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Microbial diversity and functional characterization of sediments from reservoirs of different trophic state.

FEMS microbiology ecology

Wobus A, Bleul C, Maassen S, Scheerer C, Schuppler M, Jacobs E, Röske I.
PMID: 19719563
FEMS Microbiol Ecol. 2003 Dec 01;46(3):331-47. doi: 10.1016/S0168-6496(03)00249-6.

Sediment samples from four reservoirs of different trophic state were compared with regard to chemical gradients in the pore water, composition of microbial communities and extracellular enzyme activities. The trophic state was clearly reflected by steep vertical concentration gradients...

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Wobus A, Bleul C, Maassen S, et al. Microbial diversity and functional characterization of sediments from reservoirs of different trophic state. FEMS Microbiol Ecol. 2003;46(3):331-47doi: 10.1016/S0168-6496(03)00249-6.
Wobus, A., Bleul, C., Maassen, S., Scheerer, C., Schuppler, M., Jacobs, E., & Röske, I. (2003). Microbial diversity and functional characterization of sediments from reservoirs of different trophic state. FEMS microbiology ecology, 46(3), 331-47. https://doi.org/10.1016/S0168-6496(03)00249-6
Wobus, Axel, et al. "Microbial diversity and functional characterization of sediments from reservoirs of different trophic state." FEMS microbiology ecology vol. 46,3 (2003): 331-47. doi: https://doi.org/10.1016/S0168-6496(03)00249-6
Wobus A, Bleul C, Maassen S, Scheerer C, Schuppler M, Jacobs E, Röske I. Microbial diversity and functional characterization of sediments from reservoirs of different trophic state. FEMS Microbiol Ecol. 2003 Dec 01;46(3):331-47. doi: 10.1016/S0168-6496(03)00249-6. PMID: 19719563.
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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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Design and evaluation of inhibitors of enkephalin degrading enzymes.

Neurochemistry international

Fournie-Zaluski MC.
PMID: 20501241
Neurochem Int. 1988;12(3):375-82. doi: 10.1016/0197-0186(88)90177-5.

The endogenous opioid peptides enkephalins are degraded in vitro by several metallopeptidases (aminopeptidases, enkephalinase, dipeptidylaminopeptidases). Selective and mixed inhibitors of these enzymes were obtained by a rational approach taking into account crystallographic data on Thermolysin, a bacterial enzyme, used...

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Fournie-Zaluski MC. Design and evaluation of inhibitors of enkephalin degrading enzymes. Neurochem Int. 1988;12(3):375-82doi: 10.1016/0197-0186(88)90177-5.
Fournie-Zaluski, M. C. (1988). Design and evaluation of inhibitors of enkephalin degrading enzymes. Neurochemistry international, 12(3), 375-82. https://doi.org/10.1016/0197-0186(88)90177-5
Fournie-Zaluski, M C. "Design and evaluation of inhibitors of enkephalin degrading enzymes." Neurochemistry international vol. 12,3 (1988): 375-82. doi: https://doi.org/10.1016/0197-0186(88)90177-5
Fournie-Zaluski MC. Design and evaluation of inhibitors of enkephalin degrading enzymes. Neurochem Int. 1988;12(3):375-82. doi: 10.1016/0197-0186(88)90177-5. PMID: 20501241.
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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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Bioinformatic Analysis, Molecular Modeling of Role of Lys65 Residue in Catalytic Triad of D-aminopeptidase from Ochrobactrum anthropi.

Acta naturae

Khaliullin IG, Suplatov DA, Shalaeva DN, Otsuka M, Asano Y, Svedas VK.
PMID: 22649642
Acta Naturae. 2010 Jul;2(2):66-71.

A bioinformatic and phylogenetic study has been performed on a family of penicillin-binding proteins including D-aminopeptidases, D-amino acid amidases, DD-carboxypeptidases, and β -lactamases. Significant homology between D-aminopeptidase from Ochrobactrum anthropi and other members of the family has been shown...

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Khaliullin IG, Suplatov DA, Shalaeva DN, et al. Bioinformatic Analysis, Molecular Modeling of Role of Lys65 Residue in Catalytic Triad of D-aminopeptidase from Ochrobactrum anthropi. Acta Naturae. 2010;2(2):66-71
Khaliullin, I. G., Suplatov, D. A., Shalaeva, D. N., Otsuka, M., Asano, Y., & Svedas, V. K. (2010). Bioinformatic Analysis, Molecular Modeling of Role of Lys65 Residue in Catalytic Triad of D-aminopeptidase from Ochrobactrum anthropi. Acta naturae, 2(2), 66-71.
Khaliullin, I G, et al. "Bioinformatic Analysis, Molecular Modeling of Role of Lys65 Residue in Catalytic Triad of D-aminopeptidase from Ochrobactrum anthropi." Acta naturae vol. 2,2 (2010): 66-71.
Khaliullin IG, Suplatov DA, Shalaeva DN, Otsuka M, Asano Y, Svedas VK. Bioinformatic Analysis, Molecular Modeling of Role of Lys65 Residue in Catalytic Triad of D-aminopeptidase from Ochrobactrum anthropi. Acta Naturae. 2010 Jul;2(2):66-71. PMID: 22649642; PMCID: PMC3347556.
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Physiological and pathophysiological roles of placental aminopeptidase in maternal sera: possible relation to preeclampsia and preterm delivery.

