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Interaction of Recombinant Gallus gallus SEPT5 and Brain Proteins of H5N1-Avian Influenza Virus-Infected Chickens.

Proteomes

Khairat JE, Balasubramaniam V, Othman I, Omar AR, Hassan SS.
PMID: 28895884
Proteomes. 2017 Sep 12;5(3). doi: 10.3390/proteomes5030023.

Septin forms a conserved family of cytoskeletal guanosine triphosphate (GTP) binding proteins that have diverse roles in protein scaffolding, vesicle trafficking, and cytokinesis. The involvement of septins in infectious viral disease pathogenesis has been demonstrated by the upregulation of...

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Khairat JE, Balasubramaniam V, Othman I, et al. Interaction of Recombinant Gallus gallus SEPT5 and Brain Proteins of H5N1-Avian Influenza Virus-Infected Chickens. Proteomes. 2017;5(3)doi: 10.3390/proteomes5030023.
Khairat, J. E., Balasubramaniam, V., Othman, I., Omar, A. R., & Hassan, S. S. (2017). Interaction of Recombinant Gallus gallus SEPT5 and Brain Proteins of H5N1-Avian Influenza Virus-Infected Chickens. Proteomes, 5(3), . https://doi.org/10.3390/proteomes5030023
Khairat, Jasmine Elanie, et al. "Interaction of Recombinant Gallus gallus SEPT5 and Brain Proteins of H5N1-Avian Influenza Virus-Infected Chickens." Proteomes vol. 5,3 (2017). doi: https://doi.org/10.3390/proteomes5030023
Khairat JE, Balasubramaniam V, Othman I, Omar AR, Hassan SS. Interaction of Recombinant Gallus gallus SEPT5 and Brain Proteins of H5N1-Avian Influenza Virus-Infected Chickens. Proteomes. 2017 Sep 12;5(3). doi: 10.3390/proteomes5030023. PMID: 28895884; PMCID: PMC5620540.
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G-protein Coupled Estrogen Receptor (GPER/GPR30) and Women's Health.

Journal of menopausal medicine

Kim MJ, Kim TH, Lee HH.
PMID: 26357644
J Menopausal Med. 2015 Aug;21(2):79-81. doi: 10.6118/jmm.2015.21.2.79. Epub 2015 Aug 28.

Estrogen - the female sexual hormone playing the most important role - plays a physiologically significant role, not only regulating in cell signals with second messenger but also being active in regulating transcription. Estrogen receptor (ER) which is a...

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Kim MJ, Kim TH, Lee HH. G-protein Coupled Estrogen Receptor (GPER/GPR30) and Women's Health. J Menopausal Med. 2015;21(2):79-81doi: 10.6118/jmm.2015.21.2.79.
Kim, M. J., Kim, T. H., & Lee, H. H. (2015). G-protein Coupled Estrogen Receptor (GPER/GPR30) and Women's Health. Journal of menopausal medicine, 21(2), 79-81. https://doi.org/10.6118/jmm.2015.21.2.79
Kim, Mi-Jin, et al. "G-protein Coupled Estrogen Receptor (GPER/GPR30) and Women's Health." Journal of menopausal medicine vol. 21,2 (2015): 79-81. doi: https://doi.org/10.6118/jmm.2015.21.2.79
Kim MJ, Kim TH, Lee HH. G-protein Coupled Estrogen Receptor (GPER/GPR30) and Women's Health. J Menopausal Med. 2015 Aug;21(2):79-81. doi: 10.6118/jmm.2015.21.2.79. Epub 2015 Aug 28. PMID: 26357644; PMCID: PMC4561744.
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Detection and characterization of GTP-binding proteins in the chloroplast envelope of spinach (Spinacia oleracea).

Physiologia plantarum

Kjellberg JM, Stina Sandelius A.
PMID: 11982945
Physiol Plant. 2002 Jan;114(1):142-148. doi: 10.1046/j.0031-9317.2001.1140119.x.

Proteins binding guanosine triphosphate (GTP) have emerged as important regulators in several cellular processes in plants. To investigate any role of such proteins in chloroplast functions, we subjected envelope, stroma and thylakoid fractions isolated from spinach chloroplasts to two...

