The DOI matches its Crossref record; 95 of the 95 references it cites were found in a registry or an index.
Tripping up Trp: Modification of protein tryptophan residues by reactive oxygen species, modes of detection, and biological consequences
Open accessAbstract
Proteins comprise a majority of the dry weight of a cell, rendering them a major target for oxidative modification. Oxidation of proteins can result in significant alterations in protein molecular mass such as breakage of the polypeptide backbone and/or polymerization of monomers into dimers, multimers, and sometimes insoluble aggregates. Protein oxidation can also result in structural changes to amino acid residue side chains, conversions that have only a modest effect on protein size but can have widespread consequences for protein function. There are a wide range of rate constants for amino acid reactivity, with cysteine, methionine, tyrosine, phenylalanine, and tryptophan having the highest rate constants with commonly encountered biological oxidants. Free tryptophan and tryptophan protein residues react at a diffusion-limited rate with hydroxyl radical and also have high rate constants for reactions with singlet oxygen and ozone. Although oxidation of proteins in general and tryptophan residues specifically can have effects detrimental to the health of cells and organisms, some modifications are neutral, whereas others contribute to the function of the protein in question or may act as a signal that damaged proteins need to be replaced. This review provides a brief overview of the chemical mechanisms by which tryptophan residues become oxidized, presents both the strengths and the weaknesses of some of the techniques used to detect these oxidative interactions, and discusses selected examples of the biological consequences of tryptophan oxidation in proteins from animals, plants, and microbes.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Trp• reacts very rapidly with O2•− with second order rate constants, k, in the range 0.7–2.2 × 109 M−1 s−1, the main initial products being hydroperoxides, in almost quantitative yields [145,146,147,148,149,150,151], Figure 56.”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [145]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Epstein, F. H., Steinberg, D. I., Parthasarathy, S., Carew, T. E., Khoo, J. C., & Witztum, J. L. (1989) · New England Journal of Medicine · doi:10.1056/nejm198904063201407 · Cited by 6,425
Free radical-mediated oxidation of free amino acids and amino acid residues in proteins
Stadtman, E. R., & Levine, R. L. (2003) · Amino Acids · doi:10.1007/s00726-003-0011-2 · Cited by 1,968
Steinbrecher, U. P., Parthasarathy, S., Leake, D. S., Witztum, J. L., & Steinberg, D. I. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.12.3883 · Cited by 1,626
Ion Suppression in Mass Spectrometry
Annesley, T. M. (2003) · Clinical Chemistry · doi:10.1373/49.7.1041 · Cited by 1,598
The oxidative environment and protein damage
Davies, M. J. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.08.007 · Cited by 1,392
Daugherty, A., Dunn, J. L., Rateri, D. L., & Heinecke, J. W. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117342 · Cited by 1,269
Proteomics by Mass Spectrometry: Approaches, Advances, and Applications
Yates, J. R., Ruse, C. I., & Nakorchevsky, A. (2009) · Annual Review of Biomedical Engineering · doi:10.1146/annurev-bioeng-061008-124934 · Cited by 1,078
Singlet oxygen-mediated damage to proteins and its consequences
Davies, M. J. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00817-9 · Cited by 996
Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome
Mann, M., Ong, S. E., Grønborg, M., Steen, H., Jensen, O. N., & Pandey, A. (2002) · Trends in biotechnology · doi:10.1016/s0167-7799(02)01944-3 · Cited by 916
Pattison, D. I., Rahmanto, A. S., & Davies, M. J. (2011) · Photochemical & Photobiological Sciences · doi:10.1039/c1pp05164d · Cited by 593
Research works printed but not linked: 1
- Steinberg, 1989, Modifications of low-density lipoprotein that increase its atherogenicity, N. Engl. J. Med., 320, 915
Cited by
Sorted by citations
Protein oxidation and peroxidation
Davies, M. J. (2016) · Biochemical Journal · doi:10.1042/bj20151227 · Cited by 952
Detection, identification, and quantification of oxidative protein modifications
Hawkins, C. L., & Davies, M. J. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.006217 · Cited by 449
Chloroplast ROS and stress signaling
Li, M., & Kim, C. (2021) · Plant Communications · doi:10.1016/j.xplc.2021.100264 · Cited by 368
Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity
Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031841 · Cited by 342
Tryptophan in health and disease
Comai, S., Bertazzo, A., Brughera, M., & Crotti, S. (2020) · Advances in clinical chemistry · doi:10.1016/bs.acc.2019.08.005 · Cited by 306
Dietary protein oxidation: A silent threat to human health?
