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Isoenzyme frequencies in long-term selection lines of Drosophila melanogaster: IV. Isoenzyme frequencies of the leucine aminopeptidases (LAP) in lines selected for short and long developmental rate.

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik

Muhs HJ.
PMID: 24419997
Theor Appl Genet. 1975 Jan;46(5):215-20. doi: 10.1007/BF00289372.

1) Selection lines derived from a reference line, the continuation of an initial population which were founded by a double cross of four laboratory stocks, were selected for short (line KS and K) and long (line LS and L)...

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Muhs HJ. Isoenzyme frequencies in long-term selection lines of Drosophila melanogaster: IV. Isoenzyme frequencies of the leucine aminopeptidases (LAP) in lines selected for short and long developmental rate. Theor Appl Genet. 1975;46(5):215-20doi: 10.1007/BF00289372.
Muhs, H. J. (1975). Isoenzyme frequencies in long-term selection lines of Drosophila melanogaster: IV. Isoenzyme frequencies of the leucine aminopeptidases (LAP) in lines selected for short and long developmental rate. TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik, 46(5), 215-20. https://doi.org/10.1007/BF00289372
Muhs, H J. "Isoenzyme frequencies in long-term selection lines of Drosophila melanogaster: IV. Isoenzyme frequencies of the leucine aminopeptidases (LAP) in lines selected for short and long developmental rate." TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik vol. 46,5 (1975): 215-20. doi: https://doi.org/10.1007/BF00289372
Muhs HJ. Isoenzyme frequencies in long-term selection lines of Drosophila melanogaster: IV. Isoenzyme frequencies of the leucine aminopeptidases (LAP) in lines selected for short and long developmental rate. Theor Appl Genet. 1975 Jan;46(5):215-20. doi: 10.1007/BF00289372. PMID: 24419997.
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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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Spotlight on Melphalan Flufenamide: An Up-and-Coming Therapy for the Treatment of Myeloma.

Drug design, development and therapy

Morabito F, Tripepi G, Martino EA, Vigna E, Mendicino F, Morabito L, Todoerti K, Al-Janazreh H, D'Arrigo G, Canale FA, Cutrona G, Neri A, Martino M, Gentile M.
PMID: 34262262
Drug Des Devel Ther. 2021 Jul 08;15:2969-2978. doi: 10.2147/DDDT.S295215. eCollection 2021.

Despite recent therapeutic advances, multiple myeloma (MM) patients experience relapses as they become resistant to various classes and combinations of treatment. Melphalan (L-PAM) is an ageless drug. However, its use in the autologous stem cell transplantation (ASCT) setting and...

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Morabito F, Tripepi G, Martino EA, et al. Spotlight on Melphalan Flufenamide: An Up-and-Coming Therapy for the Treatment of Myeloma. Drug Des Devel Ther. 2021;15:2969-2978doi: 10.2147/DDDT.S295215.
Morabito, F., Tripepi, G., Martino, E. A., Vigna, E., Mendicino, F., Morabito, L., Todoerti, K., Al-Janazreh, H., D'Arrigo, G., Canale, F. A., Cutrona, G., Neri, A., Martino, M., & Gentile, M. (2021). Spotlight on Melphalan Flufenamide: An Up-and-Coming Therapy for the Treatment of Myeloma. Drug design, development and therapy, 152969-2978. https://doi.org/10.2147/DDDT.S295215
Morabito, Fortunato, et al. "Spotlight on Melphalan Flufenamide: An Up-and-Coming Therapy for the Treatment of Myeloma." Drug design, development and therapy vol. 15 (2021): 2969-2978. doi: https://doi.org/10.2147/DDDT.S295215
Morabito F, Tripepi G, Martino EA, Vigna E, Mendicino F, Morabito L, Todoerti K, Al-Janazreh H, D'Arrigo G, Canale FA, Cutrona G, Neri A, Martino M, Gentile M. Spotlight on Melphalan Flufenamide: An Up-and-Coming Therapy for the Treatment of Myeloma. Drug Des Devel Ther. 2021 Jul 08;15:2969-2978. doi: 10.2147/DDDT.S295215. eCollection 2021. PMID: 34262262; PMCID: PMC8275138.
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Gene Variation of Endoplasmic Reticulum Aminopeptidases 1 and 2, and Risk of Blood Pressure Progression and Incident Hypertension among 17,255 Initially Healthy Women.

