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Molecular Features Affecting the Biological Activity of the Host-Selective Toxins from Cochliobolus victoriae.

Plant physiology

Wolpert TJ, Macko V, Acklin W, Arigoni D.
PMID: 16666275
Plant Physiol. 1988 Sep;88(1):37-41. doi: 10.1104/pp.88.1.37.

The structures of the toxins produced by Cochliobolus victoriae, victorin B, C, D, E, and victoricine, have recently been established. These toxins and modified forms of victorin C were tested for their effect on dark CO(2) fixation in susceptible...

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Wolpert TJ, Macko V, Acklin W, et al. Molecular Features Affecting the Biological Activity of the Host-Selective Toxins from Cochliobolus victoriae. Plant Physiol. 1988;88(1):37-41doi: 10.1104/pp.88.1.37.
Wolpert, T. J., Macko, V., Acklin, W., & Arigoni, D. (1988). Molecular Features Affecting the Biological Activity of the Host-Selective Toxins from Cochliobolus victoriae. Plant physiology, 88(1), 37-41. https://doi.org/10.1104/pp.88.1.37
Wolpert, T J, et al. "Molecular Features Affecting the Biological Activity of the Host-Selective Toxins from Cochliobolus victoriae." Plant physiology vol. 88,1 (1988): 37-41. doi: https://doi.org/10.1104/pp.88.1.37
Wolpert TJ, Macko V, Acklin W, Arigoni D. Molecular Features Affecting the Biological Activity of the Host-Selective Toxins from Cochliobolus victoriae. Plant Physiol. 1988 Sep;88(1):37-41. doi: 10.1104/pp.88.1.37. PMID: 16666275; PMCID: PMC1055521.
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Separation of amino acids using ion-paired reversed-phase high-performance liquid chromatography with special reference to collagen hydrolysate.

Amino acids

Frey J, Chamson A, Raby N.
PMID: 24190556
Amino Acids. 1993 Feb;4(1):45-51. doi: 10.1007/BF00805800.

The collagen study includes the analysis of its characteristic amino acids: proline, hydroxyproline, lysine, hydroxylysine. HPLC offers an interesting device if associated with on-line radiometric detection for the determination of radiolabelled amino acids in the case of metabolism studies....

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Frey J, Chamson A, Raby N. Separation of amino acids using ion-paired reversed-phase high-performance liquid chromatography with special reference to collagen hydrolysate. Amino Acids. 1993;4(1):45-51doi: 10.1007/BF00805800.
Frey, J., Chamson, A., & Raby, N. (1993). Separation of amino acids using ion-paired reversed-phase high-performance liquid chromatography with special reference to collagen hydrolysate. Amino acids, 4(1), 45-51. https://doi.org/10.1007/BF00805800
Frey, J, et al. "Separation of amino acids using ion-paired reversed-phase high-performance liquid chromatography with special reference to collagen hydrolysate." Amino acids vol. 4,1 (1993): 45-51. doi: https://doi.org/10.1007/BF00805800
Frey J, Chamson A, Raby N. Separation of amino acids using ion-paired reversed-phase high-performance liquid chromatography with special reference to collagen hydrolysate. Amino Acids. 1993 Feb;4(1):45-51. doi: 10.1007/BF00805800. PMID: 24190556.
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Studies on the catabolism of glycated haemoglobin: Glycated globin is not a substrate for the glucosyl-galactosyl-hydroxylysine glucosidase but for a peptidase activity present in rat kidney and spleen.

Amino acids

Grigorova-Borsos AM, Tacnet F, Fischer RW, Winterhalter KH, Sternberg M.
PMID: 24190558
Amino Acids. 1993 Feb;4(1):63-72. doi: 10.1007/BF00805802.

