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Showing 1 to 12 of 244 entries
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Novel roles for well-known players: from tobacco mosaic virus pests to enzymatically active assemblies.

Beilstein journal of nanotechnology

Koch C, Eber FJ, Azucena C, Förste A, Walheim S, Schimmel T, Bittner AM, Jeske H, Gliemann H, Eiben S, Geiger FC, Wege C.
PMID: 27335751
Beilstein J Nanotechnol. 2016 Apr 25;7:613-29. doi: 10.3762/bjnano.7.54. eCollection 2016.

The rod-shaped nanoparticles of the widespread plant pathogen tobacco mosaic virus (TMV) have been a matter of intense debates and cutting-edge research for more than a hundred years. During the late 19th century, their behavior in filtration tests applied...

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Koch C, Eber FJ, Azucena C, et al. Novel roles for well-known players: from tobacco mosaic virus pests to enzymatically active assemblies. Beilstein J Nanotechnol. 2016;7:613-29doi: 10.3762/bjnano.7.54.
Koch, C., Eber, F. J., Azucena, C., Förste, A., Walheim, S., Schimmel, T., Bittner, A. M., Jeske, H., Gliemann, H., Eiben, S., Geiger, F. C., & Wege, C. (2016). Novel roles for well-known players: from tobacco mosaic virus pests to enzymatically active assemblies. Beilstein journal of nanotechnology, 7613-29. https://doi.org/10.3762/bjnano.7.54
Koch, Claudia, et al. "Novel roles for well-known players: from tobacco mosaic virus pests to enzymatically active assemblies." Beilstein journal of nanotechnology vol. 7 (2016): 613-29. doi: https://doi.org/10.3762/bjnano.7.54
Koch C, Eber FJ, Azucena C, Förste A, Walheim S, Schimmel T, Bittner AM, Jeske H, Gliemann H, Eiben S, Geiger FC, Wege C. Novel roles for well-known players: from tobacco mosaic virus pests to enzymatically active assemblies. Beilstein J Nanotechnol. 2016 Apr 25;7:613-29. doi: 10.3762/bjnano.7.54. eCollection 2016. PMID: 27335751; PMCID: PMC4901926.
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Resistance of reaction centers from Rhodobacter sphaeroides against UV-B radiation. Effects on protein structure and electron transport.

Photosynthesis research

Tandori J, Máté Z, Maróti P, Vass I.
PMID: 24271934
Photosynth Res. 1996 Nov;50(2):171-9. doi: 10.1007/BF00014887.

Inhibition of electron transport and damage to the protein subunits by ultraviolet-B (UV-B, 280-320 nm) radiation have been studied in isolated reaction centers of the non-sulfur purple bacterium Rhodobacter sphaeroides R26. UV-B irradiation results in the inhibition of charge...

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Tandori J, Máté Z, Maróti P, et al. Resistance of reaction centers from Rhodobacter sphaeroides against UV-B radiation. Effects on protein structure and electron transport. Photosynth Res. 1996;50(2):171-9doi: 10.1007/BF00014887.
Tandori, J., Máté, Z., Maróti, P., & Vass, I. (1996). Resistance of reaction centers from Rhodobacter sphaeroides against UV-B radiation. Effects on protein structure and electron transport. Photosynthesis research, 50(2), 171-9. https://doi.org/10.1007/BF00014887
Tandori, J, et al. "Resistance of reaction centers from Rhodobacter sphaeroides against UV-B radiation. Effects on protein structure and electron transport." Photosynthesis research vol. 50,2 (1996): 171-9. doi: https://doi.org/10.1007/BF00014887
Tandori J, Máté Z, Maróti P, Vass I. Resistance of reaction centers from Rhodobacter sphaeroides against UV-B radiation. Effects on protein structure and electron transport. Photosynth Res. 1996 Nov;50(2):171-9. doi: 10.1007/BF00014887. PMID: 24271934.
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The cytochrome bc 1 complexes of photosynthetic purple bacteria.

Photosynthesis research

Knaff DB.
PMID: 24318679
Photosynth Res. 1993 Feb;35(2):117-33. doi: 10.1007/BF00014743.

