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Comparison of NIMS and MALDI platforms for neuropeptide and lipid mass spectrometric imaging in .

Analytical methods : advancing methods and applications

Sturm RM, Greer T, Chen R, Hensen B, Li L.
PMID: 23544036
Anal Methods. 2013;5(6):1623-1628. doi: 10.1039/C3AY26067D. Epub 2013 Jan 29.

Nanostructure-initiator mass spectrometry (NIMS) is a recently developed matrix-free laser desorption/ionization technique that has shown promise for peptide analyses. It is also useful in mass spectrometric imaging (MSI) studies of small molecule drugs, metabolites, and lipids, minimizing analyte diffusion...

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Sturm RM, Greer T, Chen R, et al. Comparison of NIMS and MALDI platforms for neuropeptide and lipid mass spectrometric imaging in . Anal Methods. 2013;5(6):1623-1628doi: 10.1039/C3AY26067D.
Sturm, R. M., Greer, T., Chen, R., Hensen, B., & Li, L. (2013). Comparison of NIMS and MALDI platforms for neuropeptide and lipid mass spectrometric imaging in . Analytical methods : advancing methods and applications, 5(6), 1623-1628. https://doi.org/10.1039/C3AY26067D
Sturm, Robert M, et al. "Comparison of NIMS and MALDI platforms for neuropeptide and lipid mass spectrometric imaging in ." Analytical methods : advancing methods and applications vol. 5,6 (2013): 1623-1628. doi: https://doi.org/10.1039/C3AY26067D
Sturm RM, Greer T, Chen R, Hensen B, Li L. Comparison of NIMS and MALDI platforms for neuropeptide and lipid mass spectrometric imaging in . Anal Methods. 2013;5(6):1623-1628. doi: 10.1039/C3AY26067D. Epub 2013 Jan 29. PMID: 23544036; PMCID: PMC3609542.
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Recent advances in mass spectrometry (MS)-based glycoproteomics in complex biological samples.

Trends in analytical chemistry : TRAC

Chen Z, Huang J, Li L.
PMID: 31579312
Trends Analyt Chem. 2019 Sep;118:880-892. doi: 10.1016/j.trac.2018.10.009. Epub 2018 Oct 15.

Protein glycosylation plays a key role in various biological processes and disease-related pathological progression. Mass spectrometry (MS)-based glycoproteomics is a powerful approach that provides a system-wide profiling of the glycoproteome in a high-throughput manner. There have been numerous significant...

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Chen Z, Huang J, Li L. Recent advances in mass spectrometry (MS)-based glycoproteomics in complex biological samples. Trends Analyt Chem. 2018;118:880-892doi: 10.1016/j.trac.2018.10.009.
Chen, Z., Huang, J., & Li, L. (2019). Recent advances in mass spectrometry (MS)-based glycoproteomics in complex biological samples. Trends in analytical chemistry : TRAC, 118880-892. https://doi.org/10.1016/j.trac.2018.10.009
Chen, Zhengwei, et al. "Recent advances in mass spectrometry (MS)-based glycoproteomics in complex biological samples." Trends in analytical chemistry : TRAC vol. 118 (2019): 880-892. doi: https://doi.org/10.1016/j.trac.2018.10.009
Chen Z, Huang J, Li L. Recent advances in mass spectrometry (MS)-based glycoproteomics in complex biological samples. Trends Analyt Chem. 2019 Sep;118:880-892. doi: 10.1016/j.trac.2018.10.009. Epub 2018 Oct 15. PMID: 31579312; PMCID: PMC6774629.
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Mass spectrometry profiling and quantitation of changes in circulating hormones secreted over time in Cancer borealis hemolymph due to feeding behavior.

Analytical and bioanalytical chemistry

DeLaney K, Hu M, Wu W, Nusbaum MP, Li L.
PMID: 34184104
Anal Bioanal Chem. 2022 Jan;414(1):533-543. doi: 10.1007/s00216-021-03479-1. Epub 2021 Jun 29.

