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High-sensitivity Analytical Approaches for the Structural Characterization of Glycoproteins
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ADVERTISEMENT RETURN TO ISSUEPREVReviewNEXTHigh-sensitivity Analytical Approaches for the Structural Characterization of GlycoproteinsWilliam R. Alley, Jr.†‡, Benjamin F. Mann†‡, and Milos V. Novotny*†‡§View Author Information† Department of Chemistry, Indiana University, Bloomington, Indiana, United States‡ National Center for Glycomics and Glycoproteomics, Indiana University, Bloomington, Indiana, United States§ Indiana University School of Medicine, Indiana University, Indianapolis, Indiana, United States*E-mail: [email protected]. Phone: (812) 855-4532. Fax: (812) 855-8300.Cite this: Chem. Rev. 2013, 113, 4, 2668–2732Publication Date (Web):March 27, 2013Publication History Received4 September 2012Published online27 March 2013Published inissue 10 April 2013https://pubs.acs.org/doi/10.1021/cr3003714https://doi.org/10.1021/cr3003714review-articleACS PublicationsCopyright © 2013 American Chemical SocietyRequest reuse permissionsArticle Views6426Altmetric-Citations263LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose SUBJECTS:Carbohydrates,Chemical biology,Chemical structure,Monomers,Peptides and proteins Get e-Alerts
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Citations
Cites
Biological roles of oligosaccharides: all of the theories are correct
Varki, A. (1993) · Glycobiology · doi:10.1093/glycob/3.2.97 · Cited by 5,195
Systems biology: a brief overview
Kitano, H. (2002) · Science · doi:10.1126/science.1069492 · Cited by 4,265
Wiederschain, G. Y. (2009) · Biochemistry (Moscow) · doi:10.1134/s0006297909090156 · Cited by 4,083
A simple and rapid method for the permethylation of carbohydrates
Ciucanu, I., & Kerek, F. (1984) · Carbohydrate Research · doi:10.1016/0008-6215(84)85242-8 · Cited by 3,580
Protein Purification by Affinity Chromatography
Cuatrecasas, P. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63022-4 · Cited by 2,796
A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates
Domon, B., & Costello, C. E. (1988) · Glycoconjugate Journal · doi:10.1007/bf01049915 · Cited by 2,729
Rowan, S. J., Cantrill, S. J., Cousins, G. R. L., Sanders, J. K. M., & Stoddart, J. F. (2002) · Angewandte Chemie International Edition · doi:10.1002/1521-3773(20020315)41:6<898::aid-anie898>3.0.co;2-e · Cited by 2,588
Cell Surface Engineering by a Modified Staudinger Reaction
Saxon, E., & Bertozzi, C. R. (2000) · Science · doi:10.1126/science.287.5460.2007 · Cited by 2,460
Intracellular Functions of N-Linked Glycans
Helenius, A., & Aebi, A. M. (2001) · Science · doi:10.1126/science.291.5512.2364 · Cited by 2,405
Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
Syka, J. E. P., Coon, J. J., Schroeder, M. J., Shabanowitz, J., & Hunt, D. F. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402700101 · Cited by 2,370
(1964) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a127869 · Cited by 2,143
Glycosyltransferases: Structures, Functions, and Mechanisms
Lairson, L. L., Henrissat, B., Davies, G. J., & Withers, S. G. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.061005.092322 · Cited by 2,079
Alpert, A. J. (1990) · Journal of Chromatography A · doi:10.1016/s0021-9673(00)96972-3 · Cited by 1,966
Electron Capture Dissociation of Multiply Charged Protein Cations. A Nonergodic Process
Zubarev, R. A., Kelleher, N. L., & McLafferty, F. W. (1998) · Journal of the American Chemical Society · doi:10.1021/ja973478k · Cited by 1,881
Analytical Properties of the Nanoelectrospray Ion Source
Wilm, M., & Mann, M. (1996) · Analytical Chemistry · doi:10.1021/ac9509519 · Cited by 1,868
Shields, R. L., Lai, J., Keck, R., O'Connell, L. Y., Hong, K., Meng, Y. G., Weikert, S. H. A., & Presta, L. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202069200 · Cited by 1,835
Copper-free click chemistry for dynamic in vivo imaging
Baskin, J. M., Prescher, J. A., Laughlin, S. T., Agard, N. J., Chang, P. V., Miller, I. A., Lo, A., Codelli, J. A., & Bertozzi, C. R. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707090104 · Cited by 1,833
Anti-Inflammatory Activity of Immunoglobulin G Resulting from Fc Sialylation
Kaneko, Y., Nimmerjahn, F., & Ravetch, J. V. (2006) · Science · doi:10.1126/science.1129594 · Cited by 1,754
Ruhland, K. (2020) · Catalysis from A to Z · doi:10.1002/9783527809080.cataz06077 · Cited by 1,724
Glycans in cancer and inflammation — potential for therapeutics and diagnostics
