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6 results on '"Dohmae N"'

1. Structure and Activity of the RNA-Targeting Type III-B CRISPR-Cas Complex of Thermus thermophilus

Author

Biomolecular Mass Spectrometry and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., Sub Biomol.Mass Spect. and Proteomics, Staals, R.H.J., Agari, Y., Maki-Yonekura, S., Zhu, Y., Taylor, D.W., van Duijn, E., Barendregt, A., Vlot, M.C., Koehorst, J.J., Sakamoto, K., Masuda, A., Dohmae, N., Schaap, P.J., Doudna, J.A., Heck, A.J.R., Yonekura, K., van der Oost, J., Shinkai, A., Biomolecular Mass Spectrometry and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., Sub Biomol.Mass Spect. and Proteomics, Staals, R.H.J., Agari, Y., Maki-Yonekura, S., Zhu, Y., Taylor, D.W., van Duijn, E., Barendregt, A., Vlot, M.C., Koehorst, J.J., Sakamoto, K., Masuda, A., Dohmae, N., Schaap, P.J., Doudna, J.A., Heck, A.J.R., Yonekura, K., van der Oost, J., and Shinkai, A.

Published
2013

2. Structure and Activity of the RNA-Targeting Type III-B CRISPR-Cas Complex of Thermus thermophilus

Author

Biomolecular Mass Spectrometry and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., Sub Biomol.Mass Spect. and Proteomics, Staals, R.H.J., Agari, Y., Maki-Yonekura, S., Zhu, Y., Taylor, D.W., van Duijn, E., Barendregt, A., Vlot, M.C., Koehorst, J.J., Sakamoto, K., Masuda, A., Dohmae, N., Schaap, P.J., Doudna, J.A., Heck, A.J.R., Yonekura, K., van der Oost, J., Shinkai, A., Biomolecular Mass Spectrometry and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., Sub Biomol.Mass Spect. and Proteomics, Staals, R.H.J., Agari, Y., Maki-Yonekura, S., Zhu, Y., Taylor, D.W., van Duijn, E., Barendregt, A., Vlot, M.C., Koehorst, J.J., Sakamoto, K., Masuda, A., Dohmae, N., Schaap, P.J., Doudna, J.A., Heck, A.J.R., Yonekura, K., van der Oost, J., and Shinkai, A.

Published
2013

3. Structure and Activity of the RNA-Targeting Type III-B CRISPR-Cas Complex of Thermus thermophilus

Author

Biomolecular Mass Spectrometry and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., Sub Biomol.Mass Spect. and Proteomics, Staals, R.H.J., Agari, Y., Maki-Yonekura, S., Zhu, Y., Taylor, D.W., van Duijn, E., Barendregt, A., Vlot, M.C., Koehorst, J.J., Sakamoto, K., Masuda, A., Dohmae, N., Schaap, P.J., Doudna, J.A., Heck, A.J.R., Yonekura, K., van der Oost, J., Shinkai, A., Biomolecular Mass Spectrometry and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., Sub Biomol.Mass Spect. and Proteomics, Staals, R.H.J., Agari, Y., Maki-Yonekura, S., Zhu, Y., Taylor, D.W., van Duijn, E., Barendregt, A., Vlot, M.C., Koehorst, J.J., Sakamoto, K., Masuda, A., Dohmae, N., Schaap, P.J., Doudna, J.A., Heck, A.J.R., Yonekura, K., van der Oost, J., and Shinkai, A.

Published
2013

4. Structure and Activity of the RNA-Targeting Type III-B CRISPR-Cas Complex of Thermus thermophilus

Author

Staals, R.H.J., Agari, Y., Maki-Yonekura, S., Zhu, Y., Taylor, D.W., van Duijn, E., Barendregt, A., Vlot, M., Koehorst, J.J., Sakamoto, K., Masuda, A., Dohmae, N., Schaap, P.J., Doudna, J.A., Heck, A., Yonekura, K., van der Oost, J., Shinkai, A., Staals, R.H.J., Agari, Y., Maki-Yonekura, S., Zhu, Y., Taylor, D.W., van Duijn, E., Barendregt, A., Vlot, M., Koehorst, J.J., Sakamoto, K., Masuda, A., Dohmae, N., Schaap, P.J., Doudna, J.A., Heck, A., Yonekura, K., van der Oost, J., and Shinkai, A.

Abstract

The CRISPR-Cas system is a prokaryotic host defense system against genetic elements. The Type III-B CRISPR-Cas system of the bacterium Thermus thermophilus, the TtCmr complex, is composed of six different protein subunits (Cmr1-6) and one crRNA with a stoichiometry of Cmr112131445361:crRNA1. The TtCmr complex copurifies with crRNA species of 40 and 46 nt, originating from a distinct subset of CRISPR loci and spacers. The TtCmr complex cleaves the target RNA at multiple sites with 6 nt intervals via a 5' ruler mechanism. Electron microscopy revealed that the structure of TtCmr resembles a "sea worm" and is composed of a Cmr2-3 heterodimer "tail," a helical backbone of Cmr4 subunits capped by Cmr5 subunits, and a curled "head" containing Cmr1 and Cmr6. Despite having a backbone of only four Cmr4 subunits and being both longer and narrower, the overall architecture of TtCmr resembles that of Type I Cascade complexes

Published
2013

5. A viable strategy for screening the effects of glycan heterogeneity on target organ adhesion and biodistribution in live mice

Author

Vong K., Suzuki T., Dohmae N., Kurbangalieva A., Watanabe Y., Tanaka K., Vong K., Suzuki T., Dohmae N., Kurbangalieva A., Watanabe Y., and Tanaka K.

Abstract

© 2018 The Royal Society of Chemistry. This work represents the first broad study of testing diverse heterogenous glycoconjugates (7 different glycoalbumins) for their differential in vivo binding (11 different cancer cell types) in both cell- and animal-based studies. As a result, various changes in biodistribution, excretion, and even tumor adhesion were observed.

6. In Situ Ligation of High- and Low-Affinity Ligands to Cell Surface Receptors Enables Highly Selective Recognition

Author

Taichi M., Nomura S., Nakase I., Imamaki R., Kizuka Y., Ota F., Dohmae N., Kitazume S., Taniguchi N., Tanaka K., Taichi M., Nomura S., Nakase I., Imamaki R., Kizuka Y., Ota F., Dohmae N., Kitazume S., Taniguchi N., and Tanaka K.

Abstract

© 2017 The Authors. Published by WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. This paper reports an entirely unexplored concept of simultaneously recognizing two receptors using high- and low-affinity ligands through ligating them in situ on the target cell surface. This de novo approach is inspired by the pretargeting strategy frequently applied in molecular imaging, and has now evolved as the basis of a new paradigm for visualizing target cells with a high imaging contrast. A distinct advantage of using a labeled low-affinity ligand such as glycan is that the excess labeled ligand can be washed away from the cells, whereas the ligand bound to the cell, even at the milli molar affinity level, can be anchored by a bioorthogonal reaction with a pretargeted high-affinity ligand on the surface. Consequently, nonspecific background is minimized, leading to improved imaging contrast. Importantly, despite previously unexplored for molecular imaging, a notoriously weak glycan/lectin interaction can now be utilized as a highly selective ligand to the targets.

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