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Roles of Rap1 signaling in tumor cell migration and invasion.

Cancer biology & medicine

Zhang YL, Wang RC, Cheng K, Ring BZ, Su L.
PMID: 28443208
Cancer Biol Med. 2017 Feb;14(1):90-99. doi: 10.20892/j.issn.2095-3941.2016.0086.

Ras-associated protein-1 (Rap1), a small GTPase in the Ras-related protein family, is an important regulator of basic cellular functions (e.g., formation and control of cell adhesions and junctions), cellular migration, and polarization. Through its interaction with other proteins, Rap1...

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Zhang YL, Wang RC, Cheng K, et al. Roles of Rap1 signaling in tumor cell migration and invasion. Cancer Biol Med. 2017;14(1):90-99doi: 10.20892/j.issn.2095-3941.2016.0086.
Zhang, Y. L., Wang, R. C., Cheng, K., Ring, B. Z., & Su, L. (2017). Roles of Rap1 signaling in tumor cell migration and invasion. Cancer biology & medicine, 14(1), 90-99. https://doi.org/10.20892/j.issn.2095-3941.2016.0086
Zhang, Yi-Lei, et al. "Roles of Rap1 signaling in tumor cell migration and invasion." Cancer biology & medicine vol. 14,1 (2017): 90-99. doi: https://doi.org/10.20892/j.issn.2095-3941.2016.0086
Zhang YL, Wang RC, Cheng K, Ring BZ, Su L. Roles of Rap1 signaling in tumor cell migration and invasion. Cancer Biol Med. 2017 Feb;14(1):90-99. doi: 10.20892/j.issn.2095-3941.2016.0086. PMID: 28443208; PMCID: PMC5365179.
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Structure, Function, Pharmacology, and Therapeutic Potential of the G Protein, Gα/q,11.

Frontiers in cardiovascular medicine

Kamato D, Thach L, Bernard R, Chan V, Zheng W, Kaur H, Brimble M, Osman N, Little PJ.
PMID: 26664886
Front Cardiovasc Med. 2015 Mar 24;2:14. doi: 10.3389/fcvm.2015.00014. eCollection 2015.

G protein coupled receptors (GPCRs) are one of the major classes of cell surface receptors and are associated with a group of G proteins consisting of three subunits termed alpha, beta, and gamma. G proteins are classified into four...

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Kamato D, Thach L, Bernard R, et al. Structure, Function, Pharmacology, and Therapeutic Potential of the G Protein, Gα/q,11. Front Cardiovasc Med. 2015;2:14doi: 10.3389/fcvm.2015.00014.
Kamato, D., Thach, L., Bernard, R., Chan, V., Zheng, W., Kaur, H., Brimble, M., Osman, N., & Little, P. J. (2015). Structure, Function, Pharmacology, and Therapeutic Potential of the G Protein, Gα/q,11. Frontiers in cardiovascular medicine, 214. https://doi.org/10.3389/fcvm.2015.00014
Kamato, Danielle, et al. "Structure, Function, Pharmacology, and Therapeutic Potential of the G Protein, Gα/q,11." Frontiers in cardiovascular medicine vol. 2 (2015): 14. doi: https://doi.org/10.3389/fcvm.2015.00014
Kamato D, Thach L, Bernard R, Chan V, Zheng W, Kaur H, Brimble M, Osman N, Little PJ. Structure, Function, Pharmacology, and Therapeutic Potential of the G Protein, Gα/q,11. Front Cardiovasc Med. 2015 Mar 24;2:14. doi: 10.3389/fcvm.2015.00014. eCollection 2015. PMID: 26664886; PMCID: PMC4671355.
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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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Fenofibrate plus Metformin Produces Cardioprotection in a Type 2 Diabetes and Acute Myocardial Infarction Model.

PPAR research

Oidor-Chan VH, Hong E, Pérez-Severiano F, Montes S, Torres-Narváez JC, Del Valle-Mondragón L, Pastelín-Hernández G, Sánchez-Mendoza A.
PMID: 27069466
PPAR Res. 2016;2016:8237264. doi: 10.1155/2016/8237264. Epub 2016 Mar 16.

We investigated whether fenofibrate, metformin, and their combination generate cardioprotection in a rat model of type 2 diabetes (T2D) and acute myocardial infarction (AMI). Streptozotocin-induced diabetic- (DB-) rats received 14 days of either vehicle, fenofibrate, metformin, or their combination...

