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Effect of high pressure treatment on colour, microbial and chemical characteristics of dry cured loin

science campus

Campus M, Flores M, Toldrá F.
GSID: ajxTF4M1weAJ
M Campus, M Flores, A Martinez, F Toldrá - Meat Science, 2008 - Elsevier

The effect of high pressure on sliced and vacuum packaged commercial dry-cured pork loin was determined by analysing the induced colour changes, the residual enzymatic activities of cathepsins, aminopeptidases and dipeptidilpeptidases and the changes in the content of …

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Campus, M., Flores, M., Martinez, A., & Toldrá, F. (2008). Effect of high pressure treatment on colour, microbial and chemical characteristics of dry cured loin. Meat Science, 80(4), 1174-1181.
Campus, Marco, et al. "Effect of high pressure treatment on colour, microbial and chemical characteristics of dry cured loin." Meat Science 80.4 (2008): 1174-1181.
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Methodological Considerations and Comparisons of Measurement Results for Extracellular Proteolytic Enzyme Activities in Seawater.

Frontiers in microbiology

Obayashi Y, Wei Bong C, Suzuki S.
PMID: 29067013
Front Microbiol. 2017 Oct 10;8:1952. doi: 10.3389/fmicb.2017.01952. eCollection 2017.

Microbial extracellular hydrolytic enzymes that degrade organic matter in aquatic ecosystems play key roles in the biogeochemical carbon cycle. To provide linkages between hydrolytic enzyme activities and genomic or metabolomic studies in aquatic environments, reliable measurements are required for...

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Obayashi Y, Wei Bong C, Suzuki S. Methodological Considerations and Comparisons of Measurement Results for Extracellular Proteolytic Enzyme Activities in Seawater. Front Microbiol. 2017;8:1952doi: 10.3389/fmicb.2017.01952.
Obayashi, Y., Wei Bong, C., & Suzuki, S. (2017). Methodological Considerations and Comparisons of Measurement Results for Extracellular Proteolytic Enzyme Activities in Seawater. Frontiers in microbiology, 81952. https://doi.org/10.3389/fmicb.2017.01952
Obayashi, Yumiko, et al. "Methodological Considerations and Comparisons of Measurement Results for Extracellular Proteolytic Enzyme Activities in Seawater." Frontiers in microbiology vol. 8 (2017): 1952. doi: https://doi.org/10.3389/fmicb.2017.01952
Obayashi Y, Wei Bong C, Suzuki S. Methodological Considerations and Comparisons of Measurement Results for Extracellular Proteolytic Enzyme Activities in Seawater. Front Microbiol. 2017 Oct 10;8:1952. doi: 10.3389/fmicb.2017.01952. eCollection 2017. PMID: 29067013; PMCID: PMC5641328.
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The role of dissolved organic nitrogen in a nitrate-rich agricultural stream.

Journal of environmental quality

Oviedo-Vargas D, Royer TV.
PMID: 26023984
J Environ Qual. 2015 Mar;44(2):668-75. doi: 10.2134/jeq2014.07.0314.

Agricultural activities have heavily altered the nitrogen (N) cycle in stream ecosystems draining croplands, particularly in the midwestern United States. However, our knowledge about dissolved organic N (DON) biogeochemistry in agricultural ecosystems is limited. From January 2011 to June...

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Oviedo-Vargas D, Royer TV. The role of dissolved organic nitrogen in a nitrate-rich agricultural stream. J Environ Qual. 2015;44(2):668-75doi: 10.2134/jeq2014.07.0314.
Oviedo-Vargas, D., & Royer, T. V. (2015). The role of dissolved organic nitrogen in a nitrate-rich agricultural stream. Journal of environmental quality, 44(2), 668-75. https://doi.org/10.2134/jeq2014.07.0314
Oviedo-Vargas, Diana, and Royer, Todd V. "The role of dissolved organic nitrogen in a nitrate-rich agricultural stream." Journal of environmental quality vol. 44,2 (2015): 668-75. doi: https://doi.org/10.2134/jeq2014.07.0314
Oviedo-Vargas D, Royer TV. The role of dissolved organic nitrogen in a nitrate-rich agricultural stream. J Environ Qual. 2015 Mar;44(2):668-75. doi: 10.2134/jeq2014.07.0314. PMID: 26023984.
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Screening Identifies Thimerosal as a Selective Inhibitor of Endoplasmic Reticulum Aminopeptidase 1.