Rat kidney and spleen glucosyl-galactosyl-hydroxylysine glucosidase (EC.3.2.1.107) whose specificity for the hydroxylysine-linked disaccharide units present in collagens depends upon the substrate's free amino group was tested for its glycosidase activity on the ketoamine form of glycated [(14)C]Glc-Globin. The most...

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Grigorova-Borsos AM, Tacnet F, Fischer RW, et al. Studies on the catabolism of glycated haemoglobin: Glycated globin is not a substrate for the glucosyl-galactosyl-hydroxylysine glucosidase but for a peptidase activity present in rat kidney and spleen. Amino Acids. 1993;4(1):63-72doi: 10.1007/BF00805802.
Grigorova-Borsos, A. M., Tacnet, F., Fischer, R. W., Winterhalter, K. H., & Sternberg, M. (1993). Studies on the catabolism of glycated haemoglobin: Glycated globin is not a substrate for the glucosyl-galactosyl-hydroxylysine glucosidase but for a peptidase activity present in rat kidney and spleen. Amino acids, 4(1), 63-72. https://doi.org/10.1007/BF00805802
Grigorova-Borsos, A M, et al. "Studies on the catabolism of glycated haemoglobin: Glycated globin is not a substrate for the glucosyl-galactosyl-hydroxylysine glucosidase but for a peptidase activity present in rat kidney and spleen." Amino acids vol. 4,1 (1993): 63-72. doi: https://doi.org/10.1007/BF00805802
Grigorova-Borsos AM, Tacnet F, Fischer RW, Winterhalter KH, Sternberg M. Studies on the catabolism of glycated haemoglobin: Glycated globin is not a substrate for the glucosyl-galactosyl-hydroxylysine glucosidase but for a peptidase activity present in rat kidney and spleen. Amino Acids. 1993 Feb;4(1):63-72. doi: 10.1007/BF00805802. PMID: 24190558.
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The challenge of determining lysyl oxidase activity: Old methods and novel approaches.

Analytical biochemistry

Rodriguez-Pascual F, Rosell-Garcia T.
PMID: 34871563
Anal Biochem. 2021 Dec 04;639:114508. doi: 10.1016/j.ab.2021.114508. Epub 2021 Dec 04.

The lysyl oxidase (LOX) family of enzymes catalyze the oxidative deamination of lysine and hydroxylysine residues in collagen and elastin in the initiation step of the formation of covalent cross-linkages, an essential process for extracellular matrix (ECM) maturation. Elevated...

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Rodriguez-Pascual F, Rosell-Garcia T. The challenge of determining lysyl oxidase activity: Old methods and novel approaches. Anal Biochem. 2021;639:114508doi: 10.1016/j.ab.2021.114508.
Rodriguez-Pascual, F., & Rosell-Garcia, T. (2021). The challenge of determining lysyl oxidase activity: Old methods and novel approaches. Analytical biochemistry, 639114508. https://doi.org/10.1016/j.ab.2021.114508
Rodriguez-Pascual, Fernando, and Rosell-Garcia, Tamara. "The challenge of determining lysyl oxidase activity: Old methods and novel approaches." Analytical biochemistry vol. 639 (2021): 114508. doi: https://doi.org/10.1016/j.ab.2021.114508
Rodriguez-Pascual F, Rosell-Garcia T. The challenge of determining lysyl oxidase activity: Old methods and novel approaches. Anal Biochem. 2021 Dec 04;639:114508. doi: 10.1016/j.ab.2021.114508. Epub 2021 Dec 04. PMID: 34871563.
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Impaired Gastric Hormone Regulation of Osteoblasts and Lysyl Oxidase Drives Bone Disease in Diabetes Mellitus.

JBMR plus

Daley EJ, Pajevic PD, Roy S, Trackman PC.
PMID: 31687648
JBMR Plus. 2019 Aug 07;3(10):e10212. doi: 10.1002/jbm4.10212. eCollection 2019 Oct.

