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Septin Polymerization Slows Synaptic Vesicle Recycling in Motor Nerve Endings.

Acta naturae

Grigoryev PN, Khisamieva GA, Zefirov AL.
PMID: 31413880
Acta Naturae. 2019 Apr-Jun;11(2):54-62. doi: 10.32607/20758251-2019-11-2-54-62.

Septins are GTP-binding proteins recognized as a component of the cytoskeleton. Despite the fact that septins are highly expressed by neurons and can interact with the proteins that participate in synaptic vesicle exocytosis and endocytosis, the role of septins...

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Grigoryev PN, Khisamieva GA, Zefirov AL. Septin Polymerization Slows Synaptic Vesicle Recycling in Motor Nerve Endings. Acta Naturae. 2019;11(2):54-62doi: 10.32607/20758251-2019-11-2-54-62.
Grigoryev, P. N., Khisamieva, G. A., & Zefirov, A. L. (2019). Septin Polymerization Slows Synaptic Vesicle Recycling in Motor Nerve Endings. Acta naturae, 11(2), 54-62. https://doi.org/10.32607/20758251-2019-11-2-54-62
Grigoryev, P N, et al. "Septin Polymerization Slows Synaptic Vesicle Recycling in Motor Nerve Endings." Acta naturae vol. 11,2 (2019): 54-62. doi: https://doi.org/10.32607/20758251-2019-11-2-54-62
Grigoryev PN, Khisamieva GA, Zefirov AL. Septin Polymerization Slows Synaptic Vesicle Recycling in Motor Nerve Endings. Acta Naturae. 2019 Apr-Jun;11(2):54-62. doi: 10.32607/20758251-2019-11-2-54-62. PMID: 31413880; PMCID: PMC6643342.
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G-protein β3-subunit gene variant, blood pressure and erythrocyte sodium/lithium countertransport in essential hypertension.

British journal of biomedical science

Poch E, González-Núñez D, Compte M, Sierra A.
PMID: 27786112
Br J Biomed Sci. 2002 Jan;59(2):101-104. doi: 10.1080/09674845.2002.11783643.

Recently, a C825T polymorphism in the gene coding for the β3 subunit of G proteins (GNB3) has been described in cells from patients with essential hypertension and enhanced Na

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Poch E, González-Núñez D, Compte M, et al. G-protein β3-subunit gene variant, blood pressure and erythrocyte sodium/lithium countertransport in essential hypertension. Br J Biomed Sci. 2002;59(2):101-104doi: 10.1080/09674845.2002.11783643.
Poch, E., González-Núñez, D., Compte, M., & Sierra, A. (2002). G-protein β3-subunit gene variant, blood pressure and erythrocyte sodium/lithium countertransport in essential hypertension. British journal of biomedical science, 59(2), 101-104. https://doi.org/10.1080/09674845.2002.11783643
Poch, Esteban, et al. "G-protein β3-subunit gene variant, blood pressure and erythrocyte sodium/lithium countertransport in essential hypertension." British journal of biomedical science vol. 59,2 (2002): 101-104. doi: https://doi.org/10.1080/09674845.2002.11783643
Poch E, González-Núñez D, Compte M, Sierra A. G-protein β3-subunit gene variant, blood pressure and erythrocyte sodium/lithium countertransport in essential hypertension. Br J Biomed Sci. 2002 Jan;59(2):101-104. doi: 10.1080/09674845.2002.11783643. PMID: 27786112.
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Septin Mutations in Human Cancers.

Frontiers in cell and developmental biology

Angelis D, Spiliotis ET.
PMID: 27882315
Front Cell Dev Biol. 2016 Nov 09;4:122. doi: 10.3389/fcell.2016.00122. eCollection 2016.

