M.Stewart & A.D.McLachlan. 1975. 14 actin binding sites on tropomyosin? Nature, 257:331-333.
M.Stewart. 1975. Location of the troponin binding site on tropomyosin. Proc. Roy. Soc. Lond. Ser. B. 190:257-266.
A.D.McLachlan & M.Stewart. 1975. Tropomyosin coiled-coil interactions. J. Mol. Biol. 97:293-304.
M.Stewart & V.Diakiw. 1978. Electron microscopic location of protein thiol groups. Nature, 274:184-186.
R.W.Kensler & M.Stewart. 1983. Frog skeletal muscle thick filaments are 3-stranded. J. Cell Biol. 96:1797-1802.
M.Stewart, R.W.Kensler & R.J.C.Levine. 1985. Three-dimensional reconstruction of thick filaments from Limulus and scorpion muscle. J. Cell Biol. 101:402-411.
M.Stewart & G.Vigers. 1986. Electron microscopy of frozen hydrated biological material. Nature, 319:631-636.
M.Stewart & R.W.Kensler. 1986. The arrangement of myosin crossbridges in relaxed frog muscle thick filaments. J. Mol. Biol. 192:831-851.
R.A.Quinlan & M.Stewart. 1987. Crystalline tubes of chicken myosin long subfragment-2 that show the coiled coil and molecular interaction geometry. J. Cell Biol. 105:403-415.
M.Stewart, R.A.Quinlan & R.D.Moir. 1989. Molecular interactions in paracrystals of the alpha-helical coiled-coil portion of GFAP: evidence for antiparallel packing of molecules and polymorphism related to intermediate filament structure. J. Cell Biol. 109:225-234.
J.E.Italiano, T.M.Roberts, M.Stewart & C.A.Fontana. 1996. Reconstitution in vitro of the motile apparatus from the amoebic sperm of Ascaris: direct evidence that filament assembly and bundling move membranes. Cell, 84:105-114.
T.L.Bullock, W.D.Clarkson, H.M.Kent & M.Stewart. 1996. The 1.6Å resolution crystal structure of nuclear transport factor 2 (NTF2). J. Mol Biol. 260:251-260.
M.Stewart, H.M.Kent & A.J.McCoy. 1998. Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran. J. Mol. Biol. 277:635-646.
T.L.Bullock, A.J.McCoy, H.M.Kent, T.M.Roberts & M.Stewart. 1998. Structural basis for amoeboid motility in nematode sperm. Nature Struct. Biol. 5:184-189.
T.M.Roberts, E.D.Salmon & M.Stewart. 1998. Hydrostatic pressure shows that lamellipodial motility in Ascaris sperm requires membrane-associated MSP filament elongation and nucleation. J. Cell Biol. 140:367-376.
K.Ribbeck, G.Lipowski, H.M.Kent, M.Stewart & D.Görlich. 1998. NTF2 mediates nuclear import of Ran. EMBO J. 17:6587-6598.
J.E.Italiano, M.Stewart & T.M.Roberts. 1999. Crawling movement of nematode sperm is propelled by coupling substrate attachment to assembly and disassembly of the MSP cytoskeleton at opposite ends of the lamellipodium. J. Cell Biol. 146:1087-1096.
A.J.McCoy, P.Fucini, A.A.Noegel & M.Stewart. 1999. Structural basis for the dimerization of the Dictyostelium gelation factor (ABP120) rod. Nature Struct. Biol. 6:836-841.
T.M.Roberts & M.Stewart. 2000. Acting like actin: the dynamics of the nematode major sperm protein (MSP) cytoskeleton indicate a push-pull mechanism for amoeboid cell motility. J. Cell Biol. 149:7-12.
R.Bayliss, T.Littlewood & M.Stewart. 2000. Structural basis for the interaction between importin-b and nucleoporin FxFG repeats in nuclear trafficking. Cell, 102:99-108.
