H. Taguchi

发表

beta-Helix is a likely core structure of yeast prion Sup35 amyloid fibers.

A. Kishimoto, K. Hasegawa, Hirofumi Suzuki, 2004, Biochemical and biophysical research communications.

On the Maximum Size of Proteins to Stay and Fold in the Cavity of GroEL underneath GroES*

H. Taguchi, M. Yoshida, C. Sakikawa, 1999, The Journal of Biological Chemistry.

Co-translational Involvement of the Chaperonin GroEL in the Folding of Newly Translated Polypeptides*

H. Taguchi, Bei-Wen Ying, T. Ueda, 2005, Journal of Biological Chemistry.

Semibiological molecular machine with an implemented "AND" logic gate for regulation of protein folding.

H. Taguchi, T. Aida, K. Kinbara, 2006, Journal of the American Chemical Society.

Difference in the distribution pattern of substrate enzymes in the metabolic network of Escherichia coli, according to chaperonin requirement

Kazuhiro Takemoto, Hideki Taguchi, Tatsuya Niwa, 2011, BMC Systems Biology.

Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity.

Hideki Taguchi, So Iwata, Masasuke Yoshida, 2004, Structure.

Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of Escherichia coli proteins

Shoji Takada, Takuya Ueda, Hideki Taguchi, 2009, Proceedings of the National Academy of Sciences.

Chaperone-assisted folding of a single-chain antibody in a reconstituted translation system.

H. Taguchi, Bei-Wen Ying, T. Ueda, 2004, Biochemical and biophysical research communications.

Single-molecule observation of protein–protein interactions in the chaperonin system

Hideki Taguchi, Taro Ueno, Masasuke Yoshida, 2001, Nature Biotechnology.

Amphiphilic polysaccharide nanogels as artificial chaperones in cell-free protein synthesis.

H. Taguchi, K. Akiyoshi, Y. Sasaki, 2011, Macromolecular bioscience.

Peptide sequences converting polyglutamine into a prion in yeast

H. Taguchi, H. Koyama, M. Kinjo, 2015, The FEBS journal.

Nascent SecM chain interacts with outer ribosomal surface to stabilize translation arrest

H. Taguchi, T. Funatsu, R. Iizuka, 2020, The Biochemical journal.

G-quadruplex-proximity protein labeling based on peroxidase activity.

H. Taguchi, Hiroyuki Nakamura, Shinichi Sato, 2020, Chemical communications.

Heat-inactivated Proteins Managed by DnaKJ-GrpE-ClpB Chaperones Are Released as a Chaperonin-recognizable Non-native Form*

H. Taguchi, Masasuke Yoshida, K. Motohashi, 2000, The Journal of Biological Chemistry.

Chaperone Properties of Mammalian Mitochondrial Translation Elongation Factor Tu*

H. Taguchi, Hiroaki Suzuki, T. Ueda, 2006, Journal of Biological Chemistry.

Novel trans-translation-associated gene regulation revealed by prophage excision-triggered switching of ribosome rescue pathway

H. Taguchi, Tatsuya Niwa, Haruka Onodera, 2022, bioRxiv.

Chaperonin from thermophile Thermus thermophilus.

H. Taguchi, M. Yoshida, 1998, Methods in enzymology.

Nano-Scale Alignment of Proteins on a Flexible DNA Backbone

H. Taguchi, Masasuke Yoshida, N. Kodera, 2012, PloS one.

Single molecule imaging of the trans-translation entry process via anchoring of the tagged ribosome.

H. Taguchi, Koichi Ito, Y. Shimizu, 2011, Journal of biochemistry.

Intracellular photocatalytic-proximity labeling for profiling protein-protein interactions in microenvironments.

H. Taguchi, Hiroyuki Nakamura, Shinichi Sato, 2022, Chemical communications.

Analysis of interaction between chaperonin GroEL and its substrate using fluorescence correlation spectroscopy.

H. Taguchi, M. Tamura, M. Yoshida, 1999, Cytometry.

Global analysis of chaperone effects using a reconstituted cell-free translation system

Takuya Ueda, Hideki Taguchi, Tatsuya Niwa, 2012, Proceedings of the National Academy of Sciences.

