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ProLuCID: An improved SEQUEST-like algorithm with enhanced sensitivity and specificity
Open accessAbstract
ProLuCID, a new algorithm for peptide identification using tandem mass spectrometry and protein sequence databases has been developed. This algorithm uses a three tier scoring scheme. First, a binomial probability is used as a preliminary scoring scheme to select candidate peptides. The binomial probability scores generated by ProLuCID minimize molecular weight bias and are independent of database size. A modified cross-correlation score is calculated for each candidate peptide identified by the binomial probability. This cross-correlation scoring function models the isotopic distributions of fragment ions of candidate peptides which ultimately results in higher sensitivity and specificity than that obtained with the SEQUEST XCorr. Finally, ProLuCID uses the distribution of XCorr values for all of the selected candidate peptides to compute a Z score for the peptide hit with the highest XCorr. The ProLuCID Z score combines the discriminative power of XCorr and DeltaCN, the standard parameters for assessing the quality of the peptide identification using SEQUEST, and displays significant improvement in specificity over ProLuCID XCorr alone. ProLuCID is also able to take advantage of high resolution MS/MS spectra leading to further improvements in specificity when compared to low resolution tandem MS data. A comparison of filtered data searched with SEQUEST and ProLuCID using the same false discovery rate as estimated by a target-decoy database strategy, shows that ProLuCID was able to identify as many as 25% more proteins than SEQUEST. ProLuCID is implemented in Java and can be easily installed on a single computer or a computer cluster. This article is part of a Special Issue entitled: Computational Proteomics.
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“Under serum-free survival conditions, we have previously observed that the cells do not proliferate, and thus we are measuring loss of viability in these cells under serum-free conditions with pharmacological treatment 49.”
From Manumycin polyketides act as molecular glues between UBR7 and P53 (2020) · cites this paper as [49]
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Cites
Measuring the Accuracy of Diagnostic Systems
Swets, J. A. (1988) · Science · doi:10.1126/science.3287615 · Cited by 10,058
Perkins, D. N., Pappin, D., Creasy, D. M., & Cottrell, J. S. (1999) · Electrophoresis · doi:10.1002/(sici)1522-2683(19991201)20:18 · Cited by 8,264
Eng, J. K., McCormack, A. L., & Yates, J. R. (1994) · Journal of the American Society for Mass Spectrometry · doi:10.1016/1044-0305(94)80016-2 · Cited by 6,484
Self-citationKeller, A., Nesvizhskii, A., Kolker, E., & Aebersold, R. (2002) · Analytical Chemistry · doi:10.1021/ac025747h · Cited by 4,970
Large-scale analysis of the yeast proteome by multidimensional protein identification technology
Washburn, M. P., Wolters, D. A., & Yates, J. R. (2001) · Nature Biotechnology · doi:10.1038/85686 · Cited by 4,768
Self-citationProcedures for Detecting Outlying Observations in Samples
Grubbs, F. E. (1969) · Technometrics · doi:10.1080/00401706.1969.10490657 · Cited by 4,105
TANDEM: matching proteins with tandem mass spectra
Craig, R., & Beavis, R. C. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bth092 · Cited by 2,546
Direct analysis of protein complexes using mass spectrometry
Link, A. J., Eng, J. K., Schieltz, D. M., Carmack, E., Mize, G. J., Morris, D. R., Garvik, B. M., & Yates, J. R. (1999) · Nature Biotechnology · doi:10.1038/10890 · Cited by 2,218
Self-citationOlsen, J. V., de Godoy, L. M. F., Li, G., Maček, B., Mortensen, P., Pesch, R., Makarov, A., Lange, O., Horning, S. R., & Mann, M. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t500030-mcp200 · Cited by 1,539
Protein Analysis by Shotgun/Bottom-up Proteomics
Zhang, Y., Fonslow, B. R., Shan, B., Baek, M.-C., & Yates, J. R. (2013) · Chemical Reviews · doi:10.1021/cr3003533 · Cited by 1,491
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Li, X., Xiong, X., Zhang, M., Wang, K., Chen, Y., Zhou, J. L., Mao, Y., Lv, J., Yi, D., Chen, X., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.10.019 · Cited by 482
Harnessing the anti-cancer natural product nimbolide for targeted protein degradation
Spradlin, J. N., Hu, X., Ward, C. C., Brittain, S. M., Jones, M. D., Ou, L., To, M., Proudfoot, A., Ornelas, E., Woldegiorgis, M., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0304-8 · Cited by 432
“…°C and the nanospray voltage was set to 2.75 kV. Data was extracted in the form of MS1 and MS2 files using Raw Extractor 1.9.9.2 (Scripps Research Institute) and searched against the Uniprot human database using ProLuCID search methodology in IP2 v.3 (Integrated Proteomics Applications, Inc) 36 .”
