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Mirolysin, a LysargiNase from Tannerella forsythia, proteolytically inactivates the human cathelicidin, LL-37.

Biological chemistry

Koneru L, Ksiazek M, Waligorska I, Straczek A, Lukasik M, Madej M, Thøgersen IB, Enghild JJ, Potempa J.
PMID: 27997347
Biol Chem. 2017 Mar;398(3):395-409. doi: 10.1515/hsz-2016-0267.

Tannerella forsythia is a periodontal pathogen expressing six secretory proteolytic enzymes with a unique multidomain structure referred to as KLIKK proteases. Two of these proteases, karilysin and mirolysin, were previously shown to protect the bacterium against complement-mediated bactericidal activity....

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Koneru L, Ksiazek M, Waligorska I, et al. Mirolysin, a LysargiNase from Tannerella forsythia, proteolytically inactivates the human cathelicidin, LL-37. Biol Chem. 2017;398(3):395-409doi: 10.1515/hsz-2016-0267.
Koneru, L., Ksiazek, M., Waligorska, I., Straczek, A., Lukasik, M., Madej, M., Thøgersen, I. B., Enghild, J. J., & Potempa, J. (2017). Mirolysin, a LysargiNase from Tannerella forsythia, proteolytically inactivates the human cathelicidin, LL-37. Biological chemistry, 398(3), 395-409. https://doi.org/10.1515/hsz-2016-0267
Koneru, Lahari, et al. "Mirolysin, a LysargiNase from Tannerella forsythia, proteolytically inactivates the human cathelicidin, LL-37." Biological chemistry vol. 398,3 (2017): 395-409. doi: https://doi.org/10.1515/hsz-2016-0267
Koneru L, Ksiazek M, Waligorska I, Straczek A, Lukasik M, Madej M, Thøgersen IB, Enghild JJ, Potempa J. Mirolysin, a LysargiNase from Tannerella forsythia, proteolytically inactivates the human cathelicidin, LL-37. Biol Chem. 2017 Mar;398(3):395-409. doi: 10.1515/hsz-2016-0267. PMID: 27997347; PMCID: PMC5478484.
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Modulation of Small RNA Signatures in Schwann-Cell-Derived Extracellular Vesicles by the p75 Neurotrophin Receptor and Sortilin.

Biomedicines

Gonçalves NP, Yan Y, Ulrichsen M, Venø MT, Poulsen ET, Enghild JJ, Kjems J, Vægter CB.
PMID: 33114403
Biomedicines. 2020 Oct 24;8(11). doi: 10.3390/biomedicines8110450.

Schwann cells (SCs) are the main glial cells of the peripheral nervous system (PNS) and are known to be involved in various pathophysiological processes, such as diabetic neuropathy and nerve regeneration, through neurotrophin signaling. Such glial trophic support to...

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Gonçalves NP, Yan Y, Ulrichsen M, et al. Modulation of Small RNA Signatures in Schwann-Cell-Derived Extracellular Vesicles by the p75 Neurotrophin Receptor and Sortilin. Biomedicines. 2020;8(11)doi: 10.3390/biomedicines8110450.
Gonçalves, N. P., Yan, Y., Ulrichsen, M., Venø, M. T., Poulsen, E. T., Enghild, J. J., Kjems, J., & Vægter, C. B. (2020). Modulation of Small RNA Signatures in Schwann-Cell-Derived Extracellular Vesicles by the p75 Neurotrophin Receptor and Sortilin. Biomedicines, 8(11), . https://doi.org/10.3390/biomedicines8110450
Gonçalves, Nádia P, et al. "Modulation of Small RNA Signatures in Schwann-Cell-Derived Extracellular Vesicles by the p75 Neurotrophin Receptor and Sortilin." Biomedicines vol. 8,11 (2020). doi: https://doi.org/10.3390/biomedicines8110450
Gonçalves NP, Yan Y, Ulrichsen M, Venø MT, Poulsen ET, Enghild JJ, Kjems J, Vægter CB. Modulation of Small RNA Signatures in Schwann-Cell-Derived Extracellular Vesicles by the p75 Neurotrophin Receptor and Sortilin. Biomedicines. 2020 Oct 24;8(11). doi: 10.3390/biomedicines8110450. PMID: 33114403; PMCID: PMC7694014.
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Author Correction: STEEP mediates STING ER exit and activation of signaling.