Dube, D. H., & Bertozzi, C. R. (2005) · Nature Reviews Drug Discovery · doi:10.1038/nrd1751 · Cited by 1,598
Glycosylation and the Immune System
Rudd, P. M., Elliott, T., Cresswell, P., Wilson, I. A., & Dwek, R. A. (2001) · Science · doi:10.1126/science.291.5512.2370 · Cited by 1,588
Larsen, M. R., Thingholm, T. E., Jensen, O. N., Roepstorff, P., & Jørgensen, T. J. D. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t500007-mcp200 · Cited by 1,476
Shinkawa, T., Nakamura, K., Yamane, N., Shoji-Hosaka, E., Kanda, Y., Sakurada, M., Uchida, K., Anazawa, H., Satoh, M., Yamasaki, M., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210665200 · Cited by 1,413
Spiro, R. G. (2002) · Glycobiology · doi:10.1093/glycob/12.4.43r · Cited by 1,409
Zhang, H., Li, X.-J., Martin, D. B., & Aebersold, R. (2003) · Nature Biotechnology · doi:10.1038/nbt827 · Cited by 1,389
The Orbitrap: a new mass spectrometer
Hu, Q., Noll, R. J., Li, H., Makarov, A., Hardman, M., & Graham Cooks, R. (2005) · Journal of Mass Spectrometry · doi:10.1002/jms.856 · Cited by 1,333
Hydrophilic interaction chromatography
Hemström, P., & Irgum, K. (2006) · Journal of Separation Science · doi:10.1002/jssc.200600199 · Cited by 1,176
Printed covalent glycan array for ligand profiling of diverse glycan binding proteins
Blixt, O., Head, S., Mondala, T., Scanlan, C., Huflejt, M. E., Alvarez, R., Bryan, M. C., Fazio, F., Calarese, D., Stevens, J., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407902101 · Cited by 1,101
GlycoWorkbench: A Tool for the Computer-Assisted Annotation of Mass Spectra of Glycans
Ceroni, A., Maass, K., Geyer, H., Geyer, R., Dell, A., & Haslam, S. M. (2008) · Journal of Proteome Research · doi:10.1021/pr7008252 · Cited by 1,057
In Vivo Imaging of Membrane-Associated Glycans in Developing Zebrafish
Laughlin, S. T., Baskin, J. M., Amacher, S. L., & Bertozzi, C. R. (2008) · Science · doi:10.1126/science.1155106 · Cited by 1,026
Electrostatic Axially Harmonic Orbital Trapping: A High-Performance Technique of Mass Analysis
Makarov, A. (2000) · Analytical Chemistry · doi:10.1021/ac991131p · Cited by 1,009
Higher-energy C-trap dissociation for peptide modification analysis
Olsen, J. V., Macek, B., Lange, O., Makarov, A., Horning, S., & Mann, M. (2007) · Nature Methods · doi:10.1038/nmeth1060 · Cited by 999
Polyol Complexes and Structure of the Benzeneboronate Ion
LORAND, J. P., & EDWARDS, J. O. (1959) · The Journal of Organic Chemistry · doi:10.1021/jo01088a011 · Cited by 987
Electron Capture Dissociation for Structural Characterization of Multiply Charged Protein Cations
Zubarev, R. A., Horn, D. M., Fridriksson, E. K., Kelleher, N. L., Kruger, N. A., Lewis, M. A., Carpenter, B. K., & McLafferty, F. W. (2000) · Analytical Chemistry · doi:10.1021/ac990811p · Cited by 986
Structures and Immunochemical Properties of Oligosaccharides Isolated from Pig Submaxillary Mucins
Carlson, D. M., & Blackwell, C. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93649-5 · Cited by 979
Glycosylation defining cancer malignancy: New wine in an old bottle
Hakomori, S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172380699 · Cited by 960
β1-6 Branching of Asn-Linked Oligosaccharides Is Directly Associated with Metastasis
Dennis, J. W., Laferté, S., Waghorne, C., Breitman, M. L., & Kerbel, R. S. (1987) · Science · doi:10.1126/science.2953071 · Cited by 940
The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea).
Lotan, R., Skutelsky, E., Danon, D., & Sharon, N. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40790-4 · Cited by 939
Precision Mapping of an In Vivo N-Glycoproteome Reveals Rigid Topological and Sequence Constraints
Zielinska, D. F., Gnad, F., Wiśniewski, J. R., & Mann, M. (2010) · Cell · doi:10.1016/j.cell.2010.04.012 · Cited by 902
Dongré, A. R., Jones, J. L., Somogyi, Á., & Wysocki, V. H. (1996) · Journal of the American Chemical Society · doi:10.1021/ja9542193 · Cited by 894
Glycosylation as a strategy to improve antibody-based therapeutics
Jefferis, R. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2804 · Cited by 829
Bigge, J. C., Patel, T. P., Bruce, J. A., Goulding, P. N., Charles, S. M., & Parekh, R. B. (1995) · Analytical Biochemistry · doi:10.1006/abio.1995.1468 · Cited by 825
Pringle, S. D., Giles, K., Wildgoose, J. L., Williams, J. P., Slade, S. E., Thalassinos, K., Bateman, R. H., Bowers, M. T., & Scrivens, J. H. (2007) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2006.07.021 · Cited by 808
The elderberry (Sambucus nigra L.) bark lectin recognizes the Neu5Ac(alpha 2-6)Gal/GalNAc sequence.
