Robson SA, Takeuchi K, Boeszoermenyi A, Coote PW, Dubey A, Hyberts S, Wagner G, Arthanari H.
Mixed pyruvate labeling enables backbone resonance assignment of large proteins using a single experiment.
Nat Commun. 2018 Jan 24;9(1):356.
Tokunaga Y1, Takeuchi K2, Shimada I3,4.
Forbidden Coherence Transfer of 19F Nuclei to Quantitatively Measure the Dynamics of a CF -Containing Ligand in Receptor-Bound States. Molecules. 2017 Sep 7;22(9).
Takeuchi K1,2, Imai M3, Shimada I4,5.
Dynamic equilibrium on DNA defines transcriptional regulation of a multidrug transcriptional repressor, LmrR.
Sci Rep. 2017 Mar 21;7(1):267.
Mizukoshi Y1,2, Takeuchi K1, Arutaki M1,2, Tokunaga Y1,2, Takizawa T3, Hanzawa H3, Shimada I4,1.
Improvement of Ligand Affinity and Thermodynamic Properties by NMR-Based Evaluation of Local Dynamics and Surface Complementarity in the Receptor-Bound State.
Angew Chem Int Ed Engl. 2016 Nov 14;55(47):14606-14609.
Takeuchi K1,2, Arthanari H3,4, Wagner G5.
Perspective: revisiting the field dependence of TROSYsensitivity.
J Biomol NMR. 2016 Dec;66(4):221-225.
Takeuchi K, Senda M, Lo YH, Kofuji S, Ikeda Y, Sasaki AT, Senda T.
Structural reverse genetics study of the PI5P4Kβ-nucleotide complexes reveals the presence of the GTP bioenergetic system in mammalian cells.
FEBS J. 2016 Oct;283(19):3556-3562.
Takeuchi K, Arthanari H, Imai M, Wagner G, Shimada I. Nitrogen-detected TROSY yields comparable sensitivity to proton-detected TROSY for non-deuterated, large proteins under physiological salt conditions. J Biomol NMR. 2016 Feb;64(2):143-51. doi: 10.1007/s10858-016-0015-3. Epub 2016 Jan 22
Takeuchi K, Arthanari H, Shimada I, Wagner G Nitrogen detected TROSY at high field yields high resolution and sensitivity for protein NMR. J Biomol NMR. 2015 Dec;63(4):323-31. doi: 10.1007/s10858-015-9991-y. Epub 2015 Oct 23
Dynamic multidrug recognition by multidrug transcriptional repressor LmrR. Takeuchi K, Tokunaga Y, Imai M, Takahashi H, Shimada I. Sci Rep. 2014, 4, 6922. doi: 10.1038/srep06922.
NMR resonance assignments of the catalytic domain of human serine/threonine phosphatase calcineurin in unligated and PVIVIT-peptide-bound states. Takeuchi K, Sun ZY, Li S, Gal M, Wagner G. Biomol NMR Assign. 2015 Apr;9(1):201-5. doi: 10.1007/s12104-014-9574-y. Epub 2014 Sep 11
Allosteric enhancement of MAP kinase p38α's activity and substrate selectivity by docking interactions. Tokunaga Y, Takeuchi K, Takahashi H, Shimada I.
Nat Struct Mol Biol. 2014 Aug;21(8):704-11. doi: 10.1038/nsmb.2861.
The LxVP and PxIxIT NFAT motifs bind jointly to overlapping epitopes on Calcineurin's catalytic domain distant to the regulatory domain. Gal M, Li S, Luna RE, Takeuchi K, Wagner G. Structure. (2014), 22, 1016-27. doi: 10.1016/j.str.2014.05.006.