Estévez, M., & Luna, C. (2016) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2016.1165182 · Cited by 288
Reactivity and degradation products of tryptophan in solution and proteins
Bellmaine, S. F., Schnellbaecher, A., & Zimmer, A. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.09.002 · Cited by 194
Cortés‐Ríos, J., Zárate, A. M., Figueroa, J. D., Medina, J., Fuentes-Lemus, E., Rodriguez-Fernández, M., Aliaga, M. E., & López‐Alarcón, C. (2020) · Analytical Biochemistry · doi:10.1016/j.ab.2020.113904 · Cited by 181
The Role of Tryptophan Metabolites in Neuropsychiatric Disorders
Davidson, M., Rashidi, N., Nurgali, K., & Apostolopoulos, V. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179968 · Cited by 182
Nazir, S., Jankowski, V., Bender, G., Zewinger, S., Rye, K.-A., & van der Vorst, E. P. C. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.10.006 · Cited by 140
Organoiridium Photosensitizers Induce Specific Oxidative Attack on Proteins within Cancer Cells
Zhang, P., Chiu, C. K. C., Huang, H., Lam, Y. P. Y., Habtemariam, A., Malcomson, T., Paterson, M. J., Clarkson, G. J., O’Connor, P. B., Chao, H., et al. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201709082 · Cited by 136
Zou, Y., Xu, P., Wu, H., Zhang, M., Sun, Z., Sun, C., Wang, D., Cao, J., & Xu, W. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.02.039 · Cited by 120
Recent advances on characterization of protein oxidation in aquatic products: A comprehensive review
Zhang, L., Li, Q., Bao, Y., Tan, Y., Lametsch, R., Hong, H., & Luo, Y. (2022) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2022.2117788 · Cited by 111
Grassi, L., & Cabrele, C. (2019) · Amino Acids · doi:10.1007/s00726-019-02787-2 · Cited by 100
Panda, S. K., Gupta, D., Patel, M., van der Vyver, C., & Koyama, H. (2024) · Plants · doi:10.3390/plants13152071 · Cited by 100
Going retro: Oxidative stress biomarkers in modern redox biology
Margaritelis, N. V., Cobley, J. N., Paschalis, V., Veskoukis, A. S., Theodorou, A. A., Kyparos, A., & Nikolaidis, M. G. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.02.005 · Cited by 84
Oxidative cyclization reagents reveal tryptophan cation–π interactions
Xie, X., Moon, P. J., Crossley, S. W. M., Bischoff, A. J., He, D., Li, G., Dao, N., Gonzalez-Valero, A., Reeves, A. G., McKenna, J. M., et al. (2024) · Nature · doi:10.1038/s41586-024-07140-6 · Cited by 72
Agazzi, M. L., Ballatore, M. B., Reynoso, E., Quiroga, E. D., & Durantini, E. N. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.10.001 · Cited by 70
Formation and detection of oxidant-generated tryptophan dimers in peptides and proteins
Carroll, L., Pattison, D. I., Davies, J. B., Anderson, R. F., Lopez-Alarcon, C., & Davies, M. J. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.09.020 · Cited by 67
Oxidative Modification of Proteins: From Damage to Catalysis, Signaling, and Beyond
Demasi, M., Augusto, O., Bechara, E. J. H., Bicev, R. N., Cerqueira, F. M., da Cunha, F. M., Denicola, A., Gomes, F., Miyamoto, S., Netto, L. E. S., et al. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8176 · Cited by 71
Oxidation of myofibrillar proteins induced by peroxyl radicals: Role of oxidizable amino acids
Dorta, E., Ávila, F., Fuentes-Lemus, E., Fuentealba, D., & López‐Alarcón, C. (2019) · Food Research International · doi:10.1016/j.foodres.2019.108580 · Cited by 56
Orthogonal Translation for Site-Specific Installation of Post-translational Modifications
Gan, Q., & Fan, C. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00850 · Cited by 55
Agazzi, M. L., Durantini, J. E., Gsponer, N. S., Durantini, A. M., Bertolotti, S. G., & Durantini, E. N. (2019) · ChemPhysChem · doi:10.1002/cphc.201900181 · Cited by 57
Oxidation of polysorbates – An underestimated degradation pathway?