Shibuya, N., Goldstein, I. J., Broekaert, W. F., Nsimba-Lubaki, M., Peeters, B., & Peumans, W. J. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75677-4 · Cited by 784
Umaña, P., Jean–Mairet, J., Moudry, R., Amstutz, H., & Bailey, J. E. (1999) · Nature Biotechnology · doi:10.1038/6179 · Cited by 764
Applications of a travelling wave‐based radio‐frequency‐only stacked ring ion guide
Giles, K., Pringle, S. D., Worthington, K. R., Little, D., Wildgoose, J. L., & Bateman, R. H. (2004) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.1641 · Cited by 727
Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates
Harvey, D. J. (1999) · Mass Spectrometry Reviews · doi:10.1002/(sici)1098-2787(1999)18:6<349::aid-mas1>3.0.co;2-h · Cited by 725
Influencing Receptor−Ligand Binding Mechanisms with Multivalent Ligand Architecture
Gestwicki, J. E., Cairo, C. W., Strong, L. E., Oetjen, K. A., & Kiessling, L. L. (2002) · Journal of the American Chemical Society · doi:10.1021/ja027184x · Cited by 706
Stable-Isotope Dimethyl Labeling for Quantitative Proteomics
Hsu, J.-L., Huang, S.-Y., Chow, N.-H., & Chen, S.-H. (2003) · Analytical Chemistry · doi:10.1021/ac0348625 · Cited by 701
A Potent and Broad Neutralizing Antibody Recognizes and Penetrates the HIV Glycan Shield
Pejchal, R., Doores, K. J., Walker, L. M., Khayat, R., Huang, P.-S., Wang, S.-K., Stanfield, R. L., Julien, J.-P., Ramos, A., Crispin, M., et al. (2011) · Science · doi:10.1126/science.1213256 · Cited by 694
Gobom, J., Nordhoff, E., Mirgorodskaya, E., Ekman, R., & Roepstorff, P. (1999) · Journal of Mass Spectrometry · doi:10.1002/(sici)1096-9888(199902)34:2<105::aid-jms768>3.0.co;2-4 · Cited by 688
Phosphofructokinase 1 Glycosylation Regulates Cell Growth and Metabolism
Yi, W., Clark, P. M., Mason, D. E., Keenan, M. C., Hill, C., Goddard, W. A., Peters, E. C., Driggers, E. M., & Hsieh-Wilson, L. C. (2012) · Science · doi:10.1126/science.1222278 · Cited by 676
Hart, G. W., & Copeland, R. J. (2010) · Cell · doi:10.1016/j.cell.2010.11.008 · Cited by 643
A systematic approach to protein glycosylation analysis: a path through the maze
Mariño, K., Bones, J., Kattla, J. J., & Rudd, P. M. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.437 · Cited by 628
Visualization of omics data for systems biology
Gehlenborg, N., O'Donoghue, S. I., Baliga, N. S., Goesmann, A., Hibbs, M. A., Kitano, H., Kohlbacher, O., Neuweger, H., Schneider, R., Tenenbaum, D., et al. (2010) · Nature Methods · doi:10.1038/nmeth.1436 · Cited by 620
Nagata, Y., & Burger, M. M. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42646-x · Cited by 606
Plummer, T. H., Elder, J. H., Alexander, S., Phelan, A. W., & Tarentino, A. L. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)90568-5 · Cited by 587
The carbohydrate-binding specificity of pea and lentil lectins. Fucose is an important determinant.
Kornfeld, K., Reitman, M. L., & Kornfeld, R. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69037-x · Cited by 563
Semi-wet peptide/protein array using supramolecular hydrogel
Kiyonaka, S., Sada, K., Yoshimura, I., Shinkai, S., Kato, N., & Hamachi, I. (2004) · Nature Materials · doi:10.1038/nmat1034 · Cited by 560
Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins
Wollscheid, B., Bausch-Fluck, D., Henderson, C., O'Brien, R., Bibel, M., Schiess, R., Aebersold, R., & Watts, J. D. (2009) · Nature Biotechnology · doi:10.1038/nbt.1532 · Cited by 547
Bruggeman, F. J., & Westerhoff, H. V. (2007) · Trends in Microbiology · doi:10.1016/j.tim.2006.11.003 · Cited by 531
Tao, M. H., & Morrison, S. L. (1989) · The Journal of Immunology · doi:10.4049/jimmunol.143.8.2595 · Cited by 530
Evanescent-field fluorescence-assisted lectin microarray: a new strategy for glycan profiling
Kuno, A., Uchiyama, N., Koseki-Kuno, S., Ebe, Y., Takashima, S., Yamada, M., & Hirabayashi, J. (2005) · Nature Methods · doi:10.1038/nmeth803 · Cited by 513
DYNAMIC O-LINKED GLYCOSYLATION OF NUCLEAR AND CYTOSKELETAL PROTEINS
Hart, G. W. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.315 · Cited by 508
Cummings, R. D., & Kornfeld, S. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33747-5 · Cited by 497
The repertoire of glycan determinants in the human glycome
Cummings, R. D. (2009) · Molecular BioSystems · doi:10.1039/b907931a · Cited by 487
Sasaki, H., Bothner, B., Dell, A., & Fukuda, M. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45317-3 · Cited by 484
Ionic Liquids as Matrixes for Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry
Armstrong, D. W., Zhang, L.-K., He, L., & Gross, M. L. (2001) · Analytical Chemistry · doi:10.1021/ac010259f · Cited by 479
Glycan labeling strategies and their use in identification and quantification
Ruhaak, L. R., Zauner, G., Huhn, C., Bruggink, C., Deelder, A. M., & Wuhrer, M. (2010) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-010-3532-z · Cited by 479
