The carbonate radical anion-induced covalent aggregation of human copper, zinc superoxide dismutase, and α-synuclein: intermediacy of tryptophan- and tyrosine-derived oxidation products

Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis

Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062 · see citing works

Oxidative Damage Linked to Neurodegeneration by Selective α-Synuclein Nitration in Synucleinopathy Lesions

Giasson, B. I., Duda, J. E., Murray, I. V. J., Chen, Q., Souza, J. M., Hurtig, H. I., Ischiropoulos, H., Trojanowski, J. Q., & Lee, V. M. ‐. (2000) · Science · doi:10.1126/science.290.5493.985 · Cited by 1,551 · see citing works

Amyotrophic Lateral Ssclerosis and Structural Defects in Cu,Zn Superoxide Dismutase

Deng, H., Hentati, A., Tainer, J. A., Iqbal, Z., Cayabyab, A., Hung, W.-Y., Getzoff, E. D., Hu, P., Herzfeldt, B., Roos, R. P., et al. (1993) · Science · doi:10.1126/science.8351519 · Cited by 1,479 · see citing works

An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria

Wong, P. C., Pardo, C. A., Borchelt, D., Lee, M. K., Copeland, N. G., Jenkins, N. A., Sisodia, S. S., Cleveland, D. W., & Price, D. L. (1995) · Neuron · doi:10.1016/0896-6273(95)90259-7 · Cited by 1,439 · see citing works

Oxidative Stress in Neurodegenerative Diseases

Simonian, N. A., & Coyle, J. T. (1996) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.36.040196.000503 · Cited by 1,377 · see citing works

ALS-Linked SOD1 Mutant G85R Mediates Damage to Astrocytes and Promotes Rapidly Progressive Disease with SOD1-Containing Inclusions

Bruijn, L. I., Becher, M. W., Lee, M. K., Anderson, K. L., Jenkins, N. A., Copeland, N. G., Sisodia, S. S., Rothstein, J. D., Borchelt, D. R., Price, D. L., et al. (1997) · Neuron · doi:10.1016/s0896-6273(00)80272-x · Cited by 1,341 · see citing works

Toxic Proteins in Neurodegenerative Disease

Taylor, J. P., Hardy, J., & Fischbeck, K. H. (2002) · Science · doi:10.1126/science.1067122 · Cited by 1,251 · see citing works

ALS, SOD and peroxynitrite

Beckman, J. S., Carson, M. A., Smith, C. D. L., & Koppenol, W. H. (1993) · Nature · doi:10.1038/364584a0 · Cited by 876 · see citing works

Interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide. Inactivation of the enzyme

Hodgson, E. K., & Fridovich, I. (1975) · Biochemistry · doi:10.1021/bi00695a010 · Cited by 785 · see citing works

Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis.

Ripps, M. E., Huntley, G. W., Hof, P. R., Morrison, J., & Gordon, J. W. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.3.689 · Cited by 725 · see citing works

Altered Reactivity of Superoxide Dismutase in Familial Amyotrophic Lateral Sclerosis

Wiedau‐Pazos, M., Goto, J. J., Rabizadeh, S., Gralla, E. B., Roe, J. A., Lee, M. K., Valentine, J. S., & Bredesen, D. E. (1996) · Science · doi:10.1126/science.271.5248.515 · Cited by 720 · see citing works

Benefit of vitamin E, riluzole, and gababapentin in a transgenic model of familial amyotrophic lateral sclerosis

Gurney, M. E., Cutting, F. B., Zhai, P., Doble, A., Taylor, C. P., Andrus, P. K., & Hall, E. D. (1996) · Annals of Neurology · doi:10.1002/ana.410390203 · Cited by 647 · see citing works

Superoxide Dismutase Activity, Oxidative Damage, and Mitochondrial Energy Metabolism in Familial and Sporadic Amyotrophic Lateral Sclerosis

Bowling, A. C., Schulz, J. B., Brown, R. H., & Beal, M. F. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb07478.x · Cited by 629 · see citing works

Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity.