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Kjellberg JM, Stina Sandelius A. Detection and characterization of GTP-binding proteins in the chloroplast envelope of spinach (Spinacia oleracea). Physiol Plant. 2002;114(1):142-148doi: 10.1046/j.0031-9317.2001.1140119.x.
Kjellberg, J. M., & Stina Sandelius, A. (2002). Detection and characterization of GTP-binding proteins in the chloroplast envelope of spinach (Spinacia oleracea). Physiologia plantarum, 114(1), 142-148. https://doi.org/10.1046/j.0031-9317.2001.1140119.x
Kjellberg, J. Magnus, and Stina Sandelius, Anna. "Detection and characterization of GTP-binding proteins in the chloroplast envelope of spinach (Spinacia oleracea)." Physiologia plantarum vol. 114,1 (2002): 142-148. doi: https://doi.org/10.1046/j.0031-9317.2001.1140119.x
Kjellberg JM, Stina Sandelius A. Detection and characterization of GTP-binding proteins in the chloroplast envelope of spinach (Spinacia oleracea). Physiol Plant. 2002 Jan;114(1):142-148. doi: 10.1046/j.0031-9317.2001.1140119.x. PMID: 11982945.
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Involvement of GTP-binding protein in the induction of phytoalexin biosynthesis in cultured carrot cells.

Plant science : an international journal of experimental plant biology

Kurosaki F, Yamashita A, Arisawa M.
PMID: 11448758
Plant Sci. 2001 Jul;161(2):273-278. doi: 10.1016/s0168-9452(01)00407-1.

Biosynthetic activity of carrot phytoalexin 6-methoxymellen was induced in cell suspension culture by the treatment with oligogalacturonide elicitor; however, the elicitor-induced activity appreciably reduced in the presence of suramin, a potent inhibitor of GTP-binding proteins. In contrast, addition of...

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Kurosaki F, Yamashita A, Arisawa M. Involvement of GTP-binding protein in the induction of phytoalexin biosynthesis in cultured carrot cells. Plant Sci. 2001;161(2):273-278doi: 10.1016/s0168-9452(01)00407-1.
Kurosaki, F., Yamashita, A., & Arisawa, M. (2001). Involvement of GTP-binding protein in the induction of phytoalexin biosynthesis in cultured carrot cells. Plant science : an international journal of experimental plant biology, 161(2), 273-278. https://doi.org/10.1016/s0168-9452(01)00407-1
Kurosaki, F, et al. "Involvement of GTP-binding protein in the induction of phytoalexin biosynthesis in cultured carrot cells." Plant science : an international journal of experimental plant biology vol. 161,2 (2001): 273-278. doi: https://doi.org/10.1016/s0168-9452(01)00407-1
Kurosaki F, Yamashita A, Arisawa M. Involvement of GTP-binding protein in the induction of phytoalexin biosynthesis in cultured carrot cells. Plant Sci. 2001 Jul;161(2):273-278. doi: 10.1016/s0168-9452(01)00407-1. PMID: 11448758.
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The role of lipid anchors for small G proteins in membrane trafficking.

Trends in cell biology

Magee T, Newman C.
PMID: 14731509
Trends Cell Biol. 1992 Nov;2(11):318-23. doi: 10.1016/0962-8924(92)90172-j.

Small GTP-binding proteins of the Ras superfamily play diverse roles in intracellular trafficking. In order to perform these functions, the proteins must associate with specific donor vesicles and be recycled after fusion of these vesicles with their acceptor membrane...

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Magee T, Newman C. The role of lipid anchors for small G proteins in membrane trafficking. Trends Cell Biol. 1992;2(11):318-23doi: 10.1016/0962-8924(92)90172-j.
Magee, T., & Newman, C. (1992). The role of lipid anchors for small G proteins in membrane trafficking. Trends in cell biology, 2(11), 318-23. https://doi.org/10.1016/0962-8924(92)90172-j
Magee, T, and Newman, C. "The role of lipid anchors for small G proteins in membrane trafficking." Trends in cell biology vol. 2,11 (1992): 318-23. doi: https://doi.org/10.1016/0962-8924(92)90172-j
Magee T, Newman C. The role of lipid anchors for small G proteins in membrane trafficking. Trends Cell Biol. 1992 Nov;2(11):318-23. doi: 10.1016/0962-8924(92)90172-j. PMID: 14731509.
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GTP-binding proteins in intracellular transport.

Trends in cell biology

Pfeffer SR.
PMID: 14731525
Trends Cell Biol. 1992 Feb;2(2):41-6. doi: 10.1016/0962-8924(92)90161-f.

One of the most exciting recent discoveries in the area of intracellular protein transport is the finding that many organelles involved in exocytic and endocytic membrane traffic have one or more Ras-like GTP-binding proteins on their cytoplasmic face that...