The crustacean stomatogastric ganglion (STG) is a valuable model for understanding circuit dynamics in neuroscience as it contains a small number of neurons, all easily distinguishable and most of which contribute to two complementary feeding-related neural circuits. These circuits...

Cite
DeLaney K, Hu M, Wu W, et al. Mass spectrometry profiling and quantitation of changes in circulating hormones secreted over time in Cancer borealis hemolymph due to feeding behavior. Anal Bioanal Chem. 2021;414(1):533-543doi: 10.1007/s00216-021-03479-1.
DeLaney, K., Hu, M., Wu, W., Nusbaum, M. P., & Li, L. (2022). Mass spectrometry profiling and quantitation of changes in circulating hormones secreted over time in Cancer borealis hemolymph due to feeding behavior. Analytical and bioanalytical chemistry, 414(1), 533-543. https://doi.org/10.1007/s00216-021-03479-1
DeLaney, Kellen, et al. "Mass spectrometry profiling and quantitation of changes in circulating hormones secreted over time in Cancer borealis hemolymph due to feeding behavior." Analytical and bioanalytical chemistry vol. 414,1 (2022): 533-543. doi: https://doi.org/10.1007/s00216-021-03479-1
DeLaney K, Hu M, Wu W, Nusbaum MP, Li L. Mass spectrometry profiling and quantitation of changes in circulating hormones secreted over time in Cancer borealis hemolymph due to feeding behavior. Anal Bioanal Chem. 2022 Jan;414(1):533-543. doi: 10.1007/s00216-021-03479-1. Epub 2021 Jun 29. PMID: 34184104; PMCID: PMC8714863.
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Recent Advances in Analytical Approaches for Glycan and Glycopeptide Quantitation.

Molecular & cellular proteomics : MCP

Delafield DG, Li L.
PMID: 32576592
Mol Cell Proteomics. 2021;20:100054. doi: 10.1074/mcp.R120.002095. Epub 2021 Feb 20.

Growing implications of glycosylation in physiological occurrences and human disease have prompted intensive focus on revealing glycomic perturbations through absolute and relative quantification. Empowered by seminal methodologies and increasing capacity for detection, identification, and characterization, the past decade has...

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Delafield DG, Li L. Recent Advances in Analytical Approaches for Glycan and Glycopeptide Quantitation. Mol Cell Proteomics. 2021;20:100054doi: 10.1074/mcp.R120.002095.
Delafield, D. G., & Li, L. (2021). Recent Advances in Analytical Approaches for Glycan and Glycopeptide Quantitation. Molecular & cellular proteomics : MCP, 20100054. https://doi.org/10.1074/mcp.R120.002095
Delafield, Daniel G, and Li, Lingjun. "Recent Advances in Analytical Approaches for Glycan and Glycopeptide Quantitation." Molecular & cellular proteomics : MCP vol. 20 (2021): 100054. doi: https://doi.org/10.1074/mcp.R120.002095
Delafield DG, Li L. Recent Advances in Analytical Approaches for Glycan and Glycopeptide Quantitation. Mol Cell Proteomics. 2021;20:100054. doi: 10.1074/mcp.R120.002095. Epub 2021 Feb 20. PMID: 32576592.
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Gold nanoparticles in virus detection: Recent advances and potential considerations for SARS-CoV-2 testing development.

Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology

Wang J, Drelich AJ, Hopkins CM, Mecozzi S, Li L, Kwon G, Hong S.
PMID: 34498423
Wiley Interdiscip Rev Nanomed Nanobiotechnol. 2021 Sep 08;e1754. doi: 10.1002/wnan.1754. Epub 2021 Sep 08.

Viruses are infectious agents that pose significant threats to plants, animals, and humans. The current coronavirus disease 2019 pandemic, which is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has spread globally and resulted in over 2 million...

