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Showing 1 to 12 of 108 entries
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Dietary Triggers in Irritable Bowel Syndrome: Is There a Role for Gluten?.

Journal of neurogastroenterology and motility

Volta U, Pinto-Sanchez MI, Boschetti E, Caio G, De Giorgio R, Verdu EF.
PMID: 27426486
J Neurogastroenterol Motil. 2016 Oct 30;22(4):547-557. doi: 10.5056/jnm16069.

A tight link exists between dietary factors and irritable bowel syndrome (IBS), one of the most common functional syndromes, characterized by abdominal pain/discomfort, bloating and alternating bowel habits. Amongst the variety of foods potentially evoking "food sensitivity", gluten and...

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Volta U, Pinto-Sanchez MI, Boschetti E, et al. Dietary Triggers in Irritable Bowel Syndrome: Is There a Role for Gluten?. J Neurogastroenterol Motil. 2016;22(4):547-557doi: 10.5056/jnm16069.
Volta, U., Pinto-Sanchez, M. I., Boschetti, E., Caio, G., De Giorgio, R., & Verdu, E. F. (2016). Dietary Triggers in Irritable Bowel Syndrome: Is There a Role for Gluten?. Journal of neurogastroenterology and motility, 22(4), 547-557. https://doi.org/10.5056/jnm16069
Volta, Umberto, et al. "Dietary Triggers in Irritable Bowel Syndrome: Is There a Role for Gluten?." Journal of neurogastroenterology and motility vol. 22,4 (2016): 547-557. doi: https://doi.org/10.5056/jnm16069
Volta U, Pinto-Sanchez MI, Boschetti E, Caio G, De Giorgio R, Verdu EF. Dietary Triggers in Irritable Bowel Syndrome: Is There a Role for Gluten?. J Neurogastroenterol Motil. 2016 Oct 30;22(4):547-557. doi: 10.5056/jnm16069. PMID: 27426486; PMCID: PMC5056565.
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Effect of extrusion variables (temperature, moisture) on the antinutrient components of cereal brans.

Journal of food science and technology

Kaur S, Sharma S, Singh B, Dar BN.
PMID: 25745239
J Food Sci Technol. 2015 Mar;52(3):1670-6. doi: 10.1007/s13197-013-1118-4. Epub 2013 Aug 24.

The study was carried out, to explore the potentiality of extrusion technology for elimination of antinutritional components of cereal brans. Extrusion variables were moisture content (14, 17 and 20 %) and temperatures (115 °C, 140 °C, 165 °C). Phytic...

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Kaur S, Sharma S, Singh B, et al. Effect of extrusion variables (temperature, moisture) on the antinutrient components of cereal brans. J Food Sci Technol. 2013;52(3):1670-6doi: 10.1007/s13197-013-1118-4.
Kaur, S., Sharma, S., Singh, B., & Dar, B. N. (2015). Effect of extrusion variables (temperature, moisture) on the antinutrient components of cereal brans. Journal of food science and technology, 52(3), 1670-6. https://doi.org/10.1007/s13197-013-1118-4
Kaur, Satinder, et al. "Effect of extrusion variables (temperature, moisture) on the antinutrient components of cereal brans." Journal of food science and technology vol. 52,3 (2015): 1670-6. doi: https://doi.org/10.1007/s13197-013-1118-4
Kaur S, Sharma S, Singh B, Dar BN. Effect of extrusion variables (temperature, moisture) on the antinutrient components of cereal brans. J Food Sci Technol. 2015 Mar;52(3):1670-6. doi: 10.1007/s13197-013-1118-4. Epub 2013 Aug 24. PMID: 25745239; PMCID: PMC4348277.
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Kaulath, a new fungal fermented food from horse gram.

Journal of food science and technology

Dwivedi M, Vasantha KY, Sreerama YN, Haware DJ, Singh RP, Sattur AP.
PMID: 26604417
J Food Sci Technol. 2015 Dec;52(12):8371-6. doi: 10.1007/s13197-015-1887-z. Epub 2015 Jun 09.

Horse gram (Macrotyloma uniflorum) is used in the traditional method for treatmentof several health complications. It is also known that fermentation of such substrates yields a number of compounds that enhance the overall activities against several disease states. Solid...

