Advanced Search
Display options
Filter resources
Text Availability
Article type
Publication date
Species
Language
Sex
Age
Showing 1 to 12 of 13 entries
Sorted by: Best Match Show Resources per page
Paracrine Signaling by Extracellular Vesicles via Osteoblasts.

Current molecular biology reports

Morhayim J, Rudjito R, van Leeuwen JP, van Driel M.
PMID: 27429899
Curr Mol Biol Rep. 2016;2:48-55. doi: 10.1007/s40610-016-0034-6. Epub 2016 Feb 23.

Extracellular vesicles (EVs), spherical bilayered proteolipids, behave as paracrine effectors since they are released from cells to deliver signals to other cells. They control a diverse range of biological processes by transferring proteins, lipids, and nucleic acids between cells...

Cite
Morhayim J, Rudjito R, van Leeuwen JP, et al. Paracrine Signaling by Extracellular Vesicles via Osteoblasts. Curr Mol Biol Rep. 2016;2:48-55doi: 10.1007/s40610-016-0034-6.
Morhayim, J., Rudjito, R., van Leeuwen, J. P., & van Driel, M. (2016). Paracrine Signaling by Extracellular Vesicles via Osteoblasts. Current molecular biology reports, 248-55. https://doi.org/10.1007/s40610-016-0034-6
Morhayim, Jess, et al. "Paracrine Signaling by Extracellular Vesicles via Osteoblasts." Current molecular biology reports vol. 2 (2016): 48-55. doi: https://doi.org/10.1007/s40610-016-0034-6
Morhayim J, Rudjito R, van Leeuwen JP, van Driel M. Paracrine Signaling by Extracellular Vesicles via Osteoblasts. Curr Mol Biol Rep. 2016;2:48-55. doi: 10.1007/s40610-016-0034-6. Epub 2016 Feb 23. PMID: 27429899; PMCID: PMC4922391.
Copy Download .nbib Format: NLM
Identification of two proteolipid antigens with different localization at torpedo neuromuscular synapses.

Neurochemistry international

Morel N, Israel M, Synguelakis M, Le Gal la Salle G.
PMID: 20504480
Neurochem Int. 1989;15(2):169-77. doi: 10.1016/0197-0186(89)90097-1.

The cholinergic nerve terminals of Torpedo electric organ are a rich source of a hydrophobic protein, the mediatophore, which endows artificial membranes with a calcium dependent mechanism that translocates acetylcholine. An antiserum raised against purified mediatophore permitted the identification...

Cite
Morel N, Israel M, Synguelakis M, et al. Identification of two proteolipid antigens with different localization at torpedo neuromuscular synapses. Neurochem Int. 1989;15(2):169-77doi: 10.1016/0197-0186(89)90097-1.
Morel, N., Israel, M., Synguelakis, M., & Le Gal la Salle, G. (1989). Identification of two proteolipid antigens with different localization at torpedo neuromuscular synapses. Neurochemistry international, 15(2), 169-77. https://doi.org/10.1016/0197-0186(89)90097-1
Morel, N, et al. "Identification of two proteolipid antigens with different localization at torpedo neuromuscular synapses." Neurochemistry international vol. 15,2 (1989): 169-77. doi: https://doi.org/10.1016/0197-0186(89)90097-1
Morel N, Israel M, Synguelakis M, Le Gal la Salle G. Identification of two proteolipid antigens with different localization at torpedo neuromuscular synapses. Neurochem Int. 1989;15(2):169-77. doi: 10.1016/0197-0186(89)90097-1. PMID: 20504480.
Copy Download .nbib Format: NLM
PROTEOLIPIDS FROM MEMBRANE SYSTEMS.

Annals of the New York Academy of Sciences

Folch-Pi J, Stoffyn PJ.
PMID: 29090791
Ann N Y Acad Sci. 1972 Jun;195(1):86-107. doi: 10.1111/j.1749-6632.1972.tb54788.x.

No abstract available.

Cite
Folch-Pi J, Stoffyn PJ. PROTEOLIPIDS FROM MEMBRANE SYSTEMS. Ann N Y Acad Sci. 1972;195(1):86-107doi: 10.1111/j.1749-6632.1972.tb54788.x.
Folch-Pi, J., & Stoffyn, P. J. (1972). PROTEOLIPIDS FROM MEMBRANE SYSTEMS. Annals of the New York Academy of Sciences, 195(1), 86-107. https://doi.org/10.1111/j.1749-6632.1972.tb54788.x
Folch-Pi, J, and Stoffyn, Pierre J. "PROTEOLIPIDS FROM MEMBRANE SYSTEMS." Annals of the New York Academy of Sciences vol. 195,1 (1972): 86-107. doi: https://doi.org/10.1111/j.1749-6632.1972.tb54788.x
Folch-Pi J, Stoffyn PJ. PROTEOLIPIDS FROM MEMBRANE SYSTEMS. Ann N Y Acad Sci. 1972 Jun;195(1):86-107. doi: 10.1111/j.1749-6632.1972.tb54788.x. PMID: 29090791.
Copy Download .nbib Format: NLM
EVpedia: an integrated database of high-throughput data for systemic analyses of extracellular vesicles.