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Wang J, Drelich AJ, Hopkins CM, et al. Gold nanoparticles in virus detection: Recent advances and potential considerations for SARS-CoV-2 testing development. Wiley Interdiscip Rev Nanomed Nanobiotechnol. 2021;e1754doi: 10.1002/wnan.1754.
Wang, J., Drelich, A. J., Hopkins, C. M., Mecozzi, S., Li, L., Kwon, G., & Hong, S. (2021). Gold nanoparticles in virus detection: Recent advances and potential considerations for SARS-CoV-2 testing development. Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology, e1754. https://doi.org/10.1002/wnan.1754
Wang, Jianxin, et al. "Gold nanoparticles in virus detection: Recent advances and potential considerations for SARS-CoV-2 testing development." Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology vol. (2021): e1754. doi: https://doi.org/10.1002/wnan.1754
Wang J, Drelich AJ, Hopkins CM, Mecozzi S, Li L, Kwon G, Hong S. Gold nanoparticles in virus detection: Recent advances and potential considerations for SARS-CoV-2 testing development. Wiley Interdiscip Rev Nanomed Nanobiotechnol. 2021 Sep 08;e1754. doi: 10.1002/wnan.1754. Epub 2021 Sep 08. PMID: 34498423; PMCID: PMC8646453.
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In-depth Site-specific Analysis of N-glycoproteome in Human Cerebrospinal Fluid and Glycosylation Landscape Changes in Alzheimer's Disease.

Molecular & cellular proteomics : MCP

Chen Z, Yu Q, Yu Q, Johnson J, Shipman R, Zhong X, Huang J, Asthana S, Carlsson C, Okonkwo O, Li L.
PMID: 33862227
Mol Cell Proteomics. 2021;20:100081. doi: 10.1016/j.mcpro.2021.100081. Epub 2021 Apr 20.

As the body fluid that directly interchanges with the extracellular fluid of the central nervous system (CNS), cerebrospinal fluid (CSF) serves as a rich source for CNS-related disease biomarker discovery. Extensive proteome profiling has been conducted for CSF, but...

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Chen Z, Yu Q, Yu Q, et al. In-depth Site-specific Analysis of N-glycoproteome in Human Cerebrospinal Fluid and Glycosylation Landscape Changes in Alzheimer's Disease. Mol Cell Proteomics. 2021;20:100081doi: 10.1016/j.mcpro.2021.100081.
Chen, Z., Yu, Q., Yu, Q., Johnson, J., Shipman, R., Zhong, X., Huang, J., Asthana, S., Carlsson, C., Okonkwo, O., & Li, L. (2021). In-depth Site-specific Analysis of N-glycoproteome in Human Cerebrospinal Fluid and Glycosylation Landscape Changes in Alzheimer's Disease. Molecular & cellular proteomics : MCP, 20100081. https://doi.org/10.1016/j.mcpro.2021.100081
Chen, Zhengwei, et al. "In-depth Site-specific Analysis of N-glycoproteome in Human Cerebrospinal Fluid and Glycosylation Landscape Changes in Alzheimer's Disease." Molecular & cellular proteomics : MCP vol. 20 (2021): 100081. doi: https://doi.org/10.1016/j.mcpro.2021.100081
Chen Z, Yu Q, Yu Q, Johnson J, Shipman R, Zhong X, Huang J, Asthana S, Carlsson C, Okonkwo O, Li L. In-depth Site-specific Analysis of N-glycoproteome in Human Cerebrospinal Fluid and Glycosylation Landscape Changes in Alzheimer's Disease. Mol Cell Proteomics. 2021;20:100081. doi: 10.1016/j.mcpro.2021.100081. Epub 2021 Apr 20. PMID: 33862227; PMCID: PMC8724636.
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Evaluation of Collagen Alterations in Early Precursor Lesions of High Grade Serous Ovarian Cancer by Second Harmonic Generation Microscopy and Mass Spectrometry.