Diabetic bone disease is a complication of type I and type II diabetes, both of which are increasing in the United States and elsewhere. Increased hip and foot fracture rates do not correlate well with changes in bone mineral...

Cite
Daley EJ, Pajevic PD, Roy S, et al. Impaired Gastric Hormone Regulation of Osteoblasts and Lysyl Oxidase Drives Bone Disease in Diabetes Mellitus. JBMR Plus. 2019;3(10):e10212doi: 10.1002/jbm4.10212.
Daley, E. J., Pajevic, P. D., Roy, S., & Trackman, P. C. (2019). Impaired Gastric Hormone Regulation of Osteoblasts and Lysyl Oxidase Drives Bone Disease in Diabetes Mellitus. JBMR plus, 3(10), e10212. https://doi.org/10.1002/jbm4.10212
Daley, Eileen J, et al. "Impaired Gastric Hormone Regulation of Osteoblasts and Lysyl Oxidase Drives Bone Disease in Diabetes Mellitus." JBMR plus vol. 3,10 (2019): e10212. doi: https://doi.org/10.1002/jbm4.10212
Daley EJ, Pajevic PD, Roy S, Trackman PC. Impaired Gastric Hormone Regulation of Osteoblasts and Lysyl Oxidase Drives Bone Disease in Diabetes Mellitus. JBMR Plus. 2019 Aug 07;3(10):e10212. doi: 10.1002/jbm4.10212. eCollection 2019 Oct. PMID: 31687648; PMCID: PMC6820454.
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Dysregulation of Lysyl Oxidases Expression in Diabetic Nephropathy and Renal Cell Carcinoma.

Current drug targets

Añazco C, Cerro S, Pereira N, Rojas C, Torres Á, Vidal-Beltrán I.
PMID: 34879794
Curr Drug Targets. 2021;22(17):1916-1925. doi: 10.2174/1389450122666210712163702.

Lysyl oxidases (LOXs) are amino oxidase enzymes that catalyze the oxidative deamination of lysine and hydroxylysine residues to form allysine, the first step towards the development of the final cross-linking reaction in collagens, a crucial macromolecule that reinforces extracellular...

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Añazco C, Cerro S, Pereira N, et al. Dysregulation of Lysyl Oxidases Expression in Diabetic Nephropathy and Renal Cell Carcinoma. Curr Drug Targets. 2021;22(17):1916-1925doi: 10.2174/1389450122666210712163702.
Añazco, C., Cerro, S., Pereira, N., Rojas, C., Torres, �. �., & Vidal-Beltrán, I. (2021). Dysregulation of Lysyl Oxidases Expression in Diabetic Nephropathy and Renal Cell Carcinoma. Current drug targets, 22(17), 1916-1925. https://doi.org/10.2174/1389450122666210712163702
Añazco, Carolina, et al. "Dysregulation of Lysyl Oxidases Expression in Diabetic Nephropathy and Renal Cell Carcinoma." Current drug targets vol. 22,17 (2021): 1916-1925. doi: https://doi.org/10.2174/1389450122666210712163702
Añazco C, Cerro S, Pereira N, Rojas C, Torres Á, Vidal-Beltrán I. Dysregulation of Lysyl Oxidases Expression in Diabetic Nephropathy and Renal Cell Carcinoma. Curr Drug Targets. 2021;22(17):1916-1925. doi: 10.2174/1389450122666210712163702. PMID: 34879794.
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New mechanistic insights to PLOD1-mediated human vascular disease.

Translational research : the journal of laboratory and clinical medicine

Koenig SN, Cavus O, Williams J, Bernier M, Tonniges J, Sucharski H, Dew T, Akel M, Baker P, Madiai F, De Giorgi F, Scietti L, Faravelli S, Forneris F, Mohler PJ, Bradley EA.
PMID: 34400365
Transl Res. 2022 Jan;239:1-17. doi: 10.1016/j.trsl.2021.08.002. Epub 2021 Aug 13.