Journal of extracellular vesicles

Kim DK, Kang B, Kim OY, Choi DS, Lee J, Kim SR, Go G, Yoon YJ, Kim JH, Jang SC, Park KS, Choi EJ, Kim KP, Desiderio DM, Kim YK, Lötvall J, Hwang D, Gho YS.
PMID: 24009897
J Extracell Vesicles. 2013 Mar 19;2. doi: 10.3402/jev.v2i0.20384. eCollection 2013.

Secretion of extracellular vesicles is a general cellular activity that spans the range from simple unicellular organisms (e.g. archaea; Gram-positive and Gram-negative bacteria) to complex multicellular ones, suggesting that this extracellular vesicle-mediated communication is evolutionarily conserved. Extracellular vesicles are...

Cite
Kim DK, Kang B, Kim OY, et al. EVpedia: an integrated database of high-throughput data for systemic analyses of extracellular vesicles. J Extracell Vesicles. 2013;2doi: 10.3402/jev.v2i0.20384.
Kim, D. K., Kang, B., Kim, O. Y., Choi, D. S., Lee, J., Kim, S. R., Go, G., Yoon, Y. J., Kim, J. H., Jang, S. C., Park, K. S., Choi, E. J., Kim, K. P., Desiderio, D. M., Kim, Y. K., Lötvall, J., Hwang, D., & Gho, Y. S. (2013). EVpedia: an integrated database of high-throughput data for systemic analyses of extracellular vesicles. Journal of extracellular vesicles, 2. https://doi.org/10.3402/jev.v2i0.20384
Kim, Dae-Kyum, et al. "EVpedia: an integrated database of high-throughput data for systemic analyses of extracellular vesicles." Journal of extracellular vesicles vol. 2 (2013). doi: https://doi.org/10.3402/jev.v2i0.20384
Kim DK, Kang B, Kim OY, Choi DS, Lee J, Kim SR, Go G, Yoon YJ, Kim JH, Jang SC, Park KS, Choi EJ, Kim KP, Desiderio DM, Kim YK, Lötvall J, Hwang D, Gho YS. EVpedia: an integrated database of high-throughput data for systemic analyses of extracellular vesicles. J Extracell Vesicles. 2013 Mar 19;2. doi: 10.3402/jev.v2i0.20384. eCollection 2013. PMID: 24009897; PMCID: PMC3760654.
Copy Download .nbib Format: NLM
Calcium content of mice brain lipids during myelination.

Neuroscience letters

Pollet S, Chaix G, Baumann N.
PMID: 19604904
Neurosci Lett. 1976 Dec;3(5):311-4. doi: 10.1016/0304-3940(76)90060-4.

Calcium levels have been determined in brain of C57Bl mice and in the Quaking dysmyelinating mutant during the myelination period. In control mice, calcium content per gram brain is maximum at 20 days, at the acme of myelination, and...

Cite
Pollet S, Chaix G, Baumann N. Calcium content of mice brain lipids during myelination. Neurosci Lett. 1976;3(5):311-4doi: 10.1016/0304-3940(76)90060-4.
Pollet, S., Chaix, G., & Baumann, N. (1976). Calcium content of mice brain lipids during myelination. Neuroscience letters, 3(5), 311-4. https://doi.org/10.1016/0304-3940(76)90060-4
Pollet, S, et al. "Calcium content of mice brain lipids during myelination." Neuroscience letters vol. 3,5 (1976): 311-4. doi: https://doi.org/10.1016/0304-3940(76)90060-4
Pollet S, Chaix G, Baumann N. Calcium content of mice brain lipids during myelination. Neurosci Lett. 1976 Dec;3(5):311-4. doi: 10.1016/0304-3940(76)90060-4. PMID: 19604904.
Copy Download .nbib Format: NLM
Targeting a Subset of the Membrane Proteome for Top-Down Mass Spectrometry: Introducing the Proteolipidome.

Proteomes

Whitelegge J.
PMID: 32164246
Proteomes. 2020 Mar 10;8(1). doi: 10.3390/proteomes8010005.