Borchelt, D., Lee, M. K., Slunt, H. S., Guarnieri, M., Xu, Z. S., Wong, P. C., Brown, R. H., Price, D. L., Sisodia, S. S., & Cleveland, D. W. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.17.8292 · Cited by 622 · see citing works

Formation of high molecular weight complexes of mutant Cu,Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis

Johnston, J. A., Dalton, M. J., Gurney, M. E., & Kopito, R. R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.220417997 · Cited by 607 · see citing works

Dityrosine Cross-linking Promotes Formation of Stable α-Synuclein Polymers

Souza, J. M., Giasson, B. I., Chen, Q., Lee, V. M. ‐., & Ischiropoulos, H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000206200 · Cited by 561 · see citing works

A gain-of-function of an amyotrophic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutant: An enhancement of free radical formation due to a decrease in Km for hydrogen peroxide.

Yim, M. B., Kang, J. H., Yim, H., Kwak, H. S., Chock, P. B., & Stadtman, E. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.12.5709 · Cited by 459 · see citing works

Glutamate uptake inhibition by oxygen free radicals in rat cortical astrocytes

Volterra, A., Trotti, D., Tromba, C., FLORIDI, S., & Racagni, G. (1994) · Journal of Neuroscience · doi:10.1523/jneurosci.14-05-02924.1994 · Cited by 457 · see citing works

Amyotrophic Lateral Sclerosis

Julien, J. (2001) · Cell · doi:10.1016/s0092-8674(01)00244-6 · Cited by 435 · see citing works

Histological Evidence of Protein Aggregation in Mutant SOD1 Transgenic Mice and in Amyotrophic Lateral Sclerosis Neural Tissues

Watanabe, M., Dykes‐Hoberg, M., Culotta, V., Price, D. L., Wong, P. C., & Rothstein, J. D. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2001.0443 · Cited by 432 · see citing works

Linkage of a Gene Causing Familial Amyotrophic Lateral Sclerosis to Chromosome 21 and Evidence of Genetic-Locus Heterogeneity

Siddique, T., Figlewigz, D. A., Pericak‐Vance, M. A., Haines, J. L., Rouleau, G. A., Jeffers, A. J., Sapp, P. C., Hung, W. ‐., Bebout, J., McKenna-Yasek, D. M., et al. (1991) · New England Journal of Medicine · doi:10.1056/nejm199105163242001 · Cited by 380 · see citing works

Amyotrophic lateral sclerosis: Recent insights from genetics and transgenic mice

Brown, R. H. (1995) · Cell · doi:10.1016/0092-8674(95)90346-1 · Cited by 352 · see citing works

Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells.

Rabizadeh, S., Gralla, E. B., Borchelt, D., Gwinn, R. P., Valentine, J. S., Sisodia, S., Wong, P., Lee, M. K., Hahn, H., & Bredesen, D. E. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.7.3024 · Cited by 335 · see citing works

Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase.

Parge, H. E., Hallewell, R. A., & Tainer, J. A. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.13.6109 · Cited by 304 · see citing works

Intense Superoxide Dismutase-1 Immunoreactivity in Intracytoplasmic Hyaline Inclusions of Familial Amyotrophic Lateral Sclerosis with Posterior Column Involvement

Shibata, N., Hirano, A., Kobayashi, M., Siddique, T., Deng, H., Hung, W.-Y., Kato, T., & Asayama, K. (1996) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199604000-00011 · Cited by 294 · see citing works

Direct EPR Detection of the Carbonate Radical Anion Produced from Peroxynitrite and Carbon Dioxide

Bonini, M. G., Radi, R., Ferrer-Sueta, G., Ferreira, A. M. D. C., & Augusto, O. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.16.10802 · Cited by 293 · see citing works

Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant

Bruijn, L. I., Beal, M. F., Bêcher, M. W., Schulz, J. B., Wong, P. C., Price, D. L., & Cleveland, D. W. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.14.7606 · Cited by 290 · see citing works

Proteasomal inhibition by misfolded mutant superoxide dismutase 1 induces selective motor neuron death in familial amyotrophic lateral sclerosis

Urushitani, M., Kurisu, J., Tsukita, K., & Takahashi, R. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01211.x · Cited by 268 · see citing works

Increased 3‐nitrotyrosine and oxidative damage in mice with a human copper/zinc superoxide dismutase mutation

