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A study of adenylate kinase locus 1 (ak 1 ) genetic polymorphism in diabetic pregnancy.

Journal of reproduction & infertility

Gloria-Bottini F, Pietropolli A, Neri A, Coppeta L, Magrini A, Bottini E.
PMID: 25202675
J Reprod Infertil. 2014 Jul;15(3):161-4.

BACKGROUND: Previous studies suggest that adenylate kinase locus 1 (Ak 1 ) has an important role in the control of blood glucose level and in the glycation of structural and functional proteins in type 2 diabetes and in the...

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Gloria-Bottini F, Pietropolli A, Neri A, et al. A study of adenylate kinase locus 1 (ak 1 ) genetic polymorphism in diabetic pregnancy. J Reprod Infertil. 2014;15(3):161-4
Gloria-Bottini, F., Pietropolli, A., Neri, A., Coppeta, L., Magrini, A., & Bottini, E. (2014). A study of adenylate kinase locus 1 (ak 1 ) genetic polymorphism in diabetic pregnancy. Journal of reproduction & infertility, 15(3), 161-4.
Gloria-Bottini, Fulvia, et al. "A study of adenylate kinase locus 1 (ak 1 ) genetic polymorphism in diabetic pregnancy." Journal of reproduction & infertility vol. 15,3 (2014): 161-4.
Gloria-Bottini F, Pietropolli A, Neri A, Coppeta L, Magrini A, Bottini E. A study of adenylate kinase locus 1 (ak 1 ) genetic polymorphism in diabetic pregnancy. J Reprod Infertil. 2014 Jul;15(3):161-4. PMID: 25202675; PMCID: PMC4138424.
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The intracellular distribution of adenylate kinase in the leaves of spinach, wheat and barley.

Planta

Birkenhead K, Walker D, Foyer C.
PMID: 24272313
Planta. 1982 Nov;156(2):171-5. doi: 10.1007/BF00395432.

Of the total adenylate-kinase activity in 10-d-old barley and wheat leaves, 40-50% is localised in the chloroplasts, while in mature spinach leaves 50-70% of the enzyme is chloroplastic. The extra-chloroplastic adenylate-kinase activity is associated with the mitochondria, very little,...

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Birkenhead K, Walker D, Foyer C. The intracellular distribution of adenylate kinase in the leaves of spinach, wheat and barley. Planta. 1982;156(2):171-5doi: 10.1007/BF00395432.
Birkenhead, K., Walker, D., & Foyer, C. (1982). The intracellular distribution of adenylate kinase in the leaves of spinach, wheat and barley. Planta, 156(2), 171-5. https://doi.org/10.1007/BF00395432
Birkenhead, K, et al. "The intracellular distribution of adenylate kinase in the leaves of spinach, wheat and barley." Planta vol. 156,2 (1982): 171-5. doi: https://doi.org/10.1007/BF00395432
Birkenhead K, Walker D, Foyer C. The intracellular distribution of adenylate kinase in the leaves of spinach, wheat and barley. Planta. 1982 Nov;156(2):171-5. doi: 10.1007/BF00395432. PMID: 24272313.
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Cooperation and Competition between Adenylate Kinase, Nucleoside Diphosphokinase, Electron Transport, and ATP Synthase in Plant Mitochondria Studied by 31P-Nuclear Magnetic Resonance.

Plant physiology

Roberts J, Aubert S, Gout E, Bligny R, Douce R.
PMID: 12223600
Plant Physiol. 1997 Jan;113(1):191-199. doi: 10.1104/pp.113.1.191.

Nucleotide metabolism in potato (Solanum tuberosum) mitochondria was studied using 31P-nuclear magnetic resonance spectroscopy and the O2 electrode. Immediately following the addition of ADP, ATP synthesis exceeded the rate of oxidative phosphorylation, fueled by succinate oxidation, due to mitochondrial...