Proteome Analysis of Phase-Separated Condensed Proteins with Ionic Surfactants Revealed Versatile Formation of Artificial Biomolecular Condensates.

H. Taguchi, Tatsuya Niwa, T. Nojima, 2018, Biomacromolecules.

Cryo-EM structure of the native GroEL-GroES complex from thermus thermophilus encapsulating substrate inside the cavity.

H. Taguchi, K. Yokoyama, K. Mitsuoka, 2009, Structure.

[Molecular chaperone].

H. Taguchi, M. Yoshida, K. Motohashi, 1994, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme.

Isolation of the stable hexameric DnaK.DnaJ complex from Thermus thermophilus.

H. Taguchi, M. Yoshida, N. Ishii, 1994, The Journal of biological chemistry.

Anatomy of footprint extension in ribosome profiling reveals translational landscape mediated by S1 protein in bacteria

H. Taguchi, M. Shirouzu, Shintaro Iwasaki, 2020 .

Shotgun Proteomics Revealed Preferential Degradation of Misfolded In Vivo Obligate GroE Substrates by Lon Protease in Escherichia coli

H. Taguchi, Tatsuya Niwa, Yuhei Chadani, 2022, Molecules.

Purification and molecular cloning of the group II chaperonin from the acidothermophilic archaeon, Sulfolobus sp. strain 7.

H. Taguchi, M. Yohda, I. Endo, 1997, Biochemical and biophysical research communications.

Conversion of a PROTAC Mutant Huntingtin Degrader into Small-Molecule Hydrophobic Tags Focusing on Drug-like Properties.

H. Taguchi, S. Nakagawa, Y. Hashimoto, 2022, ACS medicinal chemistry letters.

The landscape of translational stall sites in bacteria revealed by monosome and disome profiling

H. Taguchi, M. Shirouzu, Shintaro Iwasaki, 2021, RNA.

A method to enrich polypeptidyl-tRNAs to capture snapshots of translation in the cell

H. Taguchi, Tatsuya Niwa, Yuhei Chadani, 2022, bioRxiv.

Invitro transcription–translation using bacterial genome as a template to reconstitute intracellular proﬁle

H. Taguchi, N. Doi, Kei Fujiwara, 2017 .

Single mother–daughter pair analysis to clarify the diffusion properties of yeast prion Sup35 in guanidine‐HCl‐treated [PSI+] cells

H. Taguchi, M. Kinjo, C. Pack, 2009, Genes to cells : devoted to molecular & cellular mechanisms.

Mechanism of methionine synthase overexpression in chaperonin-depleted Escherichia coli.

H. Taguchi, Kei Fujiwara, 2012, Microbiology.

Amyloid conformation-dependent disaggregation in a reconstituted yeast prion system

H. Taguchi, Y. Sako, M. Shirouzu, 2022, Nature Chemical Biology.

Preparation of Thermus thermophilus holo-chaperonin-immobilized microspheres with high ability to facilitate protein refolding.

H. Taguchi, A. Kondo, H. Fukuda, 2000, Biotechnology and bioengineering.

Tailoring micrometer-long high-integrity 1D array of superparamagnetic nanoparticles in a nanotubular protein jacket and its lateral magnetic assembling behavior.

H. Taguchi, T. Aida, Daigo Miyajima, 2015, Journal of the American Chemical Society.

V-Type H+-ATPase/Synthase from a Thermophilic Eubacterium, Thermus Thermophilus

H. Taguchi, K. Yokoyama, M. Yoshida, 2000, The Journal of Biological Chemistry.

Analysis of interaction between chaperonin GroEL and its substrate using fluorescence correlation spectroscopy.

H. Taguchi, M. Tamura, M. Yoshida, 1999, Cytometry.

A chaperonin from a thermophilic bacterium, Thermus thermophilus.

H. Taguchi, E. Muneyuki, M. Yoshida, 1993, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

Proximity Histidine Labeling by Umpolung Strategy Using Singlet Oxygen.