Heritable thoracic aortic disease and familial thoracic aortic aneurysm/dissection are important causes of human morbidity/mortality, most without identifiable genetic cause. In a family with familial thoracic aortic aneurysm/dissection, we identified a missense p. (Ser178Arg) variant in PLOD1 segregating with...

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Koenig SN, Cavus O, Williams J, et al. New mechanistic insights to PLOD1-mediated human vascular disease. Transl Res. 2021;239:1-17doi: 10.1016/j.trsl.2021.08.002.
Koenig, S. N., Cavus, O., Williams, J., Bernier, M., Tonniges, J., Sucharski, H., Dew, T., Akel, M., Baker, P., Madiai, F., De Giorgi, F., Scietti, L., Faravelli, S., Forneris, F., Mohler, P. J., & Bradley, E. A. (2022). New mechanistic insights to PLOD1-mediated human vascular disease. Translational research : the journal of laboratory and clinical medicine, 2391-17. https://doi.org/10.1016/j.trsl.2021.08.002
Koenig, Sara N, et al. "New mechanistic insights to PLOD1-mediated human vascular disease." Translational research : the journal of laboratory and clinical medicine vol. 239 (2022): 1-17. doi: https://doi.org/10.1016/j.trsl.2021.08.002
Koenig SN, Cavus O, Williams J, Bernier M, Tonniges J, Sucharski H, Dew T, Akel M, Baker P, Madiai F, De Giorgi F, Scietti L, Faravelli S, Forneris F, Mohler PJ, Bradley EA. New mechanistic insights to PLOD1-mediated human vascular disease. Transl Res. 2022 Jan;239:1-17. doi: 10.1016/j.trsl.2021.08.002. Epub 2021 Aug 13. PMID: 34400365.
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The challenge of determining lysyl oxidase activity: Old methods and novel approaches.

Analytical biochemistry

Rodriguez-Pascual F, Rosell-Garcia T.
PMID: 34871563
Anal Biochem. 2021 Dec 03;114508. doi: 10.1016/j.ab.2021.114508. Epub 2021 Dec 03.

The lysyl oxidase (LOX) family of enzymes catalyze the oxidative deamination of lysine and hydroxylysine residues in collagen and elastin in the initiation step of the formation of covalent cross-linkages, an essential process for extracellular matrix (ECM) maturation. Elevated...

Cite
Rodriguez-Pascual F, Rosell-Garcia T. The challenge of determining lysyl oxidase activity: Old methods and novel approaches. Anal Biochem. 2021;114508doi: 10.1016/j.ab.2021.114508.
Rodriguez-Pascual, F., & Rosell-Garcia, T. (2021). The challenge of determining lysyl oxidase activity: Old methods and novel approaches. Analytical biochemistry, 114508. https://doi.org/10.1016/j.ab.2021.114508
Rodriguez-Pascual, Fernando, and Rosell-Garcia, Tamara. "The challenge of determining lysyl oxidase activity: Old methods and novel approaches." Analytical biochemistry vol. (2021): 114508. doi: https://doi.org/10.1016/j.ab.2021.114508
Rodriguez-Pascual F, Rosell-Garcia T. The challenge of determining lysyl oxidase activity: Old methods and novel approaches. Anal Biochem. 2021 Dec 03;114508. doi: 10.1016/j.ab.2021.114508. Epub 2021 Dec 03. PMID: 34871563.
Copy Download .nbib Format: NLM
The challenge of determining lysyl oxidase activity: Old methods and novel approaches.

Analytical biochemistry

Rodriguez-Pascual F, Rosell-Garcia T.
PMID: 34871563
Anal Biochem. 2021 Dec 04;639:114508. doi: 10.1016/j.ab.2021.114508. Epub 2021 Dec 04.

The lysyl oxidase (LOX) family of enzymes catalyze the oxidative deamination of lysine and hydroxylysine residues in collagen and elastin in the initiation step of the formation of covalent cross-linkages, an essential process for extracellular matrix (ECM) maturation. Elevated...

