Tamotsu Zako

Tamotsu Zako

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Tamotsu Zako

Publications by authors named "Tamotsu Zako"

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Detection of Gold Nanoparticles Aggregation Using Light Scattering for Molecular Sensing.

Anal Sci 2019 Jun 1;35(6):685-690. Epub 2019 Mar 1.

Department of Chemistry and Biology, Graduate School of Science and Engineering, Ehime University.

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http://dx.doi.org/10.2116/analsci.18P571DOI Listing
June 2019

Toxicity of insulin-derived amyloidosis: a case report.

BMC Endocr Disord 2019 Jun 13;19(1):61. Epub 2019 Jun 13.

Department of Metabolism and Endocrinology, Tokyo Medical University Ibaraki Medical Center, 3-20-1 Chuou, Ami, Ibaraki, 300-0395, Japan.

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http://dx.doi.org/10.1186/s12902-019-0385-0DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6567432PMC
June 2019

Molecular chaperone prefoldin-assisted biosynthesis of gold nanoparticles with improved size distribution and dispersion.

Biomater Sci 2019 Apr;7(5):1801-1804

Department of Applied Chemistry, Graduate School of Engineering, Kyushu University, Motooka 744, Nishi-ku, Fukuoka 819-0395, Japan.

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http://dx.doi.org/10.1039/c8bm01026aDOI Listing
April 2019

Clinical and MRI characteristics and follow-up studies of insulin-derived amyloidosis.

Amyloid 2019;26(sup1):156-157

a Department of Metabolism and Endocrinology, Tokyo Medical University Ibaraki Medical Center , Ibaraki , Japan.

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http://dx.doi.org/10.1080/13506129.2019.1582517DOI Listing
January 2019

Construction of Quenchbodies to detect and image amyloid β oligomers.

Anal Biochem 2018 06 18;550:61-67. Epub 2018 Apr 18.

Laboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama, Kanagawa 226-8503 Japan. Electronic address:

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http://dx.doi.org/10.1016/j.ab.2018.04.016DOI Listing
June 2018

Prefoldin, a jellyfish-like molecular chaperone: functional cooperation with a group II chaperonin and beyond.

Biophys Rev 2018 Apr 9;10(2):339-345. Epub 2018 Feb 9.

Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, 2-4-16 Naka-cho, Koganei, Tokyo, 184-8588, Japan.

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http://dx.doi.org/10.1007/s12551-018-0400-0DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5899742PMC
April 2018

Dark Field Microscopic Sensitive Detection of Amyloid Fibrils Using Gold Nanoparticles Modified with Antibody.

Anal Sci 2016 ;32(3):307-11

Department of Advanced Materials Science, School of Frontier Sciences, The University of Tokyo.

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http://dx.doi.org/10.2116/analsci.32.307DOI Listing
December 2016

Amorphous protein aggregation monitored using fluorescence self-quenching.

FEBS Lett 2016 Oct 18;590(20):3501-3509. Epub 2016 Oct 18.

Department of Biotechnology and Life Science, Graduate School of Engineering, Tokyo University of Agriculture and Technology, Koganei-shi, Japan.

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http://dx.doi.org/10.1002/1873-3468.12439DOI Listing
October 2016

1,5-Diazacyclooctanes, as Exclusive Oxidative Polyamine Metabolites, Inhibit Amyloid-(1-40) Fibrillization.

Adv Sci (Weinh) 2016 10 1;3(10):1600082. Epub 2016 Jun 1.

Biofunctional Synthetic Chemistry Laboratory RIKEN Hirosawa, Wako-shi Saitama 351-0198 Japan; Biofunctional Chemistry Laboratory A. Butlerov Institute of Chemistry Kazan Federal University 18 Kremlyovskaya Street Kazan 420008 Russia; JST-PRESTO Hirosawa, Wako-shi Saitama 351-0198 Japan.

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http://dx.doi.org/10.1002/advs.201600082DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5096251PMC
October 2016

Extra-luminal detection of assumed colonic tumor site by near-infrared laparoscopy.

Surg Endosc 2016 09 10;30(9):4153-9. Epub 2015 Dec 10.

