Ubiquitination of soluble and membrane-bound tyrosine hydroxylase and degradation of the soluble form
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Tyrosine hydroxylase (TH) demonstrates by two‐dimensional electrophoresis a microheterogeneity both as a soluble recombinant human TH (hTH1) and as a membrane‐bound bovine TH (bTH mem). Part of the heterogeneity is likely due to deamidation of labile asparagine residues. Wild‐type (wt)‐hTH1 was found to be a substrate for the ubiquitin (Ub) conjugating enzyme system in a reconstituted in vitro system. When wt‐hTH1 was expressed in a coupled transcription‐translation TnT R‐T7 reticulolysate system 35 S‐labelled polypeptides of the expected molecular mass of native enzyme as well as both higher and lower molecular mass forms were observed. The amount of high‐molecular‐mass forms increased by time and was enhanced in the presence of Ub and clasto‐lactacystin β‐lactone. In pulse‐chase experiments the amount of full‐length hTH1 decreased by first‐order kinetics with a half‐time of 7.4 h and 2.1 h in the absence and presence of an ATP‐regenerating system, respectively. The ATP‐dependent degradation was inhibited by clasto‐lactacystin β‐lactone. Our findings support the conclusion that hTH1 is ubiquitinated and at least partially degraded by the proteasomes in the reticulocyte lysate system. Finally, it is shown that the integral TH of the bovine␣adrenal chromaffin granule membrane (bTH mem) is ubiquitinated, most likely monoubiquitinated. Additional Ub‐conjugates of this membrane, detected by Western blot analysis, have not yet been identified.
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Human recombinant TH protein is ubiquitinated and degraded in the reticulocyte lysate system.
“Døskeland and Flatmark reported that human recombinant TH protein is ubiquitinated and degraded in the reticulocyte lysate system [98].”
From Degradation of Tyrosine Hydroxylase by the Ubiquitin-Proteasome System in the Pathogenesis of Parkinson’s Disease and Dopa-Responsive Dystonia (2020) · cites this paper as [98]
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Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961 · see citing works
Autophagy as a regulated pathway of cellular degradation.
Klionsky, D., & Emr, S. (2000) · Science · doi:10.1126/science.290.5497.1717 · Cited by 3,794 · see citing works
Görg, A., Postel, W., & Günther, S. (1988) · Electrophoresis · doi:10.1002/elps.1150090913 · Cited by 2,401 · see citing works
Nagatsu, T., Levitt, M., & Udenfriend, S. (1964) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93832-9 · Cited by 2,067 · see citing works
Fenteany, G., Standaert, R. F., Lane, W. S., Choi, S., Corey, E. J., & Schreiber, S. L. (1995) · Science · doi:10.1126/science.7732382 · Cited by 1,583 · see citing works
Posttranslational Quality Control: Folding, Refolding, and Degrading Proteins
Wickner, S., Maurizi, M. R., & Gottesman, S. (1999) · Science · doi:10.1126/science.286.5446.1888 · Cited by 1,071 · see citing works
Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity
Meng, L., Mohan, R., Kwok, B. H. B., Elofsson, M., Sin, N., & Crews, C. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10403 · Cited by 926 · see citing works
The Neuron-Specific Protein PGP 9.5 Is a Ubiquitin Carboxyl-Terminal Hydrolase
Wilkinson, K. D., Lee, K., Deshpande, S. S., Duerksen-Hughes, P. J., Boss, J. M., & Pohl, J. (1989) · Science · doi:10.1126/science.2530630 · Cited by 871 · see citing works
The dynamic range of protein expression: A challenge for proteomic research
Corthals, G. L., Wasinger, V. C., Hochstrasser, D. F., & Sanchez, J. (2000) · Electrophoresis · doi:10.1002/(sici)1522-2683(20000401)21:6 · Cited by 615 · see citing works
Udenfriend, S. (1966) · Pharmacological Reviews · doi:10.1016/s0031-6997(25)07173-x · Cited by 503 · see citing works
Ubiquitin-mediated protein degradation.
