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Protocol for high-throughput semi-automated label-free- or TMT-based phosphoproteome profiling

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dc.contributor.author Koenig, C
dc.contributor.author Martinez-Val, A
dc.contributor.author Naicker, Previn
dc.contributor.author Stoychev, S
dc.contributor.author Jordaan, J
dc.contributor.author Olsen, JV
dc.date.accessioned 2023-12-11T08:11:43Z
dc.date.available 2023-12-11T08:11:43Z
dc.date.issued 2023-09
dc.identifier.citation Koenig, C., Martinez-Val, A., Naicker, P., Stoychev, S., Jordaan, J. & Olsen, J. 2023. Protocol for high-throughput semi-automated label-free- or TMT-based phosphoproteome profiling. <i>Star Protocols, 4(3).</i> http://hdl.handle.net/10204/13384 en_ZA
dc.identifier.issn 2666-1667
dc.identifier.uri https://doi.org/10.1016/j.xpro.2023.102536
dc.identifier.uri http://hdl.handle.net/10204/13384
dc.description.abstract Tandem mass tags data-dependent acquisition (TMT-DDA) as well as data-independent acquisition-based label-free quantification (LFQ-DIA) have become the leading workflows to achieve deep proteome and phosphoproteome profiles. We present a modular pipeline for TMT-DDA and LFQ-DIA that integrates steps to perform scalable phosphoproteome profiling, including protein lysate extraction, clean-up, digestion, phosphopeptide enrichment, and TMT-labeling. We also detail peptide and/or phosphopeptide fractionation and pre-mass spectrometry desalting and provide researchers guidance on choosing the best workflow based on sample number and input. en_US
dc.format Fulltext en_US
dc.language.iso en en_US
dc.relation.uri https://www.sciencedirect.com/science/article/pii/S2666166723005038?via%3Dihub en_US
dc.source Star Protocols, 4(3) en_US
dc.subject Protein Biochemistry en_US
dc.subject Proteomics en_US
dc.subject Mass spectrometry en_US
dc.title Protocol for high-throughput semi-automated label-free- or TMT-based phosphoproteome profiling en_US
dc.type Article en_US
dc.description.pages 30 en_US
dc.description.note This is an open access article under the CC BY-NC-ND license en_US
dc.description.cluster Next Generation Health en_US
dc.description.impactarea Human Molecular Diagnostics en_US
dc.identifier.apacitation Koenig, C., Martinez-Val, A., Naicker, P., Stoychev, S., Jordaan, J., & Olsen, J. (2023). Protocol for high-throughput semi-automated label-free- or TMT-based phosphoproteome profiling. <i>Star Protocols, 4(3)</i>, http://hdl.handle.net/10204/13384 en_ZA
dc.identifier.chicagocitation Koenig, C, A Martinez-Val, Previn Naicker, S Stoychev, J Jordaan, and JV Olsen "Protocol for high-throughput semi-automated label-free- or TMT-based phosphoproteome profiling." <i>Star Protocols, 4(3)</i> (2023) http://hdl.handle.net/10204/13384 en_ZA
dc.identifier.vancouvercitation Koenig C, Martinez-Val A, Naicker P, Stoychev S, Jordaan J, Olsen J. Protocol for high-throughput semi-automated label-free- or TMT-based phosphoproteome profiling. Star Protocols, 4(3). 2023; http://hdl.handle.net/10204/13384. en_ZA
dc.identifier.ris TY - Article AU - Koenig, C AU - Martinez-Val, A AU - Naicker, Previn AU - Stoychev, S AU - Jordaan, J AU - Olsen, JV AB - Tandem mass tags data-dependent acquisition (TMT-DDA) as well as data-independent acquisition-based label-free quantification (LFQ-DIA) have become the leading workflows to achieve deep proteome and phosphoproteome profiles. We present a modular pipeline for TMT-DDA and LFQ-DIA that integrates steps to perform scalable phosphoproteome profiling, including protein lysate extraction, clean-up, digestion, phosphopeptide enrichment, and TMT-labeling. We also detail peptide and/or phosphopeptide fractionation and pre-mass spectrometry desalting and provide researchers guidance on choosing the best workflow based on sample number and input. DA - 2023-09 DB - ResearchSpace DP - CSIR J1 - Star Protocols, 4(3) KW - Protein Biochemistry KW - Proteomics KW - Mass spectrometry LK - https://researchspace.csir.co.za PY - 2023 SM - 2666-1667 T1 - Protocol for high-throughput semi-automated label-free- or TMT-based phosphoproteome profiling TI - Protocol for high-throughput semi-automated label-free- or TMT-based phosphoproteome profiling UR - http://hdl.handle.net/10204/13384 ER - en_ZA
dc.identifier.worklist 27093 en_US


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