Cite
Rodriguez-Pascual F, Rosell-Garcia T. The challenge of determining lysyl oxidase activity: Old methods and novel approaches. Anal Biochem. 2021;639:114508doi: 10.1016/j.ab.2021.114508.
Rodriguez-Pascual, F., & Rosell-Garcia, T. (2021). The challenge of determining lysyl oxidase activity: Old methods and novel approaches. Analytical biochemistry, 639114508. https://doi.org/10.1016/j.ab.2021.114508
Rodriguez-Pascual, Fernando, and Rosell-Garcia, Tamara. "The challenge of determining lysyl oxidase activity: Old methods and novel approaches." Analytical biochemistry vol. 639 (2021): 114508. doi: https://doi.org/10.1016/j.ab.2021.114508
Rodriguez-Pascual F, Rosell-Garcia T. The challenge of determining lysyl oxidase activity: Old methods and novel approaches. Anal Biochem. 2021 Dec 04;639:114508. doi: 10.1016/j.ab.2021.114508. Epub 2021 Dec 04. PMID: 34871563.
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Inhibition of Neutrophil Secretion Upon Adhesion as a Basis for the Anti-Inflammatory Effect of the Tricyclic Antidepressant Imipramine.

Frontiers in pharmacology

Galkina SI, Golenkina EA, Fedorova NV, Ksenofontov AL, Serebryakova MV, Arifulin EA, Stadnichuk VI, Baratova LA, Sud'ina GF.
PMID: 34421605
Front Pharmacol. 2021 Aug 05;12:709719. doi: 10.3389/fphar.2021.709719. eCollection 2021.

Recent studies demonstrate the involvement of inflammatory processes in the development of depression and the anti-inflammatory effects of antidepressants. Infiltration and adhesion of neutrophils to nerve tissues and their aggressive secretion are considered as possible causes of inflammatory processes...

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Galkina SI, Golenkina EA, Fedorova NV, et al. Inhibition of Neutrophil Secretion Upon Adhesion as a Basis for the Anti-Inflammatory Effect of the Tricyclic Antidepressant Imipramine. Front Pharmacol. 2021;12:709719doi: 10.3389/fphar.2021.709719.
Galkina, S. I., Golenkina, E. A., Fedorova, N. V., Ksenofontov, A. L., Serebryakova, M. V., Arifulin, E. A., Stadnichuk, V. I., Baratova, L. A., & Sud'ina, G. F. (2021). Inhibition of Neutrophil Secretion Upon Adhesion as a Basis for the Anti-Inflammatory Effect of the Tricyclic Antidepressant Imipramine. Frontiers in pharmacology, 12709719. https://doi.org/10.3389/fphar.2021.709719
Galkina, Svetlana I, et al. "Inhibition of Neutrophil Secretion Upon Adhesion as a Basis for the Anti-Inflammatory Effect of the Tricyclic Antidepressant Imipramine." Frontiers in pharmacology vol. 12 (2021): 709719. doi: https://doi.org/10.3389/fphar.2021.709719
Galkina SI, Golenkina EA, Fedorova NV, Ksenofontov AL, Serebryakova MV, Arifulin EA, Stadnichuk VI, Baratova LA, Sud'ina GF. Inhibition of Neutrophil Secretion Upon Adhesion as a Basis for the Anti-Inflammatory Effect of the Tricyclic Antidepressant Imipramine. Front Pharmacol. 2021 Aug 05;12:709719. doi: 10.3389/fphar.2021.709719. eCollection 2021. PMID: 34421605; PMCID: PMC8375473.
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Impaired Gastric Hormone Regulation of Osteoblasts and Lysyl Oxidase Drives Bone Disease in Diabetes Mellitus.