R.P.Grant, E.Hurt, D.Neuhaus & M.Stewart. 2002. Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1. Nature Struct. Biol. 9:247-251.
R.Bayliss, S.W.Leung, R.P.Baker, B.B.Quimby, A.H.Corbett & M.Stewart. 2002. Structural basis for the interaction between nuclear transport factor 2 (NTF2) and nucleoporin FxFG repeats. EMBO J. 21:2843-2853.
Y.Matsuura, A.Lange, M.Harriman, A.H.Corbett & M.Stewart. 2003. Structural basis for the function of Nup2p in cargo release and karyopherin recycling in nuclear import. EMBO J. 22:5358-5369.
L.Maio, O.Vanderlinde, M.Stewart & T.M.Roberts. 2003. Retraction in amoeboid cell motility powered by cytoskeletal dynamics. Science, 302:1405-1407.
R.P.Grant, D.Neuhaus & M.Stewart. (2003). Structural basis for the interaction between the Tap/NXF1 UBA domain and FG-nucleoporins at 1 Å resolution. J. Mol. Biol. 326:849-858.
Y.Matsuura & M.Stewart. 2004. Structural basis for the assembly of a nuclear export complex. Nature, 432:872-877.
S.M.Liu & M.Stewart. 2005. Structural basis of the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-b homologue, Kap95p. J. Mol. Biol. 349:515-525.
S.J.Lee, Y.Matsuura, S.M.Liu & M.Stewart. 2005. Structural basis for nuclear import complex disassembly by RanGTP. Nature, 435:693-696.
Y.Matsuura & M.Stewart. 2005. Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling. EMBO J. 24:3681-3689.
M.Stewart. 2007. Molecular mechanism of the nuclear protein import cycle. Nature Rev. Mol. Cell. Biol. 8:195-208.
M.Stewart. 2007. Ratcheting mRNA out of the nucleus. Molecular Cell, 25:327-330.
R.P.Grant, N.J.Marshall, J-C.Yang, M.B.Fasken, S.M.Kelly, M.T.Harreman, D.Neuhaus, A.H.Corbett & M.Stewart. 2008. Structure of the N-terminal Mlp1-binding domain of Nab2. J. Mol. Biol. 376:1048-1059.
M.L.Cutress, H.C.Whitaker, I.G.Mills, M.Stewart & D.E.Neal. 2008. Structural basis for the nuclear import of the androgen receptor. J. Cell Sci. 121:957-968.
L.Miao, O.Vanderlinde, J.Liu, R.P.Grant, A.Wouterse, K.Shimabukuro, A.Philipse, M.Stewart & T.M.Roberts. 2008. The role of filament packing dynamics in powering amoeboid cell motility. Proc. Natl. Acad. Sci., USA, 105:5390-5395.
K.Murakami, M.Stewart, K.Nozawa, K.Tomii, N.Kudou, N.Igarashi, Y.Shirakihara, S.Wakatsuki, T.Yasunaga, & T.Wakabayashi. 2008. Structural basis for tropomyosin overlap in thin (actin) filaments and the generation of a molecular swivel by troponin-T. Proc. Natl. Acad. Sci., USA. 105:7200-7205.
M.Fasken, M.Stewart & A.H.Corbett. 2008. Functional significance of the interaction between the mRNA-binding protein, Nab2, and the nuclear pore-associated protein, Mlp1, in mRNA export. J. Biol. Chem. 283:27130-27143.
D.Jani, S.Lutz, N.J.Marshall, T.Fischer, A.Köhler, A.M.Ellisdon, E.Hurt & M.Stewart. 2009. Sus1, Cdc31 and the Sac3 CID region form a conserved interaction platform that promotes nuclear pore association and mRNA export. Molecular Cell, 33:727-737.