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Dwivedi M, Vasantha KY, Sreerama YN, et al. Kaulath, a new fungal fermented food from horse gram. J Food Sci Technol. 2015;52(12):8371-6doi: 10.1007/s13197-015-1887-z.
Dwivedi, M., Vasantha, K. Y., Sreerama, Y. N., Haware, D. J., Singh, R. P., & Sattur, A. P. (2015). Kaulath, a new fungal fermented food from horse gram. Journal of food science and technology, 52(12), 8371-6. https://doi.org/10.1007/s13197-015-1887-z
Dwivedi, Minakshee, et al. "Kaulath, a new fungal fermented food from horse gram." Journal of food science and technology vol. 52,12 (2015): 8371-6. doi: https://doi.org/10.1007/s13197-015-1887-z
Dwivedi M, Vasantha KY, Sreerama YN, Haware DJ, Singh RP, Sattur AP. Kaulath, a new fungal fermented food from horse gram. J Food Sci Technol. 2015 Dec;52(12):8371-6. doi: 10.1007/s13197-015-1887-z. Epub 2015 Jun 09. PMID: 26604417; PMCID: PMC4648863.
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Comparative evaluation of Jatropha curcas L. seed meals obtained by different methods of defatting on toxic, antinutritional and nutritive factors.

Journal of food science and technology

Xiao J, Zhang H.
PMID: 24876645
J Food Sci Technol. 2014 Jun;51(6):1126-32. doi: 10.1007/s13197-011-0608-5. Epub 2011 Dec 24.

Different methods of defatting have a great impact on toxic, antinutritional and nutritive factors in the oilseed meals. In order to find the most suitable methods of defatting for Jatropha curcas seed meals, the Jatropha curcas L. seed meals,...

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Xiao J, Zhang H. Comparative evaluation of Jatropha curcas L. seed meals obtained by different methods of defatting on toxic, antinutritional and nutritive factors. J Food Sci Technol. 2011;51(6):1126-32doi: 10.1007/s13197-011-0608-5.
Xiao, J., & Zhang, H. (2014). Comparative evaluation of Jatropha curcas L. seed meals obtained by different methods of defatting on toxic, antinutritional and nutritive factors. Journal of food science and technology, 51(6), 1126-32. https://doi.org/10.1007/s13197-011-0608-5
Xiao, Jianhui, and Zhang, Hui. "Comparative evaluation of Jatropha curcas L. seed meals obtained by different methods of defatting on toxic, antinutritional and nutritive factors." Journal of food science and technology vol. 51,6 (2014): 1126-32. doi: https://doi.org/10.1007/s13197-011-0608-5
Xiao J, Zhang H. Comparative evaluation of Jatropha curcas L. seed meals obtained by different methods of defatting on toxic, antinutritional and nutritive factors. J Food Sci Technol. 2014 Jun;51(6):1126-32. doi: 10.1007/s13197-011-0608-5. Epub 2011 Dec 24. PMID: 24876645; PMCID: PMC4033745.
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Initiation of the degradation of the soybean kunitz and bowman-birk trypsin inhibitors by a cysteine protease.

Plant physiology

Papastoitsis G, Wilson KA.
PMID: 16668302
Plant Physiol. 1991 Aug;96(4):1086-92. doi: 10.1104/pp.96.4.1086.

Protease K1 activity initiates the degradation of the Kunitz soybean trypsin inhibitor (KSTI) during germination and early seedling growth. This enzyme was purified nearly 1300-fold from the cotyledons of 4-day-old soybean (Glycine max [L.] Merrill) seedlings. Protease K1 is...

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Papastoitsis G, Wilson KA. Initiation of the degradation of the soybean kunitz and bowman-birk trypsin inhibitors by a cysteine protease. Plant Physiol. 1991;96(4):1086-92doi: 10.1104/pp.96.4.1086.
Papastoitsis, G., & Wilson, K. A. (1991). Initiation of the degradation of the soybean kunitz and bowman-birk trypsin inhibitors by a cysteine protease. Plant physiology, 96(4), 1086-92. https://doi.org/10.1104/pp.96.4.1086
Papastoitsis, G, and Wilson, K A. "Initiation of the degradation of the soybean kunitz and bowman-birk trypsin inhibitors by a cysteine protease." Plant physiology vol. 96,4 (1991): 1086-92. doi: https://doi.org/10.1104/pp.96.4.1086
Papastoitsis G, Wilson KA. Initiation of the degradation of the soybean kunitz and bowman-birk trypsin inhibitors by a cysteine protease. Plant Physiol. 1991 Aug;96(4):1086-92. doi: 10.1104/pp.96.4.1086. PMID: 16668302; PMCID: PMC1080897.
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Real Time FRET Based Detection of Mechanical Stress in Cytoskeletal and Extracellular Matrix Proteins.