Tolstikov, V. V., & Fiehn, O. (2002) · Analytical Biochemistry · doi:10.1006/abio.2001.5513 · Cited by 472
GlycoMod - A software tool for determining glycosylation compositions from mass spectrometric data
Cooper, C. A., Gasteiger, E., & Packer, N. H. (2001) · PROTEOMICS · doi:10.1002/1615-9861(200102)1:2<340::aid-prot340>3.0.co;2-b · Cited by 471
HPLC-based analysis of serum N-glycans on a 96-well plate platform with dedicated database software
Royle, L., Campbell, M. P., Radcliffe, C. M., White, D. M., Harvey, D. J., Abrahams, J. L., Kim, Y.-G., Henry, G. W., Shadick, N. A., Weinblatt, M. E., et al. (2008) · Analytical Biochemistry · doi:10.1016/j.ab.2007.12.012 · Cited by 466
Hägglund, P., Bunkenborg, J., Elortza, F., Jensen, O. N., & Roepstorff, P. (2004) · Journal of Proteome Research · doi:10.1021/pr034112b · Cited by 460
Structural determinants of concanavalin A specificity for oligosaccharides
Baenziger, J. U., & Fiete, D. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30236-3 · Cited by 459
Dowlut, M., & Hall, D. G. (2006) · Journal of the American Chemical Society · doi:10.1021/ja057798c · Cited by 434
Liu, Y.-C., Yen, H.-Y., Chen, C.-Y., Chen, C.-H., Cheng, P.-F., Juan, Y.-H., Chen, C.-H., Khoo, K.-H., Yu, C.-J., Yang, P.-C., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107385108 · Cited by 424
Wells, L., Vosseller, K., Cole, R. N., Cronshaw, J. M., Matunis, M. J., & Hart, G. W. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200048-mcp200 · Cited by 420
Glycoproteomics based on tandem mass spectrometry of glycopeptides
Wuhrer, M., Catalina, M. I., Deelder, A. M., & Hokke, C. H. (2007) · Journal of Chromatography B · doi:10.1016/j.jchromb.2006.09.041 · Cited by 415
Glycoproteomic probes for fluorescent imaging of fucosylated glycans in vivo
Sawa, M., Hsu, T.-L., Itoh, T., Sugiyama, M., Hanson, S. R., Vogt, P. K., & Wong, C.-H. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605418103 · Cited by 409
Structural analysis of N- and O-glycans released from glycoproteins
Jensen, P. H., Karlsson, N. G., Kolarich, D., & Packer, N. H. (2012) · Nature Protocols · doi:10.1038/nprot.2012.063 · Cited by 407
TRETTER, V., ALTMANN, F., & MÄRZ, L. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16166.x · Cited by 406
Liu, T., Qian, W.-J., Gritsenko, M. A., Camp, D. G., Monroe, M. E., Moore, R. J., & Smith, R. D. (2005) · Journal of Proteome Research · doi:10.1021/pr0502065 · Cited by 405
Protein glycosylation in bacterial mucosal pathogens
Szymanski, C. M., & Wren, B. W. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1100 · Cited by 402
Huddleston, M. J., Bean, M. F., & Carr, S. A. (1993) · Analytical Chemistry · doi:10.1021/ac00055a009 · Cited by 395
Biological Function of Fucosylation in Cancer Biology
Miyoshi, E., Moriwaki, K., & Nakagawa, T. (2007) · Journal of Biochemistry · doi:10.1093/jb/mvn011 · Cited by 395
Depletion of Abundant Plasma Proteins and Limitations of Plasma Proteomics
Tu, C., Rudnick, P. A., Martinez, M. Y., Cheek, K. L., Stein, S. E., Slebos, R. J. C., & Liebler, D. C. (2010) · Journal of Proteome Research · doi:10.1021/pr100646w · Cited by 390
Ovarian Cancer is Associated with Changes in Glycosylation in Both Acute-Phase Proteins and IgG
Saldova, R., Royle, L., Radcliffe, C. M., Abd Hamid, U. M., Evans, R., Arnold, J. N., Banks, R. E., Hutson, R., Harvey, D. J., Antrobus, R., et al. (2007) · Glycobiology · doi:10.1093/glycob/cwm100 · Cited by 390
Analyses of N-linked oligosaccharides using a two-dimensional mapping technique
Tomiya, N., Awaya, J., Kurono, M., Endo, S., Arata, Y., & Takahashi, N. (1988) · Analytical Biochemistry · doi:10.1016/0003-2697(88)90126-1 · Cited by 389
GLYCOSYLATION IN THE NUCLEUS AND CYTOPLASM
Hart, G. W., Haltiwanger, R. S., Holt, G. D., & Kelly, W. G. (1989) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.58.070189.004205 · Cited by 386
Mirgorodskaya, E., Roepstorff, P., & Zubarev, R. A. (1999) · Analytical Chemistry · doi:10.1021/ac990578v · Cited by 381
Fernandes, B., Sagman, U., Auger, M., Demetrio, M., & Dennis, J. W. (1991) · PubMed · Cited by 367
The sugar code : fundamentals of glycosciences
Gabius, H. (2009) · Cited by 366
Swaney, D. L., McAlister, G. C., Wirtala, M., Schwartz, J. C., Syka, J. E. P., & Coon, J. J. (2007) · Analytical Chemistry · doi:10.1021/ac061457f · Cited by 363
Lloyd, K. O., Burchell, J., Kudryashov, V., Yin, B. W. T., & Taylor-Papadimitriou, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.52.33325 · Cited by 362
Qian, W.-J., Jacobs, J. M., Liu, T., Camp, D. G., & Smith, R. D. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600162-mcp200 · Cited by 362
Binding properties of a mannose-specific lectin from the snowdrop (Galanthus nivalis) bulb.