V.O.Wickramasinghe, P.I.A.McMurtrie, A.D.Mills, R.Andrews, P.Ellis, Y.Takei, S.Penrhyn-Lowe, Y.Amagase, S.Main, J.Marr, C.Langford, M.Stewart & R.A.Laskey. 2010. Mammalian mRNA export requires GANP. Curr. Biol. 20:25-31.
A.Giesecke & M.Stewart. 2010. Novel binding of the mitotic regulator TPX-2 (Target protein for Xenopus kinesin-like protein 2) to importin-a. J. Biol. Chem. 285:17628-17635.
C.Schreiber, M.Stewart & T.Duke. 2010. A simulation of cell motility that reproduces the force-velocity relationship. Proc. Natl. Acad. Sci., USA. 107:9141-9146.
C.Zheng, M.B.Faskin, N.J.Marshall, C.Brockmann, M.E.Rubinson, S.R.Wente, A.H.Corbett & M.Stewart. 2010. Structural basis for the function of the Saccharomyces cerevisiae Gfd1 protein in mRNA nuclear export. J. Biol. Chem. 285:20704-20715.
J.K.Forwood, A.Lange, U.Zachariae, M.Marfori, C.Preast, H.Grubmüller, M.Stewart, A.H.Corbett & B.Kobe. 2010. Quantitative analysis of importin-b flexibility: paradigm for solenoid protein structures. Structure, 18:1171-1183.
A.M.Ellisdon, L.Dimitrova, E.Hurt & M.Stewart. 2012. Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex. Nature Struct. Mol. Biol. 19:328-336.
Jani D., Lutz S., Hurt E., Laskey R. A., Stewart M., Wickramasinghe V. O. 2012. Functional and structural characterization of the mammalian TREX-2 complex that links transcription with nuclear messenger RNA export. Nucleic Acids Research 40(10):4562-4573.
Valkov E., Dean J. C., Jani D., Kuhlmann S. I., Stewart M. 2012 Structural basis for the assembly and disassembly of mRNA nuclear export complexes. Biochimica et Biophysica Acta 1819(6):578-592.
Brockmann C., Soucek S., Kuhlmann S. I., Mills-Lujan K., Kelly S. M., Yang J. C., Iglesias N., Stutz F., Corbett A. H., Neuhaus D., Stewart M. 2012. Structural basis for polyadenosine-RNA binding by Nab2 Zn fingers and its function in mRNA nuclear export. Structure 20(6):1007-1018.
Ellisdon A. M., Stewart M. 2012. Structural biology of the PCI-protein fold. Bioarchitecture 2(4):118-123.
Sun C., Fu G., Ciziene D., Stewart M., Musser S. M. 2013. Choreography of importin-α/CAS complex assembly and disassembly at nuclear pores. Proceedings of the National Academy of Sciences, USA 110(17):E1584-93.
Kuhlmann S. I., Valkov E., Stewart M. 2014.Structural basis for the molecular recognition of polyadenosine RNA by Nab2 Zn fingers. Nucleic Acids Research 42(1):672-680.
Wickramasinghe V. O., Andrews R., Ellis P., Langford C, Gurdon J. B., Stewart M., Venkitaraman A. R., Laskey R. A. 2014. Selective nuclear export of specific classes of mRNA from mammalian nuclei is promoted by GANP. Nucleic Acids Research 42(8):5059-5071.
Jani D., Valkov E., Stewart M. 2014. Structural basis for binding the TREX2 complex to nuclear pores, GAL1 localisation and mRNA export. Nucleic Acids Research 42(10):6686-6697.
Wolf J., Valkov E., Allen M. D., Meineke B., Gordiyenko Y., McLaughlin S. H., Olsen T. M., Robinson C. V., Bycroft M., Stewart M., Passmore L. A. 2014. Structural basis for Pan3 binding to Pan2 and its function in mRNA recruitment and deadenylation. EMBO Journal 33(14):1514-1526.