Hershko, A. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)37575-1 · Cited by 453 · see citing works
Craiu, A., Gaczynska, M. E., Akopian, T. N., Gramm, C. F., Fenteany, G., Goldberg, A. L., & Rock, K. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.20.13437 · Cited by 382 · see citing works
Doran, J. F., Jackson, P., Kynoch, P. A. M., & Thompson, R. J. (1983) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1983.tb08124.x · Cited by 364 · see citing works
The molecular function of adrenal chromaffin granules: Established facts and unresolved topics
Winkler, H. J. S., Apps, D. K., & Fischer‐Colbrie, R. (1986) · Neuroscience · doi:10.1016/0306-4522(86)90154-5 · Cited by 357 · see citing works
Adrenomedullin Expression in Human Tumor Cell Lines ITS POTENTIAL ROLE AS AN AUTOCRINE GROWTH FACTOR
Miller, M. J., Martı́nez, A., Unsworth, E. J., Thiele, C. J., Moody, T. W., Elsasser, T. H., & Cuttitta, F. F. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.38.23345 · Cited by 314 · see citing works
Prediction of protein deamidation rates from primary and three-dimensional structure
Robinson, N. E., & Robinson, A. B. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.071066498 · Cited by 260 · see citing works
Regulatory Properties of Soluble and Particulate Rat Brain Tyrosine Hydroxylase
Kuczenski, R. T., & Mandell, A. J. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45221-6 · Cited by 231 · see citing works
Mechanistic Studies on the Inactivation of the Proteasome by Lactacystin in Cultured Cells
Dick, L. R., Cruikshank, A. A., Destree, A. T., Grenier, L., McCormack, T. A., Melandri, F. D., Nunes, S. L., Palombella, V. J., Parent, L. A., Plamondon, L., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.1.182 · Cited by 229 · see citing works
Lüdecke, B. (1996) · Human Molecular Genetics · doi:10.1093/hmg/5.7.1023 · Cited by 192 · see citing works
Grenett, H. E., Ledley, F. D., Reed, L. L., & Woo, S. L. C. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.16.5530 · Cited by 183 · see citing works
Structural Insight into the Aromatic Amino Acid Hydroxylases and Their Disease-Related Mutant Forms
Flatmark, T., & Stevens, R. C. (1999) · Chemical Reviews · doi:10.1021/cr980450y · Cited by 172 · see citing works
Self-citationCatecholamine biosynthesis and physiological regulation in neuroendocrine cells
Flatmark (2000) · Acta Physiologica Scandinavica · doi:10.1046/j.1365-201x.2000.00596.x · Cited by 146 · see citing works
Glucose-induced Autophagy of Peroxisomes inPichia pastorisRequires a Unique E1-like Protein
Yuan, W., STRØMHAUG, P. E., & Dunn, W. A. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.5.1353 · Cited by 131 · see citing works
Chemistry and Biology of Pteridines and Folates
(2002) · Springer eBooks · doi:10.1007/978-1-4615-0945-5 · Cited by 129 · see citing works
Recombinant human tyrosine hydroxylase isozymes
Haavik, J., Bourdellès, B. L., Martı́nez, A., Flatmark, T., & Mallet, J. J. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16133.x · Cited by 106 · see citing works
Self-citationStimulus-Coupled Interaction of Tyrosine Hydroxylase with 14-3-3 Proteins
Itagaki, C., Isobe, T., Taoka, M., Natsume, T., Nomura, N., Horigome, T., Omata, S., Ichinose, H., Nagatsu, T., Greene, L. A., et al. (1999) · Biochemistry · doi:10.1021/bi9914255 · Cited by 96 · see citing works
Sagné, C., Isambert, M., Henry, J., & Gasnier, B. (1996) · Biochemical Journal · doi:10.1042/bj3160825 · Cited by 92 · see citing works
Ubiquitination of Neuronal Nitric-oxide Synthase in Vitro and in Vivo
Bender, A. T., Demady, D. R., & Osawa, Y. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000155200 · Cited by 90 · see citing works
Dick, F. A., Karamanou, S., & Trumpower, B. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.20.13372 · Cited by 87 · see citing works
Haavik, J., Andersson, K. K., Petersson, L., & Flatmark, T. (1988) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(88)90019-2 · Cited by 85 · see citing works