Cellular and molecular bioengineering

Meng F, Suchyna TM, Lazakovitch E, Gronostajski RM, Sachs F.
PMID: 21625401
Cell Mol Bioeng. 2011 Jun;4(2):148-159. doi: 10.1007/s12195-010-0140-0.

A molecular force sensing cassette (stFRET) was incorporated into actinin, filamin, and spectrin in vascular endothelial cells (BAECs) and into collagen-19 in Caenorhabditis elegans. To estimate the stress sensitivity of stFRET in solution, we used DNA springs. A 60-mer...

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Meng F, Suchyna TM, Lazakovitch E, et al. Real Time FRET Based Detection of Mechanical Stress in Cytoskeletal and Extracellular Matrix Proteins. Cell Mol Bioeng. 2011;4(2):148-159doi: 10.1007/s12195-010-0140-0.
Meng, F., Suchyna, T. M., Lazakovitch, E., Gronostajski, R. M., & Sachs, F. (2011). Real Time FRET Based Detection of Mechanical Stress in Cytoskeletal and Extracellular Matrix Proteins. Cellular and molecular bioengineering, 4(2), 148-159. https://doi.org/10.1007/s12195-010-0140-0
Meng, Fanjie, et al. "Real Time FRET Based Detection of Mechanical Stress in Cytoskeletal and Extracellular Matrix Proteins." Cellular and molecular bioengineering vol. 4,2 (2011): 148-159. doi: https://doi.org/10.1007/s12195-010-0140-0
Meng F, Suchyna TM, Lazakovitch E, Gronostajski RM, Sachs F. Real Time FRET Based Detection of Mechanical Stress in Cytoskeletal and Extracellular Matrix Proteins. Cell Mol Bioeng. 2011 Jun;4(2):148-159. doi: 10.1007/s12195-010-0140-0. PMID: 21625401; PMCID: PMC3101475.
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Isolation and characterization of a cDNA that encodes an agrin homolog in the marine ray.

Molecular and cellular neurosciences

Smith MA, Magill-Solc C, Rupp F, Yao YM, Schilling JW, Snow P, McMahan UJ.
PMID: 19912884
Mol Cell Neurosci. 1992 Oct;3(5):406-17. doi: 10.1016/1044-7431(92)90052-4.

Agrin, the protein thought to trigger motor neuron-induced aggregation of postsynaptic molecules at the developing neuromuscular junction, has been purified from the synapse-rich electric organ of the marine ray. In order to study agrin's role in synaptogenesis and to...

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Smith MA, Magill-Solc C, Rupp F, et al. Isolation and characterization of a cDNA that encodes an agrin homolog in the marine ray. Mol Cell Neurosci. 1992;3(5):406-17doi: 10.1016/1044-7431(92)90052-4.
Smith, M. A., Magill-Solc, C., Rupp, F., Yao, Y. M., Schilling, J. W., Snow, P., & McMahan, U. J. (1992). Isolation and characterization of a cDNA that encodes an agrin homolog in the marine ray. Molecular and cellular neurosciences, 3(5), 406-17. https://doi.org/10.1016/1044-7431(92)90052-4
Smith, M A, et al. "Isolation and characterization of a cDNA that encodes an agrin homolog in the marine ray." Molecular and cellular neurosciences vol. 3,5 (1992): 406-17. doi: https://doi.org/10.1016/1044-7431(92)90052-4
Smith MA, Magill-Solc C, Rupp F, Yao YM, Schilling JW, Snow P, McMahan UJ. Isolation and characterization of a cDNA that encodes an agrin homolog in the marine ray. Mol Cell Neurosci. 1992 Oct;3(5):406-17. doi: 10.1016/1044-7431(92)90052-4. PMID: 19912884.
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The spectrum of low molecular weight alpha-amylase/protease inhibitor genes expressed in the US bread wheat cultivar Butte 86.

BMC research notes

Altenbach SB, Vensel WH, Dupont FM.
PMID: 21774824
BMC Res Notes. 2011 Jul 20;4:242. doi: 10.1186/1756-0500-4-242.

BACKGROUND: Wheat grains accumulate a variety of low molecular weight proteins that are inhibitors of alpha-amylases and proteases and play an important protective role in the grain. These proteins have more balanced amino acid compositions than the major wheat...