H. Taguchi, Hiroyuki Nakamura, M. Ishikawa, 2021, Journal of the American Chemical Society.

Running Title: Interaction network of yeast prions in live cells Keywords: yeast prions, remodeling factors, fluorescence cross-correlation spectroscopy, live cell, protein interaction Supplementary Materials and Methods Plasmid Construction Open reading frame (ORF) sequences of SUP35, RNQ1, URE2, a

H. Taguchi, E. Craig, C. Pack, 2017 .

The Absence of Thioredoxin m1 and Thioredoxin C in Anabaena sp. PCC 7120 Leads to Oxidative Stress

H. Taguchi, T. Hisabori, Frédéric Deschoenmaeker, 2018, Plant & cell physiology.

Disruption of the Gene trx-m1 Impedes the Growth of Anabaena sp. PCC 7120 under Nitrogen Starvation.

H. Taguchi, Jiro Nomata, T. Hisabori, 2019, Plant & cell physiology.

FUS regulates RAN translation through modulating the G-quadruplex structure of GGGGCC repeat RNA in C9orf72-linked ALS/FTD

H. Taguchi, L. Petrucelli, K. Nakatani, 2022, bioRxiv.

Image analysis by electron microscopy of two-dimensional crystals developed on a mercury surface of chaperonin from Thermus thermophilus.

H. Taguchi, M. Yoshida, K. Nagayama, 1991, Journal of biochemistry.

Thioredoxin pathway in anabaena sp. PCC 7120: activity of NADPH-thioredoxin reductase C.

H. Taguchi, H. Shimizu, T. Hisabori, 2021, Journal of biochemistry.

Application of fluorescence correlation spectroscopy to investigate the dynamics of a ribosome-associated trigger factor in Escherichia coli

H. Taguchi, Koichi Ito, H. Tadakuma, 2022, Frontiers in Molecular Biosciences.

Heterogeneous interaction network of yeast prions and remodeling factors detected in live cells

H. Taguchi, E. Craig, C. Pack, 2017, BMB reports.

Single-particle tracking of quantum dot-conjugated prion proteins inside yeast cells.

H. Taguchi, M. Kinjo, Hideki Terajima, 2011, Biochemical and biophysical research communications.

Archaeal group II chaperonin mediates protein folding in the cis-cavity without a detachable GroES-like co-chaperonin.

H. Taguchi, Masasuke Yoshida, M. Yohda, 2002, Journal of molecular biology.

Highly stereocontrolled total synthesis of leukotriene B4, 20-hydroxyleukotriene B4, leukotriene B3, and their analogs

H. Taguchi, Yuichi Kobayashi, F. Sato, 1990 .

Biomolecular robotics for chemomechanically driven guest delivery fuelled by intracellular ATP.

H. Taguchi, T. Aida, K. Kataoka, 2013, Nature chemistry.

Supramolecular Nanotube of Chaperonin GroEL: Length Control for Cellular Uptake Using Single-Ring GroEL Mutant as End-Capper.

H. Taguchi, T. Aida, Tatsuya Niwa, 2016, Journal of the American Chemical Society.

Comprehensive study of liposome-assisted synthesis of membrane proteins using a reconstituted cell-free translation system

H. Taguchi, Shugo Nakamura, K. Akiyoshi, 2015, Scientific Reports.

Catalyst-proximity protein chemical labelling on affinity beads targeting endogenous lectins.

H. Taguchi, Hiroyuki Nakamura, Shinichi Sato, 2019, Chemical Communications.

The evolutionary conserved iron-sulfur protein TCR controls P700 oxidation in photosystem I

H. Taguchi, Jiro Nomata, T. Hisabori, 2021, iScience.

Large-scale analysis of macromolecular crowding effects on protein aggregation using a reconstituted cell-free translation system

H. Taguchi, Shugo Nakamura, T. Ueda, 2015, Front. Microbiol..

Molecular cloning of the human methylthioadenosine phosphorylase processed pseudogene and localization to 3q28.