InfluentialHe, M., Chiang, H.-H., Luo, H., Zheng, Z., Qiao, Q., Wang, L., Tan, M., Ohkubo, R., Mu, W.-C., Zhao, S., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.01.009 · Cited by 425
“San Diego, CA) using ProLuCID/Sequest, DTASelect2 and Census (Cociorva et al., 2007; Park et al., 2008; Tabb et al., 2002; Xu et al., 2015).”
MethodDeubiquitinase-targeting chimeras for targeted protein stabilization
Henning, N. J., Boike, L., Spradlin, J. N., Ward, C. C., Liu, G., Zhang, E., Belcher, B. P., Brittain, S. M., Hesse, M. J., Dovala, D., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-00971-2 · Cited by 344
Dynamic RNA acetylation revealed by quantitative cross-evolutionary mapping
Sas‐Chen, A., Thomas, J. M., Matzov, D., Taoka, M., Nance, K. D., Nir, R., Bryson, K. M., Shachar, R., Liman, G. L. S., Burkhart, B. W., et al. (2020) · Nature · doi:10.1038/s41586-020-2418-2 · Cited by 336
Ward, C. C., Kleinman, J. I., Brittain, S. M., Lee, P. S., Chung, C. Y. S., Kim, K., Petri, Y., Thomas, J. R., Tallarico, J. A., McKenna, J. M., et al. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.8b01083 · Cited by 336
Itaconate and itaconate derivatives target JAK1 to suppress alternative activation of macrophages
Runtsch, M. C., Angiari, S., Hooftman, A., Wadhwa, R., Zhang, Y., Zheng, Y., Spina, J. S., Ruzek, M. C., Argiriadi, M. A., McGettrick, A. F., et al. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.02.002 · Cited by 343
Cryo-EM structure of SARS-CoV-2 ORF3a in lipid nanodiscs
Kern, D. M., Sorum, B., Mali, S. S., Hoel, C., Sridharan, S., Remis, J. P., Toso, D. B., Kotecha, A., Bautista, D. M., & Brohawn, S. G. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00619-0 · Cited by 324
MatrisomeDB: the ECM-protein knowledge database
Shao, X., Taha, I. N., Clauser, K. R., Gao, Y., & Naba, A. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz849 · Cited by 314
“The raw data were searched by the ProluCID search engine (41) using an open-database search strategy (42).”
MethodSelf-citationExtracting Accurate Precursor Information for Tandem Mass Spectra by RawConverter
He, L., Diedrich, J. K., Chu, Y.-Y., & Yates, J. R. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b02721 · Cited by 295
Self-citationNucleolar expansion and elevated protein translation in premature aging
Buchwalter, A., & Hetzer, M. W. (2017) · Nature Communications · doi:10.1038/s41467-017-00322-z · Cited by 263
Accurate annotation of human protein-coding small open reading frames
Martinez, T. F., Chu, Q., Donaldson, C. J., Tan, D., Shokhirev, M. N., & Saghatelian, A. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0425-0 · Cited by 249
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Xu, X., Tang, J.-J., Peng, C., Wang, Y., Fu, L., Qiu, Z.-P., Xiong, Y., Yang, L.-F., Cui, H., He, X.-L., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.02.015 · Cited by 235
“com) using ProLuCID/Sequest (Eng et al., 1994; Xu et al., 2015), DTASelect2 (Cociorva et al.”
Self-citationDiscovery of a Covalent FEM1B Recruiter for Targeted Protein Degradation Applications
Henning, N. J., Manford, A. G., Spradlin, J. N., Brittain, S. M., Zhang, E., McKenna, J. M., Tallarico, J. A., Schirle, M., Rape, M., & Nomura, D. K. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.1c03980 · Cited by 221
Glycolytic Enzymes Coalesce in G Bodies under Hypoxic Stress
Jin, M., Fuller, G. G., Han, T., Yao, Y., Alessi, A. F., Freeberg, M. A., Roach, N. P., Moresco, J. J., Karnovsky, A., Baba, M., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.06.082 · Cited by 208
“org/sequence/S288C_reference/orf_protein/), released 1/13/ 2015with reversedsequencesand recombinant proteinsaddedusingProLuCID (Peng et al., 2003; Xu et al., 2015).”
Self-citationControl of seed dormancy and germination by DOG1-AHG1 PP2C phosphatase complex via binding to heme
Nishimura, N., Tsuchiya, W., Moresco, J. J., Hayashi, Y., Satoh, K., Kaiwa, N., Irisa, T., Kinoshita, T., Schroeder, J. I., Yates, J. R., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04437-9 · Cited by 221
“Using synthetic SnRK2s phosphopeptide as substrate, the reaction buffer was added, which is 100 μM SnRK2s phosphopeptide and 200 μM AHG1ΔΝ (1-103) with or without 800 μM heme-bound DOG1.”