Weber, J., Buske, J., Mäder, K., Garidel, P., & Diederichs, T. (2023) · International Journal of Pharmaceutics X · doi:10.1016/j.ijpx.2023.100202 · Cited by 59
Redox post-translational modifications and their interplay in plant abiotic stress tolerance
Martí-Guillén, J. M., Pardo‐Hernández, M., Martínez-Lorente, S. E., Almagro, L., & Rivero, R. M. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.1027730 · Cited by 52
Chen, Z., Leinisch, F., Greco, I., Zhang, W., Shu, N., Chuang, C. Y., Lund, M. N., & Davies, M. J. (2019) · Free Radical Research · doi:10.1080/10715762.2018.1554250 · Cited by 51
Carroll, L., Pattison, D. I., Davies, J. B., Anderson, R. F., Lopez-Alarcon, C., & Davies, M. J. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.02.033 · Cited by 48
Zhang, L., Li, Q., Hong, H., & Luo, Y. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.130510 · Cited by 45
Fizíková, I., Dragašek, J., & Račay, P. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24097991 · Cited by 45
Stanfill, B., Nakayasu, E. S., Bramer, L., Thompson, A. M., Ansong, C. K., Clauss, T. R., Gritsenko, M. A., Monroe, M. E., Moore, R., Orton, D., et al. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra118.000648 · Cited by 42
Li, X., Day, N. J., Feng, S., Gaffrey, M. J., Lin, T., Paurus, V., Monroe, M. E., Moore, R. J., Yang, B., Xian, M., et al. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102111 · Cited by 43
Stability of Protein Pharmaceuticals: Recent Advances
Manning, M. C., Holcomb, R. E., Payne, R. W., Stillahn, J. M., Connolly, B. D., Katayama, D. S., Liu, H., Matsuura, J. E., Murphy, B. M., Henry, C. S., et al. (2024) · Pharmaceutical Research · doi:10.1007/s11095-024-03726-x · Cited by 45
Plácido, A., Bueno, J., Barbosa, É. A., Moreira, D. C., Dias, J. D. N., Cabral, W. F., Albuquerque, P., Bessa, L. J., Freitas, J., Kückelhaus, S. A. S., et al. (2020) · Biomolecules · doi:10.3390/biom10040512 · Cited by 44
Photoactive antimicrobial coating based on a PEDOT-fullerene C 60 polymeric dyad
Reynoso, E., Durantini, A. M., Solis, C. A., Macor, L., Otero, L., Gervaldo, M., Durantini, E. N., & Heredia, D. A. (2021) · RSC Advances · doi:10.1039/d1ra03417k · Cited by 40
Access to 3‐Oxindoles from Allylic Alcohols and Indoles
Lauwick, H., Sun, Y., Akdas, H., Dérien, S., & Achard, M. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201800348 · Cited by 38
Fuentes-Lemus, E., Silva, E., Barrías, P., Aspée, A., Escobar, E. S., Lorentzen, L. G., Carroll, L., Leinisch, F., Davies, M. J., & López‐Alarcón, C. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.06.005 · Cited by 38
Muñoz‐Rugeles, L., Galano, A., & Alvarez-Idaboy, J. R. (2017) · Physical Chemistry Chemical Physics · doi:10.1039/c7cp01557g · Cited by 36
Ballatore, M. B., Spesia, M. B., Milanesio, M. E., & Durantini, E. N. (2018) · RSC Advances · doi:10.1039/c8ra04562c · Cited by 36
Barnett, G. V., Balakrishnan, G., Chennamsetty, N., Hoffman, L., Bongers, J., Tao, L., Huang, Y., Slaney, T., Das, T. K., Leone, A., et al. (2019) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2018.12.027 · Cited by 33
Irreversible oxidative post-translational modifications in heart disease
Tomin, T., Schittmayer, M., Honeder, S. E., Heininger, C., & Birner‐Gruenberger, R. (2019) · Expert Review of Proteomics · doi:10.1080/14789450.2019.1645602 · Cited by 35