Wagner R. S., Kapinos L. E., Marshall N. J., Stewart M., Lim R. Y. 2015. Promiscuous Binding of Karyopherinβ1 Modulates FG Nucleoporin Barrier Function and Expedites NTF2 Transport Kinetics. Biophysical Journal 108(4):918-927.
Aibara S., Valkov E., Lamers M., Stewart M. 2015. Domain organization within the nuclear export factor Mex67:Mtr2 generates an extended mRNA binding surface. Nucleic Acids Research 43(3):1927-1936.
Aibara S., Katahira J., Valkov E., Stewart M. 2015. The principal mRNA nuclear export factor NXF1:NXT1 forms a symmetric binding platform that facilitates export of retroviral CTE-RNA. Nucleic Acids Research 43(3):1883-1893.
Holvey R. S., Valkov E., Neal D., Stewart M., Abell C. 2015. Selective Targeting of the TPX2 Site of Importin-α Using Fragment-Based Ligand Design. ChemMedChem 10(7):1232-1239.
Aibara S., Valkov E., Lamers M. H., Dimitrova L., Hurt E., Stewart M. 2015. Structural characterization of the principal mRNA-export factor Mex67-Mtr2 from Chaetomium thermophilum. Acta Crystallographica. Section F, Structural Biology Communications 71(Pt 7):876-888.
Dimitrova L., Valkov E., Aibara S., Flemming D., McLaughlin S. H., Hurt E., Stewart M. 2015. Structural Characterization of the Chaetomium thermophilum TREX-2 Complex and its Interaction with the mRNA Nuclear Export Factor Mex67:Mtr2. Structure 23(7):1246-1257.
Valkov E., Stewart M. 2015. 1.25 A resolution structure of an RNA 20-mer that binds to the TREX2 complex. Acta Crystallographica. Section F, Structural Biology Communications 71(Pt 10):1318-1321.
Zahn R., Osmanovi? D., Ehret S., Araya Callis C., Frey S., Stewart M., You C., Görlich D., Hoogenboom B. W., Richter R. P. 2016. A physical model describing the interaction of nuclear transport receptors with FG nucleoporin domain assemblies. ELife 5:e14119.
Christie M., Chang C. W., Róna G., Smith K. M., Stewart A. G., Takeda A. A., Fontes M. R., Stewart M., Vértessy B. G., Forwood J. K., Kobe B. 2016. Structural Biology and Regulation of Protein Import into the Nucleus. Journal of Molecular Biology 428(10 Pt A):2060-2090.
Aibara S., Bai X. C., Stewart M. 2016. The Sac3 TPR-like region in the Saccharomyces cerevisiae TREX-2 complex is more extensive but independent of the CID region. Journal of Structural Biology 195(3):316-324.
Wiedmann M. M., Aibara S., Spring D. R., Stewart M., Brenton J. D. 2016. Structural and calorimetric studies demonstrate that the Hepatocyte Nuclear Factor1β (HNF1β) transcription factor is imported into the nucleus via a monopartite NLS sequence. Journal of Structural Biology 195(3):273-281.
Wiedmann M. M., Tan Y. S., Wu Y., Aibara S., Xu W., Sore H. F., Verma C. S., Itzhaki L., Stewart M., Brenton J. D., Spring D. R. 2017. Development of Cell-Permeable, Non-Helical Constrained Peptides to Target a Key Protein-Protein Interaction in Ovarian Cancer. Angewandte Chemie 56(2):524-529.
Aibara S., Gordon J. M., Riesterer A. S., McLaughlin S. H., Stewart M. 2017. Structural basis for the dimerization of Nab2 generated by RNA binding provides insight into its contribution to both poly(A) tail length determination and transcript compaction in Saccharomyces cerevisiae. Nucleic Acids Research 45(3):1529-1538.
Gordon J. M., Aibara S., Stewart M. 2017. Structure of the Sac3 RNA-binding M-region in the Saccharomyces cerevisiae TREX-2 complex. Nucleic Acids Research 45(9):5577-5585.