Nature immunology

Zhang BC, Nandakumar R, Reinert LS, Huang J, Laustsen A, Gao ZL, Sun CL, Jensen SB, Troldborg A, Assil S, Berthelsen MF, Scavenius C, Zhang Y, Windross SJ, Olagnier D, Prabakaran T, Bodda C, Narita R, Cai Y, Zhang CG, Stenmark H, Doucet CM, Noda T, Guo Z, Goldbach-Mansky R, Hartmann R, Chen ZJ, Enghild JJ, Bak RO, Thomsen MK, Paludan SR.
PMID: 32929276
Nat Immunol. 2020 Nov;21(11):1468-1469. doi: 10.1038/s41590-020-0803-5.

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

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Zhang BC, Nandakumar R, Reinert LS, et al. Author Correction: STEEP mediates STING ER exit and activation of signaling. Nat Immunol. 2020;21(11):1468-1469doi: 10.1038/s41590-020-0803-5.
Zhang, B. C., Nandakumar, R., Reinert, L. S., Huang, J., Laustsen, A., Gao, Z. L., Sun, C. L., Jensen, S. B., Troldborg, A., Assil, S., Berthelsen, M. F., Scavenius, C., Zhang, Y., Windross, S. J., Olagnier, D., Prabakaran, T., Bodda, C., Narita, R., Cai, Y., Zhang, C. G., Stenmark, H., Doucet, C. M., Noda, T., Guo, Z., Goldbach-Mansky, R., Hartmann, R., Chen, Z. J., Enghild, J. J., Bak, R. O., Thomsen, M. K., & Paludan, S. R. (2020). Author Correction: STEEP mediates STING ER exit and activation of signaling. Nature immunology, 21(11), 1468-1469. https://doi.org/10.1038/s41590-020-0803-5
Zhang, Bao-Cun, et al. "Author Correction: STEEP mediates STING ER exit and activation of signaling." Nature immunology vol. 21,11 (2020): 1468-1469. doi: https://doi.org/10.1038/s41590-020-0803-5
Zhang BC, Nandakumar R, Reinert LS, Huang J, Laustsen A, Gao ZL, Sun CL, Jensen SB, Troldborg A, Assil S, Berthelsen MF, Scavenius C, Zhang Y, Windross SJ, Olagnier D, Prabakaran T, Bodda C, Narita R, Cai Y, Zhang CG, Stenmark H, Doucet CM, Noda T, Guo Z, Goldbach-Mansky R, Hartmann R, Chen ZJ, Enghild JJ, Bak RO, Thomsen MK, Paludan SR. Author Correction: STEEP mediates STING ER exit and activation of signaling. Nat Immunol. 2020 Nov;21(11):1468-1469. doi: 10.1038/s41590-020-0803-5. PMID: 32929276.
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FAM20C phosphorylation of the RGDSVVYGLR motif in osteopontin inhibits interaction with the αvβ3 integrin.

Journal of cellular biochemistry

Schytte GN, Christensen B, Bregenov I, Kjøge K, Scavenius C, Petersen SV, Enghild JJ, Sørensen ES.
PMID: 32115754
J Cell Biochem. 2020 Mar 01; doi: 10.1002/jcb.29708. Epub 2020 Mar 01.

Osteopontin (OPN) is a ubiquitously expressed, multifunctional, and highly phosphorylated protein. OPN contains two neighboring integrin-binding motifs, RGD and SVVYGLR, which mediate interaction with cells. Phosphorylation and proteolytic processing affect the integrin-binding activities of OPN. Here we report that...