Baigorria, E., Milanesio, M. E., & Durantini, E. N. (2020) · European Polymer Journal · doi:10.1016/j.eurpolymj.2020.109816 · Cited by 34
Photo-Oxidation of Therapeutic Protein Formulations: From Radical Formation to Analytical Techniques
Hipper, E., Blech, M., Hinderberger, D., Garidel, P., & Kaiser, W. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics14010072 · Cited by 35
Leinisch, F., Mariotti, M., Hägglund, P., & Davies, M. J. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.07.008 · Cited by 32
Agazzi, M. L., Durantini, J. E., Quiroga, E. D., Alvarez, M. G., & Durantini, E. N. (2021) · Photochemical & Photobiological Sciences · doi:10.1007/s43630-021-00021-1 · Cited by 34
Heller, M. I., Wuttig, K., & Croot, P. L. (2016) · Frontiers in Marine Science · doi:10.3389/fmars.2016.00132 · Cited by 31
Selective Tryptophan Oxidation of Monoclonal Antibodies: Oxidative Stress and Modeling Prediction
Pavon, J. A., Xiao, L., Li, X., Zhao, J., Aldredge, D. L., Dank, E., Fridman, A., & Liu, Y. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.8b04768 · Cited by 29
Heme Induces Endoplasmic Reticulum Stress (HIER Stress) in Human Aortic Smooth Muscle Cells
Gáll, T., Pethő, D., Nagy, A., Hendrik, Z., Méhes, G., Potor, L., Gram, M., Åkerström, B., Smith, A., Nagy, P. G., et al. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01595 · Cited by 29
Post deposition aging of bloodstains probed by steady-state fluorescence spectroscopy
Weber, A. R., Wójtowicz, A., & Lednev, I. K. (2021) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2021.112251 · Cited by 28
Tryptophan: A Precursor of Signaling Molecules in Higher Plants
Corpas, F. J., Gupta, D. K., & Palma, J. M. (2021) · Plant in challenging environments · doi:10.1007/978-3-030-77477-6_11 · Cited by 28
Reactive X (where X = O, N, S, C, Cl, Br, and I) species nanomedicine
Wang, K., Mao, W., Song, X., Chen, M., Feng, W., Peng, B., & Chen, Y. (2023) · Chemical Society Reviews · doi:10.1039/d2cs00435f · Cited by 28
Jacobitz, A. W., Liu, Q., Suravajjala, S., & Agrawal, N. J. (2020) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2020.10.039 · Cited by 27
Porphyrin–Schiff Base Conjugates Bearing Basic Amino Groups as Antimicrobial Phototherapeutic Agents
Pérez, M. E., Durantini, J. E., Reynoso, E., Alvarez, M. G., Milanesio, M. E., & Durantini, E. N. (2021) · Molecules · doi:10.3390/molecules26195877 · Cited by 27
Hinterholzer, A., Stanojlović, V., Regl, C., Huber, C. G., Cabrele, C., & Schubert, M. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c00965 · Cited by 26
Probing menstrual bloodstain aging with fluorescence spectroscopy
Wójtowicz, A., Weber, A. R., Wietecha‐Posłuszny, R., & Lednev, I. K. (2020) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2020.119172 · Cited by 26
Kato, Y., Kuroda, H., Ozawa, S.-I., Saito, K., Dogra, V., Scholz, M., Zhang, G., de Vitry, C., Ishikita, H., Kim, C., et al. (2023) · eLife · doi:10.7554/elife.88822.3 · Cited by 26
Wecksler, A. T., Yin, J. B., Tao, P. L., Kabakoff, B., Sreedhara, A., & Deperalta, G. (2018) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.7b01128 · Cited by 25
Figueroa, J. D., Zárate, A. M., Fuentes-Lemus, E., Davies, M. J., & López‐Alarcón, C. (2020) · RSC Advances · doi:10.1039/d0ra04051g · Cited by 24