Self-citationProtein Expression Landscape of Mouse Embryos during Pre-implantation Development
Gao, Y., Liu, X., Tang, B., Li, C., Kou, Z., Li, L., Liu, W., Wu, Y., Kou, X., Li, J., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.11.111 · Cited by 218
Self-citationGlobal site-specific N-glycosylation analysis of HIV envelope glycoprotein
Cao, L., Diedrich, J. K., Kulp, D. W., Pauthner, M. G., He, L., Park, S.-K. R., Sok, D., Su, C.-Y., Delahunty, C. M., Menis, S., et al. (2017) · Nature Communications · doi:10.1038/ncomms14954 · Cited by 208
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Wei, Z., Yoshihara, E., He, N., Hah, N., Fan, W., Pinto, A. F. M., Huddy, T. F., Wang, Y., Ross, B., Estepa, G., et al. (2018) · Cell · doi:10.1016/j.cell.2018.04.013 · Cited by 207
“, 2015) and searched with ProLuCID (Xu et al., 2015) against rat UniProt database.”
Expanding control of the tumor cell cycle with a CDK2/4/6 inhibitor
Freeman‐Cook, K. D., Hoffman, R. L., Miller, N. L. G., Almaden, J., Chionis, J., Zhang, Q., Eisele, K. J., Liu, C., Zhang, C., Huser, N. H., et al. (2021) · Cancer Cell · doi:10.1016/j.ccell.2021.08.009 · Cited by 195
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Blewett, M. M., Xie, J., Zaro, B. W., Backus, K. M., Altman, A., Teijaro, J. R., & Cravatt, B. F. (2016) · Science Signaling · doi:10.1126/scisignal.aaf7694 · Cited by 194
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Zhang, D., Gao, J., Zhu, Z., Mao, Q., Xu, Z., Singh, P. K., Rimayi, C. C., Moreno–Yruela, C., Xu, S., Li, G., et al. (2024) · Nature Chemical Biology · doi:10.1038/s41589-024-01680-8 · Cited by 190
“ProLuCID search results were filtered and assembled by DTASelect v.2.0 (ref.”
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Chu, Q., Martinez, T. F., Novak, S. W., Donaldson, C. J., Tan, D., Vaughan, J. M., Chang, T., Diedrich, J. K., de Andrade, L. R., Kim, A., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12816-z · Cited by 195
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Chen, Y., Liu, Y., Lan, T., Qin, W., Zhu, Y., Qin, K., Gao, J., Wang, H., Hou, X., Chen, N., et al. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b01462 · Cited by 186
Luo, M., Spradlin, J. N., Boike, L., Tong, B., Brittain, S. M., McKenna, J. M., Tallarico, J. A., Schirle, M., Maimone, T. J., & Nomura, D. K. (2021) · Cell Chemical Biology · doi:10.1016/j.chembiol.2021.01.005 · Cited by 186
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Chung, C. Y., Shin, H. R., Berdan, C. A., Ford, B., Ward, C. C., Olzmann, J. A., Zoncu, R., & Nomura, D. K. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0308-4 · Cited by 182
Rapid adaptation to CDK2 inhibition exposes intrinsic cell-cycle plasticity
Arora, M., Moser, J. C., Hoffman, T. E., Watts, L. P., Min, M., Musteanu, M., Rong, Y., Ill, C. R., Nangia, V., Schneider, J., et al. (2023) · Cell · doi:10.1016/j.cell.2023.05.013 · Cited by 170
Lu, S., Hu, J., Arogundade, O. A., Goginashvili, A., Vazquez‐Sanchez, S., Diedrich, J. K., Gu, J., Blum, J. A., Oung, S., Ye, Q., et al. (2022) · Nature Cell Biology · doi:10.1038/s41556-022-00988-8 · Cited by 168
Self-citationSulfopin is a covalent inhibitor of Pin1 that blocks Myc-driven tumors in vivo
Dubiella, C., Pinch, B. J., Koikawa, K., Zaidman, D., Poon, E., Manz, T. D., Nabet, B., He, S., Resnick, E., Rogel, A., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00786-7 · Cited by 163
Discovery of a Functional Covalent Ligand Targeting an Intrinsically Disordered Cysteine within MYC
Boike, L., Cioffi, A. G., Majewski, F. C., Co, J., Henning, N. J., Jones, M. D., Liu, G., McKenna, J. M., Tallarico, J. A., Schirle, M., et al. (2021) · Cell Chemical Biology · doi:10.1016/j.chembiol.2020.09.001 · Cited by 154
Improved Identification and Analysis of Small Open Reading Frame Encoded Polypeptides
Ma, J., Diedrich, J. K., Jungreis, I., Donaldson, C. J., Vaughan, J. M., Kellis, M., Yates, J. R., & Saghatelian, A. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b00191 · Cited by 145
Self-citationOgami, K., Richard, P., Chen, Y., Hoque, M., Li, W., Moresco, J. J., Yates, J. R., Tian, B., & Manley, J. L. (2017) · Genes & Development · doi:10.1101/gad.302604.117 · Cited by 149
“Tandem mass spectra were extracted from raw files using RawConverter (He et al. 2015) andwere searched against aUniProt human database with reversed sequences using ProLuCID (Peng et al. 2003; Xu et al. 2015).”