Cross-saturation and transferred cross-saturation experiments Takumi Ueda, Koh Takeuchi, Noritaka Nishida, Pavlos Stampoulis, Yutaka Kofuku, Masanori Osawa and Ichio Shimada Quarterly Reviews of Biophysics 2014, 47, 143 - 187. DOI:http://dx.doi.org/10.1017/S0033583514000043
Structure-based approach to improve a small-molecule inhibitor by the use of a competitive Peptide ligand. Ono K, Takeuchi K, Ueda H, Morita Y, Tanimura R, Shimada I, Takahashi H. Angew Chem Int Ed Engl. 2014 Mar 3;53(10):2597-601. doi: 10.1002/anie.201310749.
Degradation of Activated K-Ras Orthologue via K-Ras Specific Lysine Residues is Required for Cytokinesis.Sumita K, Yoshino H, Sasaki M, Majd N, Kahoud ER, Takahashi H, Takeuchi K, Kuroda T, Lee S, Charest PG, Takeda K, Asara JM, Firtel RA, Anastasiou D, Sasaki AT. J Biol Chem. 2013 289(7):3950-9.
Functional dynamics of cell surface membrane proteins. Nishida N, Osawa M, Takeuchi K, Imai S, Stampoulis P, Kofuku Y, Ueda T, Shimada I. J Magn Reson. 2014 241: 86-96. doi: 10.1016/j.jmr.2013.11.007.
Kodama Y, Takeuchi K, Shimba N, Ishikawa K, Suzuki E, Shimada I, Takahashi H. Rapid identification of ligand-binding sites by using an assignment-free NMR approach. J Med Chem. 2013 Nov 27;56(22):9342-50. doi: 10.1021/jm4014357.
Miyazawa-Ohnami M, Takeuchi K, Takano T, Sugiki T, Shimada I, Takahashi H, Perdeuteration and methyl-selective 1H, 13C-labeling by using a Kluyveromyces lactis expression system. J Biomol NMR, 2013, 57, 297-304
Davis MI, Sasaki AT, Shen M, Emerling BM, Thorne N, Michael S, Pragani R, Boxer M, Sumita K, Takeuchi K, Auld DS, Li Z, Cantley LC, Simenov A A homogeneous, high-throughput assay for phosphatidylinositol 5-phosphate 4-kinase with a novel, rapid substrate preparation. PLoS One. 8, 2013, e54127 Doi: 10.1371/journal.pone.0054127
Functional Equilibrium of the KcsA Structure Revealed by NMR. Imai S, Osawa M, Mita K, Toyonaga S, Machiyama A, Ueda T, Takeuchi K, Oiki S, Shimada I. J Biol Chem. 2012, 287, 39634-39641
Functional dynamics of proteins revealed by solution NMR. Osawa M, Takeuchi K, Ueda T, Nishida N, Shimada I. Curr Opin Struct Biol. 2012, Sep 20, 22, 660-669
Structural Basis for the Golgi Association by the Pleckstrin Homology Domain of the Ceramide Trafficking Protein (CERT). Sugiki T, Takeuchi K, Yamaji T, Takano T, Tokunaga Y, Kumagai K, Hanada K, Takahashi H, Shimada I. J Biol Chem. 2012 Sep 28;287(40):33706-18.
Gal M, Edmonds KA, Milbradt AG, Takeuchi K, Wagner G. Speeding up direct (15)N detection: hCaN 2D NMR experiment. J Biomol NMR. 2011, 51, 497-504.
Fukunishi Y, Mizukoshi Y, Takeuchi K, Shimada I, Takahashi H, and Nakamura H. Protein-ligand docking guided by ligand pharmacophore-mapping experiment by NMR. J Mol Graph Model. 2011, 31, 20-7.
Sasaki AT, Carracedo A, Locasale JW, Anastasiou D, Takeuchi K, Kahoud ER, Haviv S, Asara JM, Pandolfi PP, Cantley LC. Ubiquitination of k-ras enhances activation and facilitates binding to select downstream effectors. Sci Signal. 2011, 4, ra13.