ACS medicinal chemistry letters

Stamogiannos A, Papakyriakou A, Mauvais FX, van Endert P, Stratikos E.
PMID: 27437077
ACS Med Chem Lett. 2016 May 31;7(7):681-5. doi: 10.1021/acsmedchemlett.6b00084. eCollection 2016 Jul 14.

We employed virtual screening followed by in vitro evaluation to discover novel inhibitors of ER aminopeptidase 1, an important enzyme for the human adaptive immune response that has emerged as an attractive target for cancer immunotherapy and the control...

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Stamogiannos A, Papakyriakou A, Mauvais FX, et al. Screening Identifies Thimerosal as a Selective Inhibitor of Endoplasmic Reticulum Aminopeptidase 1. ACS Med Chem Lett. 2016;7(7):681-5doi: 10.1021/acsmedchemlett.6b00084.
Stamogiannos, A., Papakyriakou, A., Mauvais, F. X., van Endert, P., & Stratikos, E. (2016). Screening Identifies Thimerosal as a Selective Inhibitor of Endoplasmic Reticulum Aminopeptidase 1. ACS medicinal chemistry letters, 7(7), 681-5. https://doi.org/10.1021/acsmedchemlett.6b00084
Stamogiannos, Athanasios, et al. "Screening Identifies Thimerosal as a Selective Inhibitor of Endoplasmic Reticulum Aminopeptidase 1." ACS medicinal chemistry letters vol. 7,7 (2016): 681-5. doi: https://doi.org/10.1021/acsmedchemlett.6b00084
Stamogiannos A, Papakyriakou A, Mauvais FX, van Endert P, Stratikos E. Screening Identifies Thimerosal as a Selective Inhibitor of Endoplasmic Reticulum Aminopeptidase 1. ACS Med Chem Lett. 2016 May 31;7(7):681-5. doi: 10.1021/acsmedchemlett.6b00084. eCollection 2016 Jul 14. PMID: 27437077; PMCID: PMC4948014.
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Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: A cytosolic enzyme with a di-nuclear active site.

FEBS open bio

Iyer S, La-Borde PJ, Payne KA, Parsons MR, Turner AJ, Isaac RE, Acharya KR.
PMID: 25905034
FEBS Open Bio. 2015 Apr 02;5:292-302. doi: 10.1016/j.fob.2015.03.013. eCollection 2015.

Eukaryotic aminopeptidase P1 (APP1), also known as X-prolyl aminopeptidase (XPNPEP1) in human tissues, is a cytosolic exopeptidase that preferentially removes amino acids from the N-terminus of peptides possessing a penultimate N-terminal proline residue. The enzyme has an important role...

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Iyer S, La-Borde PJ, Payne KA, et al. Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: A cytosolic enzyme with a di-nuclear active site. FEBS Open Bio. 2015;5:292-302doi: 10.1016/j.fob.2015.03.013.
Iyer, S., La-Borde, P. J., Payne, K. A., Parsons, M. R., Turner, A. J., Isaac, R. E., & Acharya, K. R. (2015). Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: A cytosolic enzyme with a di-nuclear active site. FEBS open bio, 5292-302. https://doi.org/10.1016/j.fob.2015.03.013
Iyer, Shalini, et al. "Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: A cytosolic enzyme with a di-nuclear active site." FEBS open bio vol. 5 (2015): 292-302. doi: https://doi.org/10.1016/j.fob.2015.03.013
Iyer S, La-Borde PJ, Payne KA, Parsons MR, Turner AJ, Isaac RE, Acharya KR. Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: A cytosolic enzyme with a di-nuclear active site. FEBS Open Bio. 2015 Apr 02;5:292-302. doi: 10.1016/j.fob.2015.03.013. eCollection 2015. PMID: 25905034; PMCID: PMC4404410.
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Determination of the amino acid sequence of peptides using dipeptidyl aminopeptidases.