Shibuya, N., Goldstein, I. J., Van Damme, E. J., & Peumans, W. J. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)35413-4 · Cited by 354
Mining the O-glycoproteome using zinc-finger nuclease–glycoengineered SimpleCell lines
Steentoft, C., Vakhrushev, S. Y., Vester-Christensen, M. B., Schjoldager, K. T.-B. G., Kong, Y., Bennett, E. P., Mandel, U., Wandall, H., Levery, S. B., & Clausen, H. (2011) · Nature Methods · doi:10.1038/nmeth.1731 · Cited by 349
Asparagine-linked protein glycosylation: from eukaryotic to prokaryotic systems
Weerapana, E., & Imperiali, B. (2006) · Glycobiology · doi:10.1093/glycob/cwj099 · Cited by 346
Vosseller, K., Trinidad, J. C., Chalkley, R. J., Specht, C. G., Thalhammer, A., Lynn, A. J., Snedecor, J. O., Guan, S., Medzihradszky, K. F., Maltby, D. A., et al. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t500040-mcp200 · Cited by 345
Structural Investigations of Glycoconjugates at High Sensitivity
Mechref, Y., & Novotny, M. V. (2002) · Chemical Reviews · doi:10.1021/cr0103017 · Cited by 341
Self-citationStahl, B., Steup, M., Karas, M., & Hillenkamp, F. (1991) · Analytical Chemistry · doi:10.1021/ac00014a022 · Cited by 339
Probing the dynamics of O-GlcNAc glycosylation in the brain using quantitative proteomics
Khidekel, N., Ficarro, S. B., Clark, P. M., Bryan, M. C., Swaney, D. L., Rexach, J. E., Sun, Y. E., Coon, J. J., Peters, E. C., & Hsieh-Wilson, L. C. (2007) · Nature Chemical Biology · doi:10.1038/nchembio881 · Cited by 339
Activated Ion Electron Capture Dissociation for Mass Spectral Sequencing of Larger (42 kDa) Proteins
Horn, D. M., Ge, Y., & McLafferty, F. W. (2000) · Analytical Chemistry · doi:10.1021/ac000494i · Cited by 333
Recombinant antibody therapeutics: the impact of glycosylation on mechanisms of action
Jefferis, R. (2009) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2009.04.007 · Cited by 330
Knibbs, R. N., Goldstein, I. J., Ratcliffe, R. M., & Shibuya, N. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52405-4 · Cited by 329
Analysis of immunoglobulin glycosylation by LC‐ESI‐MS of glycopeptides and oligosaccharides
Stadlmann, J., Pabst, M., Kolarich, D., Kunert, R., & Altmann, F. (2008) · PROTEOMICS · doi:10.1002/pmic.200700968 · Cited by 328
Scott, N. E., Parker, B. L., Connolly, A. M., Paulech, J., Edwards, A. V. G., Crossett, B., Falconer, L., Kolarich, D., Djordjevic, S. P., Højrup, P., et al. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m000031-mcp201 · Cited by 326
Toward a general mechanism of electron capture dissociation
Syrstad, E. A., & Turecček, F. (2005) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2004.11.001 · Cited by 325
Solid‐phase permethylation of glycans for mass spectrometric analysis
Kang, P., Mechref, Y., Klouckova, I., & Novotny, M. V. (2005) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.2210 · Cited by 322
Self-citationEnrichment of glycopeptides for glycan structure and attachment site identification
Nilsson, J., Rüetschi, U., Halim, A., Hesse, C., Carlsohn, E., Brinkmalm, G., & Larson, G. (2009) · Nature Methods · doi:10.1038/nmeth.1392 · Cited by 322
Mass spectrometry for structural characterization of therapeutic antibodies
Zhang, Z., Pan, H., & Chen, X. (2009) · Mass Spectrometry Reviews · doi:10.1002/mas.20190 · Cited by 316
Development of an Annotated Library of Neutral Human Milk Oligosaccharides
Wu, S., Tao, N., German, J. B., Grimm, R., & Lebrilla, C. B. (2010) · Journal of Proteome Research · doi:10.1021/pr100362f · Cited by 311
Wada, Y., Tajiri, M., & Yoshida, S. (2004) · Analytical Chemistry · doi:10.1021/ac049062o · Cited by 310
Handbook of Affinity Chromatography
(2005) · CRC Press eBooks · doi:10.1201/9780824751982 · Cited by 310
Highly Specific Enrichment of Glycopeptides Using Boronic Acid-Functionalized Mesoporous Silica
Xu, Y., Wu, Z., Zhang, L., Lu, H., Yang, P., Webley, P. A., & Zhao, D. (2009) · Analytical Chemistry · doi:10.1021/ac801912t · Cited by 308
Evaluation of the serum N ‐linked glycome for the diagnosis of cancer and chronic inflammation
Arnold, J. N., Saldova, R., Hamid, U. M. A., & Rudd, P. M. (2008) · PROTEOMICS · doi:10.1002/pmic.200800163 · Cited by 307
Carbohydrate recognition by boronolectins, small molecules, and lectins
Jin, S., Cheng, Y., Reid, S., Li, M., & Wang, B. (2010) · Medicinal Research Reviews · doi:10.1002/med.20155 · Cited by 305