Cancers

Gant KL, Jambor AN, Li Z, Rentchler EC, Weisman P, Li L, Patankar MS, Campagnola PJ.
PMID: 34199725
Cancers (Basel). 2021 Jun 04;13(11). doi: 10.3390/cancers13112794.

No abstract available.

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Gant KL, Jambor AN, Li Z, et al. Evaluation of Collagen Alterations in Early Precursor Lesions of High Grade Serous Ovarian Cancer by Second Harmonic Generation Microscopy and Mass Spectrometry. Cancers (Basel). 2021;13(11)doi: 10.3390/cancers13112794.
Gant, K. L., Jambor, A. N., Li, Z., Rentchler, E. C., Weisman, P., Li, L., Patankar, M. S., & Campagnola, P. J. (2021). Evaluation of Collagen Alterations in Early Precursor Lesions of High Grade Serous Ovarian Cancer by Second Harmonic Generation Microscopy and Mass Spectrometry. Cancers, 13(11), . https://doi.org/10.3390/cancers13112794
Gant, Kristal L, et al. "Evaluation of Collagen Alterations in Early Precursor Lesions of High Grade Serous Ovarian Cancer by Second Harmonic Generation Microscopy and Mass Spectrometry." Cancers vol. 13,11 (2021). doi: https://doi.org/10.3390/cancers13112794
Gant KL, Jambor AN, Li Z, Rentchler EC, Weisman P, Li L, Patankar MS, Campagnola PJ. Evaluation of Collagen Alterations in Early Precursor Lesions of High Grade Serous Ovarian Cancer by Second Harmonic Generation Microscopy and Mass Spectrometry. Cancers (Basel). 2021 Jun 04;13(11). doi: 10.3390/cancers13112794. PMID: 34199725; PMCID: PMC8200041.
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Effects of Trimetaphosphate on Abiotic Formation and Hydrolysis of Peptides.

Life (Basel, Switzerland)

Sibilska IK, Chen B, Li L, Yin J.
PMID: 29189724
Life (Basel). 2017 Nov 30;7(4). doi: 10.3390/life7040050.

The primordial Earth probably had most of the factors needed for the emergence and development of life. It is believed that it had not only water, but also simple inorganic and organic materials. While studies since the 1950s on...

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Sibilska IK, Chen B, Li L, et al. Effects of Trimetaphosphate on Abiotic Formation and Hydrolysis of Peptides. Life (Basel). 2017;7(4)doi: 10.3390/life7040050.
Sibilska, I. K., Chen, B., Li, L., & Yin, J. (2017). Effects of Trimetaphosphate on Abiotic Formation and Hydrolysis of Peptides. Life (Basel, Switzerland), 7(4), . https://doi.org/10.3390/life7040050
Sibilska, Izabela K, et al. "Effects of Trimetaphosphate on Abiotic Formation and Hydrolysis of Peptides." Life (Basel, Switzerland) vol. 7,4 (2017). doi: https://doi.org/10.3390/life7040050
Sibilska IK, Chen B, Li L, Yin J. Effects of Trimetaphosphate on Abiotic Formation and Hydrolysis of Peptides. Life (Basel). 2017 Nov 30;7(4). doi: 10.3390/life7040050. PMID: 29189724; PMCID: PMC5745563.
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Measurement of NMDA Receptor Antagonist, CPP, in Mouse Plasma and Brain Tissue Following Systematic Administration Using Ion-Pair LCMS/MS.

Analytical methods : advancing methods and applications

Gemperline E, Laha K, Scarlett CO, Pearce RA, Li L.
PMID: 25663848
Anal Methods. 2014 Aug 21;6(16):6389-6396. doi: 10.1039/c4ay01168f.

(RS)-3-(2-carboxypiperazin-4-yl)-propyl-1-phosphonic acid (CPP) is a competitive antagonist of the N-methyl-D-aspartate (NMDA) receptor and is routinely used with rodent models to investigate the role of NMDA receptors in brain function. This highly polar compound is difficult to separate from biological...