Self-citationConformational Properties and Stability of Tyrosine Hydroxylase Studied by Infrared Spectroscopy
Martı́nez, A., Haavik, J., Flatmark, T., Arrondo, J. L. R., & Muga, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.33.19737 · Cited by 83 · see citing works
Self-citationBourdellès, B. L., Horellou, P., Caër, J. L., Denèfle, P., Latta‐Mahieu, M., Haavik, J., Guibert, B., Mayaux, J. F., & Mallet, J. J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47348-1 · Cited by 80 · see citing works
Oxidoreductase activities of chromaffin granule ghosts isolated from the bovine adrenal medulla
Terland, O., & Flatmark, T. (1980) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(80)90109-1 · Cited by 64 · see citing works
Self-citationPasinetti, G. M., Osterburg, H. H., Kelly, A. B., Kohama, S., Morgan, D., Reinhard, J. F., Stellwagen, R. H., & Finch, C. E. (1992) · Molecular Brain Research · doi:10.1016/0169-328x(92)90045-d · Cited by 63 · see citing works
Tank, A. W., Ham, L., & Curella, P. (1986) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)10389-1 · Cited by 55 · see citing works
Solstad, T., & Flatmark, T. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01715.x · Cited by 50 · see citing works
Self-citationPocotte, S. L., Holz, R. W., & Ueda, T. (1986) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1986.tb13011.x · Cited by 50 · see citing works
Stoller, T. J., & Shields, D. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.107.6.2087 · Cited by 47 · see citing works
Phosphorylation and dephosphorylation of chromaffin cell proteins in response to stimulation
Coˆté, A., Doucet, J.-P., & Trifaró, J. M. (1986) · Neuroscience · doi:10.1016/0306-4522(86)90286-1 · Cited by 46 · see citing works
Bader, M. F., Hikita, T., & Trifaró, J. M. (1985) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1985.tb05445.x · Cited by 41 · see citing works
Kaufman, S. (1995) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470123164.ch3 · Cited by 39 · see citing works
Isoforms of mammalian ubiquitin-activating enzyme.
Cook, J. C., & Chock, P. B. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35767-3 · Cited by 38 · see citing works
Treiman, M., Weber, W., & Gratzl, M. (1983) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1983.tb08031.x · Cited by 34 · see citing works
Kuhn, D. M., Arthur, R., Yoon, H., & Sankaran, K. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39431-1 · Cited by 33 · see citing works
Kojima, M., Oguro, K., Sawabe, K., Iida, Y., Ikeda, R., Yamashita, A., Nakanishi, N., & Hasegawa, H. (2000) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a022572 · Cited by 27 · see citing works
Kent, C., & COUPLAND, R. E. (1989) · PubMed · Cited by 25 · see citing works
Pickart, C. M. (1998) · Springer eBooks · doi:10.1007/978-1-4899-1922-9_2 · Cited by 25 · see citing works
Wu, D. K., & Cepko, C. L. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.62030863.x · Cited by 23 · see citing works
Morita, K., Teraoka, K., & Oka, M. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45624-4 · Cited by 22 · see citing works
Fernández, E., & Craviso, G. L. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0730169.x · Cited by 20 · see citing works
Beesley, P. W., Mummery, R. S., Tibaldi, J., CHAPMAN, A. P., Smith, S. J., & Rider, C. C. (1995) · Biochemical Society Transactions · doi:10.1042/bst0230059 · Cited by 18 · see citing works
Haycock, J. W., George, R. J. D., & Waymire, J. C. (1985) · Neurochemistry International · doi:10.1016/0197-0186(85)90119-6 · Cited by 16 · see citing works
Conjugation of phenylalanine hydroxylase with polyubiquitin chains catalysed by rat liver enzymes
Døskeland, A. P., & Flatmark, T. (2001) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(01)00206-0 · Cited by 10 · see citing works
Self-citationThe degradative fate of ubiquitin-protein conjugates in nucleated and enucleated cells.