Complete nucleotide sequences are now available for the pet (fbc) operons coding for the three electron carrying protein subunits of the cytochrome bc 1 complexes of four photosynthetic purple non-sulfur bacteria. It has been demonstrated that, although the complex...

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Knaff DB. The cytochrome bc 1 complexes of photosynthetic purple bacteria. Photosynth Res. 1993;35(2):117-33doi: 10.1007/BF00014743.
Knaff, D. B. (1993). The cytochrome bc 1 complexes of photosynthetic purple bacteria. Photosynthesis research, 35(2), 117-33. https://doi.org/10.1007/BF00014743
Knaff, D B. "The cytochrome bc 1 complexes of photosynthetic purple bacteria." Photosynthesis research vol. 35,2 (1993): 117-33. doi: https://doi.org/10.1007/BF00014743
Knaff DB. The cytochrome bc 1 complexes of photosynthetic purple bacteria. Photosynth Res. 1993 Feb;35(2):117-33. doi: 10.1007/BF00014743. PMID: 24318679.
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Preparation of mayonnaise from extracted plant protein isolates of chickpea, broad bean and lupin flour: chemical, physiochemical, nutritional and therapeutic properties.

Journal of food science and technology

Alu'datt MH, Rababah T, Alhamad MN, Ereifej K, Gammoh S, Kubow S, Tawalbeh D.
PMID: 28559598
J Food Sci Technol. 2017 May;54(6):1395-1405. doi: 10.1007/s13197-017-2551-6. Epub 2017 Mar 10.

This investigation was aimed to study the molecular, physico-chemical, and biofunctional health properties of mayonnaise prepared using proteins isolated from broad bean, lupin and chickpea flour. Proteins were isolated from chickpea (CPPI), broad bean (BBPI) and lupin (LPPI) flour...

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Alu'datt MH, Rababah T, Alhamad MN, et al. Preparation of mayonnaise from extracted plant protein isolates of chickpea, broad bean and lupin flour: chemical, physiochemical, nutritional and therapeutic properties. J Food Sci Technol. 2017;54(6):1395-1405doi: 10.1007/s13197-017-2551-6.
Alu'datt, M. H., Rababah, T., Alhamad, M. N., Ereifej, K., Gammoh, S., Kubow, S., & Tawalbeh, D. (2017). Preparation of mayonnaise from extracted plant protein isolates of chickpea, broad bean and lupin flour: chemical, physiochemical, nutritional and therapeutic properties. Journal of food science and technology, 54(6), 1395-1405. https://doi.org/10.1007/s13197-017-2551-6
Alu'datt, Muhammad H, et al. "Preparation of mayonnaise from extracted plant protein isolates of chickpea, broad bean and lupin flour: chemical, physiochemical, nutritional and therapeutic properties." Journal of food science and technology vol. 54,6 (2017): 1395-1405. doi: https://doi.org/10.1007/s13197-017-2551-6
Alu'datt MH, Rababah T, Alhamad MN, Ereifej K, Gammoh S, Kubow S, Tawalbeh D. Preparation of mayonnaise from extracted plant protein isolates of chickpea, broad bean and lupin flour: chemical, physiochemical, nutritional and therapeutic properties. J Food Sci Technol. 2017 May;54(6):1395-1405. doi: 10.1007/s13197-017-2551-6. Epub 2017 Mar 10. PMID: 28559598; PMCID: PMC5430170.
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Delivery strategies for novel vaccine formulations.

World journal of virology

Trovato M, Krebs SJ, Haigwood NL, De Berardinis P.
PMID: 24175206
World J Virol. 2012 Feb 12;1(1):4-10. doi: 10.5501/wjv.v1.i1.4.

A major challenge in vaccine design is to identify antigen presentation and delivery systems capable of rapidly stimulating both the humoral and cellular components of the immune system to elicit a strong and sustained immunity against different viral isolates....