A subsection of integral membrane proteins partition into chloroform during a chloroform/methanol/water extraction primarily designed to extract lipids. Traditionally, these proteins were called proteolipids due to their lipid-like properties; the c-subunit of the ATP synthase integral FO component is...

Cite
Whitelegge J. Targeting a Subset of the Membrane Proteome for Top-Down Mass Spectrometry: Introducing the Proteolipidome. Proteomes. 2020;8(1)doi: 10.3390/proteomes8010005.
Whitelegge, J. (2020). Targeting a Subset of the Membrane Proteome for Top-Down Mass Spectrometry: Introducing the Proteolipidome. Proteomes, 8(1), . https://doi.org/10.3390/proteomes8010005
Whitelegge, Julian. "Targeting a Subset of the Membrane Proteome for Top-Down Mass Spectrometry: Introducing the Proteolipidome." Proteomes vol. 8,1 (2020). doi: https://doi.org/10.3390/proteomes8010005
Whitelegge J. Targeting a Subset of the Membrane Proteome for Top-Down Mass Spectrometry: Introducing the Proteolipidome. Proteomes. 2020 Mar 10;8(1). doi: 10.3390/proteomes8010005. PMID: 32164246; PMCID: PMC7151669.
Copy Download .nbib Format: NLM
The breakdown of myelin-bound proteins by intra- and extracellular proteases.

Neurochemical research

Marks N, Grynbaum A, Lajtha A.
PMID: 24271248
Neurochem Res. 1976 Feb;1(1):93-111. doi: 10.1007/BF00965635.

Changes in protein components of purified myelin were measured following incubation in vitro with purified intra- and extracellular enzymes. Incubation with calf brain cathepsin D did not result in a significant relese of acid-soluble peptides as measured by ninhydrin...

Cite
Marks N, Grynbaum A, Lajtha A. The breakdown of myelin-bound proteins by intra- and extracellular proteases. Neurochem Res. 1976;1(1):93-111doi: 10.1007/BF00965635.
Marks, N., Grynbaum, A., & Lajtha, A. (1976). The breakdown of myelin-bound proteins by intra- and extracellular proteases. Neurochemical research, 1(1), 93-111. https://doi.org/10.1007/BF00965635
Marks, N, et al. "The breakdown of myelin-bound proteins by intra- and extracellular proteases." Neurochemical research vol. 1,1 (1976): 93-111. doi: https://doi.org/10.1007/BF00965635
Marks N, Grynbaum A, Lajtha A. The breakdown of myelin-bound proteins by intra- and extracellular proteases. Neurochem Res. 1976 Feb;1(1):93-111. doi: 10.1007/BF00965635. PMID: 24271248.
Copy Download .nbib Format: NLM
Formation of decane-soluble proteolipids: Influence of monovalent and divalent cations.

FEBS letters

Gitler C, Montal M.
PMID: 11946889
FEBS Lett. 1972 Dec 15;28(3):329-332. doi: 10.1016/0014-5793(72)80743-9.

No abstract available.

Cite
Gitler C, Montal M. Formation of decane-soluble proteolipids: Influence of monovalent and divalent cations. FEBS Lett. 1972;28(3):329-332doi: 10.1016/0014-5793(72)80743-9.
Gitler, C., & Montal, M. (1972). Formation of decane-soluble proteolipids: Influence of monovalent and divalent cations. FEBS letters, 28(3), 329-332. https://doi.org/10.1016/0014-5793(72)80743-9
Gitler, C, and Montal, M. "Formation of decane-soluble proteolipids: Influence of monovalent and divalent cations." FEBS letters vol. 28,3 (1972): 329-332. doi: https://doi.org/10.1016/0014-5793(72)80743-9
Gitler C, Montal M. Formation of decane-soluble proteolipids: Influence of monovalent and divalent cations. FEBS Lett. 1972 Dec 15;28(3):329-332. doi: 10.1016/0014-5793(72)80743-9. PMID: 11946889.
Copy Download .nbib Format: NLM
Autoimmune T-cell reactivity to myelin proteolipids and glycolipids in multiple sclerosis.

Multiple sclerosis international

Greer JM.
PMID: 24312732
Mult Scler Int. 2013;2013:151427. doi: 10.1155/2013/151427. Epub 2013 Nov 07.

Central nervous system (CNS) myelin, the likely major target of autoimmune attack in multiple sclerosis (MS), contains a number of unique components that are potential targets of the attack. Two classes of molecules that are greatly enriched in CNS...