Al, W., László, L., & Fj, D. (1991) · PubMed · Cited by 4 · see citing works
de Carvalho, R. M. N., Solstad, T., Robinson, N. E., Robinson, A. B., & Flatmark, T. (2002) · Springer eBooks · doi:10.1007/978-1-4615-0945-5_17 · Cited by 2 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Tyrosine hydroxylase and regulation of dopamine synthesis
Daubner, S. C., Le, T., & Wang, S. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.12.017 · Cited by 1,092 · see citing works
The Ubiquitin Proteasome System in Neurodegenerative Diseases
Ciechanover, A. J., & Brundin, P. (2003) · Neuron · doi:10.1016/s0896-6273(03)00606-8 · Cited by 984 · see citing works
Complexity of dopamine metabolism
Meiser, J., Weindl, D., & Hiller, K. (2013) · Cell Communication and Signaling · doi:10.1186/1478-811x-11-34 · Cited by 665 · see citing works
Part II: α-synuclein and its molecular pathophysiological role in neurodegenerative disease
Dev, K. K. (2003) · Neuropharmacology · doi:10.1016/s0028-3908(03)00140-0 · Cited by 262 · see citing works
Ubiquitin–proteasome system and Parkinson's diseases
Betarbet, R. S., Sherer, T., & Greenamyre, J. T. (2004) · Experimental Neurology · doi:10.1016/j.expneurol.2004.08.021 · Cited by 245 · see citing works
Conn, K. J., Gao, W., McKee, A. C., Lan, M. S., Ullman, M. D., Eisenhauer, P. B., Fine, R. E., & Wells, J. M. (2004) · Brain Research · doi:10.1016/j.brainres.2004.07.026 · Cited by 144 · see citing works
Complex molecular regulation of tyrosine hydroxylase
Tekin, I., Roskoski, R., Carkaci-Salli, N., & Vrana, K. E. (2014) · Journal of Neural Transmission · doi:10.1007/s00702-014-1238-7 · Cited by 128 · see citing works
EH and UIM: Endocytosis and More
Polo, S., Confalonieri, S., Salcini, A. E., & Fiore, P. P. D. (2003) · Science s STKE · doi:10.1126/stke.2132003re17 · Cited by 104 · see citing works
The N‐ and C‐terminal fragments of ubiquitin are important for the antimicrobial activities
Kieffer, A., Goumon, Y., Ruh, O., Chasserot‐Golaz, S., Nullans, G., Gasnier, C., Aunis, D., & Metz‐Boutigue, M. (2003) · The FASEB Journal · doi:10.1096/fj.02-0699fje · Cited by 102 · see citing works
Tyrosine hydroxylase phosphorylation in vivo
Dunkley, P. R., & Dickson, P. W. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14675 · Cited by 85 · see citing works
Kawahata, I., & Fukunaga, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113779 · Cited by 71 · see citing works
WldS mice are protected against the Parkinsonian mimetic MPTP
HASBANI, D., & O’Malley, K. L. (2006) · Experimental Neurology · doi:10.1016/j.expneurol.2006.05.017 · Cited by 73 · see citing works
Clark, J., Silvaggi, J. M., Kiselak, T., Zheng, K., Clore, E. L., Dai, Y., Bass, C. E., & Simon, D. K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048925 · Cited by 70 · see citing works
Trojan Horse Delivery of 4,4′‐Dimethoxychalcone for Parkinsonian Neuroprotection
Zhang, W., Chen, H., Ding, L., Gong, J., Zhang, M., Guo, W., Xu, P., Li, S., & Zhang, Y. (2021) · Advanced Science · doi:10.1002/advs.202004555 · Cited by 65 · see citing works
Berends, A. M. A., Eisenhofer, G., Fishbein, L. M., van der Horst‐Schrivers, A. N. A., Kema, I. P., Links, T. P., Lenders, J. W. M., & Kerstens, M. N. (2019) · Cancers · doi:10.3390/cancers11081121 · Cited by 63 · see citing works
Role of N-terminus of tyrosine hydroxylase in the biosynthesis of catecholamines
Nakashima, A., Hayashi, N., Kaneko, Y. S., Mori, K., Sabban, E. L., Nagatsu, T., & Ota, A. (2009) · Journal of Neural Transmission · doi:10.1007/s00702-009-0227-8 · Cited by 62 · see citing works
Nakashima, A., Mori, K., Kaneko, Y. S., Hayashi, N., Nagatsu, T., & Ota, A. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.03.020 · Cited by 52 · see citing works
Nakashima, A., Ota, A., Kaneko, Y. S., Mori, K., Nagasaki, H., & Nagatsu, T. (2012) · Journal of Neural Transmission · doi:10.1007/s00702-012-0828-5 · Cited by 47 · see citing works
Singh, M., Murthy, V., & Ramassamy, C. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.01.030 · Cited by 43 · see citing works
Melatonin and ubiquitin: what’s the connection?