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Schytte GN, Christensen B, Bregenov I, et al. FAM20C phosphorylation of the RGDSVVYGLR motif in osteopontin inhibits interaction with the αvβ3 integrin. J Cell Biochem. 2020;doi: 10.1002/jcb.29708.
Schytte, G. N., Christensen, B., Bregenov, I., Kjøge, K., Scavenius, C., Petersen, S. V., Enghild, J. J., & Sørensen, E. S. (2020). FAM20C phosphorylation of the RGDSVVYGLR motif in osteopontin inhibits interaction with the αvβ3 integrin. Journal of cellular biochemistry, . https://doi.org/10.1002/jcb.29708
Schytte, Gitte N, et al. "FAM20C phosphorylation of the RGDSVVYGLR motif in osteopontin inhibits interaction with the αvβ3 integrin." Journal of cellular biochemistry vol. (2020). doi: https://doi.org/10.1002/jcb.29708
Schytte GN, Christensen B, Bregenov I, Kjøge K, Scavenius C, Petersen SV, Enghild JJ, Sørensen ES. FAM20C phosphorylation of the RGDSVVYGLR motif in osteopontin inhibits interaction with the αvβ3 integrin. J Cell Biochem. 2020 Mar 01; doi: 10.1002/jcb.29708. Epub 2020 Mar 01. PMID: 32115754.
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Analysis of Factor D Isoforms in Malpuech-Michels-Mingarelli-Carnevale Patients Highlights the Role of MASP-3 as a Maturase in the Alternative Pathway of Complement.

Journal of immunology (Baltimore, Md. : 1950)

Pihl R, Jensen L, Hansen AG, Thøgersen IB, Andres S, Dagnæs-Hansen F, Oexle K, Enghild JJ, Thiel S.
PMID: 28794230
J Immunol. 2017 Aug 09; doi: 10.4049/jimmunol.1700518. Epub 2017 Aug 09.

Factor D (FD), which is also known as adipsin, is regarded as the first-acting protease of the alternative pathway (AP) of complement. It has been suggested that FD is secreted as a mature enzyme that does not require subsequent...

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Pihl R, Jensen L, Hansen AG, et al. Analysis of Factor D Isoforms in Malpuech-Michels-Mingarelli-Carnevale Patients Highlights the Role of MASP-3 as a Maturase in the Alternative Pathway of Complement. J Immunol. 2017;doi: 10.4049/jimmunol.1700518.
Pihl, R., Jensen, L., Hansen, A. G., Thøgersen, I. B., Andres, S., Dagnæs-Hansen, F., Oexle, K., Enghild, J. J., & Thiel, S. (2017). Analysis of Factor D Isoforms in Malpuech-Michels-Mingarelli-Carnevale Patients Highlights the Role of MASP-3 as a Maturase in the Alternative Pathway of Complement. Journal of immunology (Baltimore, Md. : 1950), . https://doi.org/10.4049/jimmunol.1700518
Pihl, Rasmus, et al. "Analysis of Factor D Isoforms in Malpuech-Michels-Mingarelli-Carnevale Patients Highlights the Role of MASP-3 as a Maturase in the Alternative Pathway of Complement." Journal of immunology (Baltimore, Md. : 1950) vol. (2017). doi: https://doi.org/10.4049/jimmunol.1700518
Pihl R, Jensen L, Hansen AG, Thøgersen IB, Andres S, Dagnæs-Hansen F, Oexle K, Enghild JJ, Thiel S. Analysis of Factor D Isoforms in Malpuech-Michels-Mingarelli-Carnevale Patients Highlights the Role of MASP-3 as a Maturase in the Alternative Pathway of Complement. J Immunol. 2017 Aug 09; doi: 10.4049/jimmunol.1700518. Epub 2017 Aug 09. PMID: 28794230.
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Potential clinical importance of the activation peptide of prostate-specific antigen.

International journal of clinical and experimental pathology

Voeghtly LM, Thøgersen IB, Valnickova Z, Sanggaard KW, Chu CT, Oury TD, Enghild JJ.
PMID: 19636406
Int J Clin Exp Pathol. 2009 Jun 20;2(6):588-98.

Prostate cancer is the second leading cause of cancer death in men. Prostate specific antigen (PSA) is currently the best marker available for screening and monitoring disease recurrence, but its use has limitations. This study investigates the biosynthesis, secretion...