Ferrante, R. J., Shinobu, L. A., Schulz, J. B., Matthews, R. T., Thomas, C. E., Kowall, N. W., Gurney, M. E., & Beal, M. F. (1997) · Annals of Neurology · doi:10.1002/ana.410420309 · Cited by 251 · see citing works

Interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide. Chemiluminescence and peroxidation

Hodgson, E. K., & Fridovich, I. (1975) · Biochemistry · doi:10.1021/bi00695a011 · Cited by 250 · see citing works

Amyotrophic lateral sclerosis: A proposed mechanism

Okado‐Matsumoto, A., & Fridovich, I. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.132260399 · Cited by 247 · see citing works

Mutations in copper-zinc superoxide dismutase that cause amyotrophic lateral sclerosis alter the zinc binding site and the redox behavior of the protein.

Lyons, T. J., Liu, H., Goto, J. J., Nersissian, A. M., Roe, J. A., Graden, J. A., Café, C., Ellerby, L., Bredesen, D. E., Gralla, E. B., et al. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.22.12240 · Cited by 183 · see citing works

A frequent ala 4 to val superoxide dismutase-1 mutation is associated with a rapidly progressive familial amyotrophic lateral sclerosis

Rosen, D. R., Bowling, A. C., Patterson, D., Usdin, T. B., Sapp, P. C., Mezey, É., McKenna-Yasek, D. M., O'Regan, J., Rahmani, Z., Ferrante, R. J., et al. (1994) · Human Molecular Genetics · doi:10.1093/hmg/3.6.981 · Cited by 156 · see citing works

The mechanism of the activity-dependent luminescence of xanthine oxidase

Hodgson, E. K., & Fridovich, I. (1976) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(76)90067-9 · Cited by 122 · see citing works

Bicarbonate Enhances the Hydroxylation, Nitration, and Peroxidation Reactions Catalyzed by Copper, Zinc Superoxide Dismutase

Zhang, H., Joseph, J., Felix, C. C., & Kalyanaraman, B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.19.14038 · Cited by 118 · see citing works

Bicarbonate Enhances the Peroxidase Activity of Cu,Zn-Superoxide Dismutase

Goss, S. P. A., Singh, R. J., & Kalyanaraman, B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.40.28233 · Cited by 117 · see citing works

Increased mitochondrial antioxidative activity or decreased oxygen free radical propagation prevent mutant SOD1‐mediated motor neuron cell death and increase amyotrophic lateral sclerosis‐like transgenic mouse survival

Liu, R., Li, B., Flanagan, S. W., Oberley, L. W., Gozal, D., & Qiu, M. S. (2002) · Journal of Neurochemistry · doi:10.1046/j.0022-3042.2001.00720.x · Cited by 110 · see citing works

Bicarbonate-dependent Peroxidase Activity of Human Cu,Zn-Superoxide Dismutase Induces Covalent Aggregation of Protein

Zhang, H., Andrekopoulos, C., Joseph, J., Chandran, K., Karoui, H., Crow, J. P., & Kalyanaraman, B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302051200 · Cited by 108 · see citing works

Self-peroxidation of Metmyoglobin Results in Formation of an Oxygen-reactive Tryptophan-centered Radical

Gunther, M. R., Kelman, D. J., Corbett, J. T., & Mason, R. P. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.27.16075 · Cited by 108 · see citing works

Bicarbonate Enhances Peroxidase Activity of Cu,Zn-Superoxide Dismutase

Zhang, H., Joseph, J., Gurney, M. E., Becker, D. A., & Kalyanaraman, B. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108585200 · Cited by 103 · see citing works

Cu,Zn-Superoxide Dismutase-dependent Apoptosis Induced by Nitric Oxide in Neuronal Cells

Ciriolo, M. R., Martino, A., Lafavia, E., Rossi, L. C., Carrı̀, M. T., & Rotilio, G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.7.5065 · Cited by 103 · see citing works

Thiol Oxidase Activity of Copper,Zinc Superoxide Dismutase

Winterbourn, C. C., Peskin, A. V., & Parsons-Mair, H. N. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107256200 · Cited by 101 · see citing works

Oxidation versus aggregation — how do SOD1 mutants cause ALS?

