiers in physiology, 91022. https://doi.org/10.3389/fphys.2018.01022
Zapp, Cornelia, et al. "Tuning RGD Motif and Hyaluronan Density to Study Integrin Binding." Frontiers in physiology vol. 9 (2018): 1022. doi: https://doi.org/10.3389/fphys.2018.01022
Zapp C, Minsky BB, Boehm H. Tuning RGD Motif and Hyaluronan Density to Study Integrin Binding. Front Physiol. 2018 Aug 07;9:1022. doi: 10.3389/fphys.2018.01022. eCollection 2018. PMID: 30131707; PMCID: PMC6090076.
Copy Download .nbib Format: NLM
Showing 25 to 36 of 101 entries