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For: Brown KA, Melby JA, Roberts DS, Ge Y. Top-down proteomics: challenges, innovations, and applications in basic and clinical research. Expert Rev Proteomics 2020;17:719-33. [PMID: 33232185 DOI: 10.1080/14789450.2020.1855982] [Cited by in Crossref: 31] [Cited by in F6Publishing: 22] [Article Influence: 15.5] [Reference Citation Analysis]
Number Citing Articles
1 Ohlendieck K. Top-Down Proteomics and Comparative 2D-DIGE Analysis. Methods in Molecular Biology 2023. [DOI: 10.1007/978-1-0716-2831-7_2] [Reference Citation Analysis]
2 Dowling P, Gargan S, Swandulla D, Ohlendieck K. Identification of Subproteomic Markers for Skeletal Muscle Profiling. Methods in Molecular Biology 2023. [DOI: 10.1007/978-1-0716-2831-7_20] [Reference Citation Analysis]
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4 Radziński P, Valkenborg D, Startek MP, Gambin A. Envemind: Accurate Monoisotopic Mass Determination Based On Isotopic Envelope. J Am Soc Mass Spectrom 2022. [PMID: 36223196 DOI: 10.1021/jasms.2c00176] [Reference Citation Analysis]
5 Jeong K, Babović M, Gorshkov V, Kim J, Jensen ON, Kohlbacher O. FLASHIda enables intelligent data acquisition for top-down proteomics to boost proteoform identification counts. Nat Commun 2022;13:4407. [PMID: 35906205 DOI: 10.1038/s41467-022-31922-z] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
6 Maráková K. The Crucial Step in Every Analytical Workflow: Sample Preparation—Are We Ready For a Growing Area of Intact Protein Analysis? LCGC N Am 2022. [DOI: 10.56530/lcgc.na.ci1888f7] [Reference Citation Analysis]
7 Liu R, Xia S, Li H. Native top-down mass spectrometry for higher-order structural characterization of proteins and complexes. Mass Spectrom Rev 2022;:e21793. [PMID: 35757976 DOI: 10.1002/mas.21793] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
8 Wang C, Liang Y, Zhao B, Liang Z, Zhang L, Zhang Y. Ethane-Bridged Hybrid Monolithic Column with Large Mesopores for Boosting Top-Down Proteomic Analysis. Anal Chem 2022. [PMID: 35412811 DOI: 10.1021/acs.analchem.1c05234] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
9 Buck KM, Roberts DS, Aballo TJ, Inman DR, Jin S, Ponik S, Brown KA, Ge Y. One-Pot Exosome Proteomics Enabled by a Photocleavable Surfactant.. [DOI: 10.1101/2022.03.18.484933] [Reference Citation Analysis]
10 Lee HJ, Lee HS, Youn T, Byrne B, Chae PS. Impact of novel detergents on membrane protein studies. Chem 2022. [DOI: 10.1016/j.chempr.2022.02.007] [Cited by in Crossref: 7] [Cited by in F6Publishing: 7] [Article Influence: 7.0] [Reference Citation Analysis]
11 Tasoulis T, Pukala TL, Isbister GK. Investigating Toxin Diversity and Abundance in Snake Venom Proteomes. Front Pharmacol 2021;12:768015. [PMID: 35095489 DOI: 10.3389/fphar.2021.768015] [Cited by in Crossref: 13] [Cited by in F6Publishing: 12] [Article Influence: 13.0] [Reference Citation Analysis]
12 Melani RD, Gerbasi VR, Anderson LC, Sikora JW, Toby TK, Hutton JE, Butcher DS, Negrão F, Seckler HS, Srzentić K, Fornelli L, Camarillo JM, LeDuc RD, Cesnik AJ, Lundberg E, Greer JB, Fellers RT, Robey MT, DeHart CJ, Forte E, Hendrickson CL, Abbatiello SE, Thomas PM, Kokaji AI, Levitsky J, Kelleher NL. The Blood Proteoform Atlas: A reference map of proteoforms in human hematopoietic cells. Science 2022;375:411-8. [PMID: 35084980 DOI: 10.1126/science.aaz5284] [Cited by in Crossref: 17] [Cited by in F6Publishing: 16] [Article Influence: 17.0] [Reference Citation Analysis]