Huhn, C., Selman, M. H. J., Ruhaak, L. R., Deelder, A. M., & Wuhrer, M. (2009) · PROTEOMICS · doi:10.1002/pmic.200800715 · Cited by 301
Mysling, S., Palmisano, G., Højrup, P., & Thaysen-Andersen, M. (2010) · Analytical Chemistry · doi:10.1021/ac100530w · Cited by 298
Hofsteenge, J., Mueller, D. R., de Beer, T., Loeffler, A., Richter, W. J., & Vliegenthart, J. F. G. (1994) · Biochemistry · doi:10.1021/bi00250a003 · Cited by 298
Okuyama, N., Ide, Y., Nakano, M., Nakagawa, T., Yamanaka, K., Moriwaki, K., Murata, K., Ohigashi, H., Yokoyama, S., Eguchi, H., et al. (2006) · International Journal of Cancer · doi:10.1002/ijc.21728 · Cited by 293
Tarentino, A. L., & Plummer, T. H. (1994) · Methods in Enzymology · doi:10.1016/0076-6879(94)30006-2 · Cited by 291
Qian, J., Liu, T., Yang, L., Daus, A., Crowley, R., & Zhou, Q. (2007) · Analytical Biochemistry · doi:10.1016/j.ab.2007.01.023 · Cited by 291
Solid-phase extraction of N-linked glycopeptides
Tian, Y., Zhou, Y., Elliott, S., Aebersold, R., & Zhang, H. (2007) · Nature Protocols · doi:10.1038/nprot.2007.42 · Cited by 286
Liquid chromatography of saccharides
Linden, J. C., & Lawhead, C. L. (1975) · Journal of Chromatography A · doi:10.1016/s0021-9673(01)81096-7 · Cited by 285
Enzymes in the Synthesis of Glycoconjugates
Schmaltz, R. M., Hanson, S. R., & Wong, C.-H. (2011) · Chemical Reviews · doi:10.1021/cr200113w · Cited by 283
Yang, Z., & Hancock, W. S. (2004) · Journal of Chromatography A · doi:10.1016/j.chroma.2004.08.150 · Cited by 282
Exploring the Sialiome Using Titanium Dioxide Chromatography and Mass Spectrometry
Larsen, M. R., Jensen, S. S., Jakobsen, L. A., & Heegaard, N. H. H. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700086-mcp200 · Cited by 282
(2002) · PubMed · Cited by 279
Mann, D. A., Kanai, M., Maly, D. J., & Kiessling, L. L. (1998) · Journal of the American Chemical Society · doi:10.1021/ja9818506 · Cited by 277
Hydrophilic interaction liquid chromatography (HILIC) in proteomics
Boersema, P. J., Mohammed, S., & Heck, A. J. R. (2008) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-008-1865-7 · Cited by 275
Lee, E. U., Roth, J., & Paulson, J. C. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)80078-3 · Cited by 273
Annotation and Structural Analysis of Sialylated Human Milk Oligosaccharides
Wu, S., Grimm, R., German, J. B., & Lebrilla, C. B. (2011) · Journal of Proteome Research · doi:10.1021/pr101006u · Cited by 268
Endo-β-N-acetylglucosaminidase Acting on Carbohydrate Moieties of Glycoproteins
Koide, N., & Muramatsu, T. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42406-x · Cited by 267
Harvey, D. J., Merry, A. H., Royle, L., P. Campbell, M., Dwek, R. A., & Rudd, P. M. (2009) · PROTEOMICS · doi:10.1002/pmic.200900096 · Cited by 267
Function and glycosylation of plant-derived antiviral monoclonal antibody
Ko, K., Tekoah, Y., Rudd, P. M., Harvey, D. J., Dwek, R. A., Spitsin, S., Hanlon, C. A., Rupprecht, C., Dietzschold, B., Golovkin, M., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0832472100 · Cited by 266
Aoki, K., Perlman, M., Lim, J.-M., Cantu, R., Wells, L., & Tiemeyer, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m606711200 · Cited by 265
Van Damme, E. J. M., Allen, A. K., & Peumans, W. J. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)80129-1 · Cited by 264
Glycosylation profiling of immunoglobulin G (IgG) subclasses from human serum
Wuhrer, M., Stam, J. C., van de Geijn, F. E., Koeleman, C. A. M., Verrips, C. T., Dolhain, R. J. E. M., Hokke, C. H., & Deelder, A. M. (2007) · PROTEOMICS · doi:10.1002/pmic.200700289 · Cited by 263
Elimination of Oxidative Degradation during the per-O-Methylation of Carbohydrates
Ciucanu, I., & Costello, C. E. (2003) · Journal of the American Chemical Society · doi:10.1021/ja035660t · Cited by 263
The role of analytical sciences in medical systems biology
Greef, J. V. D., Stroobant, P., & Heijden, R. V. D. (2004) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2004.08.013 · Cited by 262
Harvey, D. J. (2011) · Journal of Chromatography B · doi:10.1016/j.jchromb.2010.11.010 · Cited by 260
Cataldi, T. R. I., Campa, C., & De Benedetto, G. E. (2000) · Fresenius' Journal of Analytical Chemistry · doi:10.1007/s002160000588 · Cited by 257
Anumula, K. R. (2006) · Analytical Biochemistry · doi:10.1016/j.ab.2005.09.037 · Cited by 254
Fractionation of L-fucose-containing oligosaccharides on immobilized Aleuria aurantia lectin.