Vriend, J. P., & Reiter, R. J. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1659-3 · Cited by 39 · see citing works
Martı́nez, A., Calvo, A. C., Teigen, K., & Pey, A. L. (2008) · Progress in molecular biology and translational science · doi:10.1016/s0079-6603(08)00603-x · Cited by 39 · see citing works
Kawahata, I., Ohtaku, S., Tomioka, Y., Ichinose, H., & Yamakuni, T. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.07.125 · Cited by 35 · see citing works
Metabolism of tetrahydrobiopterin: Its relevance in monoaminergic neurons and neurological disorders
Ichinose, H., Nomura, T., & Sumi‐Ichinose, C. (2008) · The Chemical Record · doi:10.1002/tcr.20166 · Cited by 35 · see citing works
Characterization of wild‐type and mutant forms of human tryptophan hydroxylase 2
Winge, I., McKinney, J. A., Knappskog, P. M., & Haavik, J. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04290.x · Cited by 35 · see citing works
The roles of the proteasome pathway in signal transduction and neurodegenerative diseases
Chen, J., Lin, F., & Qin, Z. (2008) · Neuroscience Bulletin · doi:10.1007/s12264-008-0183-6 · Cited by 34 · see citing works
Kawahata, I., Tokuoka, H., Parvez, H., & Ichinose, H. (2009) · Journal of Neural Transmission · doi:10.1007/s00702-009-0304-z · Cited by 31 · see citing works
Shi, X., & Habecker, B. A. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07539.x · Cited by 31 · see citing works
Urano, F., Hayashi, N., Arisaka, F., Kurita, H., Murata, S., & Ichinose, H. (2006) · The Journal of Biochemistry · doi:10.1093/jb/mvj073 · Cited by 30 · see citing works
Distinct effects of ketamine and acetyl l-carnitine on the dopamine system in zebrafish
Robinson, B. L., Dumas, M., Cuevas, E., Gu, Q., Paule, M. G., Ali, S. F., & Kanungo, J. (2016) · Neurotoxicology and Teratology · doi:10.1016/j.ntt.2016.02.004 · Cited by 30 · see citing works
Ubiquitinated annexin A2 is enriched in the cytoskeleton fraction
Lauvrak, S. U., Hollås, H., Døskeland, A. P., Aukrust, I., Flatmark, T., & Vedeler, A. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.11.076 · Cited by 30 · see citing works
Self-citationCarbajosa, N. A. L., Corradi, G., Verrilli, M. A. L., Guil, M. J., Vatta, M. S., & Gironacci, M. M. (2015) · PLOS ONE · doi:10.1371/journal.pone.0116597 · Cited by 27 · see citing works
“In accordance, the monoubiquitylation of TH has been shown in the catecholamine storage/secretory granules of the adrenal medulla [34].”