International journal of genomics

Zee RYL, Rivera A, Inostroza Y, Ridker PM, Chasman DI, Romero JR.
PMID: 29850473
Int J Genomics. 2018 Apr 19;2018:2308585. doi: 10.1155/2018/2308585. eCollection 2018.

Recent studies have demonstrated the importance of endoplasmic reticulum aminopeptidase (ERAP) in blood pressure (BP) homeostasis. To date, no large prospective, genetic-epidemiological data are available on genetic variation within ERAP and hypertension risk. The association of 45 genetic variants...

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Zee RYL, Rivera A, Inostroza Y, et al. Gene Variation of Endoplasmic Reticulum Aminopeptidases 1 and 2, and Risk of Blood Pressure Progression and Incident Hypertension among 17,255 Initially Healthy Women. Int J Genomics. 2018;2018:2308585doi: 10.1155/2018/2308585.
Zee, R. Y. L., Rivera, A., Inostroza, Y., Ridker, P. M., Chasman, D. I., & Romero, J. R. (2018). Gene Variation of Endoplasmic Reticulum Aminopeptidases 1 and 2, and Risk of Blood Pressure Progression and Incident Hypertension among 17,255 Initially Healthy Women. International journal of genomics, 20182308585. https://doi.org/10.1155/2018/2308585
Zee, Robert Y L, et al. "Gene Variation of Endoplasmic Reticulum Aminopeptidases 1 and 2, and Risk of Blood Pressure Progression and Incident Hypertension among 17,255 Initially Healthy Women." International journal of genomics vol. 2018 (2018): 2308585. doi: https://doi.org/10.1155/2018/2308585
Zee RYL, Rivera A, Inostroza Y, Ridker PM, Chasman DI, Romero JR. Gene Variation of Endoplasmic Reticulum Aminopeptidases 1 and 2, and Risk of Blood Pressure Progression and Incident Hypertension among 17,255 Initially Healthy Women. Int J Genomics. 2018 Apr 19;2018:2308585. doi: 10.1155/2018/2308585. eCollection 2018. PMID: 29850473; PMCID: PMC5933071.
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Peptidases of the rumen bacterium, Prevotella ruminicola.

Anaerobe

Wallace RJ, McKain N, Broderick GA, Rode LM, Walker ND, Newbold CJ, Kopecny J.
PMID: 16887560
Anaerobe. 1997 Feb;3(1):35-42. doi: 10.1006/anae.1996.0065.

Prevotella (formerly Bacteroides) ruminicola is a numerous rumen bacterium which plays a significant role in the metabolism of proteins and peptides in the rumen. Measurement of the hydrolysis of synthetic aminopeptidase substrates by sonicated extracts and whole cells of...

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Wallace RJ, McKain N, Broderick GA, et al. Peptidases of the rumen bacterium, Prevotella ruminicola. Anaerobe. 1997;3(1):35-42doi: 10.1006/anae.1996.0065.
Wallace, R. J., McKain, N., Broderick, G. A., Rode, L. M., Walker, N. D., Newbold, C. J., & Kopecny, J. (1997). Peptidases of the rumen bacterium, Prevotella ruminicola. Anaerobe, 3(1), 35-42. https://doi.org/10.1006/anae.1996.0065
Wallace, R J, et al. "Peptidases of the rumen bacterium, Prevotella ruminicola." Anaerobe vol. 3,1 (1997): 35-42. doi: https://doi.org/10.1006/anae.1996.0065
Wallace RJ, McKain N, Broderick GA, Rode LM, Walker ND, Newbold CJ, Kopecny J. Peptidases of the rumen bacterium, Prevotella ruminicola. Anaerobe. 1997 Feb;3(1):35-42. doi: 10.1006/anae.1996.0065. PMID: 16887560.
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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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The Analgesic Activity of Bestatin as a Potent APN Inhibitor.

