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National Library of Medicine


38. Gudimchuk, N. and Roll-Mecak, A.* Watching microtubules grow one tubulin at a time. 2019. Proc. Natl. Acad. Sci. 116(15):7163-7165.[abstract]

37. Roll-Mecak, A.* How cells exploit tubulin diversity to build functional cellular microtubule mosaics. 2019. Curr. Opin. Cell Biol. 56:102-108.[abstract]


36. McNally, F*. and Roll-Mecak, A.* Microtubule severing enzymes: from cellular functions to molecular mechanism. 2018. J. Cell Biol. 217(12):4057-4069.[abstract]

35. Vemu, A., Szczesna, E., Zehr, E.A., Spector, J.O., Grigorieff, N.G., Deaconescu, A.M., Roll-Mecak, A.* Severing enzymes amplify microtubule arrays through lattice GTP-tubulin incorporation. 2018. Science 361:6404.[article][abstract]

Commentary Stavoe and Holzbaur in Dev. Cell 47(4):402-403.                                                                     Commentary by Akhmanova in Dev. Cell 47(4):400-401.                                                                             

34. Park, J. an Roll-Mecak, A*. The tubulin code in neuronal polarity. 2018. Curr. Opinion Neurobiology. 51:95-102.[abstract]

33. Vemu, A., Atherton, J., Spector, J.O., Moores, C.M. and Roll-Mecak, A.* Tubulin isoform composition tunes microtubule dynamics. 2017. Mol. Biol. Cell. 28(25):3564-3572.[abstract]

32. Zehr, E., Szyk, A. Szczesna, E, Zuo, X and Roll-Mecak, A.* Katanin spiral and ring structures shed light on power stroke for microtubule severing. 2017. Nature Struct. & Molec. Biol. 24(9):717-725. [abstract]

31. Garnham, C.P., Yu, I, Li, Y and Roll-Mecak, A.* Crystal structure of Tubulin Tyrosine Ligase-Like 3 reveals essential architectural elements unique to tubulin monoglycylases. 2017. Proc. Natl. Acad. Sci. USA. 114(25):6545-6550. [abstract]

30. Pigino, G*. an Roll-Mecak, A.* Microtubule dynamics: 50 years after the discovery of tubulin and still going strong. 2017. Mol. Biol. Cell. 28(6):705-706. [abstract]

29. Sun, X., Park, J.H., Gumerson, J., Wu, Z., Swaroop, A., Qian, H., Roll-Mecak, A.* and Li, T.* Loss of RPGR glutamylation underlies the pathogenic mechanism of retinal dystrophy caused by TTLL5 mutations.2016. Proc. Natl. Acad. Sci. USA.,13(21): :E2925-2934. [abstract]

28. Vemu, A., Atherton, J., Spector, J.O., Szyk, A., Moores, C.M. and Roll-Mecak, A.* Structure and Dynamics of Single-Isoform Recombinant Neuronal Human Tubulin. J. Biol. Chem. Accelerated Communication, 291(25):12907-12915. [abstract]

27. Meyer PA, Socias S, Key J, Ransey E, Tjon EC, Buschiazzo A, Lei M, Botka C, Withrow J, Neau D, Rajashankar K, Anderson KS, Baxter RH, Blacklow SC, Boggon TJ, Bonvin AM, Borek D, Brett TJ, Caflisch A, Chang CI, Chazin WJ, Corbett KD, Cosgrove MS, Crosson S, Dhe-Paganon S, Di Cera E, Drennan CL, Eck MJ, Eichman BF, Fan QR, Ferré-D'Amaré AR, Christopher Fromme J, Garcia KC, Gaudet R, Gong P, Harrison SC, Heldwein EE, Jia Z, Keenan RJ, Kruse AC, Kvansakul M, McLellan JS, Modis Y, Nam Y, Otwinowski Z, Pai EF, Pereira PJ, Petosa C, Raman CS, Rapoport TA, Roll-Mecak A, Rosen MK, Rudenko G, Schlessinger J, Schwartz TU, Shamoo Y, Sondermann H, Tao YJ, Tolia NH, Tsodikov OV, Westover KD, Wu H, Foster I, Fraser JS, Maia FR, Gonen T, Kirchhausen T, Diederichs K, Crosas M, Sliz P. Data publication with the structural biology data grid supports live analysis. 2016. Nature Commun. 7:10882. doi: 10.1038/ncomms10882. [abstract]

26. Valenstein, M.L. and Roll-Mecak, A.* Graded control of microtubule severing by tubulin glutamylation. 2016. Cell. 164(5): 911-921. [abstract]

Commentary by Schaletzky and Rape in Cell 164(5): 836-837.


25. Garnham, C.P., Vemu, A., Wilson-Kubalek, E.M., Yu, I., Szyk, A., Lander, G.C., Milligan, R.A. Roll-Mecak, A.* Multivalent microtubule recognition by tubulin tyrosine ligase-like family glutamylases. 2015. Cell. 161(5):1112-1123. [abstract]

Commentary by Raunser and Gatsogiannis in Cell 151(5): 960-961.

24. Yu, I., Garnham, C.P. and Roll-Mecak, A.* Writing and Reading the Tubulin Code. 2015. J. Biol. Chem. 290(28): 17163-17172 “The State of the Cytoskeleton in 2015” special issue [abstract]

23. Roll-Mecak, A.* Intrinsically disordered tubulin tail: complex tuners of microtubule functions? 2014. Seminars Cell. Dev. Biol. 37: 11-19. [abstract]

22. Szyk, A, Deaconescu, A. M., Spector, J., Goodman, B. J., Valenstein, M. V., Ziolkowska, N. E., Kormendi, V., Grigorieff, N., Roll-Mecak, A.* Molecular basis of age dependent microtubule acetylation. 2014. Cell. 157(6): 1405-1415. [abstract]

Commentary by Kull and Sloboda in Cell, ACS Chemical Biology, Eureka Alert and Nanowerk.