Septins are GTP-binding proteins that are evolutionarily and structurally related to the

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Angelis D, Spiliotis ET. Septin Mutations in Human Cancers. Front Cell Dev Biol. 2016;4:122doi: 10.3389/fcell.2016.00122.
Angelis, D., & Spiliotis, E. T. (2016). Septin Mutations in Human Cancers. Frontiers in cell and developmental biology, 4122. https://doi.org/10.3389/fcell.2016.00122
Angelis, Dimitrios, and Spiliotis, Elias T. "Septin Mutations in Human Cancers." Frontiers in cell and developmental biology vol. 4 (2016): 122. doi: https://doi.org/10.3389/fcell.2016.00122
Angelis D, Spiliotis ET. Septin Mutations in Human Cancers. Front Cell Dev Biol. 2016 Nov 09;4:122. doi: 10.3389/fcell.2016.00122. eCollection 2016. PMID: 27882315; PMCID: PMC5101219.
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Role of Septins in Endothelial Cells and Platelets.

Frontiers in cell and developmental biology

Neubauer K, Zieger B.
PMID: 34858990
Front Cell Dev Biol. 2021 Nov 11;9:768409. doi: 10.3389/fcell.2021.768409. eCollection 2021.

Septins are conserved cytoskeletal GTP-binding proteins identified in almost all eukaryotes except higher plants. Mammalian septins comprise 13 family members with either ubiquitous or organ- and tissue-specific expression patterns. They form filamentous oligomers and complexes with other proteins to...

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Neubauer K, Zieger B. Role of Septins in Endothelial Cells and Platelets. Front Cell Dev Biol. 2021;9:768409doi: 10.3389/fcell.2021.768409.
Neubauer, K., & Zieger, B. (2021). Role of Septins in Endothelial Cells and Platelets. Frontiers in cell and developmental biology, 9768409. https://doi.org/10.3389/fcell.2021.768409
Neubauer, Katharina, and Zieger, Barbara. "Role of Septins in Endothelial Cells and Platelets." Frontiers in cell and developmental biology vol. 9 (2021): 768409. doi: https://doi.org/10.3389/fcell.2021.768409
Neubauer K, Zieger B. Role of Septins in Endothelial Cells and Platelets. Front Cell Dev Biol. 2021 Nov 11;9:768409. doi: 10.3389/fcell.2021.768409. eCollection 2021. PMID: 34858990; PMCID: PMC8632023.
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Phytochrome-regulated expression of the genes encoding the small GTP-binding proteins in peas.

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

Yoshida K, Nagano Y, Murai N, Sasaki Y.
PMID: 11607412
Proc Natl Acad Sci U S A. 1993 Jul 15;90(14):6636-40. doi: 10.1073/pnas.90.14.6636.

We examined the effect of light on the mRNA levels of 11 genes (pra1-pra9A, pra9B, and pra9C) encoding the small GTP-binding proteins that belong to the ras superfamily in Pisum sativum. When the dark-grown seedlings were exposed to continuous...

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Yoshida K, Nagano Y, Murai N, et al. Phytochrome-regulated expression of the genes encoding the small GTP-binding proteins in peas. Proc Natl Acad Sci U S A. 1993;90(14):6636-40doi: 10.1073/pnas.90.14.6636.
Yoshida, K., Nagano, Y., Murai, N., & Sasaki, Y. (1993). Phytochrome-regulated expression of the genes encoding the small GTP-binding proteins in peas. Proceedings of the National Academy of Sciences of the United States of America, 90(14), 6636-40. https://doi.org/10.1073/pnas.90.14.6636
Yoshida, K, et al. "Phytochrome-regulated expression of the genes encoding the small GTP-binding proteins in peas." Proceedings of the National Academy of Sciences of the United States of America vol. 90,14 (1993): 6636-40. doi: https://doi.org/10.1073/pnas.90.14.6636
Yoshida K, Nagano Y, Murai N, Sasaki Y. Phytochrome-regulated expression of the genes encoding the small GTP-binding proteins in peas. Proc Natl Acad Sci U S A. 1993 Jul 15;90(14):6636-40. doi: 10.1073/pnas.90.14.6636. PMID: 11607412; PMCID: PMC46987.
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Plant Defense Response to Fungal Pathogens (Activation of Host-Plasma Membrane H+-ATPase by Elicitor-Induced Enzyme Dephosphorylation).