Frontiers in neuroscience

Jia MR, Wei T, Xu WF.
PMID: 20631848
Front Neurosci. 2010 Jun 28;4:50. doi: 10.3389/fnins.2010.00050. eCollection 2010.

Bestatin, a small molecular weight dipeptide, is a potent inhibitor of various aminopeptidases as well as LTA4 hydrolase. Various physiological functions of Bestatin have been identified, viz.: (1) an immunomodifier for enhancing the proliferation of normal human bone marrow...

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Jia MR, Wei T, Xu WF. The Analgesic Activity of Bestatin as a Potent APN Inhibitor. Front Neurosci. 2010;4:50doi: 10.3389/fnins.2010.00050.
Jia, M. R., Wei, T., & Xu, W. F. (2010). The Analgesic Activity of Bestatin as a Potent APN Inhibitor. Frontiers in neuroscience, 450. https://doi.org/10.3389/fnins.2010.00050
Jia, Mei-Rong, et al. "The Analgesic Activity of Bestatin as a Potent APN Inhibitor." Frontiers in neuroscience vol. 4 (2010): 50. doi: https://doi.org/10.3389/fnins.2010.00050
Jia MR, Wei T, Xu WF. The Analgesic Activity of Bestatin as a Potent APN Inhibitor. Front Neurosci. 2010 Jun 28;4:50. doi: 10.3389/fnins.2010.00050. eCollection 2010. PMID: 20631848; PMCID: PMC2903224.
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Distribution of Soil Extracellular Enzymatic, Microbial, and Biological Functions in the C and N-Cycle Pathways Along a Forest Altitudinal Gradient.

Frontiers in microbiology

Bayranvand M, Akbarinia M, Salehi Jouzani G, Gharechahi J, Baldrian P.
PMID: 34539590
Front Microbiol. 2021 Sep 03;12:660603. doi: 10.3389/fmicb.2021.660603. eCollection 2021.

The diverse chemical, biological, and microbial properties of litter and organic matter (OM) in forest soil along an altitudinal gradient are potentially important for nutrient cycling. In the present study, we sought to evaluate soil chemical, biological, microbial, and...

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Bayranvand M, Akbarinia M, Salehi Jouzani G, et al. Distribution of Soil Extracellular Enzymatic, Microbial, and Biological Functions in the C and N-Cycle Pathways Along a Forest Altitudinal Gradient. Front Microbiol. 2021;12:660603doi: 10.3389/fmicb.2021.660603.
Bayranvand, M., Akbarinia, M., Salehi Jouzani, G., Gharechahi, J., & Baldrian, P. (2021). Distribution of Soil Extracellular Enzymatic, Microbial, and Biological Functions in the C and N-Cycle Pathways Along a Forest Altitudinal Gradient. Frontiers in microbiology, 12660603. https://doi.org/10.3389/fmicb.2021.660603
Bayranvand, Mohammad, et al. "Distribution of Soil Extracellular Enzymatic, Microbial, and Biological Functions in the C and N-Cycle Pathways Along a Forest Altitudinal Gradient." Frontiers in microbiology vol. 12 (2021): 660603. doi: https://doi.org/10.3389/fmicb.2021.660603
Bayranvand M, Akbarinia M, Salehi Jouzani G, Gharechahi J, Baldrian P. Distribution of Soil Extracellular Enzymatic, Microbial, and Biological Functions in the C and N-Cycle Pathways Along a Forest Altitudinal Gradient. Front Microbiol. 2021 Sep 03;12:660603. doi: 10.3389/fmicb.2021.660603. eCollection 2021. PMID: 34539590; PMCID: PMC8447401.
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Proteome profiling of clear cell renal cell carcinoma in von Hippel-Lindau patients highlights upregulation of Xaa-Pro aminopeptidase-1, an anti-proliferative and anti-migratory exoprotease.