FEBS letters

Ovchinnikov YA, Kiryushkin AA.
PMID: 11946532
FEBS Lett. 1972 Apr 01;21(3):300-302. doi: 10.1016/0014-5793(72)80188-1.

No abstract available.

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Ovchinnikov YA, Kiryushkin AA. Determination of the amino acid sequence of peptides using dipeptidyl aminopeptidases. FEBS Lett. 1972;21(3):300-302doi: 10.1016/0014-5793(72)80188-1.
Ovchinnikov, Y. A., & Kiryushkin, A. A. (1972). Determination of the amino acid sequence of peptides using dipeptidyl aminopeptidases. FEBS letters, 21(3), 300-302. https://doi.org/10.1016/0014-5793(72)80188-1
Ovchinnikov, Y A., and Kiryushkin, A A.. "Determination of the amino acid sequence of peptides using dipeptidyl aminopeptidases." FEBS letters vol. 21,3 (1972): 300-302. doi: https://doi.org/10.1016/0014-5793(72)80188-1
Ovchinnikov YA, Kiryushkin AA. Determination of the amino acid sequence of peptides using dipeptidyl aminopeptidases. FEBS Lett. 1972 Apr 01;21(3):300-302. doi: 10.1016/0014-5793(72)80188-1. PMID: 11946532.
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Enantiomeric synthesis of (3R)-3-amino-5-methyl-2-oxo-hexan-1-ol hydrochloride from cyclohexylideneglyceraldehyde.

Enantiomer

Sharma A, Chattopadhyay S.
PMID: 10857056
Enantiomer. 2000;5(2):175-9.

The first enantioselective synthesis of the title compound, (3R)-3-amino-5-methyl-2-oxo-hexan-1-ol hydrochloride (9a), an inhibitor of metalloprotein aminopeptidases has been developed from an enantiomerically pure 3-alkylglycerol. The required 3-alkylglycerol was, in turn, prepared by simple Grignard addition to cyclohexylideneglyceraldehyde 1 followed...

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Sharma A, Chattopadhyay S. Enantiomeric synthesis of (3R)-3-amino-5-methyl-2-oxo-hexan-1-ol hydrochloride from cyclohexylideneglyceraldehyde. Enantiomer. 2000;5(2):175-9
Sharma, A., & Chattopadhyay, S. (2000). Enantiomeric synthesis of (3R)-3-amino-5-methyl-2-oxo-hexan-1-ol hydrochloride from cyclohexylideneglyceraldehyde. Enantiomer, 5(2), 175-9.
Sharma, and Chattopadhyay. "Enantiomeric synthesis of (3R)-3-amino-5-methyl-2-oxo-hexan-1-ol hydrochloride from cyclohexylideneglyceraldehyde." Enantiomer vol. 5,2 (2000): 175-9.
Sharma A, Chattopadhyay S. Enantiomeric synthesis of (3R)-3-amino-5-methyl-2-oxo-hexan-1-ol hydrochloride from cyclohexylideneglyceraldehyde. Enantiomer. 2000;5(2):175-9. PMID: 10857056.
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Modifications of Etioplasts in Cotyledons during Prolonged Dark Growth of Sugar Beet Seedlings (Identification of Etiolation-Related Plastidial Aminopeptidase Activities).

Plant physiology

Amrani AE, Couee I, Carde JP, Gaudillere JP, Raymond P.
PMID: 12232431
Plant Physiol. 1994 Dec;106(4):1555-1565. doi: 10.1104/pp.106.4.1555.

We studied the effects of prolonged dark growth on proplastids and etioplasts in cotyledons of sugar beet (Beta vulgaris L.) seedlings. Differentiation of proplastids into etioplasts occurred between d 4 and d 6 after imbibition, with the typical characteristics...