Plant physiology

Vera-Estrella R, Barkla BJ, Higgins VJ, Blumwald E.
PMID: 12232073
Plant Physiol. 1994 Jan;104(1):209-215. doi: 10.1104/pp.104.1.209.

Elicitor preparations containing the avr5 gene products from race 4 of Cladosporium fulvum and tomato (Lycopersicon esculentum L.) cells near isogenic for the resistance gene Cf5 were used to investigate events following the treatment of host plasma membranes with...

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Vera-Estrella R, Barkla BJ, Higgins VJ, et al. Plant Defense Response to Fungal Pathogens (Activation of Host-Plasma Membrane H+-ATPase by Elicitor-Induced Enzyme Dephosphorylation). Plant Physiol. 1994;104(1):209-215doi: 10.1104/pp.104.1.209.
Vera-Estrella, R., Barkla, B. J., Higgins, V. J., & Blumwald, E. (1994). Plant Defense Response to Fungal Pathogens (Activation of Host-Plasma Membrane H+-ATPase by Elicitor-Induced Enzyme Dephosphorylation). Plant physiology, 104(1), 209-215. https://doi.org/10.1104/pp.104.1.209
Vera-Estrella, R., et al. "Plant Defense Response to Fungal Pathogens (Activation of Host-Plasma Membrane H+-ATPase by Elicitor-Induced Enzyme Dephosphorylation)." Plant physiology vol. 104,1 (1994): 209-215. doi: https://doi.org/10.1104/pp.104.1.209
Vera-Estrella R, Barkla BJ, Higgins VJ, Blumwald E. Plant Defense Response to Fungal Pathogens (Activation of Host-Plasma Membrane H+-ATPase by Elicitor-Induced Enzyme Dephosphorylation). Plant Physiol. 1994 Jan;104(1):209-215. doi: 10.1104/pp.104.1.209. PMID: 12232073; PMCID: PMC159179.
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Small GTP-Binding Proteins and Membrane Biogenesis in Plants.

Plant physiology

Verma D, Cheon C, Hong Z.
PMID: 12232299
Plant Physiol. 1994 Sep;106(1):1-6. doi: 10.1104/pp.106.1.1.

No abstract available.

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Verma D, Cheon C, Hong Z. Small GTP-Binding Proteins and Membrane Biogenesis in Plants. Plant Physiol. 1994;106(1):1-6doi: 10.1104/pp.106.1.1.
Verma, D., Cheon, C., & Hong, Z. (1994). Small GTP-Binding Proteins and Membrane Biogenesis in Plants. Plant physiology, 106(1), 1-6. https://doi.org/10.1104/pp.106.1.1
Verma, DPS., et al. "Small GTP-Binding Proteins and Membrane Biogenesis in Plants." Plant physiology vol. 106,1 (1994): 1-6. doi: https://doi.org/10.1104/pp.106.1.1
Verma D, Cheon C, Hong Z. Small GTP-Binding Proteins and Membrane Biogenesis in Plants. Plant Physiol. 1994 Sep;106(1):1-6. doi: 10.1104/pp.106.1.1. PMID: 12232299; PMCID: PMC159492.
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Septin-2 is overexpressed in epithelial ovarian cancer and mediates proliferation via regulation of cellular metabolic proteins.

Oncotarget

James NE, Cantillo E, Yano N, Chichester CO, DiSilvestro PA, Hovanesian V, Rao RSP, Kim KK, Moore RG, Ahsan N, Ribeiro JR.
PMID: 31105878
Oncotarget. 2019 Apr 26;10(31):2959-2972. doi: 10.18632/oncotarget.26836. eCollection 2019 Apr 26.