He, E., Li, X., Xu, X., Fu, Z., Romero‐Freire, A., & Qiu, H. (2024) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2024.136357 · Cited by 22
Luminescent Lanthanide Infinite Coordination Polymers for Ratiometric Sensing Applications
Song, Z., Hao, Y., Long, Y., Zhang, P., Zeng, R., Shu, C., & Chen, W. (2025) · Molecules · doi:10.3390/molecules30020396 · Cited by 22
Yan, H., Zou, H., Li, S., Sun, S. B., Xu, Q., & Yu, C. (2022) · LWT · doi:10.1016/j.lwt.2022.114086 · Cited by 22
Li, M., Karboune, S., Light, K., & Kermasha, S. (2021) · Innovative Food Science & Emerging Technologies · doi:10.1016/j.ifset.2021.102723 · Cited by 21
Analytical and pharmacological consequences of the in vivo deamidation of trastuzumab and pertuzumab
Bults, P., van der Voort, A., Meijer, C., Sonke, G. S., Bischoff, R., & van de Merbel, N. C. (2022) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-021-03756-z · Cited by 21
Effect of irradiation spectral range on porphyrin—Protein complexes
Lebedevа, N. S., Yurina, E. S., Gubarev, Y. A., Lyubimtsev, A. V., & Syrbu, S. А. (2017) · Journal of Photochemistry and Photobiology A Chemistry · doi:10.1016/j.jphotochem.2017.11.037 · Cited by 21
Photo-induced toxicity of pesticides in aqueous environment: A review
Fan, L., Zhang, X., Zang, S., & Wang, H. (2023) · Journal of Cleaner Production · doi:10.1016/j.jclepro.2023.136726 · Cited by 20
Li, H., Xiao, Y., Liu, H., & Li, X. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c12511 · Cited by 20
Heinonen, M., Gürbüz, G., & Ertbjerg, P. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-817380-0.00003-8 · Cited by 21
Larrea, G. A., Gsponer, N. S., Durantini, J. E., Heredia, D. A., & Durantini, E. N. (2023) · ACS Food Science & Technology · doi:10.1021/acsfoodscitech.3c00474 · Cited by 20
Graciotti, M., Marino, F., Pak, H., Baumgaertner, P., Thierry, A., Chiffelle, J., Perez, M. A. S., Zoete, V., Harari, A., Bassani‐Sternberg, M., et al. (2020) · Vaccines · doi:10.3390/vaccines8020271 · Cited by 18
Organoiridium Photosensitizers Induce Specific Oxidative Attack on Proteins within Cancer Cells
Zhang, P., Chiu, C. K. C., Huang, H., Lam, Y. P. Y., Habtemariam, A., Malcomson, T., Paterson, M. J., Clarkson, G. J., O’Connor, P. B., Chao, H., et al. (2017) · Angewandte Chemie · doi:10.1002/ange.201709082 · Cited by 17
Automated Solid-Phase Peptide Synthesis
Winkler, D. F. H. (2019) · Methods in molecular biology · doi:10.1007/978-1-0716-0227-0_5 · Cited by 19
Tuning the Polarity of Fullerene C60 Derivatives for Enhanced Photodynamic Inactivation†
Palacios, Y. B., Durantini, J. E., Heredia, D. A., Martínez, S. R., de la Torre, L. G., & Durantini, A. M. (2021) · Photochemistry and Photobiology · doi:10.1111/php.13465 · Cited by 16
Kato, Y., Kuroda, H., Ozawa, S.-I., Saito, K., Dogra, V., Scholz, M., Zhang, G., de Vitry, C., Ishikita, H., Kim, C., et al. (2023) · eLife · doi:10.7554/elife.88822 · Cited by 15
Li, X., Feng, Z., Pu, S., Yang, Y., Shi, X., & Zhao, X. (2018) · Plasma Chemistry and Plasma Processing · doi:10.1007/s11090-018-9910-6 · Cited by 15
Xu, S., Chuang, C. Y., Malle, E., Gamon, L. F., Hawkins, C. L., & Davies, M. J. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.06.222 · Cited by 15