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Roberts J, Aubert S, Gout E, et al. Cooperation and Competition between Adenylate Kinase, Nucleoside Diphosphokinase, Electron Transport, and ATP Synthase in Plant Mitochondria Studied by 31P-Nuclear Magnetic Resonance. Plant Physiol. 1997;113(1):191-199doi: 10.1104/pp.113.1.191.
Roberts, J., Aubert, S., Gout, E., Bligny, R., & Douce, R. (1997). Cooperation and Competition between Adenylate Kinase, Nucleoside Diphosphokinase, Electron Transport, and ATP Synthase in Plant Mitochondria Studied by 31P-Nuclear Magnetic Resonance. Plant physiology, 113(1), 191-199. https://doi.org/10.1104/pp.113.1.191
Roberts, JKM., et al. "Cooperation and Competition between Adenylate Kinase, Nucleoside Diphosphokinase, Electron Transport, and ATP Synthase in Plant Mitochondria Studied by 31P-Nuclear Magnetic Resonance." Plant physiology vol. 113,1 (1997): 191-199. doi: https://doi.org/10.1104/pp.113.1.191
Roberts J, Aubert S, Gout E, Bligny R, Douce R. Cooperation and Competition between Adenylate Kinase, Nucleoside Diphosphokinase, Electron Transport, and ATP Synthase in Plant Mitochondria Studied by 31P-Nuclear Magnetic Resonance. Plant Physiol. 1997 Jan;113(1):191-199. doi: 10.1104/pp.113.1.191. PMID: 12223600; PMCID: PMC158130.
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Effect of insulin on adenylate kinase activity and glycolysis rate of the isolated rat diaphragm in the absence of added glucose.

FEBS letters

Volfin P.
PMID: 11947703
FEBS Lett. 1970 Sep 07;9(6):317-320. doi: 10.1016/0014-5793(70)80388-x.

No abstract available.

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Volfin P. Effect of insulin on adenylate kinase activity and glycolysis rate of the isolated rat diaphragm in the absence of added glucose. FEBS Lett. 1970;9(6):317-320doi: 10.1016/0014-5793(70)80388-x.
Volfin, P. (1970). Effect of insulin on adenylate kinase activity and glycolysis rate of the isolated rat diaphragm in the absence of added glucose. FEBS letters, 9(6), 317-320. https://doi.org/10.1016/0014-5793(70)80388-x
Volfin, P. "Effect of insulin on adenylate kinase activity and glycolysis rate of the isolated rat diaphragm in the absence of added glucose." FEBS letters vol. 9,6 (1970): 317-320. doi: https://doi.org/10.1016/0014-5793(70)80388-x
Volfin P. Effect of insulin on adenylate kinase activity and glycolysis rate of the isolated rat diaphragm in the absence of added glucose. FEBS Lett. 1970 Sep 07;9(6):317-320. doi: 10.1016/0014-5793(70)80388-x. PMID: 11947703.
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The coupling of the adenylate kinase and creatine kinase equilibria. Calculation of substrate and feedback signal levels in muscle.

FEBS letters

Vincent A, Blair JM.
PMID: 11947481
FEBS Lett. 1970 Apr 16;7(3):239-244. doi: 10.1016/0014-5793(70)80170-3.

No abstract available.

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Vincent A, Blair JM. The coupling of the adenylate kinase and creatine kinase equilibria. Calculation of substrate and feedback signal levels in muscle. FEBS Lett. 1970;7(3):239-244doi: 10.1016/0014-5793(70)80170-3.
Vincent, A., & Blair, J. M. (1970). The coupling of the adenylate kinase and creatine kinase equilibria. Calculation of substrate and feedback signal levels in muscle. FEBS letters, 7(3), 239-244. https://doi.org/10.1016/0014-5793(70)80170-3
Vincent, A, and Blair, J M.. "The coupling of the adenylate kinase and creatine kinase equilibria. Calculation of substrate and feedback signal levels in muscle." FEBS letters vol. 7,3 (1970): 239-244. doi: https://doi.org/10.1016/0014-5793(70)80170-3
Vincent A, Blair JM. The coupling of the adenylate kinase and creatine kinase equilibria. Calculation of substrate and feedback signal levels in muscle. FEBS Lett. 1970 Apr 16;7(3):239-244. doi: 10.1016/0014-5793(70)80170-3. PMID: 11947481.
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Adenylate kinase in the interconversion of adenine nucleotides in muscle cytosol.

FEBS letters

Lagunas R, Sols A.
PMID: 11947576
FEBS Lett. 1970 Jun 08;8(4):221-223. doi: 10.1016/0014-5793(70)80269-1.

No abstract available.