Epithelial Ovarian Cancer (EOC) is associated with dismal survival rates due to the fact that patients are frequently diagnosed at an advanced stage and eventually become resistant to traditional chemotherapeutics. Hence, there is a crucial need for new and...

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James NE, Cantillo E, Yano N, et al. Septin-2 is overexpressed in epithelial ovarian cancer and mediates proliferation via regulation of cellular metabolic proteins. Oncotarget. 2019;10(31):2959-2972doi: 10.18632/oncotarget.26836.
James, N. E., Cantillo, E., Yano, N., Chichester, C. O., DiSilvestro, P. A., Hovanesian, V., Rao, R. S. P., Kim, K. K., Moore, R. G., Ahsan, N., & Ribeiro, J. R. (2019). Septin-2 is overexpressed in epithelial ovarian cancer and mediates proliferation via regulation of cellular metabolic proteins. Oncotarget, 10(31), 2959-2972. https://doi.org/10.18632/oncotarget.26836
James, Nicole E, et al. "Septin-2 is overexpressed in epithelial ovarian cancer and mediates proliferation via regulation of cellular metabolic proteins." Oncotarget vol. 10,31 (2019): 2959-2972. doi: https://doi.org/10.18632/oncotarget.26836
James NE, Cantillo E, Yano N, Chichester CO, DiSilvestro PA, Hovanesian V, Rao RSP, Kim KK, Moore RG, Ahsan N, Ribeiro JR. Septin-2 is overexpressed in epithelial ovarian cancer and mediates proliferation via regulation of cellular metabolic proteins. Oncotarget. 2019 Apr 26;10(31):2959-2972. doi: 10.18632/oncotarget.26836. eCollection 2019 Apr 26. PMID: 31105878; PMCID: PMC6508204.
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Regulation of Cytoskeleton and Cell Adhesions by the Small GTPase Rho and Its Targets.

Trends in cardiovascular medicine

Amano M, Fukata Y, Kaibuchi K.
PMID: 21235928
Trends Cardiovasc Med. 1998 May;8(4):162-8. doi: 10.1016/S1050-1738(97)00145-X.

The Rho GTPase is a member of the Rho family, which belongs to the Ras superfamily of GTP-binding proteins. Like other GTP-binding proteins, Rho exhibits both GDP/GTP-binding activities and functions as a molecular switch, cycling between an inactive GDP-bound...

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Amano M, Fukata Y, Kaibuchi K. Regulation of Cytoskeleton and Cell Adhesions by the Small GTPase Rho and Its Targets. Trends Cardiovasc Med. 1998;8(4):162-8doi: 10.1016/S1050-1738(97)00145-X.
Amano, M., Fukata, Y., & Kaibuchi, K. (1998). Regulation of Cytoskeleton and Cell Adhesions by the Small GTPase Rho and Its Targets. Trends in cardiovascular medicine, 8(4), 162-8. https://doi.org/10.1016/S1050-1738(97)00145-X
Amano, M, et al. "Regulation of Cytoskeleton and Cell Adhesions by the Small GTPase Rho and Its Targets." Trends in cardiovascular medicine vol. 8,4 (1998): 162-8. doi: https://doi.org/10.1016/S1050-1738(97)00145-X
Amano M, Fukata Y, Kaibuchi K. Regulation of Cytoskeleton and Cell Adhesions by the Small GTPase Rho and Its Targets. Trends Cardiovasc Med. 1998 May;8(4):162-8. doi: 10.1016/S1050-1738(97)00145-X. PMID: 21235928.
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Protein translocation across chloroplast envelope membranes.

Trends in cell biology

Gray JC, Row PE.
PMID: 14732129
Trends Cell Biol. 1995 Jun;5(6):243-7. doi: 10.1016/s0962-8924(00)89018-2.