Cleveland, D. W., & Liu, J. (2000) · Nature Medicine · doi:10.1038/82122 · Cited by 99 · see citing works

Mechanisms of selective motor neuron death in ALS: insights from transgenic mouse models of motor neuron disease

Bruijn, L. I., & Cleveland, D. W. (1996) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.1996.tb00907.x · Cited by 99 · see citing works

Upregulation of HSP27 in a Transgenic Model of ALS

Vleminckx, V., Damme, P. V., Goffin, K. E., Delye, H., Bosch, L. V. D., & Robberecht, W. (2002) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/61.11.968 · Cited by 96 · see citing works

Copper, Zinc Superoxide Dismutase and H2O2

Liochev, S. I., & Fridovich, I. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204726200 · Cited by 88 · see citing works

Increased reactive oxygen species in familial amyotrophic lateral sclerosis with mutations in SOD1

Ahmed, M., Hung, W.-Y., Zu, J. S., Hockberger, P. E., & Siddique, T. (2000) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(00)00317-8 · Cited by 86 · see citing works

Erratum: Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant (Proceedings of the Nat. Acad. of Sci. of the USA (July 8, 1997) 94:14 (7606-7611))

Bruijn, L. I., Beal, M. F., Bêcher, M. W., Schulz, J., Wong, P. C., Price, D. L., & Cleveland, D. W. (1998) · Proceedings of the National Academy of Sciences · Cited by 76 · see citing works

Involvement of α-synuclein in Parkinson's disease and other neurodegenerative disorders

Krüger, R., Müller, T., & Riess, O. H. (2000) · Journal of Neural Transmission · doi:10.1007/s007020050002 · Cited by 70 · see citing works

Mutant Cu,Zn superoxide dismutases and familial amyotrophic lateral sclerosis: evaluation of oxidative hypotheses

Liochev, S. I., & Fridovich, I. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00153-9 · Cited by 70 · see citing works

Modification of a single tryptophan residue in human Cu,Zn-superoxide dismutase by peroxynitrite in the presence of bicarbonate

Yamakura, F., Matsumoto, T., Fujimura, T., Taka, H., Murayama, K., Imai, T., & Uchida, K. (2001) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(01)00212-6 · Cited by 69 · see citing works

Do oxidatively modified proteins cause ALS?

Valentine, J. S. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01080-8 · Cited by 68 · see citing works

Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase

(1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.22.11106 · Cited by 66 · see citing works

Dynamic Properties of the G93A Mutant of Copper−Zinc Superoxide Dismutase As Detected by NMR Spectroscopy: Implications for the Pathology of Familial Amyotrophic Lateral Sclerosis

Shipp, E. L., Cantini, F., Bertini, I., et al. (2003) · Biochemistry · doi:10.1021/bi026704y · Cited by 60 · see citing works

Aggregation of α-synuclein induced by the Cu,Zn-superoxide dismutase and hydrogen peroxide system

Kim, K. S., Choi, S. Y., Kwon, H. Y., Won, M. H., Kang, T., & Kang, J. H. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00741-4 · Cited by 60 · see citing works

Formation of Constrained, Fluorescent Peptides via Tryptophan Dimerization and Oxidation

Stachel, S. J., Habeeb, R. L., & Vranken, D. L. V. (1996) · Journal of the American Chemical Society · doi:10.1021/ja9533297 · Cited by 60 · see citing works

Motor neurone disease and animal models

Price, D. L., Cleveland, D. W., & Koliatsos, V. E. (1994) · Neurobiology of Disease · doi:10.1006/nbdi.1994.0002 · Cited by 58 · see citing works

On the role of bicarbonate in peroxidations catalyzed by Cu,Zn superoxide dismutase

Liochev, S. I., & Fridovich, I. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00190-2 · Cited by 56 · see citing works

Bicarbonate enhances alpha-synuclein oligomerization and nitration: intermediacy of carbonate radical anion and nitrogen dioxide radical

Andrekopoulos, C., Zhang, H., Joseph, J., et al. (2004) · Biochemical Journal · doi:10.1042/bj20031466 · Cited by 45 · see citing works

Elucidation of a Novel Polypeptide Cross-Link Involving 3-Hydroxykynurenine

Aquilina, J. A., Carver, J. A., & Truscott, R. J. W. (1999) · Biochemistry · doi:10.1021/bi990458h · Cited by 43 · see citing works

Enhanced oligomerization of the alpha-synuclein mutant by the Cu,Zn-superoxide dismutase and hydrogen peroxide system.

