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Showing 1 to 12 of 12 entries
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The “human side” of open innovation: The role of employee diversity in firm-level openness

Stem workforce diversity

Bogers M, Foss NJ, Lyngsie J.
GSID: TDEsozJrLnIJ
M Bogers, NJ Foss, J Lyngsie - Research Policy, 2018 - Elsevier

The use of external knowledge for innovation (ie, inbound or outside-in open innovation) has received substantial attention in the innovation literature. However, the “human side” of open innovation is still poorly understood. We consider the role of employee characteristics...

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Bogers, M., Foss, N. J., & Lyngsie, J. (2018). The “human side” of open innovation: The role of employee diversity in firm-level openness. Research Policy, 47(1), 218-231.
Bogers, Marcel, Nicolai J. Foss, and Jacob Lyngsie. "The “human side” of open innovation: The role of employee diversity in firm-level openness." Research Policy 47.1 (2018): 218-231.
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Modeling Small-Angle X-ray Scattering Data for Low-Density Lipoproteins: Insights into the Fatty Core Packing and Phase Transition.

ACS nano

Maric S, Lind TK, Lyngsø J, Cárdenas M, Pedersen JS.
PMID: 28048943
ACS Nano. 2017 Jan 24;11(1):1080-1090. doi: 10.1021/acsnano.6b08089. Epub 2017 Jan 10.

Atherosclerosis and its clinical consequences are the leading cause of death in the western hemisphere. While many studies throughout the last decades have aimed at understanding the disease, the clinical markers in use today still fail to accurately predict...

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Maric S, Lind TK, Lyngsø J, et al. Modeling Small-Angle X-ray Scattering Data for Low-Density Lipoproteins: Insights into the Fatty Core Packing and Phase Transition. ACS Nano. 2017;11(1):1080-1090doi: 10.1021/acsnano.6b08089.
Maric, S., Lind, T. K., Lyngsø, J., Cárdenas, M., & Pedersen, J. S. (2017). Modeling Small-Angle X-ray Scattering Data for Low-Density Lipoproteins: Insights into the Fatty Core Packing and Phase Transition. ACS nano, 11(1), 1080-1090. https://doi.org/10.1021/acsnano.6b08089
Maric, Selma, et al. "Modeling Small-Angle X-ray Scattering Data for Low-Density Lipoproteins: Insights into the Fatty Core Packing and Phase Transition." ACS nano vol. 11,1 (2017): 1080-1090. doi: https://doi.org/10.1021/acsnano.6b08089
Maric S, Lind TK, Lyngsø J, Cárdenas M, Pedersen JS. Modeling Small-Angle X-ray Scattering Data for Low-Density Lipoproteins: Insights into the Fatty Core Packing and Phase Transition. ACS Nano. 2017 Jan 24;11(1):1080-1090. doi: 10.1021/acsnano.6b08089. Epub 2017 Jan 10. PMID: 28048943.
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A complete picture of protein unfolding and refolding in surfactants.

Chemical science

Pedersen JN, Lyngsø J, Zinn T, Otzen DE, Pedersen JS.
PMID: 34123043
Chem Sci. 2019 Nov 22;11(3):699-712. doi: 10.1039/c9sc04831f.

Interactions between proteins and surfactants are of relevance in many applications including food, washing powder formulations, and drug formulation. The anionic surfactant sodium dodecyl sulfate (SDS) is known to unfold globular proteins, while the non-ionic surfactant octaethyleneglycol monododecyl ether...

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Pedersen JN, Lyngsø J, Zinn T, et al. A complete picture of protein unfolding and refolding in surfactants. Chem Sci. 2019;11(3):699-712doi: 10.1039/c9sc04831f.
Pedersen, J. N., Lyngsø, J., Zinn, T., Otzen, D. E., & Pedersen, J. S. (2019). A complete picture of protein unfolding and refolding in surfactants. Chemical science, 11(3), 699-712. https://doi.org/10.1039/c9sc04831f
Pedersen, Jannik Nedergaard, et al. "A complete picture of protein unfolding and refolding in surfactants." Chemical science vol. 11,3 (2019): 699-712. doi: https://doi.org/10.1039/c9sc04831f
Pedersen JN, Lyngsø J, Zinn T, Otzen DE, Pedersen JS. A complete picture of protein unfolding and refolding in surfactants. Chem Sci. 2019 Nov 22;11(3):699-712. doi: 10.1039/c9sc04831f. PMID: 34123043; PMCID: PMC8145811.
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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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Stain-free histopathology by programmable supercontinuum pulses.