Nuclear-encoded chloroplast proteins are imported from the cytosol into the chloroplast stroma by a common translocation machinery. Several components of the import apparatus, including GTP-binding proteins and Hsp70 proteins, have recently been identified and characterized. This review discusses the...

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Gray JC, Row PE. Protein translocation across chloroplast envelope membranes. Trends Cell Biol. 1995;5(6):243-7doi: 10.1016/s0962-8924(00)89018-2.
Gray, J. C., & Row, P. E. (1995). Protein translocation across chloroplast envelope membranes. Trends in cell biology, 5(6), 243-7. https://doi.org/10.1016/s0962-8924(00)89018-2
Gray, J C, and Row, P E. "Protein translocation across chloroplast envelope membranes." Trends in cell biology vol. 5,6 (1995): 243-7. doi: https://doi.org/10.1016/s0962-8924(00)89018-2
Gray JC, Row PE. Protein translocation across chloroplast envelope membranes. Trends Cell Biol. 1995 Jun;5(6):243-7. doi: 10.1016/s0962-8924(00)89018-2. PMID: 14732129.
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G proteins and low-molecular-weight GTP-binding proteins in platelets.

Trends in cardiovascular medicine

Brass LF, Manning DR.
PMID: 21239337
Trends Cardiovasc Med. 1991 Mar;1(2):92-8. doi: 10.1016/1050-1738(91)90017-9.

Platelets contain at least two distinct families of proteins that can bind GTP: the G proteins and the low-molecular-weight GTP-binding proteins. G proteins are heterotrimeric regulatory proteins that mediate the interaction between cell surface receptors and the enzymes that...

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Brass LF, Manning DR. G proteins and low-molecular-weight GTP-binding proteins in platelets. Trends Cardiovasc Med. 1991;1(2):92-8doi: 10.1016/1050-1738(91)90017-9.
Brass, L. F., & Manning, D. R. (1991). G proteins and low-molecular-weight GTP-binding proteins in platelets. Trends in cardiovascular medicine, 1(2), 92-8. https://doi.org/10.1016/1050-1738(91)90017-9
Brass, L F, and Manning, D R. "G proteins and low-molecular-weight GTP-binding proteins in platelets." Trends in cardiovascular medicine vol. 1,2 (1991): 92-8. doi: https://doi.org/10.1016/1050-1738(91)90017-9
Brass LF, Manning DR. G proteins and low-molecular-weight GTP-binding proteins in platelets. Trends Cardiovasc Med. 1991 Mar;1(2):92-8. doi: 10.1016/1050-1738(91)90017-9. PMID: 21239337.
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Small GTP-Binding Proteins of the Rho Family in the Dictyostelium Cytoskeleton.

Protist

Rivero F, Noegel AA.
PMID: 23196108
Protist. 1998 Feb;149(1):11-5. doi: 10.1016/S1434-4610(98)70004-5. Epub 2009 Jul 13.

No abstract available.

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Rivero F, Noegel AA. Small GTP-Binding Proteins of the Rho Family in the Dictyostelium Cytoskeleton. Protist. 2009;149(1):11-5doi: 10.1016/S1434-4610(98)70004-5.
Rivero, F., & Noegel, A. A. (1998). Small GTP-Binding Proteins of the Rho Family in the Dictyostelium Cytoskeleton. Protist, 149(1), 11-5. https://doi.org/10.1016/S1434-4610(98)70004-5
Rivero, F, and Noegel, A A. "Small GTP-Binding Proteins of the Rho Family in the Dictyostelium Cytoskeleton." Protist vol. 149,1 (1998): 11-5. doi: https://doi.org/10.1016/S1434-4610(98)70004-5
Rivero F, Noegel AA. Small GTP-Binding Proteins of the Rho Family in the Dictyostelium Cytoskeleton. Protist. 1998 Feb;149(1):11-5. doi: 10.1016/S1434-4610(98)70004-5. Epub 2009 Jul 13. PMID: 23196108.
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Showing 25 to 36 of 135 entries