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Lagunas R, Sols A. Adenylate kinase in the interconversion of adenine nucleotides in muscle cytosol. FEBS Lett. 1970;8(4):221-223doi: 10.1016/0014-5793(70)80269-1.
Lagunas, R., & Sols, A. (1970). Adenylate kinase in the interconversion of adenine nucleotides in muscle cytosol. FEBS letters, 8(4), 221-223. https://doi.org/10.1016/0014-5793(70)80269-1
Lagunas, R, and Sols, A. "Adenylate kinase in the interconversion of adenine nucleotides in muscle cytosol." FEBS letters vol. 8,4 (1970): 221-223. doi: https://doi.org/10.1016/0014-5793(70)80269-1
Lagunas R, Sols A. Adenylate kinase in the interconversion of adenine nucleotides in muscle cytosol. FEBS Lett. 1970 Jun 08;8(4):221-223. doi: 10.1016/0014-5793(70)80269-1. PMID: 11947576.
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Oxidative phosphorylation by mitochondria extracted from dry sunflower seeds.

Plant physiology

Attucci S, Carde JP, Raymond P, Saint-Gès V, Spiteri A, Pradet A.
PMID: 16667996
Plant Physiol. 1991 Feb;95(2):390-8. doi: 10.1104/pp.95.2.390.

The role of mitochondria in the phosphorylation of ADP to ATP in the early steps of seed germination has been studied. Mitochondria were extracted from dry sunflower (Helianthus annuus) seeds. Adenylate kinase-dependent ATP synthesis was inhibited by p(1),p(5)-di(adenosine-5')pentaphosphate. Synthesis...

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Attucci S, Carde JP, Raymond P, et al. Oxidative phosphorylation by mitochondria extracted from dry sunflower seeds. Plant Physiol. 1991;95(2):390-8doi: 10.1104/pp.95.2.390.
Attucci, S., Carde, J. P., Raymond, P., Saint-Gès, V., Spiteri, A., & Pradet, A. (1991). Oxidative phosphorylation by mitochondria extracted from dry sunflower seeds. Plant physiology, 95(2), 390-8. https://doi.org/10.1104/pp.95.2.390
Attucci, S, et al. "Oxidative phosphorylation by mitochondria extracted from dry sunflower seeds." Plant physiology vol. 95,2 (1991): 390-8. doi: https://doi.org/10.1104/pp.95.2.390
Attucci S, Carde JP, Raymond P, Saint-Gès V, Spiteri A, Pradet A. Oxidative phosphorylation by mitochondria extracted from dry sunflower seeds. Plant Physiol. 1991 Feb;95(2):390-8. doi: 10.1104/pp.95.2.390. PMID: 16667996; PMCID: PMC1077543.
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Role of the testa in preventing cellular rupture during imbibition of legume seeds.

Plant physiology

Duke SH, Kakefuda G.
PMID: 16661692
Plant Physiol. 1981 Mar;67(3):449-56. doi: 10.1104/pp.67.3.449.

Studies with the seeds of soybean, navy bean, pea, and peanut were made to determine the extent of leakage of intracellular enzymes during imbition. Embryos with intact testae from all four species were found to leak detectable activities of...

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Duke SH, Kakefuda G. Role of the testa in preventing cellular rupture during imbibition of legume seeds. Plant Physiol. 1981;67(3):449-56doi: 10.1104/pp.67.3.449.
Duke, S. H., & Kakefuda, G. (1981). Role of the testa in preventing cellular rupture during imbibition of legume seeds. Plant physiology, 67(3), 449-56. https://doi.org/10.1104/pp.67.3.449
Duke, S H, and Kakefuda, G. "Role of the testa in preventing cellular rupture during imbibition of legume seeds." Plant physiology vol. 67,3 (1981): 449-56. doi: https://doi.org/10.1104/pp.67.3.449
Duke SH, Kakefuda G. Role of the testa in preventing cellular rupture during imbibition of legume seeds. Plant Physiol. 1981 Mar;67(3):449-56. doi: 10.1104/pp.67.3.449. PMID: 16661692; PMCID: PMC425703.
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Regulation of Plant Acetyl-CoA Carboxylase by Adenylate Nucleotides.

Plant physiology

Eastwell KC, Stumpf PK.
PMID: 16662980
Plant Physiol. 1983 May;72(1):50-5. doi: 10.1104/pp.72.1.50.

The assay of acetyl-CoA carboxylase (EC 6.4.1.2) does not follow ideal zero-order kinetics when assayed in a crude extract from wheat (Triticum aestivum L.) germ. Our results show that the lack of ideality is the consequence of contamination by...