Nature photonics

Tu H, Liu Y, Turchinovich D, Marjanovic M, Lyngsø J, Lægsgaard J, Chaney EJ, Zhao Y, You S, Wilson WL, Xu B, Dantus M, Boppart SA.
PMID: 27668009
Nat Photonics. 2016 Aug;10(8):534-540. doi: 10.1038/nphoton.2016.94. Epub 2016 May 23.

The preparation, staining, visualization, and interpretation of histological images of tissue is well-accepted as the gold standard process for the diagnosis of disease. These methods were developed historically, and are used ubiquitously in pathology, despite being highly time and...

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Tu H, Liu Y, Turchinovich D, et al. Stain-free histopathology by programmable supercontinuum pulses. Nat Photonics. 2016;10(8):534-540doi: 10.1038/nphoton.2016.94.
Tu, H., Liu, Y., Turchinovich, D., Marjanovic, M., Lyngsø, J., Lægsgaard, J., Chaney, E. J., Zhao, Y., You, S., Wilson, W. L., Xu, B., Dantus, M., & Boppart, S. A. (2016). Stain-free histopathology by programmable supercontinuum pulses. Nature photonics, 10(8), 534-540. https://doi.org/10.1038/nphoton.2016.94
Tu, Haohua, et al. "Stain-free histopathology by programmable supercontinuum pulses." Nature photonics vol. 10,8 (2016): 534-540. doi: https://doi.org/10.1038/nphoton.2016.94
Tu H, Liu Y, Turchinovich D, Marjanovic M, Lyngsø J, Lægsgaard J, Chaney EJ, Zhao Y, You S, Wilson WL, Xu B, Dantus M, Boppart SA. Stain-free histopathology by programmable supercontinuum pulses. Nat Photonics. 2016 Aug;10(8):534-540. doi: 10.1038/nphoton.2016.94. Epub 2016 May 23. PMID: 27668009; PMCID: PMC5031149.
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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

Cite
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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Relating clinical measures of pain with experimentally assessed pain mechanisms in patients with knee osteoarthritis.

Scandinavian journal of pain

Skou ST, Graven-Nielsen T, Lengsoe L, Simonsen O, Laursen MB, Arendt-Nielsen L.
PMID: 29913902
Scand J Pain. 2013 Apr 01;4(2):111-117. doi: 10.1016/j.sjpain.2012.07.001.

Background Peripheral and central sensitisation is prominent in knee osteoarthritis (KOA) and could be important for the reduced efficacy in some cases after as well surgery as pharmacological interventions. Although sensitisation is important in KOA it is not known...

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Skou ST, Graven-Nielsen T, Lengsoe L, et al. Relating clinical measures of pain with experimentally assessed pain mechanisms in patients with knee osteoarthritis. Scand J Pain. 2013;4(2):111-117doi: 10.1016/j.sjpain.2012.07.001.
Skou, S. T., Graven-Nielsen, T., Lengsoe, L., Simonsen, O., Laursen, M. B., & Arendt-Nielsen, L. (2013). Relating clinical measures of pain with experimentally assessed pain mechanisms in patients with knee osteoarthritis. Scandinavian journal of pain, 4(2), 111-117. https://doi.org/10.1016/j.sjpain.2012.07.001
Skou, Soren T, et al. "Relating clinical measures of pain with experimentally assessed pain mechanisms in patients with knee osteoarthritis." Scandinavian journal of pain vol. 4,2 (2013): 111-117. doi: https://doi.org/10.1016/j.sjpain.2012.07.001
Skou ST, Graven-Nielsen T, Lengsoe L, Simonsen O, Laursen MB, Arendt-Nielsen L. Relating clinical measures of pain with experimentally assessed pain mechanisms in patients with knee osteoarthritis. Scand J Pain. 2013 Apr 01;4(2):111-117. doi: 10.1016/j.sjpain.2012.07.001. PMID: 29913902.
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Suppressing Short-term Polarization Noise and Related Spectral Decoherence in All-normal Dispersion Fiber Supercontinuum Generation.