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Oidor-Chan VH, Hong E, Pérez-Severiano F, et al. Fenofibrate plus Metformin Produces Cardioprotection in a Type 2 Diabetes and Acute Myocardial Infarction Model. PPAR Res. 2016;2016:8237264doi: 10.1155/2016/8237264.
Oidor-Chan, V. H., Hong, E., Pérez-Severiano, F., Montes, S., Torres-Narváez, J. C., Del Valle-Mondragón, L., Pastelín-Hernández, G., & Sánchez-Mendoza, A. (2016). Fenofibrate plus Metformin Produces Cardioprotection in a Type 2 Diabetes and Acute Myocardial Infarction Model. PPAR research, 20168237264. https://doi.org/10.1155/2016/8237264
Oidor-Chan, Víctor Hugo, et al. "Fenofibrate plus Metformin Produces Cardioprotection in a Type 2 Diabetes and Acute Myocardial Infarction Model." PPAR research vol. 2016 (2016): 8237264. doi: https://doi.org/10.1155/2016/8237264
Oidor-Chan VH, Hong E, Pérez-Severiano F, Montes S, Torres-Narváez JC, Del Valle-Mondragón L, Pastelín-Hernández G, Sánchez-Mendoza A. Fenofibrate plus Metformin Produces Cardioprotection in a Type 2 Diabetes and Acute Myocardial Infarction Model. PPAR Res. 2016;2016:8237264. doi: 10.1155/2016/8237264. Epub 2016 Mar 16. PMID: 27069466; PMCID: PMC4812489.
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Influence of nucleoside triphosphates, inorganic salts, NADH, catecholamines, and oxygen saturation on nitrite-induced oxidation of rainbow trout haemoglobin.

Fish physiology and biochemistry

Jensen FB.
PMID: 24202690
Fish Physiol Biochem. 1993 Aug;12(2):111-7. doi: 10.1007/BF00004376.

Oxidation of rainbow trout haemoglobin (Hb) by nitrite proceeded via an initial lag phase followed by autocatalysis when the O2 saturation of the Hb was high. At low O2 saturations, the rate of methaemoglobin (metHb) formation was strongly reduced...

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Jensen FB. Influence of nucleoside triphosphates, inorganic salts, NADH, catecholamines, and oxygen saturation on nitrite-induced oxidation of rainbow trout haemoglobin. Fish Physiol Biochem. 1993;12(2):111-7doi: 10.1007/BF00004376.
Jensen, F. B. (1993). Influence of nucleoside triphosphates, inorganic salts, NADH, catecholamines, and oxygen saturation on nitrite-induced oxidation of rainbow trout haemoglobin. Fish physiology and biochemistry, 12(2), 111-7. https://doi.org/10.1007/BF00004376
Jensen, F B. "Influence of nucleoside triphosphates, inorganic salts, NADH, catecholamines, and oxygen saturation on nitrite-induced oxidation of rainbow trout haemoglobin." Fish physiology and biochemistry vol. 12,2 (1993): 111-7. doi: https://doi.org/10.1007/BF00004376
Jensen FB. Influence of nucleoside triphosphates, inorganic salts, NADH, catecholamines, and oxygen saturation on nitrite-induced oxidation of rainbow trout haemoglobin. Fish Physiol Biochem. 1993 Aug;12(2):111-7. doi: 10.1007/BF00004376. PMID: 24202690.
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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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Aminoacyl-tRNA-dependent interaction of a transfer enzyme from yeast with a complex formed by two other transfer factors with guanosine triphosphate.

FEBS letters

Richter D, Klink F.
PMID: 11946266
FEBS Lett. 1968 Nov;2(1):49-52. doi: 10.1016/0014-5793(68)80098-5.

No abstract available.

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Richter D, Klink F. Aminoacyl-tRNA-dependent interaction of a transfer enzyme from yeast with a complex formed by two other transfer factors with guanosine triphosphate. FEBS Lett. 1968;2(1):49-52doi: 10.1016/0014-5793(68)80098-5.
Richter, D., & Klink, F. (1968). Aminoacyl-tRNA-dependent interaction of a transfer enzyme from yeast with a complex formed by two other transfer factors with guanosine triphosphate. FEBS letters, 2(1), 49-52. https://doi.org/10.1016/0014-5793(68)80098-5
Richter, D, and Klink, F. "Aminoacyl-tRNA-dependent interaction of a transfer enzyme from yeast with a complex formed by two other transfer factors with guanosine triphosphate." FEBS letters vol. 2,1 (1968): 49-52. doi: https://doi.org/10.1016/0014-5793(68)80098-5
Richter D, Klink F. Aminoacyl-tRNA-dependent interaction of a transfer enzyme from yeast with a complex formed by two other transfer factors with guanosine triphosphate. FEBS Lett. 1968 Nov;2(1):49-52. doi: 10.1016/0014-5793(68)80098-5. PMID: 11946266.
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Amino Acid incorporation by wheat chloroplasts.

Plant physiology

Bamji MS, Jagendorf AT.
PMID: 16656318
Plant Physiol. 1966 May;41(5):764-70. doi: 10.1104/pp.41.5.764.

Isolated chloroplasts from wheat leaves incorporate radioactive amino acids into protein. Both physiological and biochemical evidence show that contaminating bacteria are not responsible for the activity. Activity is best in plastids from 5-day-old or younger seedlings; a sharp drop...