Yamashita, K., Kochibe, N., Ohkura, T., Ueda, I., & Kobata, A. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89125-6 · Cited by 252
Harvey, D. J. (2005) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2005.01.004 · Cited by 252
Quantitative Analysis of the Intra- and Inter-Individual Variability of the Normal Urinary Proteome
Nagaraj, N., & Mann, M. (2011) · Journal of Proteome Research · doi:10.1021/pr100835s · Cited by 252
Powell, A. K., & Harvey, D. J. (1996) · Rapid Communications in Mass Spectrometry · doi:10.1002/(sici)1097-0231(19960715)10:9<1027::aid-rcm634>3.0.co;2-y · Cited by 252
Altered glycan structures: the molecular basis of congenital disorders of glycosylation
Freeze, H. H., & Aebi, M. (2005) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2005.08.010 · Cited by 250
Anumula, K. R. (1994) · Analytical Biochemistry · doi:10.1006/abio.1994.1338 · Cited by 247
Halim, A., Brinkmalm, G., Rüetschi, U., Westman-Brinkmalm, A., Portelius, E., Zetterberg, H., Blennow, K., Larson, G., & Nilsson, J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102664108 · Cited by 246
Lauc, G., Essafi, A., Huffman, J. E., Hayward, C., Knežević, A., Kattla, J. J., Polašek, O., Gornik, O., Vitart, V., Abrahams, J. L., et al. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001256 · Cited by 244
Geisler, C., & Jarvis, D. L. (2011) · Glycobiology · doi:10.1093/glycob/cwr080 · Cited by 243
Determination of N-Glycosylation Sites and Site Heterogeneity in Glycoproteins
An, H. J., Peavy, T. R., Hedrick, J. L., & Lebrilla, C. B. (2003) · Analytical Chemistry · doi:10.1021/ac034414x · Cited by 242
Structural glycomics using hydrophilic interaction chromatography (HILIC) with mass spectrometry
Wuhrer, M., de Boer, A. R., & Deelder, A. M. (2009) · Mass Spectrometry Reviews · doi:10.1002/mas.20195 · Cited by 242
Cummings, R. D., & Kornfeld, S. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)82134-6 · Cited by 241
Palmisano, G., Lendal, S. E., Engholm-Keller, K., Leth-Larsen, R., Parker, B. L., & Larsen, M. R. (2010) · Nature Protocols · doi:10.1038/nprot.2010.167 · Cited by 241
Multiplexed analysis of glycan variation on native proteins captured by antibody microarrays
Chen, S., LaRoche, T., Hamelinck, D., Bergsma, D., Brenner, D., Simeone, D., Brand, R. E., & Haab, B. B. (2007) · Nature Methods · doi:10.1038/nmeth1035 · Cited by 239
A family of concanavalin A-binding peptides from a hexapeptide epitope library.
Scott, J. K., Loganathan, D., Easley, R. B., Gong, X., & Goldstein, I. J. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.12.5398 · Cited by 238
Electron transfer dissociation of peptide anions
Coon, J. J., Shabanowitz, J., Hunt, D. F., & Syka, J. E. P. (2005) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2005.01.015 · Cited by 238
Chalkley, R. J., Thalhammer, A., Schoepfer, R., & Burlingame, A. L. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900288106 · Cited by 237
Novel Fluorescent Glycan Microarray Strategy Reveals Ligands for Galectins
Song, X., Xia, B., Stowell, S. R., Lasanajak, Y., Smith, D. F., & Cummings, R. D. (2009) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.11.004 · Cited by 235
Variability, Heritability and Environmental Determinants of Human Plasma N-Glycome
Gornik, O., Rudan, I., Campbell, H., Hayward, C., Bones, J., Rudd, P. M., Lauc, G., & Wright, A. F. (2008) · Cited by 235
Effects of aging, body mass index, plasma lipid profiles, and smoking on human plasma N-glycans
Knežević, A., Gornik, O., Polašek, O., Pučić, M., Redžić, I., Novokmet, M., Rudd, P. M., Wright, A. F., Campbell, H., Rudan, I., et al. (2010) · Glycobiology · doi:10.1093/glycob/cwq051 · Cited by 234
Sublancin is not a lantibiotic but an S-linked glycopeptide
Oman, T. J., Boettcher, J. M., Wang, H., Okalibe, X. N., & van der Donk, W. A. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.509 · Cited by 225
Harvey, D. J. (2005) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2005.01.006 · Cited by 225
Yamashita, K., Totani, K., Ohkura, T., Takasaki, S., Goldstein, I. J., & Kobata, A. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75678-6 · Cited by 222
Structure of the lipophosphoglycan from Leishmania major.