Bioengineering Laboratory, RIKEN Institute, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan.

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http://dx.doi.org/10.1007/s00464-015-4669-9DOI Listing
September 2016

Contribution of the C-Terminal Region of a Group II Chaperonin to its Interaction with Prefoldin and Substrate Transfer.

J Mol Biol 2016 06 11;428(11):2405-2417. Epub 2016 Apr 11.

Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Tokyo, Japan. Electronic address:

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http://dx.doi.org/10.1016/j.jmb.2016.04.006DOI Listing
June 2016

Nanoscopic and photonic ultrastructural characterization of two distinct insulin amyloid states.

Int J Mol Sci 2012 1;13(2):1461-80. Epub 2012 Feb 1.

Department of Physics, Norwegian University of Science and Technology,7491 Trondheim, Norway; E-Mails: (K.M.P.-A.); (J.D.); (B.T.S.).

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http://dx.doi.org/10.3390/ijms13021461DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3291971PMC
July 2015

Cancer-targeted near infrared imaging using rare earth ion-doped ceramic nanoparticles.

Biomater Sci 2015 Jan 2;3(1):59-64. Epub 2014 Sep 2.

Bioengineering Laboratory, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.

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http://xlink.rsc.org/?DOI=C4BM00232F
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http://dx.doi.org/10.1039/c4bm00232fDOI Listing
January 2015

Cysteine inhibits amyloid fibrillation of lysozyme and directs the formation of small worm-like aggregates through non-covalent interactions.

Biotechnol Prog 2014 Mar-Apr;30(2):470-8. Epub 2014 Jan 16.

Faculty of Pure and Applied Sciences, University of Tsukuba, Tsukuba, Ibaraki, 305-8573, Japan.

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http://dx.doi.org/10.1002/btpr.1866DOI Listing
December 2014

Cysteine inhibits the fibrillisation and cytotoxicity of amyloid-β 40 and 42: implications for the contribution of the thiophilic interaction.

Phys Chem Chem Phys 2014 Feb;16(8):3566-72

Faculty of Pure and Applied Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8573, Japan.

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http://dx.doi.org/10.1039/c3cp54245aDOI Listing
February 2014

Rapid surface-biostructure interaction analysis using strong metal-based nanomagnets.

Langmuir 2013 Nov 8;29(46):14117-23. Epub 2013 Nov 8.

ETH Zurich, Institute for Chemical and Bioengineering , Wolfgang-Pauli-Strasse 10, CH-8093 Zurich, Switzerland.

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http://dx.doi.org/10.1021/la4026427DOI Listing
November 2013

Detection of DNA induced gold nanoparticle aggregation with dark field imaging.

Chem Commun (Camb) 2013 Sep;49(68):7531-3

Department of Advanced Materials Science, School of Frontier Sciences, The University of Tokyo, Kashiwa, Chiba 227-8561, Japan.

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http://dx.doi.org/10.1039/c3cc44182bDOI Listing
September 2013

Human prefoldin inhibits amyloid-β (Aβ) fibrillation and contributes to formation of nontoxic Aβ aggregates.

Biochemistry 2013 May 8;52(20):3532-42. Epub 2013 May 8.

Bioengineering Laboratory, RIKEN , 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.

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http://dx.doi.org/10.1021/bi301705cDOI Listing
May 2013

Formation of non-toxic Aβ fibrils by small heat shock protein under heat-stress conditions.

Biochem Biophys Res Commun 2013 Jan 19;430(4):1259-64. Epub 2012 Dec 19.

Bioengineering Laboratory, RIKEN Institute, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.

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http://dx.doi.org/10.1016/j.bbrc.2012.12.059DOI Listing
January 2013

Naked-eye detection of amyloid aggregates using gold nanoparticles modified with amyloid beta antibody.

Anal Sci 2012 ;28(1):73

PRESTO, Japan Science and Technology Agency, Sanbancho, Chiyoda, Tokyo, Japan.

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http://dx.doi.org/10.2116/analsci.28.73DOI Listing
June 2012

Analysis of the interaction mode between hyperthermophilic archaeal group II chaperonin and prefoldin using a platform of chaperonin oligomers of various subunit arrangements.