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Pfeffer SR. GTP-binding proteins in intracellular transport. Trends Cell Biol. 1992;2(2):41-6doi: 10.1016/0962-8924(92)90161-f.
Pfeffer, S. R. (1992). GTP-binding proteins in intracellular transport. Trends in cell biology, 2(2), 41-6. https://doi.org/10.1016/0962-8924(92)90161-f
Pfeffer, S R. "GTP-binding proteins in intracellular transport." Trends in cell biology vol. 2,2 (1992): 41-6. doi: https://doi.org/10.1016/0962-8924(92)90161-f
Pfeffer SR. GTP-binding proteins in intracellular transport. Trends Cell Biol. 1992 Feb;2(2):41-6. doi: 10.1016/0962-8924(92)90161-f. PMID: 14731525.
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TGN38/41: a molecule on the move.

Trends in cell biology

Stanley KK, Howell KE.
PMID: 14731742
Trends Cell Biol. 1993 Aug;3(8):252-5. doi: 10.1016/0962-8924(93)90046-4.

TGN38/41 is a heterodimeric integral membrane protein that cycles between the trans Golgi network and the cell surface. A tyrosine-containing tetrapeptide motif within its cytoplasmic tail is necessary and sufficient for determining its steady-state location in the TGN. Recent...

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Stanley KK, Howell KE. TGN38/41: a molecule on the move. Trends Cell Biol. 1993;3(8):252-5doi: 10.1016/0962-8924(93)90046-4.
Stanley, K. K., & Howell, K. E. (1993). TGN38/41: a molecule on the move. Trends in cell biology, 3(8), 252-5. https://doi.org/10.1016/0962-8924(93)90046-4
Stanley, K K, and Howell, K E. "TGN38/41: a molecule on the move." Trends in cell biology vol. 3,8 (1993): 252-5. doi: https://doi.org/10.1016/0962-8924(93)90046-4
Stanley KK, Howell KE. TGN38/41: a molecule on the move. Trends Cell Biol. 1993 Aug;3(8):252-5. doi: 10.1016/0962-8924(93)90046-4. PMID: 14731742.
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Expression of GTP-binding proteins and protein kinase C isozymes in platelet-like particles derived from megakaryoblastic leukemia cells (MEG-01).

Platelets

Nagata K, Okano Y, Nozawa Y.
PMID: 16793752
Platelets. 1998;9(5):291-6. doi: 10.1080/09537109876528.

The expression of the various GTP-binding proteins and protein kinase C (PKC) in the platelet-like particles produced by MEG-01 cells was analyzed by RT-PCR and immunoblotting. We selected 14 human low Mr GTPbinding proteins (LMW-GPs) and nine PKCs expressed...

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Nagata K, Okano Y, Nozawa Y. Expression of GTP-binding proteins and protein kinase C isozymes in platelet-like particles derived from megakaryoblastic leukemia cells (MEG-01). Platelets. 1998;9(5):291-6doi: 10.1080/09537109876528.
Nagata, K., Okano, Y., & Nozawa, Y. (1998). Expression of GTP-binding proteins and protein kinase C isozymes in platelet-like particles derived from megakaryoblastic leukemia cells (MEG-01). Platelets, 9(5), 291-6. https://doi.org/10.1080/09537109876528
Nagata, K, et al. "Expression of GTP-binding proteins and protein kinase C isozymes in platelet-like particles derived from megakaryoblastic leukemia cells (MEG-01)." Platelets vol. 9,5 (1998): 291-6. doi: https://doi.org/10.1080/09537109876528
Nagata K, Okano Y, Nozawa Y. Expression of GTP-binding proteins and protein kinase C isozymes in platelet-like particles derived from megakaryoblastic leukemia cells (MEG-01). Platelets. 1998;9(5):291-6. doi: 10.1080/09537109876528. PMID: 16793752.
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Effects of histamine on polyphosphoinositide metabolism in NG108-15 cells.

Neurochemistry international

Tohda M, Nomura Y.
PMID: 20504402
Neurochem Int. 1989;14(1):73-8. doi: 10.1016/0197-0186(89)90012-0.

Effects of histamine on metabolism of phosphatidylinositol and its related phospholipids were studied in NG108-15 cells. Histamine (100 ?M) significantly caused formation of both inositol trisphosphate (IP(3)) and inositol bisphosphate (IP(2)) in NG108-15 cells whose phosphatidylinositol was prelabelled with...