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Altenbach SB, Vensel WH, Dupont FM. The spectrum of low molecular weight alpha-amylase/protease inhibitor genes expressed in the US bread wheat cultivar Butte 86. BMC Res Notes. 2011;4:242doi: 10.1186/1756-0500-4-242.
Altenbach, S. B., Vensel, W. H., & Dupont, F. M. (2011). The spectrum of low molecular weight alpha-amylase/protease inhibitor genes expressed in the US bread wheat cultivar Butte 86. BMC research notes, 4242. https://doi.org/10.1186/1756-0500-4-242
Altenbach, Susan B, et al. "The spectrum of low molecular weight alpha-amylase/protease inhibitor genes expressed in the US bread wheat cultivar Butte 86." BMC research notes vol. 4 (2011): 242. doi: https://doi.org/10.1186/1756-0500-4-242
Altenbach SB, Vensel WH, Dupont FM. The spectrum of low molecular weight alpha-amylase/protease inhibitor genes expressed in the US bread wheat cultivar Butte 86. BMC Res Notes. 2011 Jul 20;4:242. doi: 10.1186/1756-0500-4-242. PMID: 21774824; PMCID: PMC3154163.
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[Analysis of protein bodies isolated from Lablab purpureus (L.) Sweet: Intracellular localisation of globulins, proteases and trypsin inhibitors].

Planta

Miège MN, Mascherpa JM, Royer-Spierer A, Grange A, Miège J.
PMID: 24424699
Planta. 1976 Jan;131(1):81-6. doi: 10.1007/BF00387349.

Cotyledonary cells are submitted to fractionation by isopycnic centrifugation. Small intact protein bodies are collected in the densest zones (d=1.205-1.237 g/cm(3)). Fragments of larger bodies are gathered in zones of lower density (d=1.205 g/cm(3)). Small dense bodies are largely...

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Miège MN, Mascherpa JM, Royer-Spierer A, et al. Analyse des corps proteiques isolés de Lablab purpureus (L.) Sweet: Localisation intracellulaire des globulines, protéases et inhibiteurs de la trypsine. [Analysis of protein bodies isolated from Lablab purpureus (L.) Sweet: Intracellular localisation of globulins, proteases and trypsin inhibitors]. Planta. 1976;131(1):81-6doi: 10.1007/BF00387349.
Miège, M. N., Mascherpa, J. M., Royer-Spierer, A., Grange, A., & Miège, J. (1976). Analyse des corps proteiques isolés de Lablab purpureus (L.) Sweet: Localisation intracellulaire des globulines, protéases et inhibiteurs de la trypsine. [Analysis of protein bodies isolated from Lablab purpureus (L.) Sweet: Intracellular localisation of globulins, proteases and trypsin inhibitors]. Planta, 131(1), 81-6. https://doi.org/10.1007/BF00387349
Miège, M N, et al. "Analyse des corps proteiques isolés de Lablab purpureus (L.) Sweet: Localisation intracellulaire des globulines, protéases et inhibiteurs de la trypsine." [Analysis of protein bodies isolated from Lablab purpureus (L.) Sweet: Intracellular localisation of globulins, proteases and trypsin inhibitors]. Planta vol. 131,1 (1976): 81-6. doi: https://doi.org/10.1007/BF00387349
Miège MN, Mascherpa JM, Royer-Spierer A, Grange A, Miège J. Analyse des corps proteiques isolés de Lablab purpureus (L.) Sweet: Localisation intracellulaire des globulines, protéases et inhibiteurs de la trypsine. [Analysis of protein bodies isolated from Lablab purpureus (L.) Sweet: Intracellular localisation of globulins, proteases and trypsin inhibitors]. Planta. 1976 Jan;131(1):81-6. doi: 10.1007/BF00387349. French. PMID: 24424699.
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Effect of legume seed extracts on the inhibition of proteolytic activity and muscle degradation of fresh water prawn (Macrobrachiumrosenbergii).

Food chemistry

Sriket C, Benjakul S, Visessanguan W, Hara K.
PMID: 25212342
Food Chem. 2011 Dec 01;129(3):1093-9. doi: 10.1016/j.foodchem.2011.05.080. Epub 2011 May 25.

Trypsin inhibitors in the extracts from soybean (Glycine max), adzuki bean (Vigna angularis), bambara groundnut (Vigna subterranea) and red kidney bean (Phaseoulus vulgaris) varied in amount and molecular weight. The soybean extract had the highest level of trypsin inhibitor...