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Remsberg, J. R., Suciu, R. M., Zambetti, N. A., Hanigan, T. W., Firestone, A. J., Sheth, A. I., Long, A. M., Ngo, N., Lum, K. M., Henry, C. L., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00785-8 · Cited by 144
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Kim, T. K., Tirloni, L., Pinto, A. F. M., Moresco, J. J., Yates, J. R., Vaz, I. D. S., & Mulenga, A. (2016) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0004323 · Cited by 141
“For each group, ProLuCID XCorr, DeltaCN, DeltaMass, ZScore, number of peaks matched and secondary rank values were used to generate a Bayesian discriminating function.”
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Urresti, J., Zhang, P., Losada, P. M., Yu, N., Negraes, P. D., Trujillo, C. A., Antaki, D., Amar, M., Chau, K. K., Pramod, A. B., et al. (2021) · Molecular Psychiatry · doi:10.1038/s41380-021-01243-6 · Cited by 135
Self-citationCatania, S., Dumesic, P. A., Pimentel, H., Nasif, A., Stoddard, C. I., Burke, J. E., Diedrich, J. K., Cooke, S. L., Shea, T., Gienger, E., et al. (2020) · Cell · doi:10.1016/j.cell.2019.12.012 · Cited by 132
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Li, J., Li, X., Da, Y., Yu, J., Long, B., Zhang, P., Bakker, C., McCarl, B. A., Yuan, J. S., & Dai, S. Y. (2022) · Nature Communications · doi:10.1038/s41467-022-31881-5 · Cited by 141
Oh, C.-K., Sultan, A., Platzer, J., Dolatabadi, N., Soldner, F., McClatchy, D. B., Diedrich, J. K., Yates, J. R., Ambasudhan, R., Nakamura, T., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.10.068 · Cited by 136
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Patel, R., Santoro, A., Hofer, P., Tan, D., Oberer, M., Nelson, A. T., Konduri, S., Siegel, D. R., Zechner, R., Saghatelian, A., et al. (2022) · Nature · doi:10.1038/s41586-022-04787-x · Cited by 131
Intracellular amyloid toxicity induces oxytosis/ferroptosis regulated cell death
Huang, L., McClatchy, D. B., Maher, P. A., Liang, Z., Diedrich, J. K., Soriano‐Castell, D., Goldberg, J., Shokhirev, M. N., Yates, J. R., Schubert, D. A., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03020-9 · Cited by 130
Self-citationImpact of the Identification Strategy on the Reproducibility of the DDA and DIA Results
Fernández-Costa, C., Martínez‐Bartolomé, S., McClatchy, D. B., Saviola, A. J., Yu, N., & Yates, J. R. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00153 · Cited by 130
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Grossman, E. A., Ward, C. C., Spradlin, J. N., Bateman, L. A., Huffman, T. R., Miyamoto, D. K., Kleinman, J. I., & Nomura, D. K. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.08.013 · Cited by 121
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Isobe, Y., Okumura, M., McGregor, L. M., Brittain, S. M., Jones, M. D., Liang, X., White, R., Forrester, W., McKenna, J. M., Tallarico, J. A., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0557-2 · Cited by 124
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Kulkarni, R. A., Bak, D. W., Wei, D., Bergholtz, S. E., Briney, C. A., Shrimp, J. H., Alpsoy, A., Thorpe, A. L., Bavari, A. E., Crooks, D. R., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-018-0217-y · Cited by 122
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Reid, D. A., Reed, P. J., Schlachetzki, J. C. M., Nitulescu, I. I., Chou, G., Tsui, E. C., Jones, J. R., Chandran, S., Lu, A. T., McClain, C. A., et al. (2021) · Science · doi:10.1126/science.abb9032 · Cited by 121
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Ho, C.-M., Li, X., Lai, M., Terwilliger, T. C., Beck, J. R., Wohlschlegel, J., Goldberg, D. E., Fitzpatrick, A. W. P., & Zhou, Z. H. (2020) · Nature Methods · doi:10.1038/s41592-019-0637-y · Cited by 115
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Fuller, G. G., Han, T., Freeberg, M., Moresco, J. J., Niaki, A. G., Roach, N. P., Yates, J. R., Myong, S., & Kim, J. K. (2020) · eLife · doi:10.7554/elife.48480 · Cited by 119
“org) with reversed sequences using ProLuCID (Peng et al., 2003; Xu et al., 2015).”