Oncotarget

Drendel V, Heckelmann B, Chen CY, Weisser J, Espadas G, Schell C, Sabido E, Werner M, Jilg CA, Schilling O.
PMID: 29245961
Oncotarget. 2017 Oct 19;8(59):100066-100078. doi: 10.18632/oncotarget.21929. eCollection 2017 Nov 21.

Patients of the von Hippel-Lindau (VHL) disease frequently develop clear cell renal cell carcinoma (ccRCC). Using archived, formalin-fixed, paraffin-embedded (FFPE) samples, we sought to determine global proteome alterations that distinguish ccRCC tissue from adjacent, non-malignant kidney tissue in VHL-patients....

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Drendel V, Heckelmann B, Chen CY, et al. Proteome profiling of clear cell renal cell carcinoma in von Hippel-Lindau patients highlights upregulation of Xaa-Pro aminopeptidase-1, an anti-proliferative and anti-migratory exoprotease. Oncotarget. 2017;8(59):100066-100078doi: 10.18632/oncotarget.21929.
Drendel, V., Heckelmann, B., Chen, C. Y., Weisser, J., Espadas, G., Schell, C., Sabido, E., Werner, M., Jilg, C. A., & Schilling, O. (2017). Proteome profiling of clear cell renal cell carcinoma in von Hippel-Lindau patients highlights upregulation of Xaa-Pro aminopeptidase-1, an anti-proliferative and anti-migratory exoprotease. Oncotarget, 8(59), 100066-100078. https://doi.org/10.18632/oncotarget.21929
Drendel, Vanessa, et al. "Proteome profiling of clear cell renal cell carcinoma in von Hippel-Lindau patients highlights upregulation of Xaa-Pro aminopeptidase-1, an anti-proliferative and anti-migratory exoprotease." Oncotarget vol. 8,59 (2017): 100066-100078. doi: https://doi.org/10.18632/oncotarget.21929
Drendel V, Heckelmann B, Chen CY, Weisser J, Espadas G, Schell C, Sabido E, Werner M, Jilg CA, Schilling O. Proteome profiling of clear cell renal cell carcinoma in von Hippel-Lindau patients highlights upregulation of Xaa-Pro aminopeptidase-1, an anti-proliferative and anti-migratory exoprotease. Oncotarget. 2017 Oct 19;8(59):100066-100078. doi: 10.18632/oncotarget.21929. eCollection 2017 Nov 21. PMID: 29245961; PMCID: PMC5725003.
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Evidence for conversion of N-Tyr-MIF-1 into MIF-1 by a specific brain aminopeptidase.

Neurochemistry international

Marks N, Berg MJ, Kastin AJ, Coy DH.
PMID: 20488055
Neurochem Int. 1984;6(3):347-53. doi: 10.1016/0197-0186(84)90077-9.

N-Tyr-MIF-1 (Tyr-Pro-Leu-Gly.NH(2)), an immunoreactive neuropeptide exhibiting saturable high affinity binding in rat brain was found to be converted into MIF-1 (Pro-Leu-Gly.NH(2)) by a specific brain aminopeptidase present in rat brain homogenates or cytosol, but with low activity associated with...

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Marks N, Berg MJ, Kastin AJ, et al. Evidence for conversion of N-Tyr-MIF-1 into MIF-1 by a specific brain aminopeptidase. Neurochem Int. 1984;6(3):347-53doi: 10.1016/0197-0186(84)90077-9.
Marks, N., Berg, M. J., Kastin, A. J., & Coy, D. H. (1984). Evidence for conversion of N-Tyr-MIF-1 into MIF-1 by a specific brain aminopeptidase. Neurochemistry international, 6(3), 347-53. https://doi.org/10.1016/0197-0186(84)90077-9
Marks, N, et al. "Evidence for conversion of N-Tyr-MIF-1 into MIF-1 by a specific brain aminopeptidase." Neurochemistry international vol. 6,3 (1984): 347-53. doi: https://doi.org/10.1016/0197-0186(84)90077-9
Marks N, Berg MJ, Kastin AJ, Coy DH. Evidence for conversion of N-Tyr-MIF-1 into MIF-1 by a specific brain aminopeptidase. Neurochem Int. 1984;6(3):347-53. doi: 10.1016/0197-0186(84)90077-9. PMID: 20488055.
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Structural Characterization of Acidic M17 Leucine Aminopeptidases from the TriTryps and Evaluation of Their Role in Nutrient Starvation in .