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Tohda M, Nomura Y. Effects of histamine on polyphosphoinositide metabolism in NG108-15 cells. Neurochem Int. 1989;14(1):73-8doi: 10.1016/0197-0186(89)90012-0.
Tohda, M., & Nomura, Y. (1989). Effects of histamine on polyphosphoinositide metabolism in NG108-15 cells. Neurochemistry international, 14(1), 73-8. https://doi.org/10.1016/0197-0186(89)90012-0
Tohda, M, and Nomura, Y. "Effects of histamine on polyphosphoinositide metabolism in NG108-15 cells." Neurochemistry international vol. 14,1 (1989): 73-8. doi: https://doi.org/10.1016/0197-0186(89)90012-0
Tohda M, Nomura Y. Effects of histamine on polyphosphoinositide metabolism in NG108-15 cells. Neurochem Int. 1989;14(1):73-8. doi: 10.1016/0197-0186(89)90012-0. PMID: 20504402.
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Expression of the small GTP-binding protein Rab3A in the adult rat brain.

Molecular and cellular neurosciences

Stettler O, Zahraoui A, Moya KL, Tavitian B.
PMID: 19912893
Mol Cell Neurosci. 1992 Dec;3(6):497-507. doi: 10.1016/1044-7431(92)90062-7.

The ras-related rab genes code for small GTP-binding proteins that are thought to control intracellular membrane trafficking. Some of the rab proteins are localized to the membrane of specific subcellular organelles, and rab3A is associated with small synaptic vesicles....

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Stettler O, Zahraoui A, Moya KL, et al. Expression of the small GTP-binding protein Rab3A in the adult rat brain. Mol Cell Neurosci. 1992;3(6):497-507doi: 10.1016/1044-7431(92)90062-7.
Stettler, O., Zahraoui, A., Moya, K. L., & Tavitian, B. (1992). Expression of the small GTP-binding protein Rab3A in the adult rat brain. Molecular and cellular neurosciences, 3(6), 497-507. https://doi.org/10.1016/1044-7431(92)90062-7
Stettler, O, et al. "Expression of the small GTP-binding protein Rab3A in the adult rat brain." Molecular and cellular neurosciences vol. 3,6 (1992): 497-507. doi: https://doi.org/10.1016/1044-7431(92)90062-7
Stettler O, Zahraoui A, Moya KL, Tavitian B. Expression of the small GTP-binding protein Rab3A in the adult rat brain. Mol Cell Neurosci. 1992 Dec;3(6):497-507. doi: 10.1016/1044-7431(92)90062-7. PMID: 19912893.
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Genetic basis of cognitive disability.

Dialogues in clinical neuroscience

Flint J.
PMID: 22034445
Dialogues Clin Neurosci. 2001 Mar;3(1):37-46.

The importance of genetic influences on cognitive disability has been recognized for a long time, but molecular analysis has only recently begun to yield insights into the pathogenesis of this common and disabling condition. The availability of genome sequences...

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Flint J. Genetic basis of cognitive disability. Dialogues Clin Neurosci. 2001;3(1):37-46
Flint, J. (2001). Genetic basis of cognitive disability. Dialogues in clinical neuroscience, 3(1), 37-46.
Flint, J. "Genetic basis of cognitive disability." Dialogues in clinical neuroscience vol. 3,1 (2001): 37-46.
Flint J. Genetic basis of cognitive disability. Dialogues Clin Neurosci. 2001 Mar;3(1):37-46. PMID: 22034445; PMCID: PMC3181642.
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G proteins as regulators of ion channel function.

Trends in neurosciences

Dunlap K, Holz GG, Rane SG.
PMID: 22241937
Trends Neurosci. 1987 Jun 01;10(6):241-244. doi: 10.1016/0166-2236(87)90166-4.

Virtually unknown just a decade ago, GTP-binding proteins (G proteins) have become a major focus of current research. This family of closely related proteins transduce extracellular signals (such as hormones, neurotransmitters and sensory stimuli) into effector responses (1,2). It...

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Dunlap K, Holz GG, Rane SG. G proteins as regulators of ion channel function. Trends Neurosci. 1987;10(6):241-244doi: 10.1016/0166-2236(87)90166-4.
Dunlap, K., Holz, G. G., & Rane, S. G. (1987). G proteins as regulators of ion channel function. Trends in neurosciences, 10(6), 241-244. https://doi.org/10.1016/0166-2236(87)90166-4
Dunlap, Kathleen, et al. "G proteins as regulators of ion channel function." Trends in neurosciences vol. 10,6 (1987): 241-244. doi: https://doi.org/10.1016/0166-2236(87)90166-4
Dunlap K, Holz GG, Rane SG. G proteins as regulators of ion channel function. Trends Neurosci. 1987 Jun 01;10(6):241-244. doi: 10.1016/0166-2236(87)90166-4. PMID: 22241937; PMCID: PMC3254587.
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Showing 1 to 12 of 135 entries