H. Taguchi, P. Tran, D. Carson, 1997, Gene.

A chaperonin from a thermophilic bacterium, Thermus thermophilus, that controls refoldings of several thermophilic enzymes.

H. Taguchi, M. Yoshida, N. Ishii, 1991, The Journal of biological chemistry.

Chaperonin GroEL meets the substrate protein as a "load" of the rings.

H. Taguchi, 2005, Journal of biochemistry.

A systematic survey of in vivo obligate chaperonin‐dependent substrates

H. Taguchi, Y. Ishihama, K. Nakahigashi, 2010, The EMBO journal.

Large-scale aggregation analysis of eukaryotic proteins reveals an involvement of intrinsically disordered regions in protein folding

H. Taguchi, M. Ota, S. Fukuchi, 2018, Scientific Reports.

D-loop of Actin Differently Regulates the Motor Function of Myosins II and V*

H. Taguchi, S. Ishiwata, H. Kubota, 2009, The Journal of Biological Chemistry.

Yeast prion protein New1 can break Sup35 amyloid fibrils into fragments in an ATP‐dependent manner

H. Taguchi, Masasuke Yoshida, A. Koike-Takeshita, 2011, Genes to cells : devoted to molecular & cellular mechanisms.

Effect of thrombomodulin on the kinetics of the interaction of thrombin with substrates and inhibitors.

H. Taguchi, J. Hofsteenge, S. Stone, 1986, The Biochemical journal.

Single-molecule imaging of full protein synthesis by immobilized ribosomes

H. Taguchi, J. Puglisi, S. Uemura, 2008, Nucleic acids research.

Amyloid oligomers: diffuse oligomer‐based transmission of yeast prions

H. Taguchi, S. Kawai-Noma, 2010, The FEBS journal.

Integrated in vivo and in vitro nascent chain profiling reveals widespread translational pausing

H. Taguchi, Koreaki Ito, Tatsuya Niwa, 2016, Proceedings of the National Academy of Sciences.

Prophage excision switches the primary ribosome rescue pathway and rescue‐associated gene regulations in Escherichia coli

H. Taguchi, Tatsuya Niwa, Haruka Onodera, 2022, Molecular microbiology.

Nascent polypeptide within the exit tunnel stabilizes the ribosome to counteract risky translation

H. Taguchi, Shintaro Iwasaki, Tatsuya Niwa, 2021, The EMBO journal.

Escherichia coli small heat shock protein IbpA is an aggregation‐sensor that self‐regulates its own expression at posttranscriptional levels

H. Taguchi, Yuhei Chadani, T. Miwa, 2020, Molecular microbiology.

Escherichia coli small heat shock protein IbpA is an aggregation-sensor that self-regulates its own expression at a translational level

H. Taguchi, Yuhei Chadani, T. Miwa, 2020, bioRxiv.

In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells

H. Taguchi, Y. Hiraoka, T. Haraguchi, 2010, The Journal of cell biology.

Structural properties of cellulose and cellulase reaction mechanism

H. Taguchi, H. Taguchi, Sun Bok Lee, 1983, Biotechnology and bioengineering.

Intrinsic Ribosome Destabilization Underlies Translation and Provides an Organism with a Strategy of Environmental Sensing.

H. Taguchi, Tsutomu Suzuki, Koreaki Ito, 2017, Molecular cell.

Identification of novel in vivo obligate GroEL/ES substrates based on data from a cell‐free proteomics approach

H. Taguchi, Kei Fujiwara, Tatsuya Niwa, 2016, FEBS letters.

Hsp104 Binds to Yeast Sup35 Prion Fiber but Needs Other Factor(s) to Sever It*

A. Kishimoto, H. Taguchi, Masasuke Yoshida, 2004, Journal of Biological Chemistry.

The Interaction Networks of E. coli Chaperones

H. Taguchi, 2014 .

The interaction of Hsp104 with yeast prion Sup35 as analyzed by fluorescence cross-correlation spectroscopy.

H. Taguchi, M. Kinjo, C. Pack, 2013, Biochemical and biophysical research communications.

Stabilization of FtsH-unfolded protein complex by binding of ATP and blocking of protease.