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Trovato M, Krebs SJ, Haigwood NL, et al. Delivery strategies for novel vaccine formulations. World J Virol. 2012;1(1):4-10doi: 10.5501/wjv.v1.i1.4.
Trovato, M., Krebs, S. J., Haigwood, N. L., & De Berardinis, P. (2012). Delivery strategies for novel vaccine formulations. World journal of virology, 1(1), 4-10. https://doi.org/10.5501/wjv.v1.i1.4
Trovato, Maria, et al. "Delivery strategies for novel vaccine formulations." World journal of virology vol. 1,1 (2012): 4-10. doi: https://doi.org/10.5501/wjv.v1.i1.4
Trovato M, Krebs SJ, Haigwood NL, De Berardinis P. Delivery strategies for novel vaccine formulations. World J Virol. 2012 Feb 12;1(1):4-10. doi: 10.5501/wjv.v1.i1.4. PMID: 24175206; PMCID: PMC3782264.
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CALCOM: a software for calculating the center of mass of proteins.

Bioinformation

Costantini S, Paladino A, Facchiano AM.
PMID: 18478078
Bioinformation. 2008 Feb 09;2(7):271-2. doi: 10.6026/97320630002271.

UNLABELLED: The center of mass of a protein is an artificial point useful for detecting important and simple features of proteins structure, shape and association.CALCOM is a software which calculates the center of mass of a protein, starting from...

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Costantini S, Paladino A, Facchiano AM. CALCOM: a software for calculating the center of mass of proteins. Bioinformation. 2008;2(7):271-2doi: 10.6026/97320630002271.
Costantini, S., Paladino, A., & Facchiano, A. M. (2008). CALCOM: a software for calculating the center of mass of proteins. Bioinformation, 2(7), 271-2. https://doi.org/10.6026/97320630002271
Costantini, Susan, et al. "CALCOM: a software for calculating the center of mass of proteins." Bioinformation vol. 2,7 (2008): 271-2. doi: https://doi.org/10.6026/97320630002271
Costantini S, Paladino A, Facchiano AM. CALCOM: a software for calculating the center of mass of proteins. Bioinformation. 2008 Feb 09;2(7):271-2. doi: 10.6026/97320630002271. PMID: 18478078; PMCID: PMC2374369.
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Purification and properties of ribulosebisphosphate carboxylase large subunit binding protein.

Plant physiology

Hemmingsen SM, Ellis RJ.
PMID: 16664596
Plant Physiol. 1986 Jan;80(1):269-76. doi: 10.1104/pp.80.1.269.

The large subunit binding protein, an abundant plastid protein implicated in the assembly of ribulose-1,5-bisphosphate carboxylase-oxygenase (RubisCO), has been highly purified from leaves of Pisum sativum. The 720 kilodaltons purified binding protein is composed of two types of subunits...

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Hemmingsen SM, Ellis RJ. Purification and properties of ribulosebisphosphate carboxylase large subunit binding protein. Plant Physiol. 1986;80(1):269-76doi: 10.1104/pp.80.1.269.
Hemmingsen, S. M., & Ellis, R. J. (1986). Purification and properties of ribulosebisphosphate carboxylase large subunit binding protein. Plant physiology, 80(1), 269-76. https://doi.org/10.1104/pp.80.1.269
Hemmingsen, S M, and Ellis, R J. "Purification and properties of ribulosebisphosphate carboxylase large subunit binding protein." Plant physiology vol. 80,1 (1986): 269-76. doi: https://doi.org/10.1104/pp.80.1.269
Hemmingsen SM, Ellis RJ. Purification and properties of ribulosebisphosphate carboxylase large subunit binding protein. Plant Physiol. 1986 Jan;80(1):269-76. doi: 10.1104/pp.80.1.269. PMID: 16664596; PMCID: PMC1075095.
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Urea-Elicited Changes in Relative Electrophoretic Mobility of Certain Glycinin and beta-Conglycinin Subunits.

Plant physiology

Fontes EP, Moreira MA, Davies CS, Nielsen NC.
PMID: 16663936
Plant Physiol. 1984 Nov;76(3):840-2. doi: 10.1104/pp.76.3.840.