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Amrani AE, Couee I, Carde JP, et al. Modifications of Etioplasts in Cotyledons during Prolonged Dark Growth of Sugar Beet Seedlings (Identification of Etiolation-Related Plastidial Aminopeptidase Activities). Plant Physiol. 1994;106(4):1555-1565doi: 10.1104/pp.106.4.1555.
Amrani, A. E., Couee, I., Carde, J. P., Gaudillere, J. P., & Raymond, P. (1994). Modifications of Etioplasts in Cotyledons during Prolonged Dark Growth of Sugar Beet Seedlings (Identification of Etiolation-Related Plastidial Aminopeptidase Activities). Plant physiology, 106(4), 1555-1565. https://doi.org/10.1104/pp.106.4.1555
Amrani, A. E., et al. "Modifications of Etioplasts in Cotyledons during Prolonged Dark Growth of Sugar Beet Seedlings (Identification of Etiolation-Related Plastidial Aminopeptidase Activities)." Plant physiology vol. 106,4 (1994): 1555-1565. doi: https://doi.org/10.1104/pp.106.4.1555
Amrani AE, Couee I, Carde JP, Gaudillere JP, Raymond P. Modifications of Etioplasts in Cotyledons during Prolonged Dark Growth of Sugar Beet Seedlings (Identification of Etiolation-Related Plastidial Aminopeptidase Activities). Plant Physiol. 1994 Dec;106(4):1555-1565. doi: 10.1104/pp.106.4.1555. PMID: 12232431; PMCID: PMC159698.
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Partial Purification and Characterization of Aminopeptidase II from Chara australis.

Plant physiology

Moriyasu Y, Miyoshi Y.
PMID: 16666602
Plant Physiol. 1989 Feb;89(2):687-91. doi: 10.1104/pp.89.2.687.

Aminopeptidase II, one of the two major aminopeptidases in the giant alga Chara australis, was partially purified. Its molecular weight was estimated to be about 80,000 by gel permeation chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis showed that it...

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Moriyasu Y, Miyoshi Y. Partial Purification and Characterization of Aminopeptidase II from Chara australis. Plant Physiol. 1989;89(2):687-91doi: 10.1104/pp.89.2.687.
Moriyasu, Y., & Miyoshi, Y. (1989). Partial Purification and Characterization of Aminopeptidase II from Chara australis. Plant physiology, 89(2), 687-91. https://doi.org/10.1104/pp.89.2.687
Moriyasu, Y, and Miyoshi, Y. "Partial Purification and Characterization of Aminopeptidase II from Chara australis." Plant physiology vol. 89,2 (1989): 687-91. doi: https://doi.org/10.1104/pp.89.2.687
Moriyasu Y, Miyoshi Y. Partial Purification and Characterization of Aminopeptidase II from Chara australis. Plant Physiol. 1989 Feb;89(2):687-91. doi: 10.1104/pp.89.2.687. PMID: 16666602; PMCID: PMC1055902.
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Proteases and Peptidases of Castor Bean Endosperm: Enzyme Characterization and Changes during Germination.

Plant physiology

Tully RE, Beevers H.
PMID: 16660598
Plant Physiol. 1978 Nov;62(5):746-50. doi: 10.1104/pp.62.5.746.

The endosperm of castor bean seeds (Ricinus communis L.) contains two -SH-dependent aminopeptidases, one hydrolyzing l-leucine-beta-naphthylamide optimally at pH 7.0, and the other hydrolyzing l-proline-beta-naphthylamide optimally at pH 7.5. After germination the endosperm contains in addition an -SH-dependent hemoglobin...