Proteomics in relation to abiotic stress tolerance in plants
Gautam, A., Pandey, P., & Pandey, A. K. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-818204-8.00023-0 · Cited by 15
Figueroa, J. D., Barroso-Torres, N., Morales, M., Herrera, B., Aranda, M., Dorta, E., & López‐Alarcón, C. (2023) · Foods · doi:10.3390/foods12234360 · Cited by 14
Kovaĺ, T., Švecová, L., Østergaard, L., Skálová, T., Dušková, J., Hašek, J., Kolenko, P., Fejfarová, K., Stránský, J., Trundová, M., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-50105-3 · Cited by 14
Marchelak, A., Kołodziejczyk-Czepas, J., Wasielewska, P., Nowak, P., & Olszewska, M. A. (2021) · Antioxidants · doi:10.3390/antiox10040581 · Cited by 14
Boarini, M. B., Gsponer, N. S., Milanesio, M. E., & Durantini, E. N. (2023) · European Polymer Journal · doi:10.1016/j.eurpolymj.2023.112512 · Cited by 13
“Illuminated Glycoporphyrins”: A photodynamic approach for Candida albicans inactivation
Palacios, Y. B., Simonetti, S. O., Chavez, C. H., Álvarez, M. G., Cordero, P. V., Cuello, E. A., López, E. J. G., Larghi, E. L., Agazzi, M. L., Durantini, E. N., et al. (2025) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2025.113105 · Cited by 13
Fullerene C60-chitosan conjugate applied in the photoinactivation of Staphylococcus aureus
Gsponer, N. S., Baigorria, E., Durantini, E. N., & Milanesio, M. E. (2023) · European Polymer Journal · doi:10.1016/j.eurpolymj.2023.112678 · Cited by 12
Graham, R. J., Ketcham, S. A., Mohammad, A., Paregol, E., Yoon, S., Zou, G., Ju, T., Faustino, P. J., Ashraf, M., & Madhavarao, C. N. (2021) · Biochemical Engineering Journal · doi:10.1016/j.bej.2021.107928 · Cited by 11
Baigorria, E., Durantini, J. E., Palma, M. A. D., Gsponer, N. S., Milanesio, M. E., & Durantini, E. N. (2021) · Photochemical & Photobiological Sciences · doi:10.1007/s43630-021-00074-2 · Cited by 12
Escobar‐Álvarez, E., Leinisch, F., Araya, G., Monasterio, O., Lorentzen, L. G., Silva, E., Davies, M. J., & López‐Alarcón, C. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.07.014 · Cited by 12
Bikaki, M., & Kuhnert, N. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b01056 · Cited by 12
Oxidative Post-translational Protein Modifications upon Ischemia/Reperfusion Injury
Binek, A., Castans, C., Jorge, I., Bagwan, N., Rodrı́guez, J. M., Fernández‐Jiménez, R., Galán‐Arriola, C., Oliver, E., Gómez, M., Clemente‐Moragón, A., et al. (2024) · Antioxidants · doi:10.3390/antiox13010106 · Cited by 10
Structure and Function of Tryptophan–Tyrosine Dyads in Biomimetic β Hairpins
McCaslin, T. G., Pagba, C. V., Chi, S., Hwang, H. J., Gumbart, J. C., Perry, J. W., Olivieri, C., Porcelli, F., Veglia, G., Guo, Z., et al. (2019) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b12452 · Cited by 11
Đukić, T., Smiljanić, K., Mihailović, J. M., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Veličković, T. Ć. (2022) · Foods · doi:10.3390/foods11243993 · Cited by 11
Chemical engineering of protein cages and nanoparticles for pharmaceutical applications
Aljabali, A. A. A., Zoubi, M. S. A., Alzoubi, L., Al‐Batayneh, K., Obeid, M. A., & Tambuwala, M. M. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-820702-4.00017-9 · Cited by 11
Multifarious analytical capabilities of the UV/Vis protein fluorescence in blood plasma