Six molar urea in sodium dodecyl sulfate-polyacrylamide gels altered the relative electrophoretic mobility of several soybean protein subunits. Glycinin acidic polypeptide components A(3) and A(4) could be resolved from the other acidic polypeptides. A variant of the delta' subunit...

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Fontes EP, Moreira MA, Davies CS, et al. Urea-Elicited Changes in Relative Electrophoretic Mobility of Certain Glycinin and beta-Conglycinin Subunits. Plant Physiol. 1984;76(3):840-2doi: 10.1104/pp.76.3.840.
Fontes, E. P., Moreira, M. A., Davies, C. S., & Nielsen, N. C. (1984). Urea-Elicited Changes in Relative Electrophoretic Mobility of Certain Glycinin and beta-Conglycinin Subunits. Plant physiology, 76(3), 840-2. https://doi.org/10.1104/pp.76.3.840
Fontes, E P, et al. "Urea-Elicited Changes in Relative Electrophoretic Mobility of Certain Glycinin and beta-Conglycinin Subunits." Plant physiology vol. 76,3 (1984): 840-2. doi: https://doi.org/10.1104/pp.76.3.840
Fontes EP, Moreira MA, Davies CS, Nielsen NC. Urea-Elicited Changes in Relative Electrophoretic Mobility of Certain Glycinin and beta-Conglycinin Subunits. Plant Physiol. 1984 Nov;76(3):840-2. doi: 10.1104/pp.76.3.840. PMID: 16663936; PMCID: PMC1064385.
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The polar alkaline disassembly of papaya mosaic virus.

Virology

Lok S, Abouhaidar M.
PMID: 18635087
Virology. 1981 Sep;113(2):637-43. doi: 10.1016/0042-6822(81)90192-6.

The disassembly of papaya mosaic virus (PMV) at alkaline pH (pH 10) was monitored by following the decrease of turbidity at 320 nm and by electron microscopy. Most of the virion particle population undergoes a sequential loss of protein...

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Lok S, Abouhaidar M. The polar alkaline disassembly of papaya mosaic virus. Virology. 1981;113(2):637-43doi: 10.1016/0042-6822(81)90192-6.
Lok, S., & Abouhaidar, M. (1981). The polar alkaline disassembly of papaya mosaic virus. Virology, 113(2), 637-43. https://doi.org/10.1016/0042-6822(81)90192-6
Lok, S, and Abouhaidar, M. "The polar alkaline disassembly of papaya mosaic virus." Virology vol. 113,2 (1981): 637-43. doi: https://doi.org/10.1016/0042-6822(81)90192-6
Lok S, Abouhaidar M. The polar alkaline disassembly of papaya mosaic virus. Virology. 1981 Sep;113(2):637-43. doi: 10.1016/0042-6822(81)90192-6. PMID: 18635087.
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Intermediates of the in vitro assembly and disassembly of southern bean mosaic virus.

Virology

Tremaine JH, Ronald WP, Kelly EM.
PMID: 18635126
Virology. 1982 Apr 15;118(1):35-44. doi: 10.1016/0042-6822(82)90317-8.

Southern bean mosaic virus (SBMV) was swollen by treatment with EDTA at pH 7.5 and dissociated into RNA and protein in 1 M NaCl. Aliquots of this preparation were diluted with appropriate buffers to obtain samples in varying concentrations...

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Tremaine JH, Ronald WP, Kelly EM. Intermediates of the in vitro assembly and disassembly of southern bean mosaic virus. Virology. 1982;118(1):35-44doi: 10.1016/0042-6822(82)90317-8.
Tremaine, J. H., Ronald, W. P., & Kelly, E. M. (1982). Intermediates of the in vitro assembly and disassembly of southern bean mosaic virus. Virology, 118(1), 35-44. https://doi.org/10.1016/0042-6822(82)90317-8
Tremaine, J H, et al. "Intermediates of the in vitro assembly and disassembly of southern bean mosaic virus." Virology vol. 118,1 (1982): 35-44. doi: https://doi.org/10.1016/0042-6822(82)90317-8
Tremaine JH, Ronald WP, Kelly EM. Intermediates of the in vitro assembly and disassembly of southern bean mosaic virus. Virology. 1982 Apr 15;118(1):35-44. doi: 10.1016/0042-6822(82)90317-8. PMID: 18635126.
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Horse carboxylesterases: evidence for six CES1 and four families of CES genes on chromosome 3.