21. Vemu, A., Garnham, C. P., Lee, D.Y., Roll-Mecak, A.* Generation of differentially modified microtubules using in vitro enzymatic approaches. 2014. Methods in Enzymology. 540: 149-166. [abstract]

20. Roll-Mecak, A.* (2013). Shining light at microtubule crossroads. Science 342(6163):1180-1181. [abstract]

19. Ziolkowska, N. and Roll-Mecak, A.* In vitro microtubule severing assays. 2013. Methods in Molecular Biology. 1046: 323-334. [abstract]

18. Szyk, A., Piszczek, G. and Roll-Mecak, A.* Tubulin tyrosine ligase and stathmin compete for tubulin binding in vitro. 2013. J. Mol. Biol. 425(14): 2412-2414. [abstract]

17. Liu, Y., Garnham, C.P., Roll-Mecak, A.* and Tanner, M.E.* Phosphinic Acid-Based Inhibitors of Tubulin Polyglutamylases. 2013. Bioorg. Med. Chem. Lett. 23(15): 4408-4412. [abstract]


16. Garnham, C. P. and Roll-Mecak, A.* The chemical complexity of cellular microtubules: Tubulin post-translational modification enzymes and their roles in tuning microtubule functions. 2012. Cytoskeleton. 69(7): 442-463. [abstract]

15. Kormendi, V., Szyk, A., Piszczek, G., Roll-Mecak, A.* Crystal structures of tubulin acetyltransferase reveal a conserved catalytic core and the plasticity of the essential N-terminus. 2012. J. Biol. Chem. 287(50): 41569-41575. [abstract]

14. Szyk, A., Deaconescu, A.M., Piszczek, G., Roll-Mecak, A.* Tubulin tyrosine structure reveals adaptation of an ancient fold to bind and modify tubulin. 2011. Nature Struct. & Molec. Biol. 8(11): 1250-1258. [cover] [abstract]

13. Roll-Mecak, A.* and McNally, F.J.* Microtubule severing enzymes, 2010. Curr. Opin. Cell Biol., 22(1): 96-103. [abstract]

A. Roll-Mecak Publications 1999-2009

12. Roll-Mecak, A. and Vale, R.D. Structural basis for microtubule severing by the hereditary spastic paraplegia protein spastin. 2008. Nature, 451(7176): 363-367. [abstract]

11. Roll-Mecak, A. and Vale, R.D. Making more microtubules by severing: a common theme of noncentrosomal microtubule arrays? 2006. J. Cell. Biol. 175 (6): 849-851. [abstract]

10. Padyana, A. K., Qiu, H., Roll-Mecak, A., Hinnebusch, A. G., Burley, S. K. Structural basis for autoinhibition and mutational activation of eIF2a protein kinase GCN2. 2005. J. Biol. Chem. 280(32): 29289-29299. [abstract]

9. Roll-Mecak, A. and Vale, R. D. The Drosophila Homologue of the Hereditary Spastic Paraplegia Protein, Spastin, Severs and Disassembles Microtubules. 2005. Curr. Biol. 5(7): 650-655. [abstract]

8. Roll-Mecak, A., Alone, P., Cao, C., Dever, T. E., and Burley, S. K. X-ray structure of translation initiation factor eIF2g: implications for tRNA and eIF2a binding. 2004. J. Biol. Chem. 279(11): 10634-10642. [abstract]

7. Shin, B-S., Maag, D., Roll-Mecak, A., Arefin, S.M., Burley, S.K., Lorsch, J.R., and Dever, T.E. Uncoupling the GTPase and Translational Activity of Initiation Factor eIF5B/IF2 by Mutations that Lower Ribosome Affinity. 2003. Cell 111: 1015-1025. [abstract]

6. Deaconescu, A.M., Roll-Mecak, A., Bonanno, J.B., Gerchman, S. E., Kycia, H., William, B.F., and Burley, S.K.  X-ray Structure of Saccharomyces Mitochondrial Matrix Factor 1 (Hmf1). 2002. Proteins 42(2): 431-436. [abstract]

5. Roll-Mecak, A., Shin, B-S, Dever, T.E., and Burley, S.K. Engaging the ribosome: Universal IFs of translation. 2001. Trends Biochem. Sci. 26(12): 705-709. [abstract]

4. Dever, T.E., Roll-Mecak, A., Choi, S.K., Lee, J.H., Cao, C., Shin, B-S., and Burley, S.K. The Universal Translation Initiation Factor IF2/eIF5B. 2001. Cold Spring Harbor Symp. Quant. Biol. 66: 417-424.

3. Roll-Mecak, A., Cao, C., Dever, T.E., and Burley, S.K. X-ray structures of the Universal Translation Initiation Factor IF2/eIF5B: Conformational Changes on GDP and GTP Binding. 2000. Cell 103 (5): 781-792. [abstract]

2. Choi, S. K., Olsen, D.S., Roll-Mecak, A., Martung, A., Remo, K. L., Burley, S. K., Hinnebusch, A. G., and Dever, T. E.  Physical and functional interaction between the eukaryotic orthologs of prokaryotic translation initiation factors IF1 and IF2. 2000. Mol. Cell. Biol. 20: 7183-7191. [abstract]

1. Lee, J.H., Choi, S.K., Roll-Mecak, A., Burley, S. K., and Dever, T. E.  Universal conservation in translation initiation revealed by human and archaeal homologs of bacterial translation initiation factor IF2.1999. Proc. Natl. Acad. Sci. USA. 96: 4342-4347. [abstract]

* denotes corresponding author

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