Journal of lightwave technology : a joint IEEE/OSA publication

Liu Y, Zhao Y, Lyngsø J, You S, Wilson WL, Tu H, Boppart SA.
PMID: 26166939
J Lightwave Technol. 2015 May 01;33(9):1814-1820. doi: 10.1109/JLT.2015.2397276.

The supercontinuum generated exclusively in the normal dispersion regime of a nonlinear fiber is widely believed to possess low optical noise and high spectral coherence. The recent development of flattened all-normal dispersion fibers has been motivated by this belief...

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Liu Y, Zhao Y, Lyngsø J, et al. Suppressing Short-term Polarization Noise and Related Spectral Decoherence in All-normal Dispersion Fiber Supercontinuum Generation. J Lightwave Technol. 2015;33(9):1814-1820doi: 10.1109/JLT.2015.2397276.
Liu, Y., Zhao, Y., Lyngsø, J., You, S., Wilson, W. L., Tu, H., & Boppart, S. A. (2015). Suppressing Short-term Polarization Noise and Related Spectral Decoherence in All-normal Dispersion Fiber Supercontinuum Generation. Journal of lightwave technology : a joint IEEE/OSA publication, 33(9), 1814-1820. https://doi.org/10.1109/JLT.2015.2397276
Liu, Yuan, et al. "Suppressing Short-term Polarization Noise and Related Spectral Decoherence in All-normal Dispersion Fiber Supercontinuum Generation." Journal of lightwave technology : a joint IEEE/OSA publication vol. 33,9 (2015): 1814-1820. doi: https://doi.org/10.1109/JLT.2015.2397276
Liu Y, Zhao Y, Lyngsø J, You S, Wilson WL, Tu H, Boppart SA. Suppressing Short-term Polarization Noise and Related Spectral Decoherence in All-normal Dispersion Fiber Supercontinuum Generation. J Lightwave Technol. 2015 May 01;33(9):1814-1820. doi: 10.1109/JLT.2015.2397276. PMID: 26166939; PMCID: PMC4495961.
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Generation of hydroxyl radicals from reactions between a dimethoxyhydroquinone and iron oxide nanoparticles.

Scientific reports

Lyngsie G, Krumina L, Tunlid A, Persson P.
PMID: 30018415
Sci Rep. 2018 Jul 17;8(1):10834. doi: 10.1038/s41598-018-29075-5.

The hydroxyl radical (·OH) is a powerful oxidant that is produced in a wide range of environments via the Fenton reaction (Fe

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Lyngsie G, Krumina L, Tunlid A, et al. Generation of hydroxyl radicals from reactions between a dimethoxyhydroquinone and iron oxide nanoparticles. Sci Rep. 2018;8(1):10834doi: 10.1038/s41598-018-29075-5.
Lyngsie, G., Krumina, L., Tunlid, A., & Persson, P. (2018). Generation of hydroxyl radicals from reactions between a dimethoxyhydroquinone and iron oxide nanoparticles. Scientific reports, 8(1), 10834. https://doi.org/10.1038/s41598-018-29075-5
Lyngsie, Gry, et al. "Generation of hydroxyl radicals from reactions between a dimethoxyhydroquinone and iron oxide nanoparticles." Scientific reports vol. 8,1 (2018): 10834. doi: https://doi.org/10.1038/s41598-018-29075-5
Lyngsie G, Krumina L, Tunlid A, Persson P. Generation of hydroxyl radicals from reactions between a dimethoxyhydroquinone and iron oxide nanoparticles. Sci Rep. 2018 Jul 17;8(1):10834. doi: 10.1038/s41598-018-29075-5. PMID: 30018415; PMCID: PMC6050337.
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Danish Registry of Childhood and Adolescent Diabetes.