McConville, M. J., Thomas-Oates, J. E., Ferguson, M. A., & Homans, S. W. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)45416-0 · Cited by 220
Specificity of purified hemagglutinin (lectin) from Lotus tetragonolobus
Pereira, M. E. A., & Kabat, E. A. (1974) · Biochemistry · doi:10.1021/bi00712a029 · Cited by 220
Drake, R. R., Schwegler, E. E., Malik, G., Diaz, J., Block, T., Mehta, A., & Semmes, O. J. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600176-mcp200 · Cited by 216
Abd Hamid, U. M., Royle, L., Saldova, R., Radcliffe, C. M., Harvey, D. J., Storr, S. J., Pardo, M., Antrobus, R., Chapman, C. J., Zitzmann, N., et al. (2008) · Glycobiology · doi:10.1093/glycob/cwn095 · Cited by 215
Zhao, J., Simeone, D. M., Heidt, D., Anderson, M. A., & Lubman, D. M. (2006) · Journal of Proteome Research · doi:10.1021/pr060034r · Cited by 214
Ramachandran, P., Boontheung, P., Xie, Y., Sondej, M., Wong, D. T., & Loo, J. A. (2006) · Journal of Proteome Research · doi:10.1021/pr050492k · Cited by 214
Bacterial Glycans: Key Mediators of Diverse Host Immune Responses
Comstock, L. E., & Kasper, D. L. (2006) · Cell · doi:10.1016/j.cell.2006.08.021 · Cited by 214
Cummings, R. D., Trowbridge, I. S., & Kornfeld, S. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33465-3 · Cited by 213
High‐throughput solid‐phase permethylation of glycans prior to mass spectrometry
Kang, P., Mechref, Y., & Novotny, M. V. (2008) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.3395 · Cited by 213
Self-citationHuang, Y., Mechref, Y., & Novotny, M. V. (2001) · Analytical Chemistry · doi:10.1021/ac015534c · Cited by 211
Self-citationMank, M., Stahl, B., & Boehm, G. (2004) · Analytical Chemistry · doi:10.1021/ac030354j · Cited by 210
Nutrigenomics: exploiting systems biology in the nutrition and health arena
van Ommen, B., & Stierum, R. (2002) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(02)00349-x · Cited by 209
Harvey, D. J. (2005) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2005.01.005 · Cited by 207
Tran, J. C., & Doucette, A. A. (2008) · Analytical Chemistry · doi:10.1021/ac702197w · Cited by 206
Regulation of Glycan Structures in Animal Tissues
Nairn, A. V., York, W. S., Harris, K., Hall, E. M., Pierce, J. M., & Moremen, K. W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801964200 · Cited by 206
Pabst, M., Bondili, J. S., Stadlmann, J., Mach, L., & Altmann, F. (2007) · Analytical Chemistry · doi:10.1021/ac070363i · Cited by 205
Schulz, B. L., Packer, N. H., & Karlsson, N. G. (2002) · Analytical Chemistry · doi:10.1021/ac025890a · Cited by 202
Not just for Eukarya anymore: protein glycosylation in Bacteria and Archaea
Abu-Qarn, M., Eichler, J., & Sharon, N. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.06.010 · Cited by 199
Harvey, D. J. (2000) · Journal of the American Society for Mass Spectrometry · doi:10.1016/s1044-0305(00)00156-2 · Cited by 194
Nwosu, C. C., Aldredge, D. L., Lee, H., Lerno, L. A., Zivkovic, A. M., German, J. B., & Lebrilla, C. B. (2012) · Journal of Proteome Research · doi:10.1021/pr300008u · Cited by 193
Lawrence, R., Olson, S. K., Steele, R. E., Wang, L., Warrior, R., Cummings, R. D., & Esko, J. D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804288200 · Cited by 193
Ahn, J., Bones, J., Yu, Y. Q., Rudd, P. M., & Gilar, M. (2010) · Journal of Chromatography B · doi:10.1016/j.jchromb.2009.12.013 · Cited by 193
Hart, G. W. (1992) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(92)90134-x · Cited by 193
Recent advances in hydrophilic interaction liquid chromatography (HILIC) for structural glycomics
Zauner, G., Deelder, A. M., & Wuhrer, M. (2011) · ELECTROPHORESIS · doi:10.1002/elps.201100247 · Cited by 192
Lectin Arrays for Profiling Cell Surface Carbohydrate Expression
Zheng, T., Peelen, D., & Smith, L. M. (2005) · Journal of the American Chemical Society · doi:10.1021/ja0505550 · Cited by 190
Sweet new world: glycoproteins in bacterial pathogens
Schmidt, M. A., Riley, L. W., & Benz, I. (2003) · Trends in Microbiology · doi:10.1016/j.tim.2003.10.004 · Cited by 190
Hogan, J. M., Pitteri, S. J., Chrisman, P. A., & McLuckey, S. A. (2005) · Journal of Proteome Research · doi:10.1021/pr049770q · Cited by 190
Royle, L., Mattu, T. S., Hart, E., Langridge, J. I., Merry, A. H., Murphy, N., Harvey, D. J., Dwek, R. A., & Rudd, P. M. (2002) · Analytical Biochemistry · doi:10.1006/abio.2002.5619 · Cited by 188
Determination of site-specific glycan heterogeneity on glycoproteins
Kolarich, D., Jensen, P. H., Altmann, F., & Packer, N. H. (2012) · Nature Protocols · doi:10.1038/nprot.2012.062 · Cited by 188
Crystal Structure of Fungal Lectin
Wimmerova, M., Mitchell, E., Sanchez, J.-F., Gautier, C., & Imberty, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302642200 · Cited by 183
2‐Picoline‐borane: A non‐toxic reducing agent for oligosaccharide labeling by reductive amination
Ruhaak, L. R., Steenvoorden, E., Koeleman, C. A. M., Deelder, A. M., & Wuhrer, M. (2010) · PROTEOMICS · doi:10.1002/pmic.200900804 · Cited by 181
Clowers, B. H., Dwivedi, P., Steiner, W. E., Hill, H. H., & Bendiak, B. (2005) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2005.01.010 · Cited by 177
Three-Dimensional Elution Mapping of Pyridylaminated N-Linked Neutral and Sialyl Oligosaccharides
Takahashi, N., Nakagawa, H., Fujikawa, K., Kawamura, Y., & Tomiya, N. (1995) · Analytical Biochemistry · doi:10.1006/abio.1995.1201 · Cited by 175
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Metadata
- Authors
- Alley, W. R., Mann, B. F., & Novotny, M. V.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2013-03-27
- Volume
- 113
- Issue
- 4
- Pages
- 2668-2732
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W1973083584
- Cited by
- 310
- References
- 477
- FWCI
- 2.65
- Type
- journal article
- Language
- en
- Open access
- green
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