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Gemperline E, Laha K, Scarlett CO, et al. Measurement of NMDA Receptor Antagonist, CPP, in Mouse Plasma and Brain Tissue Following Systematic Administration Using Ion-Pair LCMS/MS. Anal Methods. 2014;6(16):6389-6396doi: 10.1039/c4ay01168f.
Gemperline, E., Laha, K., Scarlett, C. O., Pearce, R. A., & Li, L. (2014). Measurement of NMDA Receptor Antagonist, CPP, in Mouse Plasma and Brain Tissue Following Systematic Administration Using Ion-Pair LCMS/MS. Analytical methods : advancing methods and applications, 6(16), 6389-6396. https://doi.org/10.1039/c4ay01168f
Gemperline, Erin, et al. "Measurement of NMDA Receptor Antagonist, CPP, in Mouse Plasma and Brain Tissue Following Systematic Administration Using Ion-Pair LCMS/MS." Analytical methods : advancing methods and applications vol. 6,16 (2014): 6389-6396. doi: https://doi.org/10.1039/c4ay01168f
Gemperline E, Laha K, Scarlett CO, Pearce RA, Li L. Measurement of NMDA Receptor Antagonist, CPP, in Mouse Plasma and Brain Tissue Following Systematic Administration Using Ion-Pair LCMS/MS. Anal Methods. 2014 Aug 21;6(16):6389-6396. doi: 10.1039/c4ay01168f. PMID: 25663848; PMCID: PMC4317794.
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Comprehensive urinary metabolomic characterization of a genetically induced mouse model of prostatic inflammation.

International journal of mass spectrometry

Hao L, Shi Y, Thomas S, Vezina CM, Bajpai S, Ashok A, Bieberich CJ, Ricke WA, Li L.
PMID: 30872949
Int J Mass Spectrom. 2018 Nov;434:185-192. doi: 10.1016/j.ijms.2018.09.017. Epub 2018 Sep 22.

Dysfunction of the lower urinary tract commonly afflicts the middle-aged and aging male population. The etiology of lower urinary tract symptoms (LUTS) is multifactorial. Benign prostate hyperplasia, fibrosis, smooth muscle contractility, and inflammation likely contribute. Here we aim to...

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Hao L, Shi Y, Thomas S, et al. Comprehensive urinary metabolomic characterization of a genetically induced mouse model of prostatic inflammation. Int J Mass Spectrom. 2018;434:185-192doi: 10.1016/j.ijms.2018.09.017.
Hao, L., Shi, Y., Thomas, S., Vezina, C. M., Bajpai, S., Ashok, A., Bieberich, C. J., Ricke, W. A., & Li, L. (2018). Comprehensive urinary metabolomic characterization of a genetically induced mouse model of prostatic inflammation. International journal of mass spectrometry, 434185-192. https://doi.org/10.1016/j.ijms.2018.09.017
Hao, Ling, et al. "Comprehensive urinary metabolomic characterization of a genetically induced mouse model of prostatic inflammation." International journal of mass spectrometry vol. 434 (2018): 185-192. doi: https://doi.org/10.1016/j.ijms.2018.09.017
Hao L, Shi Y, Thomas S, Vezina CM, Bajpai S, Ashok A, Bieberich CJ, Ricke WA, Li L. Comprehensive urinary metabolomic characterization of a genetically induced mouse model of prostatic inflammation. Int J Mass Spectrom. 2018 Nov;434:185-192. doi: 10.1016/j.ijms.2018.09.017. Epub 2018 Sep 22. PMID: 30872949; PMCID: PMC6414212.
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Urinary Metabolomic and Proteomic Analyses in a Mouse Model of Prostatic Inflammation.