Milbradt AG, Kulkarni M, Yi T, Takeuchi K, Sun ZY, Luna RE, Selenko P, Naar AM, Wagner G. Structure of the VP16 transactivator target in the Mediator. Nat Struct Mol Biol. 2011, 18, 410-418
Ｔakeuchi K, Gal M, Takahashi H, Shimada I, Wagner G. HNCA-TOCSY-CANH experiments with alternate (13)C- (12)C labeling: a set of 3D experiment with unique supra-sequential information for mainchain resonance assignment. J Biomol NMR. (2011), 49, 17-26.
Yokogawa M, Osawa M, Takeuchi K, Mase Y, Shimada I. NMR analyses of the G{beta}{gamma} binding and conformational rearrangements of the cytoplasmic pore of G protein-activated inwardly rectifying potassium channel 1 (GIRK1). J Biol Chem. (2010) 286, 2215-23.
Kim ST, Touma M, Takeuchi K, Sun ZY, Dave VP, Kappes DJ, Wagner G, Reinherz EL. Distinctive CD3 Heterodimeric Ectodomain Topologies Maximize Antigen-triggered Activation of αβ T Cell Receptors J Immunol, (2010) 185,2951-2959
Takeuchi K, Heffron G, Sun ZY, Frueh DP, Wagner G. Nitrogen-detected CAN and CON experiments as alternative experiments for main chain NMR resonance assignments. J Biomol NMR. (2010) , 47, 271-282
Takeuchi K, Sun ZY, Park S, Wagner G, Autoinhibitory Interaction in the Multidomain Adaptor Protein Nck: Possible Roles in Improving Specificity and Functional Diversity. Biochemistry. (2010), 49, 5634-5641
Takeuchi K, Frueh D, Sun ZY, Hiller S and Wagner G, CACA-TOCSY with alternate 13C-12C labeling: a 13Cα direct detection experiment for mainchain resonance assignment, dihedral angle information, and amino acid type identification" J Biomol NMR (2010), 47, 55-63
Imai S, Osawa M, Takeuchi K, and Shimada I, Structural basis underlying the dual gate properties of KcsA. Proc Natl Acad Sci U S A. (2010), 107, 6216-6221
Takeuchi K, Frueh D, Hyberts S, Sun ZY, and Wagner G, High-resolution 3D CANCA NMR experiments for complete mainchain assignments using Cα direct-detection, J Am Chem Soc (2010), 132, 2945-2951.
Hyberts, SG., Takeuchi, K., and Wagner, G. Poisson-gap sampling and forward maximum entropy reconstruction for enhancing the resolution and sensitivity of protein NMR Data. J Am Chem Soc, (2010) 132: 2145-2147.
Kim ST, Takeuchi K, Sun ZY, Touma M, Castro CE, Fahmy A, Lang MJ, Wagner G, Reinherz EL. The alphabeta T cell receptor is an anisotropic mechanosensor. J Biol Chem. 284, 31028-37, (2009).
Yokogawa M., Muramatsu T., Takeuchi K., Osawa M., Shimada I., Backbone resonance assignments for the cytoplasmic regions of G protein-activated inwardly rectifying potassium channel 1 (GIRK1). Biomol NMR Assign. 3, 125-8, (2009).
Shimada I., Ueda T., Matsumoto M., Sakakura M., Osawa M., Takeuchi K., Nishida N., Takahashi H., Cross-saturation and transferred cross-saturation experiments, Prog Nucl Magn Reson Spect, 54, 123-140, (2009)
Takeuchi K., Sun ZY., and Wagner, G., Alternate 13C-12C labeling for complete mainchain resonance assignments using C alpha direct-detection with applicability toward fast relaxing protein systems., J. Am. Chem. Soc., 130, 17210-1, (2008).
Igarashi, S., Osawa, M., Takeuchi, K., Ozawa, S., and Shimada, I., Amino acid-selective cross-saturation method for identification of proximal residue pairs in a protein-protein complex, J. Am. Chem. Soc, 130, 12168-76, (2008).
