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5. Akhmadi, A., Yeskendir, A., Dey, N., Mussakhmetov, A., Shatkenova, Z., Kulyyassov, A., Andreeva, A. & Utepbergenov, D. (2024) DJ-1 protects proteins from acylation by catalyzing the hydrolysis of highly reactive cyclic 3-phosphoglyceric anhydride. Nat. Commun., 15(1), 2004.

4. Yedigenov, M., Amire, N., Abdirassil, A., Mulikova, T., Begenov, A., Kiesilä, A., Peshkov, A.A., Peshkov, V.A. & Utepbergenov, D. (2024). Glyoxalase-based toolbox for the enantioselective synthesis of α-hydroxy carboxylic acids. Org. Biomol. Chem., 2024, 22(13), 2539-2543


3. Mulikova, T., Bekkhozhin, Z., Abdirassil, A., & Utepbergenov D. (2021). A continuous spectrophotometric assay for glutathione-independent glyoxalases. Analytical Biochemistry, 630:114317

2.  Andreeva, A., Bekkhozhin, Z., Omertassova, N., Baizhumanov, T., Yeltay, G., Akhmetali, M., Toibazar, D., & Utepbergenov, D. (2019). The apparent deglycase activity of DJ-1 results from the conversion of free methylglyoxal present in fast equilibrium with hemithioacetals and hemiaminals. The Journal of Biological Chemistry, 294(49), 18863–18872

1.  Mussakhmetov, A., Shumilin, I. A., Nugmanova, R., Shabalin, I. G., Baizhumanov, T., Toibazar, D., Khassenov, B., Minor, W., & Utepbergenov, D. (2018). A transient post-translational modification of active site cysteine alters binding properties of the parkinsonism protein DJ-1. Biochemical and Biophysical Research Communications, 504(1), 328–333

Before NU (2001-2016)

17. Utepbergenov, D., Hennig, P. M., Derewenda, U., Artamonov, M. V., Somlyo, A. V., & Derewenda, Z. S. (2016). Bacterial Expression, Purification and In Vitro Phosphorylation of Full-Length Ribosomal S6 Kinase 2 (RSK2). PloS One, 11(10), e0164343

16.  Baker, L. E., Ellena, J. F., Handing, K. B., Derewenda, U., Utepbergenov, D., Engel, D. A., & Derewenda, Z. S. (2016). Molecular architecture of the nucleoprotein C-terminal domain from the Ebola and Marburg viruses. Acta Crystallographica (D), 72(Pt 1), 49–58

15.  Utepbergenov, D., & Derewenda, Z. S. (2013). The unusual mechanism of inhibition of the p90 ribosomal S6 kinase (RSK) by flavonol rhamnosides. Biochimica et Biophysica Acta, 1834(7), 1285–1291

14.  Derewenda, U., Artamonov, M., Szukalska, G., Utepbergenov, D., Olekhnovich, N., Parikh, H. I., Kellogg, G. E., Somlyo, A. V., & Derewenda, Z. S. (2013). Identification of quercitrin as an inhibitor of the p90 S6 ribosomal kinase (RSK): structure of its complex with the N-terminal domain of RSK2 at 1.8 Å resolution. Acta Crystallographica (D), 69(Pt 2), 266–275

13.  Artamonov, M., Momotani, K., Utepbergenov, D., Franke, A., Khromov, A., Derewenda, Z. S., & Somlyo, A. V. (2013). The p90 ribosomal S6 kinase (RSK) is a mediator of smooth muscle contractility. PloS One, 8(3), e58703

12.  Utepbergenov, D., Derewenda, U., Olekhnovich, N., Szukalska, G., Banerjee, B., Hilinski, M. K., Lannigan, D. A., Stukenberg, P. T., & Derewenda, Z. S. (2012). Insights into the inhibition of the p90 ribosomal S6 kinase (RSK) by the flavonol glycoside SL0101 from the 1.5 Å crystal structure of the N-terminal domain of RSK2 with bound inhibitor. Biochemistry, 51(33), 6499–6510

11.  Momotani, K., Artamonov, M. V., Utepbergenov, D., Derewenda, U., Derewenda, Z. S., & Somlyo, A. V. (2011). p63RhoGEF couples Gα(q/11)-mediated signaling to Ca2+ sensitization of vascular smooth muscle contractility. Circulation Research, 109(9), 993–1002

10.  Zheng, M., Cierpicki, T., Burdette, A. J., Utepbergenov, D., Janczyk, P. Ł., Derewenda, U., Stukenberg, P. T., Caldwell, K. A., & Derewenda, Z. S. (2011). Structural features and chaperone activity of the NudC protein family. Journal of Molecular Biology, 409(5), 722–741

9.  Fanning, A. S., Little, B. P., Rahner, C., Utepbergenov, D., Walther, Z., & Anderson, J. M. (2007). The unique-5 and -6 motifs of ZO-1 regulate tight junction strand localization and scaffolding properties. Molecular Biology of the Cell, 18(3), 721–731

8.  Utepbergenov, D. I., Fanning, A. S., & Anderson, J. M. (2006). Dimerization of the scaffolding protein ZO-1 through the second PDZ domain. The Journal of Biological Chemistry, 281(34), 24671–24677.

7.  Andreeva, A. Y., Piontek, J., Blasig, I. E., & Utepbergenov, D. I. (2006). Assembly of tight junction is regulated by the antagonism of conventional and novel protein kinase C isoforms. The International Journal of Biochemistry & Cell Biology, 38(2), 222–233

6.  Müller, S. L., Portwich, M., Schmidt, A., Utepbergenov, D. I., Huber, O., Blasig, I. E., & Krause, G. (2005). The tight junction protein occludin and the adherens junction protein alpha-catenin share a common interaction mechanism with ZO-1. The Journal of Biological Chemistry, 280(5), 3747–3756. 

5.  Schmidt, A., Utepbergenov, D. I., Mueller, S. L., Beyermann, M., Schneider-Mergener, J., Krause, G., & Blasig, I. E. (2004). Occludin binds to the SH3-hinge-GuK unit of zonula occludens protein 1: potential mechanism of tight junction regulation. Cellular and Molecular Life Sciences, 61(11), 1354–1365.

4.  Schmidt, A., Utepbergenov, D. I., Krause, G., & Blasig, I. E. (2001). Use of surface plasmon resonance for real-time analysis of the interaction of ZO-1 and occludin. Biochemical and Biophysical Research Communications, 288(5), 1194–1199

3.  Blasig, I. E., Giese, H., Schroeter, M. L., Sporbert, A., Utepbergenov, D. I., Buchwalow, I. B., Neubert, K., Schönfelder, G., Freyer, D., Schimke, I., Siems, W. E., Paul, M., Haseloff, R. F., & Blasig, R. (2001). *NO and oxyradical metabolism in new cell lines of rat brain capillary endothelial cells forming the blood-brain barrier. Microvascular Research, 62(2), 114–127 

2.  Andreeva, A. Y., Krause, E., Müller, E. C., Blasig, I. E., & Utepbergenov, D. I. (2001). Protein kinase C regulates the phosphorylation and cellular localization of occludin. The Journal of Biological Chemistry, 276(42), 38480–38486


1.  Lisdat, F., Utepbergenov, D., Haseloff, R. F., Blasig, I. E., Stöcklein, W., Scheller, F. W., & Brigelius-Flohé, R. (2001). An optical method for the detection of oxidative stress using protein-RNA interaction. Analytical Chemistry, 73(5), 957–962​

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