InfluentialSelf-citationChemoproteomic Screening of Covalent Ligands Reveals UBA5 As a Novel Pancreatic Cancer Target
Roberts, A. M., Miyamoto, D. K., Huffman, T. R., Bateman, L. A., Ives, A. N., Akopian, D., Heslin, M. J., Contreras, C. M., Rapé, M., Skibola, C. F., et al. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00020 · Cited by 113
Pan, M., Zheng, Q., Yu, Y., Ai, H., Xie, Y., Zeng, X., Wang, C., Liu, L., & Zhao, M. (2021) · Nature Communications · doi:10.1038/s41467-020-20359-x · Cited by 108
Schiebenhoefer, H., Bossche, T. V. D., Fuchs, S., Renard, B. Y., Muth, T., & Martens, L. (2019) · Expert Review of Proteomics · doi:10.1080/14789450.2019.1609944 · Cited by 108
“The searches are performed using an adapted form of the ProLuCID algorithm [86], which was optimized for querying experimental spectra from metapro-teomics experiments.”
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Benegiamo, G., Mure, L. S., Erikson, G. A., Le, H. D., Moriggi, E., Brown, S. A., & Panda, S. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2017.12.010 · Cited by 104
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King, E. A., Cho, Y. J., Hsu, N. T., Dovala, D., McKenna, J. M., Tallarico, J. A., Schirle, M., & Nomura, D. K. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.02.008 · Cited by 107
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“Data was extracted in the form of MS1 and MS2 files using Raw Converter (Scripps Research Institute) and searched against the Uniprot human database using ProLuCID search methodology in IP2 v.3-v.5 (Integrated Proteomics Applications, Inc.) 32 .”
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Nechemia‐Arbely, Y., Miga, K. H., Shoshani, O., Aslanian, A., McMahon, M. A., Lee, A. Y., Fachinetti, D., Yates, J. R., Ren, B., & Cleveland, D. W. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0331-4 · Cited by 98
Self-citationQin, W., Lv, P., Fan, X., Quan, B., Zhu, Y., Qin, K., Chen, Y., Wang, C., & Chen, X. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1702688114 · Cited by 98
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Jha, S. S., Rollins, M. G., Fuchs, G., Procter, D. J., Hall, E., Cozzolino, K., Sarnow, P., Savas, J. N., & Walsh, D. (2017) · Nature · doi:10.1038/nature22814 · Cited by 91
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Berdan, C. A., Ho, R. Y., Lehtola, H. S., To, M., Hu, X., Huffman, T. R., Petri, Y. D., Altobelli, C. R., Demeulenaere, S. K., Olzmann, J. A., et al. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.03.016 · Cited by 94
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Lau, E., Cao, Q., Lam, M. P. Y., Wang, J., Ng, D. C. M., Bleakley, B. J., Lee, J. M., Liem, D. A., Wang, D., Hermjakob, H., et al. (2018) · Nature Communications · doi:10.1038/s41467-017-02467-3 · Cited by 85
Metaproteomics: A strategy to study the taxonomy and functionality of the gut microbiota
Wang, Y., Zhou, Y., Xiao, X., Zheng, J., & Zhou, H. (2020) · Journal of Proteomics · doi:10.1016/j.jprot.2020.103737 · Cited by 97
Mitohormesis reprogrammes macrophage metabolism to enforce tolerance
Timblin, G. A., Tharp, K. M., Ford, B., Winchester, J., Wang, J., Zhu, S., Khan, R. I., Louie, S. K., Iavarone, A. T., ten Hoeve, J., et al. (2021) · Nature Metabolism · doi:10.1038/s42255-021-00392-w · Cited by 91
A large dataset of protein dynamics in the mammalian heart proteome
Lau, E., Cao, Q., Ng, D. C. M., Bleakley, B. J., Dincer, T. U., Bot, B. M., Wang, D., Liem, D. A., Lam, M. P. Y., Ge, J., et al. (2016) · Scientific Data · doi:10.1038/sdata.2016.15 · Cited by 87
Insulin signaling regulates longevity through protein phosphorylation in Caenorhabditis elegans
Li, W.-J., Wang, C., Li, T., Yan, Y.-H., Zhang, M.-J., Liu, Z., Li, Y.-X., Zhao, H., Li, X.-M., He, X.-D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24816-z · Cited by 86
Tirloni, L., Kim, T. K., Pinto, A. F. M., Yates, J. R., Vaz, I. D. S., & Mulenga, A. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00517 · Cited by 86
“Tandem mass spectra were extracted from Thermo RAW files using RawExtract 1.9.9.2 (McDonald et al., 2004) and searched with ProLuCID (Xu et al., 2015) against a non-redundant tick databases.”