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Voeghtly LM, Thøgersen IB, Valnickova Z, et al. Potential clinical importance of the activation peptide of prostate-specific antigen. Int J Clin Exp Pathol. 2009;2(6):588-98
Voeghtly, L. M., Thøgersen, I. B., Valnickova, Z., Sanggaard, K. W., Chu, C. T., Oury, T. D., & Enghild, J. J. (2009). Potential clinical importance of the activation peptide of prostate-specific antigen. International journal of clinical and experimental pathology, 2(6), 588-98.
Voeghtly, Laura M, et al. "Potential clinical importance of the activation peptide of prostate-specific antigen." International journal of clinical and experimental pathology vol. 2,6 (2009): 588-98.
Voeghtly LM, Thøgersen IB, Valnickova Z, Sanggaard KW, Chu CT, Oury TD, Enghild JJ. Potential clinical importance of the activation peptide of prostate-specific antigen. Int J Clin Exp Pathol. 2009 Jun 20;2(6):588-98. PMID: 19636406; PMCID: PMC2713450.
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Unconditioned commercial embryo culture media contain a large variety of non-declared proteins: a comprehensive proteomics analysis.

Human reproduction (Oxford, England)

Dyrlund TF, Kirkegaard K, Poulsen ET, Sanggaard KW, Hindkjær JJ, Kjems J, Enghild JJ, Ingerslev HJ.
PMID: 25164020
Hum Reprod. 2014 Nov;29(11):2421-30. doi: 10.1093/humrep/deu220. Epub 2014 Aug 27.

STUDY QUESTION: Which non-declared proteins (proteins not listed on the composition list of the product data sheet) are present in unconditioned commercial embryo culture media?SUMMARY ANSWER: A total of 110 non-declared proteins were identified in unconditioned media and between...

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Dyrlund TF, Kirkegaard K, Poulsen ET, et al. Unconditioned commercial embryo culture media contain a large variety of non-declared proteins: a comprehensive proteomics analysis. Hum Reprod. 2014;29(11):2421-30doi: 10.1093/humrep/deu220.
Dyrlund, T. F., Kirkegaard, K., Poulsen, E. T., Sanggaard, K. W., Hindkjær, J. J., Kjems, J., Enghild, J. J., & Ingerslev, H. J. (2014). Unconditioned commercial embryo culture media contain a large variety of non-declared proteins: a comprehensive proteomics analysis. Human reproduction (Oxford, England), 29(11), 2421-30. https://doi.org/10.1093/humrep/deu220
Dyrlund, Thomas F, et al. "Unconditioned commercial embryo culture media contain a large variety of non-declared proteins: a comprehensive proteomics analysis." Human reproduction (Oxford, England) vol. 29,11 (2014): 2421-30. doi: https://doi.org/10.1093/humrep/deu220
Dyrlund TF, Kirkegaard K, Poulsen ET, Sanggaard KW, Hindkjær JJ, Kjems J, Enghild JJ, Ingerslev HJ. Unconditioned commercial embryo culture media contain a large variety of non-declared proteins: a comprehensive proteomics analysis. Hum Reprod. 2014 Nov;29(11):2421-30. doi: 10.1093/humrep/deu220. Epub 2014 Aug 27. PMID: 25164020.
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A Protein Corona Modulates Interactions of α-Synuclein with Nanoparticles and Alters the Rates of the Microscopic Steps of Amyloid Formation.

ACS nano

Mohammad-Beigi H, Zanganeh M, Scavenius C, Eskandari H, Farzadfard A, Shojaosadati SA, Enghild JJ, Otzen DE, Buell AK, Sutherland DS.
PMID: 34982538
ACS Nano. 2022 Jan 04; doi: 10.1021/acsnano.1c08825. Epub 2022 Jan 04.

Nanoparticles (NPs) can modulate protein aggregation and fibril formation in the context of amyloid diseases. Understanding the mechanism of this action remains a critical next step in developing nanomedicines for the treatment or prevention of Parkinson's disease. α-Synuclein (α-Syn)...