JBMR plus

Daley EJ, Pajevic PD, Roy S, Trackman PC.
PMID: 31687648
JBMR Plus. 2019 Aug 07;3(10):e10212. doi: 10.1002/jbm4.10212. eCollection 2019 Oct.

Diabetic bone disease is a complication of type I and type II diabetes, both of which are increasing in the United States and elsewhere. Increased hip and foot fracture rates do not correlate well with changes in bone mineral...

Cite
Daley EJ, Pajevic PD, Roy S, et al. Impaired Gastric Hormone Regulation of Osteoblasts and Lysyl Oxidase Drives Bone Disease in Diabetes Mellitus. JBMR Plus. 2019;3(10):e10212doi: 10.1002/jbm4.10212.
Daley, E. J., Pajevic, P. D., Roy, S., & Trackman, P. C. (2019). Impaired Gastric Hormone Regulation of Osteoblasts and Lysyl Oxidase Drives Bone Disease in Diabetes Mellitus. JBMR plus, 3(10), e10212. https://doi.org/10.1002/jbm4.10212
Daley, Eileen J, et al. "Impaired Gastric Hormone Regulation of Osteoblasts and Lysyl Oxidase Drives Bone Disease in Diabetes Mellitus." JBMR plus vol. 3,10 (2019): e10212. doi: https://doi.org/10.1002/jbm4.10212
Daley EJ, Pajevic PD, Roy S, Trackman PC. Impaired Gastric Hormone Regulation of Osteoblasts and Lysyl Oxidase Drives Bone Disease in Diabetes Mellitus. JBMR Plus. 2019 Aug 07;3(10):e10212. doi: 10.1002/jbm4.10212. eCollection 2019 Oct. PMID: 31687648; PMCID: PMC6820454.
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iHyd-LysSite (EPSV): Identifying Hydroxylysine Sites in Protein Using Statistical Formulation by Extracting Enhanced Position and Sequence Variant Feature Technique.

Current genomics

Mahmood MK, Ehsan A, Khan YD, Chou KC.
PMID: 33214770
Curr Genomics. 2020 Nov;21(7):536-545. doi: 10.2174/1389202921999200831142629.

INTRODUCTION: Hydroxylation is one of the most important post-translational modifications (PTM) in cellular functions and is linked to various diseases. The addition of one of the hydroxyl groups (OH) to the lysine sites produces hydroxylysine when undergoes chemical modification.METHODS:...

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Mahmood MK, Ehsan A, Khan YD, et al. iHyd-LysSite (EPSV): Identifying Hydroxylysine Sites in Protein Using Statistical Formulation by Extracting Enhanced Position and Sequence Variant Feature Technique. Curr Genomics. 2020;21(7):536-545doi: 10.2174/1389202921999200831142629.
Mahmood, M. K., Ehsan, A., Khan, Y. D., & Chou, K. C. (2020). iHyd-LysSite (EPSV): Identifying Hydroxylysine Sites in Protein Using Statistical Formulation by Extracting Enhanced Position and Sequence Variant Feature Technique. Current genomics, 21(7), 536-545. https://doi.org/10.2174/1389202921999200831142629
Mahmood, Muhammad Khalid, et al. "iHyd-LysSite (EPSV): Identifying Hydroxylysine Sites in Protein Using Statistical Formulation by Extracting Enhanced Position and Sequence Variant Feature Technique." Current genomics vol. 21,7 (2020): 536-545. doi: https://doi.org/10.2174/1389202921999200831142629
Mahmood MK, Ehsan A, Khan YD, Chou KC. iHyd-LysSite (EPSV): Identifying Hydroxylysine Sites in Protein Using Statistical Formulation by Extracting Enhanced Position and Sequence Variant Feature Technique. Curr Genomics. 2020 Nov;21(7):536-545. doi: 10.2174/1389202921999200831142629. PMID: 33214770; PMCID: PMC7604750.
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Showing 1 to 12 of 54 entries