MethodInfluentialSelf-citationCaldwell, A. L. M., Sancho, L., Deng, J., Bosworth, A., Miglietta, A., Diedrich, J. K., Shokhirev, M. N., & Allen, N. J. (2022) · Nature Neuroscience · doi:10.1038/s41593-022-01150-1 · Cited by 86
Self-citationProtein signatures of seminal plasma from bulls with contrasting frozen-thawed sperm viability
Gomes, F. P., Park, S. K. R., Viana, A. G. D. A., Fernández-Costa, C., Topper, E., Kaya, A., Memili, E., Yates, J. R., & Moura, A. A. (2020) · Scientific Reports · doi:10.1038/s41598-020-71015-9 · Cited by 85
Self-citationOrphan receptor GPR158 controls stress-induced depression
Sutton, L. P., Orlandi, C., Song, C., Oh, W. C., Muntean, B. S., Xie, K., Filippini, A., Xie, X., Satterfield, R., Yaeger, J. D. W., et al. (2018) · eLife · doi:10.7554/elife.33273 · Cited by 88
Ortega, J. A., Daley, E. L., Kour, S., Samani, M., Tellez, L., Smith, H. S., Hall, E., Esengul, Y. T., Tsai, Y., Gendron, T. F., et al. (2020) · Neuron · doi:10.1016/j.neuron.2020.01.020 · Cited by 81
Willis, J. R., Berndsen, Z. T., Krystal, M., Steichen, J. M., Schiffner, T., Landais, E., Liguori, A., Kalyuzhniy, O., Allen, J. D., Baboo, S., et al. (2022) · Immunity · doi:10.1016/j.immuni.2022.09.001 · Cited by 76
“, 2015) and searched with ProLuCID (Xu et al., 2015) against a database comprising UniProt reviewed (Swiss-Prot) proteome for Homo sapiens (UP000005640), UniProt amino acid sequences for Endo H (P04067), PNGase F (Q9XBM8), and PK (P06873), amino acid sequences for the examined proteins, and a list of general protein c…”
MethodSelf-citationSharma, S., Chung, C., Uryu, S. A., Petrovic, J., Cao, J. Q., Rickard, A. J., Nady, N., Greasley, S. E., Johnson, E., Brodsky, O., et al. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.07.005 · Cited by 82
Katz, Z., Novotná, L., Blount, A. L., & Lillemeier, B. F. (2016) · Nature Immunology · doi:10.1038/ni.3631 · Cited by 79
Park, D. E., Cheng, J., McGrath, J. P., Lim, M. Y., Cushman, C. H., Swanson, S. K., Tillgren, M. L., Paulo, J. A., Gokhale, P. C., Florens, L. A., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0503-2 · Cited by 77
Across intra-mammalian stages of the liver f luke Fasciola hepatica: a proteomic study
Maggio, L. S. D., Tirloni, L., Pinto, A. F. M., Diedrich, J. K., Yates, J. R., Benavides, U., Carmona, C., Vaz, I. D. S., & Berasain, P. (2016) · Scientific Reports · doi:10.1038/srep32796 · Cited by 77
Self-citationSimple, efficient and thorough shotgun proteomic analysis with PatternLab V
Santos, M. D. M., Lima, D. B., Fischer, J. D. S. D. G., Clasen, M. A., Kurt, L. U., Camillo-Andrade, A. C., Monteiro, L. C., de Aquino, P. F., Neves‐Ferreira, A. G. C., Valente, R. H., et al. (2022) · Nature Protocols · doi:10.1038/s41596-022-00690-x · Cited by 77
Self-citationMutlu, B., Chen, H.-M., Moresco, J. J., Orelo, B. D., Yang, B., Gaspar, J. M., Keppler‐Ross, S., Yates, J. R., Hall, D. H., Maine, E. M., et al. (2018) · Science Advances · doi:10.1126/sciadv.aat6224 · Cited by 77
Self-citationBenjamin, D. I., Both, P., Benjamin, J. S., Nutter, C. W., Tan, J. H., Kang, J., Machado, L. A., Klein, J. D. D., de Morree, A., Kim, S., et al. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.04.012 · Cited by 79
Multiomics reveals glutathione metabolism as a driver of bimodality during stem cell aging
Benjamin, D. I., Brett, J. O., Both, P., Benjamin, J. S., Ishak, H. D., Kang, J., Kim, S., Chung, M., Arjona, M., Nutter, C. W., et al. (2023) · Cell Metabolism · doi:10.1016/j.cmet.2023.02.001 · Cited by 80
Wang, L., Collings, C. K., Zhao, Z., Cozzolino, K., Ma, Q., Liang, K., Marshall, S. A., Sze, C. C., Hashizume, R., Savas, J. N., et al. (2017) · Genes & Development · doi:10.1101/gad.306092.117 · Cited by 78
“…al. 2015), and the tandem mass spectra were searched against the UniProt humanprotein databaseandmatched to sequences using the ProLuCID/SEQUEST algorithm (ProLuCID version 3.1) (Eng et al. 1994; Xu et al. 2015) with peptide mass tolerance of 50 ppm for precursorions and 600 ppm forfragment ions.”