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Bamji MS, Jagendorf AT. Amino Acid incorporation by wheat chloroplasts. Plant Physiol. 1966;41(5):764-70doi: 10.1104/pp.41.5.764.
Bamji, M. S., & Jagendorf, A. T. (1966). Amino Acid incorporation by wheat chloroplasts. Plant physiology, 41(5), 764-70. https://doi.org/10.1104/pp.41.5.764
Bamji, M S, and Jagendorf, A T. "Amino Acid incorporation by wheat chloroplasts." Plant physiology vol. 41,5 (1966): 764-70. doi: https://doi.org/10.1104/pp.41.5.764
Bamji MS, Jagendorf AT. Amino Acid incorporation by wheat chloroplasts. Plant Physiol. 1966 May;41(5):764-70. doi: 10.1104/pp.41.5.764. PMID: 16656318; PMCID: PMC1086421.
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A soluble fraction requirement in the transfer reaction of protein synthesis by rice embryo ribosomes.

Plant physiology

App AA, Gerosa MM.
PMID: 16656417
Plant Physiol. 1966 Nov;41(9):1420-4. doi: 10.1104/pp.41.9.1420.

The requirements for the transfer of (14)C-phenylalanine from yeast soluble ribonucleic acid to protein in vitro by rice (Oryza sativa L. var. Bluebonnet) ribosomes have been investigated. An absolute requirement for polyuridylic acid, 2-mercaptoethanol, guanosine triphosphate, magnesium, and potassium...

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App AA, Gerosa MM. A soluble fraction requirement in the transfer reaction of protein synthesis by rice embryo ribosomes. Plant Physiol. 1966;41(9):1420-4doi: 10.1104/pp.41.9.1420.
App, A. A., & Gerosa, M. M. (1966). A soluble fraction requirement in the transfer reaction of protein synthesis by rice embryo ribosomes. Plant physiology, 41(9), 1420-4. https://doi.org/10.1104/pp.41.9.1420
App, A A, and Gerosa, M M. "A soluble fraction requirement in the transfer reaction of protein synthesis by rice embryo ribosomes." Plant physiology vol. 41,9 (1966): 1420-4. doi: https://doi.org/10.1104/pp.41.9.1420
App AA, Gerosa MM. A soluble fraction requirement in the transfer reaction of protein synthesis by rice embryo ribosomes. Plant Physiol. 1966 Nov;41(9):1420-4. doi: 10.1104/pp.41.9.1420. PMID: 16656417; PMCID: PMC550547.
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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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Molecular connections between nuclear and ciliary import processes.

Cilia

Kee HL, Verhey KJ.
PMID: 23985042
Cilia. 2013 Aug 28;2(1):11. doi: 10.1186/2046-2530-2-11.

As an organelle, the cilium contains a unique complement of protein and lipid. Recent work has begun to shed light on the mechanisms that regulate entry of ciliary proteins into the compartment. Here, we focus on the mechanisms that...

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Kee HL, Verhey KJ. Molecular connections between nuclear and ciliary import processes. Cilia. 2013;2(1):11doi: 10.1186/2046-2530-2-11.
Kee, H. L., & Verhey, K. J. (2013). Molecular connections between nuclear and ciliary import processes. Cilia, 2(1), 11. https://doi.org/10.1186/2046-2530-2-11
Kee, H Lynn, and Verhey, Kristen J. "Molecular connections between nuclear and ciliary import processes." Cilia vol. 2,1 (2013): 11. doi: https://doi.org/10.1186/2046-2530-2-11
Kee HL, Verhey KJ. Molecular connections between nuclear and ciliary import processes. Cilia. 2013 Aug 28;2(1):11. doi: 10.1186/2046-2530-2-11. PMID: 23985042; PMCID: PMC3765448.
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Localization of adenylate kinase 4 in mouse tissues.

Acta histochemica et cytochemica

Miyoshi K, Akazawa Y, Horiguchi T, Noma T.
PMID: 19492028
Acta Histochem Cytochem. 2009 Apr 28;42(2):55-64. doi: 10.1267/ahc.08012. Epub 2009 Apr 07.

Adenylate kinase (AK) is a key enzyme in the high-energy phosphoryl transfer reaction in living cells. Of its isoforms, AK4 has a similar sequence and subcellular localization to that of AK3 in the mitochondrial matrix. However, unlike AK3, AK4...

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Miyoshi K, Akazawa Y, Horiguchi T, et al. Localization of adenylate kinase 4 in mouse tissues. Acta Histochem Cytochem. 2009;42(2):55-64doi: 10.1267/ahc.08012.
Miyoshi, K., Akazawa, Y., Horiguchi, T., & Noma, T. (2009). Localization of adenylate kinase 4 in mouse tissues. Acta histochemica et cytochemica, 42(2), 55-64. https://doi.org/10.1267/ahc.08012
Miyoshi, Keiko, et al. "Localization of adenylate kinase 4 in mouse tissues." Acta histochemica et cytochemica vol. 42,2 (2009): 55-64. doi: https://doi.org/10.1267/ahc.08012
Miyoshi K, Akazawa Y, Horiguchi T, Noma T. Localization of adenylate kinase 4 in mouse tissues. Acta Histochem Cytochem. 2009 Apr 28;42(2):55-64. doi: 10.1267/ahc.08012. Epub 2009 Apr 07. PMID: 19492028; PMCID: PMC2685024.
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Showing 1 to 12 of 144 entries