Expert opinion on medical diagnostics

Mizutani S, Naruse K, Hattori A, Tsujimoto M, Kobayashi H.
PMID: 23495979
Expert Opin Med Diagn. 2009 Sep;3(5):479-91. doi: 10.1517/17530050903074556. Epub 2009 Jul 29.

BACKGROUND: Both preeclampsia and preterm delivery are important complications in pregnancy and are still diseases of unknown causes, despite considerable research in recent times. These complications constitute obstetric emergencies that require expert knowledge and management skills.OBJECTIVES: This article reviews...

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Mizutani S, Naruse K, Hattori A, et al. Physiological and pathophysiological roles of placental aminopeptidase in maternal sera: possible relation to preeclampsia and preterm delivery. Expert Opin Med Diagn. 2009;3(5):479-91doi: 10.1517/17530050903074556.
Mizutani, S., Naruse, K., Hattori, A., Tsujimoto, M., & Kobayashi, H. (2009). Physiological and pathophysiological roles of placental aminopeptidase in maternal sera: possible relation to preeclampsia and preterm delivery. Expert opinion on medical diagnostics, 3(5), 479-91. https://doi.org/10.1517/17530050903074556
Mizutani, Shigehiko, et al. "Physiological and pathophysiological roles of placental aminopeptidase in maternal sera: possible relation to preeclampsia and preterm delivery." Expert opinion on medical diagnostics vol. 3,5 (2009): 479-91. doi: https://doi.org/10.1517/17530050903074556
Mizutani S, Naruse K, Hattori A, Tsujimoto M, Kobayashi H. Physiological and pathophysiological roles of placental aminopeptidase in maternal sera: possible relation to preeclampsia and preterm delivery. Expert Opin Med Diagn. 2009 Sep;3(5):479-91. doi: 10.1517/17530050903074556. Epub 2009 Jul 29. PMID: 23495979.
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Characterization of aspartyl aminopeptidase from Toxoplasma gondii.

Scientific reports

Zheng J, Cheng Z, Jia H, Zheng Y.
PMID: 27678060
Sci Rep. 2016 Sep 28;6:34448. doi: 10.1038/srep34448.

Aminopeptidases have emerged as new promising drug targets for the development of novel anti-parasitic drugs. An aspartyl aminopeptidase-like gene has been identified in the Toxoplasma gondii genome (TgAAP), although its function remains unknown. In this study, we characterized TgAAP...

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Zheng J, Cheng Z, Jia H, et al. Characterization of aspartyl aminopeptidase from Toxoplasma gondii. Sci Rep. 2016;6:34448doi: 10.1038/srep34448.
Zheng, J., Cheng, Z., Jia, H., & Zheng, Y. (2016). Characterization of aspartyl aminopeptidase from Toxoplasma gondii. Scientific reports, 634448. https://doi.org/10.1038/srep34448
Zheng, Jun, et al. "Characterization of aspartyl aminopeptidase from Toxoplasma gondii." Scientific reports vol. 6 (2016): 34448. doi: https://doi.org/10.1038/srep34448
Zheng J, Cheng Z, Jia H, Zheng Y. Characterization of aspartyl aminopeptidase from Toxoplasma gondii. Sci Rep. 2016 Sep 28;6:34448. doi: 10.1038/srep34448. PMID: 27678060; PMCID: PMC5039622.
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Comparative effects of angiotensin II and angiotensin-(4-8) on blood pressure and ANP secretion in rats.

The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology

Phuong HTA, Yu L, Park BM, Kim SH.
PMID: 29200910
Korean J Physiol Pharmacol. 2017 Nov;21(6):667-674. doi: 10.4196/kjpp.2017.21.6.667. Epub 2017 Oct 30.

Angiotensin II (Ang II) is metabolized from N-terminal by aminopeptidases and from C-terminal by Ang converting enzyme (ACE) to generate several truncated angiotensin peptides (Angs). The truncated Angs have different biological effects but it remains unknown whether Ang-(4-8) is...