InfluentialNievas, Y. R., Cóceres, V. M., Midlej, V. D. V. P., de Souza, W., Benchimol, M., Pereira‐Neves, A., Vashisht, A. A., Wohlschlegel, J. A., Johnson, P. J., & de Miguel, N. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2726-3 · Cited by 81
“Spectra were analyzed using the ProLuCID [27] algorithm and searching against a fasta protein database consisting of all predicted open reading frames downloaded from TrichDB on January 4, 2015 [28] concatenated to a decoy database in which the amino acid sequence of each entry was reversed.”
MethodSelf-citationSelenium-Encoded Isotopic Signature Targeted Profiling
Gao, J., Yang, F., Che, J., Han, Y., Wang, Y., Chen, N., Bak, D. W., Lai, S., Xie, X., Weerapana, E., et al. (2018) · ACS Central Science · doi:10.1021/acscentsci.8b00112 · Cited by 73
Krishna, S., Arrojo e Drigo, R., Capitanio, J. S., Ramachandra, R., Ellisman, M., & Hetzer, M. W. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.10.008 · Cited by 73
A Dimethyl-Labeling-Based Strategy for Site-Specifically Quantitative Chemical Proteomics
Yang, F., Gao, J., Che, J., Jia, G., & Wang, C. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b02426 · Cited by 74
Vaccine priming of rare HIV broadly neutralizing antibody precursors in nonhuman primates
Steichen, J. M., Phung, I., Salcedo, E., Ozorowski, G., Willis, J. R., Baboo, S., Liguori, A., Cottrell, C. A., Torres, J. L., Madden, P. J., et al. (2024) · Science · doi:10.1126/science.adj8321 · Cited by 74
“Tan-demmassspectra were extracted from raw files using RawConverter ( 61 ) and searched with ProLuCID ( 62 ) against a database comprising the UniProt reviewed (Swiss-Prot) proteome for Homo sapiens (UP000005640); UniProt amino acid sequences for Endo H (P04067), PNGase F (Q9XBM8), and proteinase K…”
MethodSelf-citationdCas9-targeted locus-specific protein isolation method identifies histone gene regulators
Tsui, C., Inouye, C. J., Levy, M. J., Lu, A. C., Florens, L. A., Washburn, M. P., & Tjian, R. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1718844115 · Cited by 74
“3) on the fly dataset (59) and were searched against a nonredundant protein D.”
MethodBhattacharya, S., Levy, M. J., Zhang, N., Li, H., Florens, L. A., Washburn, M. P., & Workman, J. L. (2021) · Nature Communications · doi:10.1038/s41467-021-21663-w · Cited by 77
Defining the functional targets of cap'n'collar transcription factors NRF1, NRF2, and NRF3
Ibrahim, L., Mesgarzadeh, J., Xu, I., Powers, E. T., Wiseman, R. L., & Bollong, M. J. (2020) · Antioxidants · doi:10.3390/antiox9101025 · Cited by 67
“Protein identification and quantification were performed using the Integrated Proteomics Pipeline (IP2) [21,22].”
MethodLong-lived mitochondrial cristae proteins in mouse heart and brain
Bomba-Warczak, E. K., Edassery, S. L., Hark, T. J., & Savas, J. N. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202005193 · Cited by 71
“MS data analysis and quantification Protein identification/quantification and analysis were performed with the Integrated Proteomics Pipeline–IP2 (Integrated Proteomics Applications) using ProLuCID (Eng et al., 1994; Xu et al., 2015), DTASelect2 (Cociorva et al.”
MethodInfluentialPedros, C., Zhang, Y., Hu, J. K., Choi, Y. S., Canonigo-Balancio, A. J., Yates, J. R., Altman, A., Crotty, S., & Kong, K. (2016) · Nature Immunology · doi:10.1038/ni.3463 · Cited by 76
Self-citationLee, H. J., Bartsch, D., Xiao, C., Guerrero, S. X., Ahuja, G., Schindler, C., Moresco, J. J., Yates, J. R., Gebauer, F., Bazzi, H., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01744-5 · Cited by 73
Self-citationBamberger, C., Pankow, S., Martínez-Bartolomé, S., Ma, M., Diedrich, J., Rissman, R. A., & Yates, J. R. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00912 · Cited by 70
Self-citationmRNA-LNP HIV-1 trimer boosters elicit precursors to broad neutralizing antibodies
Xie, Z., Lin, Y., Steichen, J. M., Ozorowski, G., Kratochvil, S., Ray, R., Torres, J. L., Liguori, A., Kalyuzhniy, O., Wang, X., et al. (2024) · Science · doi:10.1126/science.adk0582 · Cited by 71
Self-citationDimethyl Fumarate Disrupts Human Innate Immune Signaling by Targeting the IRAK4–MyD88 Complex
Zaro, B. W., Vinogradova, E. V., Lazar, D. C., Blewett, M. M., Suciu, R. M., Takaya, J., Studer, S., de la Torre, J. C., Casanova, J.-L., Cravatt, B. F., et al. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.1801627 · Cited by 68
Chen, H., Victor, A. K., Klein, J. D., Tacer, K. F., Tai, D. J. C., de Esch, C. E. F., Nuttle, A., Temirov, J. P., Burnett, L. C., ROSENBAUM, M. S., et al. (2020) · JCI Insight · doi:10.1172/jci.insight.138576 · Cited by 66
“For peptide identification, tandem mass spectra were searched against a database including the UniProt mouse database 1 entry per gene (21,982 entries released December 1, 2019) with common contaminants and reversed sequences using ProLuCID (69).”
