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Identification and bioinformatic analysis of neprilysin and neprilysin-like metalloendopeptidases in .

microPublication biology

Meyer H, Buhr A, Callaerts P, Schiemann R, Wolfner MF, Marygold SJ.
PMID: 34189422
MicroPubl Biol. 2021 Jun 23;2021. doi: 10.17912/micropub.biology.000410.

The neprilysin (M13) family of metalloendopeptidases comprises highly conserved ectoenzymes that cleave and thereby inactivate many physiologically relevant peptides in the extracellular space. Impaired neprilysin activity is associated with numerous human diseases. Here, we present a comprehensive list and...

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Meyer H, Buhr A, Callaerts P, et al. Identification and bioinformatic analysis of neprilysin and neprilysin-like metalloendopeptidases in . MicroPubl Biol. 2021;2021doi: 10.17912/micropub.biology.000410.
Meyer, H., Buhr, A., Callaerts, P., Schiemann, R., Wolfner, M. F., & Marygold, S. J. (2021). Identification and bioinformatic analysis of neprilysin and neprilysin-like metalloendopeptidases in . microPublication biology, 2021. https://doi.org/10.17912/micropub.biology.000410
Meyer, Heiko, et al. "Identification and bioinformatic analysis of neprilysin and neprilysin-like metalloendopeptidases in ." microPublication biology vol. 2021 (2021). doi: https://doi.org/10.17912/micropub.biology.000410
Meyer H, Buhr A, Callaerts P, Schiemann R, Wolfner MF, Marygold SJ. Identification and bioinformatic analysis of neprilysin and neprilysin-like metalloendopeptidases in . MicroPubl Biol. 2021 Jun 23;2021. doi: 10.17912/micropub.biology.000410. PMID: 34189422; PMCID: PMC8223033.
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Development of Endopeptidase Activities in Maize (Zea mays L.) Endosperms.

Plant physiology

Mitsuhashi W, Oaks A.
PMID: 12232091
Plant Physiol. 1994 Feb;104(2):401-407. doi: 10.1104/pp.104.2.401.

An activity stain was used after native polyacrylamide gel electrophoresis, and at least 17 different endopeptidase activities were detected in maize (Zea mays L.) endosperm extracts prepared during the first 6 d after imbibition. The enzymes detected were classified...

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Mitsuhashi W, Oaks A. Development of Endopeptidase Activities in Maize (Zea mays L.) Endosperms. Plant Physiol. 1994;104(2):401-407doi: 10.1104/pp.104.2.401.
Mitsuhashi, W., & Oaks, A. (1994). Development of Endopeptidase Activities in Maize (Zea mays L.) Endosperms. Plant physiology, 104(2), 401-407. https://doi.org/10.1104/pp.104.2.401
Mitsuhashi, W., and Oaks, A.. "Development of Endopeptidase Activities in Maize (Zea mays L.) Endosperms." Plant physiology vol. 104,2 (1994): 401-407. doi: https://doi.org/10.1104/pp.104.2.401
Mitsuhashi W, Oaks A. Development of Endopeptidase Activities in Maize (Zea mays L.) Endosperms. Plant Physiol. 1994 Feb;104(2):401-407. doi: 10.1104/pp.104.2.401. PMID: 12232091; PMCID: PMC159212.
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Purification, characterization, and structural elucidation of serralysin-like alkaline metalloprotease from a novel source.

Journal, genetic engineering & biotechnology

Nageswara S, Guntuku G, Yakkali BL.
PMID: 31659553
J Genet Eng Biotechnol. 2019 Sep 23;17(1):1. doi: 10.1186/s43141-019-0002-7.

BACKGROUND: Serratiopeptidase is an alkaline metalloendopeptidase, which acquired wide significance because of its therapeutic applications. The present study was undertaken for purification, characterization, and structural elucidation of serratiopeptidase produced from Streptomyces hydrogenans var. MGS13.RESULT: The crude enzyme was purified...

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Nageswara S, Guntuku G, Yakkali BL. Purification, characterization, and structural elucidation of serralysin-like alkaline metalloprotease from a novel source. J Genet Eng Biotechnol. 2019;17(1):1doi: 10.1186/s43141-019-0002-7.
Nageswara, S., Guntuku, G., & Yakkali, B. L. (2019). Purification, characterization, and structural elucidation of serralysin-like alkaline metalloprotease from a novel source. Journal, genetic engineering & biotechnology, 17(1), 1. https://doi.org/10.1186/s43141-019-0002-7
Nageswara, Swathi, et al. "Purification, characterization, and structural elucidation of serralysin-like alkaline metalloprotease from a novel source." Journal, genetic engineering & biotechnology vol. 17,1 (2019): 1. doi: https://doi.org/10.1186/s43141-019-0002-7
Nageswara S, Guntuku G, Yakkali BL. Purification, characterization, and structural elucidation of serralysin-like alkaline metalloprotease from a novel source. J Genet Eng Biotechnol. 2019 Sep 23;17(1):1. doi: 10.1186/s43141-019-0002-7. PMID: 31659553; PMCID: PMC6821148.
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Proteolytic processing and inactivation of CCL2/MCP-1 by meprins.