Comparative biochemistry and physiology. Part D, Genomics & proteomics

Holmes RS, Cox LA, Vandeberg JL.
PMID: 20403742
Comp Biochem Physiol Part D Genomics Proteomics. 2009 Mar;4(1):54-65. doi: 10.1016/j.cbd.2008.10.004. Epub 2008 Nov 05.

Carboxylesterases (CES) are responsible for the detoxification of a wide range of drugs and xenobiotics, and may contribute to cholesterol, fatty acid and lung surfactant metabolism. In this study, in silico methods were used to predict the amino acid...

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Holmes RS, Cox LA, Vandeberg JL. Horse carboxylesterases: evidence for six CES1 and four families of CES genes on chromosome 3. Comp Biochem Physiol Part D Genomics Proteomics. 2008;4(1):54-65doi: 10.1016/j.cbd.2008.10.004.
Holmes, R. S., Cox, L. A., & Vandeberg, J. L. (2009). Horse carboxylesterases: evidence for six CES1 and four families of CES genes on chromosome 3. Comparative biochemistry and physiology. Part D, Genomics & proteomics, 4(1), 54-65. https://doi.org/10.1016/j.cbd.2008.10.004
Holmes, Roger S, et al. "Horse carboxylesterases: evidence for six CES1 and four families of CES genes on chromosome 3." Comparative biochemistry and physiology. Part D, Genomics & proteomics vol. 4,1 (2009): 54-65. doi: https://doi.org/10.1016/j.cbd.2008.10.004
Holmes RS, Cox LA, Vandeberg JL. Horse carboxylesterases: evidence for six CES1 and four families of CES genes on chromosome 3. Comp Biochem Physiol Part D Genomics Proteomics. 2009 Mar;4(1):54-65. doi: 10.1016/j.cbd.2008.10.004. Epub 2008 Nov 05. PMID: 20403742; PMCID: PMC2916739.
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Correlation of glutamate binding activity with glutamate-binding protein immunoreactivity in the brain of control and alcohol-treated rats.

Neurochemistry international

Michaelis E, Roy S, Galton N, Cunningham M, Lecluyse E, Michaelis M.
PMID: 20501163
Neurochem Int. 1987;11(2):209-18. doi: 10.1016/0197-0186(87)90011-8.

Specific antibodies raised against a glutamate binding protein purified from bovine brain were used to trace the immunoreactivity of this protein in rat brain subcellular fractions. In the subcellular fractions obtained from whole brain homogenates, the synaptic membranes had...

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Michaelis E, Roy S, Galton N, et al. Correlation of glutamate binding activity with glutamate-binding protein immunoreactivity in the brain of control and alcohol-treated rats. Neurochem Int. 1987;11(2):209-18doi: 10.1016/0197-0186(87)90011-8.
Michaelis, E., Roy, S., Galton, N., Cunningham, M., Lecluyse, E., & Michaelis, M. (1987). Correlation of glutamate binding activity with glutamate-binding protein immunoreactivity in the brain of control and alcohol-treated rats. Neurochemistry international, 11(2), 209-18. https://doi.org/10.1016/0197-0186(87)90011-8
Michaelis, E, et al. "Correlation of glutamate binding activity with glutamate-binding protein immunoreactivity in the brain of control and alcohol-treated rats." Neurochemistry international vol. 11,2 (1987): 209-18. doi: https://doi.org/10.1016/0197-0186(87)90011-8
Michaelis E, Roy S, Galton N, Cunningham M, Lecluyse E, Michaelis M. Correlation of glutamate binding activity with glutamate-binding protein immunoreactivity in the brain of control and alcohol-treated rats. Neurochem Int. 1987;11(2):209-18. doi: 10.1016/0197-0186(87)90011-8. PMID: 20501163.
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Showing 1 to 12 of 244 entries