Self-citationTime-resolved proteomic profile of Amblyomma americanum tick saliva during feeding
Kim, T. K., Tirloni, L., Pinto, A. F. M., Diedrich, J. K., Moresco, J. J., Yates, J. R., Vaz, I. D. S., & Mulenga, A. (2020) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0007758 · Cited by 66
Self-citationAbiraami, T. V., Singh, S., & Nain, L. (2019) · Reviews in Environmental Science and Bio/Technology · doi:10.1007/s11157-019-09519-8 · Cited by 63
Song, Y., Zhou, H., Vo, M.-N., Shi, Y., Nawaz, M. H., Vargas‐Rodriguez, O., Diedrich, J. K., Yates, J. R., Kishi, S., Musier‐Forsyth, K., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-02201-z · Cited by 64
Self-citationStructural Basis of Karrikin and Non-natural Strigolactone Perception in Physcomitrella patens
Bürger, M., Mashiguchi, K., Lee, H. J., Nakano, M., Takemoto, K., Seto, Y., Yamaguchi, S., & Chory, J. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.003 · Cited by 65
“Tandem mass spectra were extracted from raw files using RawConverter (He et al., 2015) and searched with ProLuCID (Xu et al., 2015) against an E. coli protein database with recombinant proteins added.”
MethodInfluentialHark, T. J., Rao, N. R., Castillon, C., Basta, T., Smukowski, S. N., Bao, H., Upadhyay, A., Bomba-Warczak, E. K., Nomura, T., O'Toole, E. T., et al. (2020) · Cell Systems · doi:10.1016/j.cels.2020.11.007 · Cited by 60
Thompson, A. J., Cao, L., Ma, Y., Wang, X., Diedrich, J. K., Kikuchi, C., Willis, S., Worth, C. S., McBride, R., Yates, J. R., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.03.009 · Cited by 63
Self-citationDiscovery of Itaconate-Mediated Lysine Acylation
Liu, D., Xiao, W., Li, H., Zhang, Y., Yuan, S., Li, C., Dong, S., & Wang, C. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c02332 · Cited by 62
Metadata
- Authors
- Xu, T., Park, S. K., Venable, J. D., Wohlschlegel, J. A., Diedrich, J. K., Cociorva, D., Lu, B., Liao, L., Hewel, J., Han, X., Wong, C. C. L., Fonslow, B., Delahunty, C., Gao, Y., Shah, H., & Yates, J. R.
- Affiliations
- Scripps Research Institute (US)
- Corresponding author
- Yates, J.R.
- ORCID
- Venue
- Journal of Proteomics
- Publisher
- Elsevier BV
- Published
- 2015-11
- Volume
- 129
- Pages
- 16-24
- ISSN
- 1874-3919 (ISSN-L)
- PMC
- PMC4630125
- OpenAlex
- W2182963873
- Cited by
- 511
- References
- 51
- Citations by year
- 2026: 23 · 2025: 41 · 2024: 65 · 2023: 45 · 2022: 51 · 2021: 56 · 2020: 56 · 2019: 60 · 2018: 43 · 2017: 46 · 2016: 22 · 2015: 3
- FWCI
- 16.92
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Journal of Proteomics (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion, cc-by)
- Funders
- NIH (5U01 DE016267-04, 5R01 HL079442-04, R01 MH067880, P41 GM103533)
- NHLBI (HHSN268201000035C)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Phylogenetic Studies
- Keywords
- peptide identification, tandem mass spectrometry, SEQUEST, Z-score
- MeSH terms
- Algorithms, Amino Acid Sequence, Molecular Sequence Data, Pattern Recognition, Automated, Peptide Mapping, Proteins, Sensitivity and Specificity, Software, Reproducibility of Results, Sequence Analysis, Protein, Databases, Protein, Tandem Mass Spectrometry, Data Mining
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