Cite
Greer JM. Autoimmune T-cell reactivity to myelin proteolipids and glycolipids in multiple sclerosis. Mult Scler Int. 2013;2013:151427doi: 10.1155/2013/151427.
Greer, J. M. (2013). Autoimmune T-cell reactivity to myelin proteolipids and glycolipids in multiple sclerosis. Multiple sclerosis international, 2013151427. https://doi.org/10.1155/2013/151427
Greer, Judith M. "Autoimmune T-cell reactivity to myelin proteolipids and glycolipids in multiple sclerosis." Multiple sclerosis international vol. 2013 (2013): 151427. doi: https://doi.org/10.1155/2013/151427
Greer JM. Autoimmune T-cell reactivity to myelin proteolipids and glycolipids in multiple sclerosis. Mult Scler Int. 2013;2013:151427. doi: 10.1155/2013/151427. Epub 2013 Nov 07. PMID: 24312732; PMCID: PMC3839122.
Copy Download .nbib Format: NLM
Plasmolipin and Its Role in Cell Processes.

Molecular biology

Shulgin AA, Lebedev TD, Prassolov VS, Spirin PV.
PMID: 34955555
Mol Biol. 2021;55(6):773-785. doi: 10.1134/S0026893321050113. Epub 2021 Dec 17.

The mechanisms involved in the origin and development of malignant and neurodegenerative diseases are an important area of modern biomedicine. A crucial task is to identify new molecular markers that are associated with rearrangements of intracellular signaling and can...

Cite
Shulgin AA, Lebedev TD, Prassolov VS, et al. Plasmolipin and Its Role in Cell Processes. Mol Biol. 2021;55(6):773-785doi: 10.1134/S0026893321050113.
Shulgin, A. A., Lebedev, T. D., Prassolov, V. S., & Spirin, P. V. (2021). Plasmolipin and Its Role in Cell Processes. Molecular biology, 55(6), 773-785. https://doi.org/10.1134/S0026893321050113
Shulgin, A A, et al. "Plasmolipin and Its Role in Cell Processes." Molecular biology vol. 55,6 (2021): 773-785. doi: https://doi.org/10.1134/S0026893321050113
Shulgin AA, Lebedev TD, Prassolov VS, Spirin PV. Plasmolipin and Its Role in Cell Processes. Mol Biol. 2021;55(6):773-785. doi: 10.1134/S0026893321050113. Epub 2021 Dec 17. PMID: 34955555; PMCID: PMC8682038.
Copy Download .nbib Format: NLM
The behavior of proteolipids on dextran gel columns eluted with organic solvents.

Lipids

Prensky AL, Carr S.
PMID: 17805826
Lipids. 1968 Sep;3(5):453-4. doi: 10.1007/BF02531286.

No abstract available.

Cite
Prensky AL, Carr S. The behavior of proteolipids on dextran gel columns eluted with organic solvents. Lipids. 1968;3(5):453-4doi: 10.1007/BF02531286.
Prensky, A. L., & Carr, S. (1968). The behavior of proteolipids on dextran gel columns eluted with organic solvents. Lipids, 3(5), 453-4. https://doi.org/10.1007/BF02531286
Prensky, A L, and Carr, S. "The behavior of proteolipids on dextran gel columns eluted with organic solvents." Lipids vol. 3,5 (1968): 453-4. doi: https://doi.org/10.1007/BF02531286
Prensky AL, Carr S. The behavior of proteolipids on dextran gel columns eluted with organic solvents. Lipids. 1968 Sep;3(5):453-4. doi: 10.1007/BF02531286. PMID: 17805826.
Copy Download .nbib Format: NLM
The rate of incorporation of [S]methionine and [S]cystine into proteolipids and proteins of rat brain.

The Biochemical journal

Gaitonde MK.
PMID: 16748914
Biochem J. 1961 Aug;80(2):277-84. doi: 10.1042/bj0800277.

No abstract available.

Cite
Gaitonde MK. The rate of incorporation of [S]methionine and [S]cystine into proteolipids and proteins of rat brain. Biochem J. 1961;80(2):277-84doi: 10.1042/bj0800277.
Gaitonde, M. K. (1961). The rate of incorporation of [S]methionine and [S]cystine into proteolipids and proteins of rat brain. The Biochemical journal, 80(2), 277-84. https://doi.org/10.1042/bj0800277
Gaitonde, M K. "The rate of incorporation of [S]methionine and [S]cystine into proteolipids and proteins of rat brain." The Biochemical journal vol. 80,2 (1961): 277-84. doi: https://doi.org/10.1042/bj0800277
Gaitonde MK. The rate of incorporation of [S]methionine and [S]cystine into proteolipids and proteins of rat brain. Biochem J. 1961 Aug;80(2):277-84. doi: 10.1042/bj0800277. PMID: 16748914; PMCID: PMC1243994.
Copy Download .nbib Format: NLM
Showing 1 to 12 of 13 entries