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Mohammad-Beigi H, Zanganeh M, Scavenius C, et al. A Protein Corona Modulates Interactions of α-Synuclein with Nanoparticles and Alters the Rates of the Microscopic Steps of Amyloid Formation. ACS Nano. 2022;doi: 10.1021/acsnano.1c08825.
Mohammad-Beigi, H., Zanganeh, M., Scavenius, C., Eskandari, H., Farzadfard, A., Shojaosadati, S. A., Enghild, J. J., Otzen, D. E., Buell, A. K., & Sutherland, D. S. (2022). A Protein Corona Modulates Interactions of α-Synuclein with Nanoparticles and Alters the Rates of the Microscopic Steps of Amyloid Formation. ACS nano, . https://doi.org/10.1021/acsnano.1c08825
Mohammad-Beigi, Hossein, et al. "A Protein Corona Modulates Interactions of α-Synuclein with Nanoparticles and Alters the Rates of the Microscopic Steps of Amyloid Formation." ACS nano vol. (2022). doi: https://doi.org/10.1021/acsnano.1c08825
Mohammad-Beigi H, Zanganeh M, Scavenius C, Eskandari H, Farzadfard A, Shojaosadati SA, Enghild JJ, Otzen DE, Buell AK, Sutherland DS. A Protein Corona Modulates Interactions of α-Synuclein with Nanoparticles and Alters the Rates of the Microscopic Steps of Amyloid Formation. ACS Nano. 2022 Jan 04; doi: 10.1021/acsnano.1c08825. Epub 2022 Jan 04. PMID: 34982538.
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Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism.

Molecular & cellular proteomics : MCP

Harwood SL, Lyngsø J, Zarantonello A, Kjøge K, Nielsen PK, Andersen GR, Pedersen JS, Enghild JJ.
PMID: 33964423
Mol Cell Proteomics. 2021;20:100090. doi: 10.1016/j.mcpro.2021.100090. Epub 2021 May 06.

Human α

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Harwood SL, Lyngsø J, Zarantonello A, et al. Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism. Mol Cell Proteomics. 2021;20:100090doi: 10.1016/j.mcpro.2021.100090.
Harwood, S. L., Lyngsø, J., Zarantonello, A., Kjøge, K., Nielsen, P. K., Andersen, G. R., Pedersen, J. S., & Enghild, J. J. (2021). Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism. Molecular & cellular proteomics : MCP, 20100090. https://doi.org/10.1016/j.mcpro.2021.100090
Harwood, Seandean Lykke, et al. "Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism." Molecular & cellular proteomics : MCP vol. 20 (2021): 100090. doi: https://doi.org/10.1016/j.mcpro.2021.100090
Harwood SL, Lyngsø J, Zarantonello A, Kjøge K, Nielsen PK, Andersen GR, Pedersen JS, Enghild JJ. Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism. Mol Cell Proteomics. 2021;20:100090. doi: 10.1016/j.mcpro.2021.100090. Epub 2021 May 06. PMID: 33964423; PMCID: PMC8167298.
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Insight into the Protein Composition of Immunoglobulin Light Chain Deposits of Eyelid, Orbital and Conjunctival Amyloidosis.

Journal of proteomics & bioinformatics

Nielsen NS, Poulsen ET, Klintworth GK, Enghild JJ.
PMID: 26500418
J Proteomics Bioinform. 2014; doi: 10.4172/jpb.S8-002. Epub 2014 Apr 21.

Amyloidosis is a disease characterized by the formation of extracellular amyloid deposits. Immunoglobulin light-chain amyloidosis can appear as a local disorder presenting with mild symptoms or as a life threatening systemic disease. The systemic form of immunoglobulin light-chain amyloidosis...

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Nielsen NS, Poulsen ET, Klintworth GK, et al. Insight into the Protein Composition of Immunoglobulin Light Chain Deposits of Eyelid, Orbital and Conjunctival Amyloidosis. J Proteomics Bioinform. 2014;doi: 10.4172/jpb.S8-002.
Nielsen, N. S., Poulsen, E. T., Klintworth, G. K., & Enghild, J. J. (2014). Insight into the Protein Composition of Immunoglobulin Light Chain Deposits of Eyelid, Orbital and Conjunctival Amyloidosis. Journal of proteomics & bioinformatics, . https://doi.org/10.4172/jpb.S8-002
Nielsen, Nadia Sukusu, et al. "Insight into the Protein Composition of Immunoglobulin Light Chain Deposits of Eyelid, Orbital and Conjunctival Amyloidosis." Journal of proteomics & bioinformatics vol. (2014). doi: https://doi.org/10.4172/jpb.S8-002
Nielsen NS, Poulsen ET, Klintworth GK, Enghild JJ. Insight into the Protein Composition of Immunoglobulin Light Chain Deposits of Eyelid, Orbital and Conjunctival Amyloidosis. J Proteomics Bioinform. 2014; doi: 10.4172/jpb.S8-002. Epub 2014 Apr 21. PMID: 26500418; PMCID: PMC4617654.
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[No title available]