mSphere

Timm J, Valente M, García-Caballero D, Wilson KS, González-Pacanowska D.
PMID: 28815215
mSphere. 2017 Aug 16;2(4). doi: 10.1128/mSphere.00226-17. eCollection 2017.

Leucine aminopeptidase (LAP) is found in all kingdoms of life and catalyzes the metal-dependent hydrolysis of the N-terminal amino acid residue of peptide or amino acyl substrates. LAPs have been shown to participate in the N-terminal processing of certain...

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Timm J, Valente M, García-Caballero D, et al. Structural Characterization of Acidic M17 Leucine Aminopeptidases from the TriTryps and Evaluation of Their Role in Nutrient Starvation in . mSphere. 2017;2(4)doi: 10.1128/mSphere.00226-17.
Timm, J., Valente, M., García-Caballero, D., Wilson, K. S., & González-Pacanowska, D. (2017). Structural Characterization of Acidic M17 Leucine Aminopeptidases from the TriTryps and Evaluation of Their Role in Nutrient Starvation in . mSphere, 2(4), . https://doi.org/10.1128/mSphere.00226-17
Timm, Jennifer, et al. "Structural Characterization of Acidic M17 Leucine Aminopeptidases from the TriTryps and Evaluation of Their Role in Nutrient Starvation in ." mSphere vol. 2,4 (2017). doi: https://doi.org/10.1128/mSphere.00226-17
Timm J, Valente M, García-Caballero D, Wilson KS, González-Pacanowska D. Structural Characterization of Acidic M17 Leucine Aminopeptidases from the TriTryps and Evaluation of Their Role in Nutrient Starvation in . mSphere. 2017 Aug 16;2(4). doi: 10.1128/mSphere.00226-17. eCollection 2017. PMID: 28815215; PMCID: PMC5557676.
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Is There an Interplay Between the Functional Domains of IRAP?.

Frontiers in cell and developmental biology

Vear A, Gaspari T, Thompson P, Chai SY.
PMID: 33134302
Front Cell Dev Biol. 2020 Sep 29;8:585237. doi: 10.3389/fcell.2020.585237. eCollection 2020.

As a member of the M1 family of aminopeptidases, insulin regulated aminopeptidase (IRAP) is characterized by distinct binding motifs at the active site in the C-terminal domain that mediate the catalysis of peptide substrates. However, what makes IRAP unique...

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Vear A, Gaspari T, Thompson P, et al. Is There an Interplay Between the Functional Domains of IRAP?. Front Cell Dev Biol. 2020;8:585237doi: 10.3389/fcell.2020.585237.
Vear, A., Gaspari, T., Thompson, P., & Chai, S. Y. (2020). Is There an Interplay Between the Functional Domains of IRAP?. Frontiers in cell and developmental biology, 8585237. https://doi.org/10.3389/fcell.2020.585237
Vear, Anika, et al. "Is There an Interplay Between the Functional Domains of IRAP?." Frontiers in cell and developmental biology vol. 8 (2020): 585237. doi: https://doi.org/10.3389/fcell.2020.585237
Vear A, Gaspari T, Thompson P, Chai SY. Is There an Interplay Between the Functional Domains of IRAP?. Front Cell Dev Biol. 2020 Sep 29;8:585237. doi: 10.3389/fcell.2020.585237. eCollection 2020. PMID: 33134302; PMCID: PMC7550531.
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Showing 1 to 12 of 101 entries