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Phuong HTA, Yu L, Park BM, et al. Comparative effects of angiotensin II and angiotensin-(4-8) on blood pressure and ANP secretion in rats. Korean J Physiol Pharmacol. 2017;21(6):667-674doi: 10.4196/kjpp.2017.21.6.667.
Phuong, H. T. A., Yu, L., Park, B. M., & Kim, S. H. (2017). Comparative effects of angiotensin II and angiotensin-(4-8) on blood pressure and ANP secretion in rats. The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology, 21(6), 667-674. https://doi.org/10.4196/kjpp.2017.21.6.667
Phuong, Hoang Thi Ai, et al. "Comparative effects of angiotensin II and angiotensin-(4-8) on blood pressure and ANP secretion in rats." The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology vol. 21,6 (2017): 667-674. doi: https://doi.org/10.4196/kjpp.2017.21.6.667
Phuong HTA, Yu L, Park BM, Kim SH. Comparative effects of angiotensin II and angiotensin-(4-8) on blood pressure and ANP secretion in rats. Korean J Physiol Pharmacol. 2017 Nov;21(6):667-674. doi: 10.4196/kjpp.2017.21.6.667. Epub 2017 Oct 30. PMID: 29200910; PMCID: PMC5709484.
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Thyroid Disorders Change the Pattern of Response of Angiotensinase Activities in the Hypothalamus-Pituitary-Adrenal Axis of Male Rats.

Frontiers in endocrinology

Segarra AB, Prieto I, Martínez-Cañamero M, de Gasparo M, Luna JD, Ramírez-Sánchez M.
PMID: 30555423
Front Endocrinol (Lausanne). 2018 Nov 30;9:731. doi: 10.3389/fendo.2018.00731. eCollection 2018.

Thyroid disorders affect the hypothalamic-pituitary-adrenal axis with important consequences on the cardiovascular function in which the renin-angiotensin system plays a major role. Hypo and hyperthyroidism influence the classic main components of the renin-angiotensin system. However, the behavior of other...

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Segarra AB, Prieto I, Martínez-Cañamero M, et al. Thyroid Disorders Change the Pattern of Response of Angiotensinase Activities in the Hypothalamus-Pituitary-Adrenal Axis of Male Rats. Front Endocrinol (Lausanne). 2018;9:731doi: 10.3389/fendo.2018.00731.
Segarra, A. B., Prieto, I., Martínez-Cañamero, M., de Gasparo, M., Luna, J. D., & Ramírez-Sánchez, M. (2018). Thyroid Disorders Change the Pattern of Response of Angiotensinase Activities in the Hypothalamus-Pituitary-Adrenal Axis of Male Rats. Frontiers in endocrinology, 9731. https://doi.org/10.3389/fendo.2018.00731
Segarra, Ana B, et al. "Thyroid Disorders Change the Pattern of Response of Angiotensinase Activities in the Hypothalamus-Pituitary-Adrenal Axis of Male Rats." Frontiers in endocrinology vol. 9 (2018): 731. doi: https://doi.org/10.3389/fendo.2018.00731
Segarra AB, Prieto I, Martínez-Cañamero M, de Gasparo M, Luna JD, Ramírez-Sánchez M. Thyroid Disorders Change the Pattern of Response of Angiotensinase Activities in the Hypothalamus-Pituitary-Adrenal Axis of Male Rats. Front Endocrinol (Lausanne). 2018 Nov 30;9:731. doi: 10.3389/fendo.2018.00731. eCollection 2018. PMID: 30555423; PMCID: PMC6283893.
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Klotho and Aminopeptidases as Early Biomarkers of Renal Injury in Zucker Obese Rats.

Frontiers in physiology

Montoro-Molina S, López-Carmona A, Quesada A, O'Valle F, Martín-Morales N, Osuna A, Vargas F, Wangensteen R.
PMID: 30483154
Front Physiol. 2018 Nov 13;9:1599. doi: 10.3389/fphys.2018.01599. eCollection 2018.

The aim of this study was to investigate if urinary glutamyl aminopeptidase (GluAp), alanyl aminopeptidase (AlaAp), Klotho and hydroxyproline can be considered as potential biomarkers of renal injury and fibrosis in an experimental model of obesity. Male Zucker lean...