Frontiers in microbiology

Brüggemann H, Poehlein A, Brzuszkiewicz E, Scavenius C, Enghild JJ, Al-Zeer MA, Brinkmann V, Jensen A, Söderquist B.
PMID: 30915059
Front Microbiol. 2019 Mar 12;10:478. doi: 10.3389/fmicb.2019.00478. eCollection 2019.

The slow-growing, anaerobic, coagulase-negative species

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Brüggemann H, Poehlein A, Brzuszkiewicz E, et al. . Front Microbiol. 2019;10:478doi: 10.3389/fmicb.2019.00478.
Brüggemann, H., Poehlein, A., Brzuszkiewicz, E., Scavenius, C., Enghild, J. J., Al-Zeer, M. A., Brinkmann, V., Jensen, A., & Söderquist, B. (2019). . Frontiers in microbiology, 10478. https://doi.org/10.3389/fmicb.2019.00478
Brüggemann, Holger, et al. "." Frontiers in microbiology vol. 10 (2019): 478. doi: https://doi.org/10.3389/fmicb.2019.00478
Brüggemann H, Poehlein A, Brzuszkiewicz E, Scavenius C, Enghild JJ, Al-Zeer MA, Brinkmann V, Jensen A, Söderquist B. . Front Microbiol. 2019 Mar 12;10:478. doi: 10.3389/fmicb.2019.00478. eCollection 2019. PMID: 30915059; PMCID: PMC6423177.
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A Screening Method for the Isolation of Bacteria Capable of Degrading Toxic Steroidal Glycoalkaloids Present in Potato.

Frontiers in microbiology

Hennessy RC, Jørgensen NOG, Scavenius C, Enghild JJ, Greve-Poulsen M, Sørensen OB, Stougaard P.
PMID: 30455676
Front Microbiol. 2018 Nov 05;9:2648. doi: 10.3389/fmicb.2018.02648. eCollection 2018.

Potato juice, a by-product of starch processing, is a potential high-value food ingredient due to its high protein content. However, conversion from feed to human protein requires the removal of the toxic antinutritional glycoalkaloids (GAs) α-chaconine and α-solanine. Detoxification...

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Hennessy RC, Jørgensen NOG, Scavenius C, et al. A Screening Method for the Isolation of Bacteria Capable of Degrading Toxic Steroidal Glycoalkaloids Present in Potato. Front Microbiol. 2018;9:2648doi: 10.3389/fmicb.2018.02648.
Hennessy, R. C., Jørgensen, N. O. G., Scavenius, C., Enghild, J. J., Greve-Poulsen, M., Sørensen, O. B., & Stougaard, P. (2018). A Screening Method for the Isolation of Bacteria Capable of Degrading Toxic Steroidal Glycoalkaloids Present in Potato. Frontiers in microbiology, 92648. https://doi.org/10.3389/fmicb.2018.02648
Hennessy, Rosanna C, et al. "A Screening Method for the Isolation of Bacteria Capable of Degrading Toxic Steroidal Glycoalkaloids Present in Potato." Frontiers in microbiology vol. 9 (2018): 2648. doi: https://doi.org/10.3389/fmicb.2018.02648
Hennessy RC, Jørgensen NOG, Scavenius C, Enghild JJ, Greve-Poulsen M, Sørensen OB, Stougaard P. A Screening Method for the Isolation of Bacteria Capable of Degrading Toxic Steroidal Glycoalkaloids Present in Potato. Front Microbiol. 2018 Nov 05;9:2648. doi: 10.3389/fmicb.2018.02648. eCollection 2018. PMID: 30455676; PMCID: PMC6230958.
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