Kang, J. H., & Kim, K. S. (2003) · PubMed · Cited by 40 · see citing works

Amyotrophic lateral sclerosis: human challenge for neuroscience.

Rowland, L. P. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.5.1251 · Cited by 39 · see citing works

Enhanced Oligomerization of the α-Synuclein Mutant by the Cu,Zn-Superoxide Dismutase and Hydrogen Peroxide System

Kang, J. H., & Kim, K. S. (2003) · Molecules and Cells · doi:10.1016/s1016-8478(23)13712-5 · Cited by 38 · see citing works

Erratum: Direct EPR detection of the carbonate radical anion produced from peroxynitrite and carbon doxide (Journal of Biological Chemistry (1999) 274 (10802-10806))

Bonini, M. G., Radí, R., Ferrer‐Sueta, G., et al. (1999) · Journal of Biological Chemistry · Cited by 37 · see citing works

Polypeptide Modification and Cross-Linking by Oxidized 3-Hydroxykynurenine

Aquilina, J. A., Carver, J. A., & Truscott, R. J. W. (2000) · Biochemistry · doi:10.1021/bi001230t · Cited by 36 · see citing works

MOLECULAR APPROACHES TO AMYOTROPHIC LATERAL SCLEROSIS

Smith, R. G., & Appel, S. H. (1995) · Annual Review of Medicine · doi:10.1146/annurev.med.46.1.133 · Cited by 32 · see citing works

Superoxide dismutase and familial amyotrophic lateral sclerosis: New insights into mechanisms and treatments

Brown, R. H. (1996) · Annals of Neurology · doi:10.1002/ana.410390202 · Cited by 30 · see citing works

Immunocytochemical method for investigating in vivo neuronal oxygen radical-induced lipid peroxidation

Hall, E. D., Oostveen, J. A., Andrus, P. K., et al. (1997) · Journal of Neuroscience Methods · doi:10.1016/s0165-0270(97)00089-7 · Cited by 28 · see citing works

Cell death mechanisms in ALS

Bredesen, D. E., Wiedau‐Pazos, M., Goto, J. J., et al. (1996) · Neurology · doi:10.1212/wnl.47.4_suppl_2.36s · Cited by 19 · see citing works

Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation

Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541 · see citing works

Tryptophan Oxidation by Singlet Molecular Oxygen [O₂(¹Δ_g)]: Mechanistic Studies Using¹⁸O-Labeled Hydroperoxides, Mass Spectrometry, and Light Emission Measurements

Ronsein, G. E., Oliveira, M. C. B., Miyamoto, S., Medeiros, M. H. G., & Di Mascio, P. (2008) · Chemical Research in Toxicology · doi:10.1021/tx800026g · Cited by 142 · see citing works

Failure of protein quality control in amyotrophic lateral sclerosis

Kabashi, E., & Durham, H. D. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.06.006 · Cited by 90 · see citing works

Products of Photochemical Degradtion of Tryptophan

Sakamura, S., & OBATA, Y. (1955) · Nippon Nōgeikagaku Kaishi · doi:10.1271/nogeikagaku1924.29.817 · Cited by 3 · see citing works

Activated Cellular Immunity and Decreased Serum Tryptophan in Healthy Pregnancy

Fuchs, D., Schröcksnadel, H., Baier‐Bitterlich, G., et al. (1996) · Advances in experimental medicine and biology · doi:10.1007/978-1-4613-0381-7_24 · Cited by 17 · see citing works

Newly developed method for quantification of tryptophan and its metabolites : clinical application

Bipath, P., Laurens, J. B., & Viljoen, M. (2008) · UpSpace Institutional Repository (University of Pretoria)

How Decreased Level of Plasma Tryptophan Play Role in Diabetic Patients?

Qudsia, H. A. (2022) · International Journal of Current Science Research and Review · doi:10.47191/ijcsrr/v5-i7-01

Enzymatic Conversion of L- and D-Tryptophan to Kynurenine by Rat Liver

Rodden, F. A., & Berg, C. P. (1974) · Journal of Nutrition · doi:10.1093/jn/104.2.227 · Cited by 7 · see citing works