Urine (Amsterdam, Netherlands)

Wei P, Hao L, Ma F, Yu Q, Buchberger AR, Lee S, Bushman W, Li L.
PMID: 33870183
Urine (Amst). 2019 Jun;1:17-23. doi: 10.1016/j.urine.2020.05.002. Epub 2020 May 27.

Lower urinary tract symptoms (LUTS) are common among aging men. Since prostatic inflammation is one of its etiologies, it is plausible that urinary metabolite and protein biomarkers could be identified and used to diagnose inflammation-induced LUTS. We characterized the...

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Wei P, Hao L, Ma F, et al. Urinary Metabolomic and Proteomic Analyses in a Mouse Model of Prostatic Inflammation. Urine (Amst). 2020;1:17-23doi: 10.1016/j.urine.2020.05.002.
Wei, P., Hao, L., Ma, F., Yu, Q., Buchberger, A. R., Lee, S., Bushman, W., & Li, L. (2019). Urinary Metabolomic and Proteomic Analyses in a Mouse Model of Prostatic Inflammation. Urine (Amsterdam, Netherlands), 117-23. https://doi.org/10.1016/j.urine.2020.05.002
Wei, Pingli, et al. "Urinary Metabolomic and Proteomic Analyses in a Mouse Model of Prostatic Inflammation." Urine (Amsterdam, Netherlands) vol. 1 (2019): 17-23. doi: https://doi.org/10.1016/j.urine.2020.05.002
Wei P, Hao L, Ma F, Yu Q, Buchberger AR, Lee S, Bushman W, Li L. Urinary Metabolomic and Proteomic Analyses in a Mouse Model of Prostatic Inflammation. Urine (Amst). 2019 Jun;1:17-23. doi: 10.1016/j.urine.2020.05.002. Epub 2020 May 27. PMID: 33870183; PMCID: PMC8052098.
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Mass spectrometry profiling and quantitation of changes in circulating hormones secreted over time in Cancer borealis hemolymph due to feeding behavior.

Analytical and bioanalytical chemistry

DeLaney K, Hu M, Wu W, Nusbaum MP, Li L.
PMID: 34184104
Anal Bioanal Chem. 2022 Jan;414(1):533-543. doi: 10.1007/s00216-021-03479-1. Epub 2021 Jun 29.

The crustacean stomatogastric ganglion (STG) is a valuable model for understanding circuit dynamics in neuroscience as it contains a small number of neurons, all easily distinguishable and most of which contribute to two complementary feeding-related neural circuits. These circuits...

Cite
DeLaney K, Hu M, Wu W, et al. Mass spectrometry profiling and quantitation of changes in circulating hormones secreted over time in Cancer borealis hemolymph due to feeding behavior. Anal Bioanal Chem. 2021;414(1):533-543doi: 10.1007/s00216-021-03479-1.
DeLaney, K., Hu, M., Wu, W., Nusbaum, M. P., & Li, L. (2022). Mass spectrometry profiling and quantitation of changes in circulating hormones secreted over time in Cancer borealis hemolymph due to feeding behavior. Analytical and bioanalytical chemistry, 414(1), 533-543. https://doi.org/10.1007/s00216-021-03479-1
DeLaney, Kellen, et al. "Mass spectrometry profiling and quantitation of changes in circulating hormones secreted over time in Cancer borealis hemolymph due to feeding behavior." Analytical and bioanalytical chemistry vol. 414,1 (2022): 533-543. doi: https://doi.org/10.1007/s00216-021-03479-1
DeLaney K, Hu M, Wu W, Nusbaum MP, Li L. Mass spectrometry profiling and quantitation of changes in circulating hormones secreted over time in Cancer borealis hemolymph due to feeding behavior. Anal Bioanal Chem. 2022 Jan;414(1):533-543. doi: 10.1007/s00216-021-03479-1. Epub 2021 Jun 29. PMID: 34184104; PMCID: PMC8714863.
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Showing 1 to 12 of 39 entries