13 Sun R, Wang R, Luo L, Liu C, Chi H, Zeng W, He S. Accurate Proteoform Identification and Quantitation Using pTop 2.0. Proteoform Identification 2022. [DOI: 10.1007/978-1-0716-2325-1_9] [Reference Citation Analysis]
14 Tiambeng TN, Wu Z, Melby JA, Ge Y. Size Exclusion Chromatography Strategies and MASH Explorer for Large Proteoform Characterization. Proteoform Identification 2022. [DOI: 10.1007/978-1-0716-2325-1_3] [Reference Citation Analysis]
15 Bondt A, Dingess KA, Hoek M, van Rijswijck DMH, Heck AJR. A Direct MS-Based Approach to Profile Human Milk Secretory Immunoglobulin A (IgA1) Reveals Donor-Specific Clonal Repertoires With High Longitudinal Stability. Front Immunol 2021;12:789748. [PMID: 34938298 DOI: 10.3389/fimmu.2021.789748] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
16 Cline EN, Alvarez C, Duan J, Patrie SM. Online μSEC2-nRPLC-MS for Improved Sensitivity of Intact Protein Detection of IEF-Separated Nonhuman Primate Cerebrospinal Fluid Proteins. Anal Chem 2021;93:16741-50. [PMID: 34881887 DOI: 10.1021/acs.analchem.1c00396] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
17 Jeong K, Babović M, Gorshkov V, Kim J, Jensen ON, Kohlbacher O. FLASHIda: Intelligent data acquisition for top-down proteomics that doubles proteoform level identification count.. [DOI: 10.1101/2021.11.11.468203] [Reference Citation Analysis]
18 Brown KA, Anderson C, Reilly L, Sondhi K, Ge Y, Eckhardt LL. Proteomic Analysis of the Functional Inward Rectifier Potassium Channel (Kir) 2.1 Reveals Several Novel Phosphorylation Sites. Biochemistry 2021;60:3292-301. [PMID: 34676745 DOI: 10.1021/acs.biochem.1c00555] [Cited by in Crossref: 2] [Cited by in F6Publishing: 3] [Article Influence: 2.0] [Reference Citation Analysis]
19 Miles HN, Delafield DG, Li L. Recent Developments and Applications of Quantitative Proteomics Strategies for High-Throughput Biomolecular Analyses in Cancer Research. RSC Chem Biol 2021;4:1050-72. [PMID: 34430874 DOI: 10.1039/d1cb00039j] [Cited by in Crossref: 4] [Cited by in F6Publishing: 4] [Article Influence: 4.0] [Reference Citation Analysis]
20 Lill JR, Mathews WR, Rose CM, Schirle M. Proteomics in the pharmaceutical and biotechnology industry: a look to the next decade. Expert Rev Proteomics 2021;:1-24. [PMID: 34320887 DOI: 10.1080/14789450.2021.1962300] [Cited by in Crossref: 6] [Cited by in F6Publishing: 1] [Article Influence: 6.0] [Reference Citation Analysis]
21 Roberts DS, Mann M, Melby JA, Larson EJ, Zhu Y, Brasier AR, Jin S, Ge Y. Structural O-Glycoform Heterogeneity of the SARS-CoV-2 Spike Protein Receptor-Binding Domain Revealed by Top-Down Mass Spectrometry. J Am Chem Soc 2021;143:12014-24. [PMID: 34328324 DOI: 10.1021/jacs.1c02713] [Cited by in Crossref: 25] [Cited by in F6Publishing: 25] [Article Influence: 25.0] [Reference Citation Analysis]
22 Ni W, Jagust W, Wang D. Multiplex Mass Spectrometry Analysis of Amyloid Proteins in Human Plasma for Alzheimer's Disease Diagnosis. J Proteome Res 2021;20:4106-12. [PMID: 34314176 DOI: 10.1021/acs.jproteome.1c00424] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