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Eastwell KC, Stumpf PK. Regulation of Plant Acetyl-CoA Carboxylase by Adenylate Nucleotides. Plant Physiol. 1983;72(1):50-5doi: 10.1104/pp.72.1.50.
Eastwell, K. C., & Stumpf, P. K. (1983). Regulation of Plant Acetyl-CoA Carboxylase by Adenylate Nucleotides. Plant physiology, 72(1), 50-5. https://doi.org/10.1104/pp.72.1.50
Eastwell, K C, and Stumpf, P K. "Regulation of Plant Acetyl-CoA Carboxylase by Adenylate Nucleotides." Plant physiology vol. 72,1 (1983): 50-5. doi: https://doi.org/10.1104/pp.72.1.50
Eastwell KC, Stumpf PK. Regulation of Plant Acetyl-CoA Carboxylase by Adenylate Nucleotides. Plant Physiol. 1983 May;72(1):50-5. doi: 10.1104/pp.72.1.50. PMID: 16662980; PMCID: PMC1066167.
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Luciferin incorporation in the structure of acrylic microspheres with subsequent confinement in a polymeric film: A new method to develop a controlled release-based biosensor for ATP, ADP and AMP.

Talanta

Michel PE, Gautier-Sauvigné SM, Blum LJ.
PMID: 18967316
Talanta. 1998 Sep;47(1):169-81. doi: 10.1016/s0039-9140(98)00068-x.

The controlled release of coreactants at the sensing tip of a biosensor is a possible approach to develop self-contained devices. For luciferin which is a firefly luciferase cosubstrate, a new method of retention is evaluated. The two-step procedure consists...

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Michel PE, Gautier-Sauvigné SM, Blum LJ. Luciferin incorporation in the structure of acrylic microspheres with subsequent confinement in a polymeric film: A new method to develop a controlled release-based biosensor for ATP, ADP and AMP. Talanta. 1998;47(1):169-81doi: 10.1016/s0039-9140(98)00068-x.
Michel, P. E., Gautier-Sauvigné, S. M., & Blum, L. J. (1998). Luciferin incorporation in the structure of acrylic microspheres with subsequent confinement in a polymeric film: A new method to develop a controlled release-based biosensor for ATP, ADP and AMP. Talanta, 47(1), 169-81. https://doi.org/10.1016/s0039-9140(98)00068-x
Michel, P E, et al. "Luciferin incorporation in the structure of acrylic microspheres with subsequent confinement in a polymeric film: A new method to develop a controlled release-based biosensor for ATP, ADP and AMP." Talanta vol. 47,1 (1998): 169-81. doi: https://doi.org/10.1016/s0039-9140(98)00068-x
Michel PE, Gautier-Sauvigné SM, Blum LJ. Luciferin incorporation in the structure of acrylic microspheres with subsequent confinement in a polymeric film: A new method to develop a controlled release-based biosensor for ATP, ADP and AMP. Talanta. 1998 Sep;47(1):169-81. doi: 10.1016/s0039-9140(98)00068-x. PMID: 18967316.
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Photosynthetic CO(2) Fixation Products and Activities of Enzymes Related to Photosynthesis in Bermudagrass and Other Plants.

Plant physiology

Chen TM, Brown RH, Black CC.
PMID: 16657595
Plant Physiol. 1971 Feb;47(2):199-203. doi: 10.1104/pp.47.2.199.

After a 5-second exposure of illuminated bermudagrass (Cynodon dactylon L. var. ;Coastal') leaves to (14)CO(2), 84% of the incorporated (14)C was recovered as aspartate and malate. After transfer from (14)CO(2)-air to (12)CO(2)-air under continuous illumination, total radioactivity decreased in...

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Chen TM, Brown RH, Black CC. Photosynthetic CO(2) Fixation Products and Activities of Enzymes Related to Photosynthesis in Bermudagrass and Other Plants. Plant Physiol. 1971;47(2):199-203doi: 10.1104/pp.47.2.199.
Chen, T. M., Brown, R. H., & Black, C. C. (1971). Photosynthetic CO(2) Fixation Products and Activities of Enzymes Related to Photosynthesis in Bermudagrass and Other Plants. Plant physiology, 47(2), 199-203. https://doi.org/10.1104/pp.47.2.199
Chen, T M, et al. "Photosynthetic CO(2) Fixation Products and Activities of Enzymes Related to Photosynthesis in Bermudagrass and Other Plants." Plant physiology vol. 47,2 (1971): 199-203. doi: https://doi.org/10.1104/pp.47.2.199
Chen TM, Brown RH, Black CC. Photosynthetic CO(2) Fixation Products and Activities of Enzymes Related to Photosynthesis in Bermudagrass and Other Plants. Plant Physiol. 1971 Feb;47(2):199-203. doi: 10.1104/pp.47.2.199. PMID: 16657595; PMCID: PMC365841.
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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 138 entries