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Tully RE, Beevers H. Proteases and Peptidases of Castor Bean Endosperm: Enzyme Characterization and Changes during Germination. Plant Physiol. 1978;62(5):746-50doi: 10.1104/pp.62.5.746.
Tully, R. E., & Beevers, H. (1978). Proteases and Peptidases of Castor Bean Endosperm: Enzyme Characterization and Changes during Germination. Plant physiology, 62(5), 746-50. https://doi.org/10.1104/pp.62.5.746
Tully, R E, and Beevers, H. "Proteases and Peptidases of Castor Bean Endosperm: Enzyme Characterization and Changes during Germination." Plant physiology vol. 62,5 (1978): 746-50. doi: https://doi.org/10.1104/pp.62.5.746
Tully RE, Beevers H. Proteases and Peptidases of Castor Bean Endosperm: Enzyme Characterization and Changes during Germination. Plant Physiol. 1978 Nov;62(5):746-50. doi: 10.1104/pp.62.5.746. PMID: 16660598; PMCID: PMC1092213.
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Neutral peptidases in the stroma of pea chloroplasts.

Plant physiology

Liu XQ, Jagendorf AT.
PMID: 16664864
Plant Physiol. 1986 Jun;81(2):603-8. doi: 10.1104/pp.81.2.603.

One endopeptidase (EP1) and at least three aminopeptidases (AP1, AP2, and AP3) were discovered in the stroma of chloroplasts isolated from pea seedlings (Pisum sativum L.), and purified over 100-fold. EP1 requires added Mg(2+) or Ca(2+) for activity, may...

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Liu XQ, Jagendorf AT. Neutral peptidases in the stroma of pea chloroplasts. Plant Physiol. 1986;81(2):603-8doi: 10.1104/pp.81.2.603.
Liu, X. Q., & Jagendorf, A. T. (1986). Neutral peptidases in the stroma of pea chloroplasts. Plant physiology, 81(2), 603-8. https://doi.org/10.1104/pp.81.2.603
Liu, X Q, and Jagendorf, A T. "Neutral peptidases in the stroma of pea chloroplasts." Plant physiology vol. 81,2 (1986): 603-8. doi: https://doi.org/10.1104/pp.81.2.603
Liu XQ, Jagendorf AT. Neutral peptidases in the stroma of pea chloroplasts. Plant Physiol. 1986 Jun;81(2):603-8. doi: 10.1104/pp.81.2.603. PMID: 16664864; PMCID: PMC1075384.
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Localization of peptidases in lactococci.

Applied and environmental microbiology

Tan PS, Chapot-Chartier MP, Pos KM, Rousseau M, Boquien CY, Gripon JC, Konings WN.
PMID: 16348629
Appl Environ Microbiol. 1992 Jan;58(1):285-90. doi: 10.1128/aem.58.1.285-290.1992.

The localization of two aminopeptidases, an X-prolyl-dipeptidyl aminopeptidase, an endopeptidase, and a tripeptidase in Lactococcus lactis was studied. Polyclonal antibodies raised against each purified peptidase are specific and do not cross-react with other peptidases. Experiments were performed by immunoblotting...

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Tan PS, Chapot-Chartier MP, Pos KM, et al. Localization of peptidases in lactococci. Appl Environ Microbiol. 1992;58(1):285-90doi: 10.1128/aem.58.1.285-290.1992.
Tan, P. S., Chapot-Chartier, M. P., Pos, K. M., Rousseau, M., Boquien, C. Y., Gripon, J. C., & Konings, W. N. (1992). Localization of peptidases in lactococci. Applied and environmental microbiology, 58(1), 285-90. https://doi.org/10.1128/aem.58.1.285-290.1992
Tan, P S, et al. "Localization of peptidases in lactococci." Applied and environmental microbiology vol. 58,1 (1992): 285-90. doi: https://doi.org/10.1128/aem.58.1.285-290.1992
Tan PS, Chapot-Chartier MP, Pos KM, Rousseau M, Boquien CY, Gripon JC, Konings WN. Localization of peptidases in lactococci. Appl Environ Microbiol. 1992 Jan;58(1):285-90. doi: 10.1128/aem.58.1.285-290.1992. PMID: 16348629; PMCID: PMC195205.
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Showing 1 to 12 of 100 entries