Biochim Biophys Acta 2010 Sep 6;1804(9):1810-6. Epub 2010 May 6.

Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei-shi, Tokyo 184-8588, Japan.

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http://dx.doi.org/10.1016/j.bbapap.2010.04.013DOI Listing
September 2010

A facile method towards cyclic assembly of gold nanoparticles using DNA template alone.

Chem Commun (Camb) 2010 Sep 27;46(33):6132-4. Epub 2010 Jul 27.

Bioengineering Laboratory, RIKEN Institute, Wako, Japan.

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http://dx.doi.org/10.1039/c0cc00305kDOI Listing
September 2010

Thermodynamic characterization of the interaction between prefoldin and group II chaperonin.

J Mol Biol 2010 Jun 29;399(4):628-36. Epub 2010 Apr 29.

Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei-shi, Tokyo 184-8588, Japan.

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http://dx.doi.org/10.1016/j.jmb.2010.04.046DOI Listing
June 2010

Amyloid oligomers: formation and toxicity of Abeta oligomers.

FEBS J 2010 Mar 9;277(6):1348-58. Epub 2010 Feb 9.

Bioengineering Laboratory, RIKEN Institute, Wako, Saitama, Japan.

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http://dx.doi.org/10.1111/j.1742-4658.2010.07568.xDOI Listing
March 2010

Amyloid oligomers.

Authors:
Tamotsu Zako

FEBS J 2010 Mar 9;277(6):1347. Epub 2010 Feb 9.

RIKEN Institute, Japan.

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http://dx.doi.org/10.1111/j.1742-4658.2010.07567.xDOI Listing
March 2010

Hyperthermophilic archaeal prefoldin shows refolding activity at low temperature.

Biochem Biophys Res Commun 2010 Jan 15;391(1):467-70. Epub 2009 Nov 15.

Bioengineering Laboratory, RIKEN Institute, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.

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http://dx.doi.org/10.1016/j.bbrc.2009.11.081DOI Listing
January 2010

Cyclic RGD peptide-labeled upconversion nanophosphors for tumor cell-targeted imaging.

Biochem Biophys Res Commun 2009 Mar 8;381(1):54-8. Epub 2009 Feb 8.

Bioengineering Laboratory, RIKEN Institute, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.

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http://dx.doi.org/10.1016/j.bbrc.2009.02.004DOI Listing
March 2009

Formation of highly toxic soluble amyloid beta oligomers by the molecular chaperone prefoldin.

FEBS J 2008 Dec;275(23):5982-93

Bioengineering Laboratory, RIKEN Institute, Saitama, Japan.

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http://dx.doi.org/10.1111/j.1742-4658.2008.06727.xDOI Listing
December 2008

Kinetic analysis of conformational changes of GroEL based on the fluorescence of tyrosine 506.

Protein J 2008 Dec;27(7-8):461-8

Major in Integrated Bioscience and Biomedical Engineering, Graduate School of Science and Engineering, Waseda University, Shinjuku-ku, Tokyo 169-8555, Japan.

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http://dx.doi.org/10.1007/s10930-008-9157-9DOI Listing
December 2008

Dynamics of group II chaperonin and prefoldin probed by 13C NMR spectroscopy.

Proteins 2008 Mar;70(4):1257-63

Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan.

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http://doi.wiley.com/10.1002/prot.21606
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http://dx.doi.org/10.1002/prot.21606DOI Listing
March 2008

Localization of prefoldin interaction sites in the hyperthermophilic group II chaperonin and correlations between binding rate and protein transfer rate.

J Mol Biol 2006 Nov 5;364(1):110-20. Epub 2006 Sep 5.

Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Koganei-Shi, Tokyo, Japan.

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http://dx.doi.org/10.1016/j.jmb.2006.08.088DOI Listing
November 2006

Contribution of the C-terminal region to the thermostability of the archaeal group II chaperonin from Thermococcus sp. strain KS-1.

Extremophiles 2006 Oct 10;10(5):451-9. Epub 2006 May 10.

Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, 184-8588 Koganei, Tokyo, Japan.

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http://dx.doi.org/10.1007/s00792-006-0519-yDOI Listing
October 2006

Characterization of archaeal group II chaperonin-ADP-metal fluoride complexes: implications that group II chaperonins operate as a "two-stroke engine".

J Biol Chem 2005 Dec 23;280(48):40375-83. Epub 2005 Sep 23.

Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-8588, Japan.

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http://www.jbc.org/content/early/2005/09/23/jbc.M506785200.f
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http://www.jbc.org/cgi/doi/10.1074/jbc.M506785200
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http://dx.doi.org/10.1074/jbc.M506785200DOI Listing
December 2005

Genetically engineered active Qbeta replicase in rabbit reticulocyte cell-free system: a fusion protein of EF-Tu and EF-Ts is functional as the subunit of Qbeta replicase.

J Biosci Bioeng 2002 ;93(1):20-4

Department of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.

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November 2005

Interaction of a small heat shock protein of the fission yeast, Schizosaccharomyces pombe, with a denatured protein at elevated temperature.

J Biol Chem 2005 Sep 29;280(38):32586-93. Epub 2005 Jul 29.

Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, 2-24-16, Naka-cho, Koganei-shi, Tokyo 184-8588.

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http://dx.doi.org/10.1074/jbc.M504121200DOI Listing
September 2005

The role of firefly luciferase C-terminal domain in efficient coupling of adenylation and oxidative steps.

FEBS Lett 2005 Aug;579(20):4389-94

Department of Chemistry and Biotechnology, School of Engineering, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.

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http://dx.doi.org/10.1016/j.febslet.2005.07.004DOI Listing
August 2005

Nanoscale patterning of protein using electron beam lithography of organosilane self-assembled monolayers.

Small 2005 Aug;1(8-9):833-7

Nanotechnology Research Center and Institute of Biomedical Engineering, Waseda University, Waseda Tsurumaki-cho 513, Shinjuku-ku, Tokyo 162-0041, Japan.

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http://dx.doi.org/10.1002/smll.200500091DOI Listing
August 2005

Facilitated release of substrate protein from prefoldin by chaperonin.

FEBS Lett 2005 Jul;579(17):3718-24

Department of Physics, School of Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjyuku-ku, Tokyo 169-8555, Japan.

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http://dx.doi.org/10.1016/j.febslet.2005.05.061DOI Listing
July 2005

Kinetics and binding sites for interaction of the prefoldin with a group II chaperonin: contiguous non-native substrate and chaperonin binding sites in the archaeal prefoldin.

J Biol Chem 2004 Jul 15;279(30):31788-95. Epub 2004 May 15.

Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, 2-24-16, Naka-cho, Koganei, Tokyo 184-8588, Japan.

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http://dx.doi.org/10.1074/jbc.M402889200DOI Listing
July 2004

Measuring adsorption of a hydrophobic probe with a surface plasmon resonance sensor to monitor conformational changes in immobilized proteins.

Biotechnol Prog 2003 Jul-Aug;19(4):1348-54

Department of Chemistry and Biotechnology, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.

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http://dx.doi.org/10.1021/bp034015nDOI Listing
June 2004

[Reaction mechanism of archaeal molecular chaperones].

Tanpakushitsu Kakusan Koso 2004 May;49(7 Suppl):858-61

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May 2004

Role of the helical protrusion in the conformational change and molecular chaperone activity of the archaeal group II chaperonin.

J Biol Chem 2004 Apr 20;279(18):18834-9. Epub 2004 Feb 20.

Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-8588, Japan.

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http://dx.doi.org/10.1074/jbc.M400839200DOI Listing
April 2004

Luminescent and substrate binding activities of firefly luciferase N-terminal domain.

Biochim Biophys Acta 2003 Jul;1649(2):183-9

Department of Chemistry and Biotechnology, School of Engineering, University of Tokyo, 7-3-1 Hongo, Bunkyo, Tokyo 113-8656, Japan.

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http://dx.doi.org/10.1016/s1570-9639(03)00179-1DOI Listing
July 2003