Takeuchi, K., Yang, H., Ng, E., Park, S., Sun, Z.Y., Reinherz, E.L., and Wagner, G., Structural and functional evidence that Nck interaction with CD3ε regulates T cell receptor activity, J. Mol. Biol., 180, 704-16, (2008), PMCID: PMC1989110
Takeuchi K, Takahashi H, Kawano S, Shimada I. Identification and characterization of the slowly exchanging pH-dependent conformational rearrangement in KcsA .J Biol Chem. 282, 15179-86, (2007).
Takeuchi, K., Roehrl, M.H., Sun, Z.Y. & Wagner, G. Structure of the calcineurin-NFAT complex: defining a T cell activation switch using solution NMR and crystal coordinates. Structure 15, 587-97 (2007).
Takeuchi, K., Ng, E., Malia, T.J. & Wagner, G. 1-13C amino acid selective labeling in a 2H15N background for NMR studies of large proteins. J Biomol NMR 38, 89-98 (2007).
Takeuchi, K. & Wagner, G. NMR studies of protein interactions. Curr Opin Struct Biol 16, 109-17 (2006).
Park, S., Takeuchi, K. & Wagner, G. Solution structure of the first SRC homology 3 domain of human Nck2. J Biomol NMR 34, 203-8 (2006).
Yokogawa, M., Takeuchi, K. & Shimada, I. Bead-linked proteoliposomes: a reconstitution method for NMR analyses of membrane protein-ligand interactions. J Am Chem Soc 127, 12021-7 (2005).
Sakakura, M., Takahashi, H., Terasawa, H., Takeuchi, K., Fujii, I. & Shimada, I. Backbone resonance assignments for the Fv fragment of catalytic antibody 6D9 complexed with a transition state analogue. J Biomol NMR 33, 282 (2005).
Nakamura, T., Takahashi, H., Takeuchi, K., Kohno, T., Wakamatsu, K. & Shimada, I. Direct determination of a membrane-peptide interface using the nuclear magnetic resonance cross-saturation method. Biophys J 89, 4051-5 (2005).
Takeuchi, K., Takahashi, H., Sugai, M., Iwai, H., Kohno, T., Sekimizu, K. et al. Channel-forming membrane permeabilization by an antibacterial protein, sapecin: determination of membrane-buried and oligomerization surfaces by NMR. J Biol Chem 279, 4981-7 (2004).
Lee, C.W., Lee, E.H., Takeuchi, K., Takahashi, H., Shimada, I., Sato, K. et al. Molecular basis of the high-affinity activation of type 1 ryanodine receptors by imperatoxin A. Biochem J 377, 385-94 (2004).
Takeuchi, K., Yokogawa, M., Matsuda, T., Sugai, M., Kawano, S., Kohno, T. et al. Structural basis of the KcsA K+ channel and agitoxin2 pore-blocking toxin interaction by using the transferred cross-saturation method. Structure 11, 1381-92 (2003).
Takeuchi, K., Park, E., Lee, C., Kim, J., Takahashi, H., Swartz, K., Shimada, I., Solution structure of omega-grammotoxin SIA, a gating modifier of P/Q and N-type Ca2+ channel.J Mol Biol. 321, 517-26 (2002)
Tsuji Y, Aoyama T, Takeuchi K, Homma Ki, Takahashi H, Nakajima Y, Shimada I, Natori S.Identification and characterization of an antibacterial peptide of the 26-kDa protease of Sarcophaga peregrina with antibacterial activity. J Biochem., 130, 313-8, (2001).
“Low γ-nuclei detection experiments for bimolecular NMR” Takeuchi K, Gal M, Shimada I, and Wagner G, Recent Developments in Biomolecular NMR, eds Marius Clore and Jennifer Potts, Royal Society of Chemistry, Cambridge, Chapter 2, 25-52, (2012) Doi: 10.1039/9781849735391-00025
Takeuchi, K. & Shimada, I. [Structural basis of the K+ channel inhibition by pore-blocking toxins, revealed by NMR]. Tanpakushitsu Kakusan Koso 50, 1297-302 (2005).