23 Tabang DN, Ford M, Li L. Recent Advances in Mass Spectrometry-Based Glycomic and Glycoproteomic Studies of Pancreatic Diseases. Front Chem 2021;9:707387. [PMID: 34368082 DOI: 10.3389/fchem.2021.707387] [Cited by in Crossref: 7] [Cited by in F6Publishing: 7] [Article Influence: 7.0] [Reference Citation Analysis]
24 Fiani B, Covarrubias C, Jarrah R. Bench to Bedside: Proteomic Biomarker Analysis of Cerebrospinal Fluid in Patients With Spondylomyelopathy. Cureus 2021;13:e16003. [PMID: 34336494 DOI: 10.7759/cureus.16003] [Reference Citation Analysis]
25 Cline EN, Alvarez C, Duan J, Patrie SM. Online μSEC2-nRPLC-MS for improved sensitivity of intact protein detection of IEF separated non-human primate cerebrospinal fluid proteins.. [DOI: 10.1101/2021.06.08.447575] [Reference Citation Analysis]
26 Nickerson JL, Baghalabadi V, Rajendran SRCK, Jakubec PJ, Said H, McMillen TS, Dang Z, Doucette AA. Recent advances in top-down proteome sample processing ahead of MS analysis. Mass Spectrom Rev 2021. [PMID: 34047392 DOI: 10.1002/mas.21706] [Cited by in Crossref: 9] [Cited by in F6Publishing: 9] [Article Influence: 9.0] [Reference Citation Analysis]
27 Su M, Zhang Z, Zhou L, Han C, Huang C, Nice EC. Proteomics, Personalized Medicine and Cancer. Cancers (Basel) 2021;13:2512. [PMID: 34063807 DOI: 10.3390/cancers13112512] [Cited by in Crossref: 9] [Cited by in F6Publishing: 10] [Article Influence: 9.0] [Reference Citation Analysis]
28 Melby JA, Roberts DS, Larson EJ, Brown KA, Bayne EF, Jin S, Ge Y. Novel Strategies to Address the Challenges in Top-Down Proteomics. J Am Soc Mass Spectrom 2021;32:1278-94. [PMID: 33983025 DOI: 10.1021/jasms.1c00099] [Cited by in Crossref: 38] [Cited by in F6Publishing: 42] [Article Influence: 38.0] [Reference Citation Analysis]
29 Deol KK, Strieter ER. The ubiquitin proteoform problem. Curr Opin Chem Biol 2021;63:95-104. [PMID: 33813043 DOI: 10.1016/j.cbpa.2021.02.015] [Cited by in Crossref: 4] [Cited by in F6Publishing: 4] [Article Influence: 4.0] [Reference Citation Analysis]
30 Van Eyk JE. The World of Protein Interactions: Defining the Caveolin 3 Cardiac Interactome. Circ Res 2021;128:720-2. [PMID: 33734816 DOI: 10.1161/CIRCRESAHA.121.318922] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
31 Roberts DS, Mann MW, Melby JA, Larson EJ, Zhu Y, Brasier AR, Jin S, Ge Y. Structural O-Glycoform Heterogeneity of the SARS-CoV-2 Spike Protein Receptor-Binding Domain Revealed by Native Top-Down Mass Spectrometry. bioRxiv 2021:2021. [PMID: 33688648 DOI: 10.1101/2021.02.28.433291] [Cited by in Crossref: 1] [Article Influence: 1.0] [Reference Citation Analysis]
32 Hesketh SJ, Stansfield BN, Stead CA, Burniston JG. The application of proteomics in muscle exercise physiology. Expert Rev Proteomics 2020;17:813-25. [PMID: 33470862 DOI: 10.1080/14789450.2020.1879647] [Cited by in Crossref: 5] [Cited by in F6Publishing: 5] [Article Influence: 5.0] [Reference Citation Analysis]
33 Alfaro-espinoza ER, Paiva LF, Faria-campos AC, Baracat-pereira MC, Campos SVA. FluxPRT: An Adaptable and Extensible Proteomics LIMS. Advances in Bioinformatics and Computational Biology 2021. [DOI: 10.1007/978-3-030-91814-9_12] [Reference Citation Analysis]