Clinical epidemiology

Svensson J, Cerqueira C, Kjærsgaard P, Lyngsøe L, Hertel NT, Madsen M, Mortensen HB, Johannesen J.
PMID: 27822115
Clin Epidemiol. 2016 Oct 25;8:679-683. doi: 10.2147/CLEP.S99469. eCollection 2016.

AIM: The aims of the Danish Registry of Childhood and Adolescent Diabetes (DanDiabKids) are to monitor and improve the quality of care for children and adolescents with diabetes in Denmark and to follow the incidence and prevalence of diabetes.STUDY...

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Svensson J, Cerqueira C, Kjærsgaard P, et al. Danish Registry of Childhood and Adolescent Diabetes. Clin Epidemiol. 2016;8:679-683doi: 10.2147/CLEP.S99469.
Svensson, J., Cerqueira, C., Kjærsgaard, P., Lyngsøe, L., Hertel, N. T., Madsen, M., Mortensen, H. B., & Johannesen, J. (2016). Danish Registry of Childhood and Adolescent Diabetes. Clinical epidemiology, 8679-683. https://doi.org/10.2147/CLEP.S99469
Svensson, Jannet, et al. "Danish Registry of Childhood and Adolescent Diabetes." Clinical epidemiology vol. 8 (2016): 679-683. doi: https://doi.org/10.2147/CLEP.S99469
Svensson J, Cerqueira C, Kjærsgaard P, Lyngsøe L, Hertel NT, Madsen M, Mortensen HB, Johannesen J. Danish Registry of Childhood and Adolescent Diabetes. Clin Epidemiol. 2016 Oct 25;8:679-683. doi: 10.2147/CLEP.S99469. eCollection 2016. PMID: 27822115; PMCID: PMC5094642.
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Association between coffee or caffeine consumption and fecundity and fertility: a systematic review and dose-response meta-analysis.

Clinical epidemiology

Lyngsø J, Ramlau-Hansen CH, Bay B, Ingerslev HJ, Hulman A, Kesmodel US.
PMID: 29276412
Clin Epidemiol. 2017 Dec 15;9:699-719. doi: 10.2147/CLEP.S146496. eCollection 2017.

OBJECTIVE: The aim was to investigate whether coffee or caffeine consumption is associated with reproductive endpoints among women with natural fertility (ie, time to pregnancy [TTP] and spontaneous abortion [SAB]) and among women in fertility treatment (ie, clinical pregnancy...

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Lyngsø J, Ramlau-Hansen CH, Bay B, et al. Association between coffee or caffeine consumption and fecundity and fertility: a systematic review and dose-response meta-analysis. Clin Epidemiol. 2017;9:699-719doi: 10.2147/CLEP.S146496.
Lyngsø, J., Ramlau-Hansen, C. H., Bay, B., Ingerslev, H. J., Hulman, A., & Kesmodel, U. S. (2017). Association between coffee or caffeine consumption and fecundity and fertility: a systematic review and dose-response meta-analysis. Clinical epidemiology, 9699-719. https://doi.org/10.2147/CLEP.S146496
Lyngsø, Julie, et al. "Association between coffee or caffeine consumption and fecundity and fertility: a systematic review and dose-response meta-analysis." Clinical epidemiology vol. 9 (2017): 699-719. doi: https://doi.org/10.2147/CLEP.S146496
Lyngsø J, Ramlau-Hansen CH, Bay B, Ingerslev HJ, Hulman A, Kesmodel US. Association between coffee or caffeine consumption and fecundity and fertility: a systematic review and dose-response meta-analysis. Clin Epidemiol. 2017 Dec 15;9:699-719. doi: 10.2147/CLEP.S146496. eCollection 2017. PMID: 29276412; PMCID: PMC5733907.
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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 May 06;20:100090. doi: 10.1016/j.mcpro.2021.100090. Epub 2021 May 06.

Human α

Cite
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 May 06;20:100090. doi: 10.1016/j.mcpro.2021.100090. Epub 2021 May 06. PMID: 33964423; PMCID: PMC8167298.
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