BackgroundInfluentialKonieczny, J., Czarnecka, A. M., Lenda, T., Kamińska, K., & Lorenc‐Koci, E. (2013) · Behavioural Brain Research · doi:10.1016/j.bbr.2013.12.019 · Cited by 25 · see citing works
Nakashima, A., Ohnuma, S., Kodani, Y., Kaneko, Y. S., Nagasaki, H., Nagatsu, T., & Ota, A. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.03.022 · Cited by 22 · see citing works
Szigetvari, P. D., Patil, S. S., Birkeland, E., Kleppe, R., & Haavik, J. (2023) · Neurochemistry International · doi:10.1016/j.neuint.2023.105629 · Cited by 23 · see citing works
Tetrahydrobiopterin and Related Biologically Important Pterins
Murata, S., Ichinose, H., & Urano, F. (2007) · Springer eBooks · doi:10.1007/7081_2007_061 · Cited by 19 · see citing works
Kawahata, K., & Fukunaga, K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242317037 · Cited by 18 · see citing works
Intracellular Stability of Tyrosine Hydroxylase
Nakashima, A., Kaneko, Y. S., Kodani, Y., Mori, K., Nagasaki, H., Nagatsu, T., & Ota, A. (2013) · Advances in pharmacology · doi:10.1016/b978-0-12-411512-5.00001-4 · Cited by 17 · see citing works
Growth‐associated protein of 43 kDa (GAP‐43) is cleaved nonprocessively by the 20S proteasome
Denny, J. B. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04179.x · Cited by 13 · see citing works
Gu, Y., Zhang, K., Biswas, N., Friese, R. S., Lin, D. H., Mahata, S. K., Hoshijima, M., O’Connor, D. T., Peterson, K. L., & Brar, B. K. (2010) · Endocrinology · doi:10.1210/en.2009-1454 · Cited by 12 · see citing works
Wang, J., Sheng, Y., & Jang, S. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.02.040 · Cited by 12 · see citing works
Proteasomal degradation of tyrosine hydroxylase and neurodegeneration
Nakashima, A. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07562.x · Cited by 12 · see citing works
Regulation of tyrosine hydroxylase: relevance to Parkinson's disease
Alam, G., & Richardson, J. R. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-815950-7.00004-7 · Cited by 11 · see citing works
RNAi of 14-3-3η protein increases intracellular stability of tyrosine hydroxylase
Nakashima, A., Hayashi, N., Kaneko, Y. S., Mori, K., Sabban, E. L., Nagatsu, T., & Ota, A. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.09.042 · Cited by 11 · see citing works
Lee, E. J., Yoon, H. H., Park, E. S., Min, J., & Jeon, S. R. (2018) · Stereotactic and Functional Neurosurgery · doi:10.1159/000486644 · Cited by 11 · see citing works
Li, X., Zhang, Y., Xie, P., Piao, J., Hu, Y., Chang, M., Liu, T., & Hu, L. (2010) · BMC Neuroscience · doi:10.1186/1471-2202-11-95 · Cited by 10 · see citing works
Nakashima, A., Hayashi, N., Kaneko, Y. S., Mori, K., Egusa, H., Nagatsu, T., & Ota, A. (2005) · Journal of Neuroscience Research · doi:10.1002/jnr.20540 · Cited by 10 · see citing works
Bezem, M. T., Johannessen, F. G., Kråkenes, T.-A., Sailor, M. J., & Martı́nez, A. (2021) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.0c00960 · Cited by 9 · see citing works
Nakashima, A., Kodani, Y., Kaneko, Y. S., Nagasaki, H., & Ota, A. (2016) · Journal of Neural Transmission · doi:10.1007/s00702-016-1653-z · Cited by 8 · see citing works
Sazali, A. S. B., Natsume, R., Sakimura, K., Abe, M., & Ichinose, H. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.153129 · Cited by 1 · see citing works
Structural Determinants of Post-transcriptional Protein Regulation as Modulators
Murphy, K. L. (2008)
Buneeva, O. A., Medvedeva, M. V., & Medvedev, A. E. (2008) · Biochemistry (Moscow) Supplement Series B Biomedical Chemistry · doi:10.1007/s11828-008-1012-1
Szigetvari, P. D., Patil, S. S., Birkeland, E., Kleppe, R., & Haavik, J. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.05.556372
- Authors
- Døskeland, A. P., & Flatmark, T.
- Affiliations
- University of Bergen (NO)
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 2002-03
- Volume
- 269
- Issue
- 5
- Pages
- 1561-1569
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W1917032649
- Cited by
- 53
- References
- 55
- Citations by year
- 2025: 1 · 2023: 3 · 2021: 2 · 2020: 2 · 2019: 2 · 2018: 1 · 2016: 3 · 2015: 2 · 2014: 2 · 2013: 4 · 2012: 3
- FWCI
- 1.04
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- European Journal of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- tyrosine hydroxylase, ubiquitination, protein degradation, proteasome, asparagine deamidation, protein microheterogeneity, membrane-bound enzyme, chromaffin granule membrane, clasto-lactacystin beta-lactone, E2 ubiquitin-conjugating enzyme
- MeSH terms
- Adenosine Triphosphate, Animals, Cattle, Chromaffin Granules, Membrane Proteins, Recombinant Proteins, Reticulocytes, Tyrosine 3-Monooxygenase, Electrophoresis, Gel, Two-Dimensional, Ubiquitin, Mice
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