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Sriket C, Benjakul S, Visessanguan W, et al. Effect of legume seed extracts on the inhibition of proteolytic activity and muscle degradation of fresh water prawn (Macrobrachiumrosenbergii). Food Chem. 2011;129(3):1093-9doi: 10.1016/j.foodchem.2011.05.080.
Sriket, C., Benjakul, S., Visessanguan, W., & Hara, K. (2011). Effect of legume seed extracts on the inhibition of proteolytic activity and muscle degradation of fresh water prawn (Macrobrachiumrosenbergii). Food chemistry, 129(3), 1093-9. https://doi.org/10.1016/j.foodchem.2011.05.080
Sriket, Chodsana, et al. "Effect of legume seed extracts on the inhibition of proteolytic activity and muscle degradation of fresh water prawn (Macrobrachiumrosenbergii)." Food chemistry vol. 129,3 (2011): 1093-9. doi: https://doi.org/10.1016/j.foodchem.2011.05.080
Sriket C, Benjakul S, Visessanguan W, Hara K. Effect of legume seed extracts on the inhibition of proteolytic activity and muscle degradation of fresh water prawn (Macrobrachiumrosenbergii). Food Chem. 2011 Dec 01;129(3):1093-9. doi: 10.1016/j.foodchem.2011.05.080. Epub 2011 May 25. PMID: 25212342.
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Urinary trypsin inhibitor attenuates liver enzyme elevation after liver resection.

Korean journal of anesthesiology

Jeong CW, Lee CS, Lee SH, Jeung HJ, Kwak SH.
PMID: 22949978
Korean J Anesthesiol. 2012 Aug;63(2):120-3. doi: 10.4097/kjae.2012.63.2.120. Epub 2012 Aug 14.

BACKGROUND: Urinary trypsin inhibitors (UTI) have been widely used for the treatment of diseases including disseminated intravascular coagulation, shock, and pancreatitis. Since UTI synthesis is likely to be reduced in patients who have undergone liver resection, the incidence of...

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Jeong CW, Lee CS, Lee SH, et al. Urinary trypsin inhibitor attenuates liver enzyme elevation after liver resection. Korean J Anesthesiol. 2012;63(2):120-3doi: 10.4097/kjae.2012.63.2.120.
Jeong, C. W., Lee, C. S., Lee, S. H., Jeung, H. J., & Kwak, S. H. (2012). Urinary trypsin inhibitor attenuates liver enzyme elevation after liver resection. Korean journal of anesthesiology, 63(2), 120-3. https://doi.org/10.4097/kjae.2012.63.2.120
Jeong, Cheol-Won, et al. "Urinary trypsin inhibitor attenuates liver enzyme elevation after liver resection." Korean journal of anesthesiology vol. 63,2 (2012): 120-3. doi: https://doi.org/10.4097/kjae.2012.63.2.120
Jeong CW, Lee CS, Lee SH, Jeung HJ, Kwak SH. Urinary trypsin inhibitor attenuates liver enzyme elevation after liver resection. Korean J Anesthesiol. 2012 Aug;63(2):120-3. doi: 10.4097/kjae.2012.63.2.120. Epub 2012 Aug 14. PMID: 22949978; PMCID: PMC3427803.
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Screening, Purification and Characterization of Protease Inhibitor from .

Bioinformation

Mohan M, Kozhithodi S, Nayarisseri A, Elyas KK.
PMID: 30237674
Bioinformation. 2018 Jun 30;14(6):285-293. doi: 10.6026/97320630014285. eCollection 2018.

Plants are rich in protease inhibitors (PI) and trypsin inhibitors are the most common. Therefore, it is of interest to screen PI from plant sources. We report the screening, purification and characterization of PI from Capsicum frutescenes. The partially...

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Mohan M, Kozhithodi S, Nayarisseri A, et al. Screening, Purification and Characterization of Protease Inhibitor from . Bioinformation. 2018;14(6):285-293doi: 10.6026/97320630014285.
Mohan, M., Kozhithodi, S., Nayarisseri, A., & Elyas, K. K. (2018). Screening, Purification and Characterization of Protease Inhibitor from . Bioinformation, 14(6), 285-293. https://doi.org/10.6026/97320630014285
Mohan, Manju, et al. "Screening, Purification and Characterization of Protease Inhibitor from ." Bioinformation vol. 14,6 (2018): 285-293. doi: https://doi.org/10.6026/97320630014285
Mohan M, Kozhithodi S, Nayarisseri A, Elyas KK. Screening, Purification and Characterization of Protease Inhibitor from . Bioinformation. 2018 Jun 30;14(6):285-293. doi: 10.6026/97320630014285. eCollection 2018. PMID: 30237674; PMCID: PMC6137568.
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Showing 1 to 12 of 108 entries