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Montoro-Molina S, López-Carmona A, Quesada A, et al. Klotho and Aminopeptidases as Early Biomarkers of Renal Injury in Zucker Obese Rats. Front Physiol. 2018;9:1599doi: 10.3389/fphys.2018.01599.
Montoro-Molina, S., López-Carmona, A., Quesada, A., O'Valle, F., Martín-Morales, N., Osuna, A., Vargas, F., & Wangensteen, R. (2018). Klotho and Aminopeptidases as Early Biomarkers of Renal Injury in Zucker Obese Rats. Frontiers in physiology, 91599. https://doi.org/10.3389/fphys.2018.01599
Montoro-Molina, Sebastián, et al. "Klotho and Aminopeptidases as Early Biomarkers of Renal Injury in Zucker Obese Rats." Frontiers in physiology vol. 9 (2018): 1599. doi: https://doi.org/10.3389/fphys.2018.01599
Montoro-Molina S, López-Carmona A, Quesada A, O'Valle F, Martín-Morales N, Osuna A, Vargas F, Wangensteen R. Klotho and Aminopeptidases as Early Biomarkers of Renal Injury in Zucker Obese Rats. Front Physiol. 2018 Nov 13;9:1599. doi: 10.3389/fphys.2018.01599. eCollection 2018. PMID: 30483154; PMCID: PMC6243116.
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Selective inhibition of Helicobacter pylori methionine aminopeptidase by azaindole hydroxamic acid derivatives: Design, synthesis, in vitro biochemical and structural studies.

Bioorganic chemistry

Bala S, Yellamanda KV, Kadari A, Ravinuthala VSU, Kattula B, Singh OV, Gundla R, Addlagatta A.
PMID: 34329997
Bioorg Chem. 2021 Oct;115:105185. doi: 10.1016/j.bioorg.2021.105185. Epub 2021 Jul 21.

Methionine aminopeptidases (MetAPs) are an important class of enzymes that work co-translationally for the removal of initiator methionine. Chemical inhibition or gene knockdown is lethal to the microbes suggesting that they can be used as antibiotic targets. However, sequence...

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Bala S, Yellamanda KV, Kadari A, et al. Selective inhibition of Helicobacter pylori methionine aminopeptidase by azaindole hydroxamic acid derivatives: Design, synthesis, in vitro biochemical and structural studies. Bioorg Chem. 2021;115:105185doi: 10.1016/j.bioorg.2021.105185.
Bala, S., Yellamanda, K. V., Kadari, A., Ravinuthala, V. S. U., Kattula, B., Singh, O. V., Gundla, R., & Addlagatta, A. (2021). Selective inhibition of Helicobacter pylori methionine aminopeptidase by azaindole hydroxamic acid derivatives: Design, synthesis, in vitro biochemical and structural studies. Bioorganic chemistry, 115105185. https://doi.org/10.1016/j.bioorg.2021.105185
Bala, Sandeepchowdary, et al. "Selective inhibition of Helicobacter pylori methionine aminopeptidase by azaindole hydroxamic acid derivatives: Design, synthesis, in vitro biochemical and structural studies." Bioorganic chemistry vol. 115 (2021): 105185. doi: https://doi.org/10.1016/j.bioorg.2021.105185
Bala S, Yellamanda KV, Kadari A, Ravinuthala VSU, Kattula B, Singh OV, Gundla R, Addlagatta A. Selective inhibition of Helicobacter pylori methionine aminopeptidase by azaindole hydroxamic acid derivatives: Design, synthesis, in vitro biochemical and structural studies. Bioorg Chem. 2021 Oct;115:105185. doi: 10.1016/j.bioorg.2021.105185. Epub 2021 Jul 21. PMID: 34329997.
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Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway.

Proceedings of the National Academy of Sciences of the United States of America

Chen SJ, Kim L, Song HK, Varshavsky A.
PMID: 34663735
Proc Natl Acad Sci U S A. 2021 Oct 26;118(43). doi: 10.1073/pnas.2115430118.

N-degron pathways are proteolytic systems that recognize proteins bearing N-terminal (Nt) degradation signals (degrons) called N-degrons. Our previous work identified Gid4 as a recognition component (N-recognin) of the

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Chen SJ, Kim L, Song HK, et al. Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway. Proc Natl Acad Sci U S A. 2021;118(43)doi: 10.1073/pnas.2115430118.
Chen, S. J., Kim, L., Song, H. K., & Varshavsky, A. (2021). Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway. Proceedings of the National Academy of Sciences of the United States of America, 118(43), . https://doi.org/10.1073/pnas.2115430118
Chen, Shun-Jia, et al. "Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway." Proceedings of the National Academy of Sciences of the United States of America vol. 118,43 (2021). doi: https://doi.org/10.1073/pnas.2115430118
Chen SJ, Kim L, Song HK, Varshavsky A. Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway. Proc Natl Acad Sci U S A. 2021 Oct 26;118(43). doi: 10.1073/pnas.2115430118. PMID: 34663735; PMCID: PMC8639330.
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Showing 13 to 24 of 100 entries