Biochemistry and biophysics reports

Herzog C, Haun RS, Shah SV, Kaushal GP.
PMID: 28955950
Biochem Biophys Rep. 2016 Aug 21;8:146-150. doi: 10.1016/j.bbrep.2016.08.019. eCollection 2016 Dec.

Monocyte chemotactic protein 1 (CCL2/MCP-1) is a small chemokine involved in the recruitment and trafficking of mononuclear immune cells to inflammation sites. Our studies demonstrate that the metalloendopeptidases meprin A (purified from kidney cortex), recombinant meprin α, and recombinant...

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Herzog C, Haun RS, Shah SV, et al. Proteolytic processing and inactivation of CCL2/MCP-1 by meprins. Biochem Biophys Rep. 2016;8:146-150doi: 10.1016/j.bbrep.2016.08.019.
Herzog, C., Haun, R. S., Shah, S. V., & Kaushal, G. P. (2016). Proteolytic processing and inactivation of CCL2/MCP-1 by meprins. Biochemistry and biophysics reports, 8146-150. https://doi.org/10.1016/j.bbrep.2016.08.019
Herzog, Christian, et al. "Proteolytic processing and inactivation of CCL2/MCP-1 by meprins." Biochemistry and biophysics reports vol. 8 (2016): 146-150. doi: https://doi.org/10.1016/j.bbrep.2016.08.019
Herzog C, Haun RS, Shah SV, Kaushal GP. Proteolytic processing and inactivation of CCL2/MCP-1 by meprins. Biochem Biophys Rep. 2016 Aug 21;8:146-150. doi: 10.1016/j.bbrep.2016.08.019. eCollection 2016 Dec. PMID: 28955950; PMCID: PMC5613766.
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Enhanced Systemic Response of Matrix Metalloproteinases and Their Regulators in .

Diagnostics (Basel, Switzerland)

Nilsson A, Tervahartiala T, Lennebratt D, Lannergård A, Sorsa T, Rautelin H.
PMID: 30551610
Diagnostics (Basel). 2018 Dec 13;8(4). doi: 10.3390/diagnostics8040082.

Campylobacters are major enteropathogens worldwide with a substantial financial burden. Matrix metalloproteinases (MMPs) are proteolytic metalloendopeptidases with ability to modify immune response and shown to be upregulated in patients with several tissue destructive diseases, including infections. We measured here...

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Nilsson A, Tervahartiala T, Lennebratt D, et al. Enhanced Systemic Response of Matrix Metalloproteinases and Their Regulators in . Diagnostics (Basel). 2018;8(4)doi: 10.3390/diagnostics8040082.
Nilsson, A., Tervahartiala, T., Lennebratt, D., Lannergård, A., Sorsa, T., & Rautelin, H. (2018). Enhanced Systemic Response of Matrix Metalloproteinases and Their Regulators in . Diagnostics (Basel, Switzerland), 8(4), . https://doi.org/10.3390/diagnostics8040082
Nilsson, Anna, et al. "Enhanced Systemic Response of Matrix Metalloproteinases and Their Regulators in ." Diagnostics (Basel, Switzerland) vol. 8,4 (2018). doi: https://doi.org/10.3390/diagnostics8040082
Nilsson A, Tervahartiala T, Lennebratt D, Lannergård A, Sorsa T, Rautelin H. Enhanced Systemic Response of Matrix Metalloproteinases and Their Regulators in . Diagnostics (Basel). 2018 Dec 13;8(4). doi: 10.3390/diagnostics8040082. PMID: 30551610; PMCID: PMC6315616.
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Modulation of Matrix Metalloproteinases by Plant-derived Products.

Current cancer drug targets

Anuar NNM, Zulkafali NIN, Ugusman A.
PMID: 33222671
Curr Cancer Drug Targets. 2021;21(2):91-106. doi: 10.2174/1568009620666201120144838.

Matrix metalloproteinases (MMPs) are a group of zinc-dependent metalloendopeptidases that are responsible for the degradation, repair, and remodeling of extracellular matrix components. MMPs play an important role in maintaining a normal physiological function and preventing diseases, such as cancer...

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Anuar NNM, Zulkafali NIN, Ugusman A. Modulation of Matrix Metalloproteinases by Plant-derived Products. Curr Cancer Drug Targets. 2021;21(2):91-106doi: 10.2174/1568009620666201120144838.
Anuar, N. N. M., Zulkafali, N. I. N., & Ugusman, A. (2021). Modulation of Matrix Metalloproteinases by Plant-derived Products. Current cancer drug targets, 21(2), 91-106. https://doi.org/10.2174/1568009620666201120144838
Anuar, Nur Najmi Mohamad, et al. "Modulation of Matrix Metalloproteinases by Plant-derived Products." Current cancer drug targets vol. 21,2 (2021): 91-106. doi: https://doi.org/10.2174/1568009620666201120144838
Anuar NNM, Zulkafali NIN, Ugusman A. Modulation of Matrix Metalloproteinases by Plant-derived Products. Curr Cancer Drug Targets. 2021;21(2):91-106. doi: 10.2174/1568009620666201120144838. PMID: 33222671.
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Showing 1 to 6 of 6 entries