Gayer, A. V., Yakimov, B. P., Sluchanko, N. N., & Shirshin, E. A. (2022) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2022.122028 · Cited by 10
Analysis of the Propionate Metabolism in Bacillus subtilis during 3-Indolacetic Production
Castillo-Alfonso, F., Quintana-Menéndez, A., Vigueras-Ramírez, G., Sales‐Cruz, M., Rosales-Colunga, L. M., & Olivares‐Hernández, R. (2022) · Microorganisms · doi:10.3390/microorganisms10122352 · Cited by 8
Raman Spectroscopy investigate structural change of rice bran protein induced by three oxidants
Zhou, L., Zhang, M., Cheng, J., Wang, Z., Guo, Z., & Li, B. (2022) · CyTA - Journal of Food · doi:10.1080/19476337.2022.2107705 · Cited by 8
The Different Colors of mAbs in Solution
Ambrogelly, A. (2021) · Antibodies · doi:10.3390/antib10020021 · Cited by 8
Porphyrin−BODIPY Dyad: Enhancing Photodynamic Inactivation via Antenna Effect
Pérez, M. E., Durantini, J. E., Martínez, S. R., Durantini, A. M., Milanesio, M. E., & Durantini, E. N. (2024) · ChemBioChem · doi:10.1002/cbic.202400138 · Cited by 7
Gowthami, N., Pursotham, N., Dey, G., Ghose, V., Sathe, G. J., Pruthi, N., Shukla, D. P., Gayathri, N., Santhoshkumar, R., Padmanabhan, B., et al. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15953 · Cited by 8
Effect of Boiling Treatment on Linoleic Acid-Induced Oxidation of Myofibrillar Protein in Grass Carp
Liu, M., Li, F., Tang, Y., Zhao, J., Lei, X., & Ming, J. (2024) · Foods · doi:10.3390/foods13244153 · Cited by 6
Weber, J., Pedri, L., Peters, L. P., Quoika, P. K., Dinu, D. F., Liedl, K. R., Tautermann, C. S., Diederichs, T., & Garidel, P. (2025) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.4c01015 · Cited by 7
BODIPY-Loaded ZIF-8 Nanomaterials for Enhanced Photodynamic Inactivation of Staphylococcus aureus
Pérez, M. E., Durantini, J. E., Milanesio, M. E., & Durantini, E. N. (2025) · ACS Applied Bio Materials · doi:10.1021/acsabm.5c00787 · Cited by 6
Development of a high throughput oxidation profiling strategy for monoclonal antibody products
Fischer, P. L., Merkel, O. M., Siedler, M., & Huelsmeyer, M. (2024) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2024.114301 · Cited by 6
Elliott, C. I., Simmons, D. B. D., & Stotesbury, T. E. (2024) · Talanta · doi:10.1016/j.talanta.2024.127234 · Cited by 6
Metadata
- Authors
- Ehrenshaft, M., Deterding, L. J., & Mason, R. P.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Ehrenshaft, Marilyn
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2015-12
- Volume
- 89
- Pages
- 220-228
- ISSN
- 0891-5849 (ISSN-L)
- PMC
- PMC4684788
- OpenAlex
- W2187856084
- Cited by
- 158
- References
- 95
- Citations by year
- 2026: 16 · 2025: 13 · 2024: 15 · 2023: 20 · 2022: 16 · 2021: 22 · 2020: 15 · 2019: 15 · 2018: 14 · 2017: 6 · 2016: 6
- FWCI
- 0.84
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Environmental Health Sciences
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- tryptophan oxidation, protein oxidative modification, reactive oxygen species, hydroxyl radicals, singlet oxygen, ozone, protein aggregation, protein misfolding, protein function
- MeSH terms
- Animals, Humans, Oxidation-Reduction, Proteins, Mass Spectrometry, Tryptophan, Reactive Oxygen Species
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