H. Taguchi, Masasuke Yoshida, K. Motohashi, 2002, Biochemical and biophysical research communications.

Nascent peptide-induced translation discontinuation in eukaryotes impacts biased amino acid usage in proteomes

H. Taguchi, H. Imataka, Tatsuya Niwa, 2022, bioRxiv.

Title Effects of C-terminal Truncation of Chaperonin GroEL on the Yield of In-cage Folding of the Green Fluorescent Protein

H. Taguchi, K. Matsuzaki, Y. Kawata, 2016 .

Effects of C-terminal Truncation of Chaperonin GroEL on the Yield of In-cage Folding of the Green Fluorescent Protein*

H. Taguchi, K. Matsuzaki, Y. Kawata, 2015, The Journal of Biological Chemistry.

Kinetic Analysis of Conformational Changes of GroEL Based on the Fluorescence of Tyrosine 506

H. Taguchi, Masasuke Yoshida, T. Funatsu, 2008, The protein journal.

Co-translational Binding of GroEL to Nascent Polypeptides Is Followed by Post-translational Encapsulation by GroES to Mediate Protein Folding*

H. Taguchi, Bei-Wen Ying, T. Ueda, 2006, Journal of Biological Chemistry.

GroEL mediates protein folding with a two successive timer mechanism.

H. Taguchi, Masasuke Yoshida, T. Funatsu, 2004, Molecular cell.

Crystal structure of chaperonin-60 from Paracoccus denitrificans.

H. Taguchi, M. Yohda, M. Yoshida, 2001, Journal of molecular biology.

Protein refolding system using holo-chaperonin from the thermophilic bacterium Thermus thermophilus

H. Taguchi, A. Kondo, H. Fukuda, 1998 .

ATP-, K+-dependent Heptamer Exchange Reaction Produces Hybrids between GroEL and Chaperonin from Thermus thermophilus *

H. Taguchi, Masasuke Yoshida, N. Murai, 1997, The Journal of Biological Chemistry.

Chaperonin-mediated Folding of Green Fluorescent Protein*

H. Taguchi, Masasuke Yoshida, Y. Makino, 1997, The Journal of Biological Chemistry.

Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin

H. Taguchi, Masasuke Yoshida, 1995, FEBS letters.

Assembly of the Yeast Prion Ure2p into Protein Fibrils

H. Taguchi, R. Melki, L. Bousset, 2003, Journal of Biological Chemistry.

Prediction of chaperonin GroE substrates using small structural patterns of proteins

H. Taguchi, M. Ota, R. Koike, 2023, FEBS open bio.

Reaction Cycle of Chaperonin GroEL via Symmetric "Football" Intermediate.

H. Taguchi, 2015, Journal of molecular biology.

Conversion of a Chaperonin GroEL-independent Protein into an Obligate Substrate*

H. Taguchi, T. Ishimoto, Kei Fujiwara, 2014, The Journal of Biological Chemistry.

Asp-52 in Combination with Asp-398 Plays a Critical Role in ATP Hydrolysis of Chaperonin GroEL*

H. Taguchi, K. Mitsuoka, A. Koike-Takeshita, 2014, The Journal of Biological Chemistry.

Flexibility of GroES mobile loop is required for efficient chaperonin function.

H. Taguchi, Masasuke Yoshida, T. Ikegami, 2012, Journal of molecular biology.

Revisiting the GroEL-GroES Reaction Cycle via the Symmetric Intermediate Implied by Novel Aspects of the GroEL(D398A) Mutant*♦

H. Taguchi, Masasuke Yoshida, A. Koike-Takeshita, 2008, Journal of Biological Chemistry.

BeFx Stops the Chaperonin Cycle of GroEL-GroES and Generates a Complex with Double Folding Chambers*

H. Taguchi, Masasuke Yoshida, A. Koike-Takeshita, 2004, Journal of Biological Chemistry.

Kinetic analysis of interactions between GroEL and reduced alpha-lactalbumin. Effect of GroES and nucleotides.

H. Taguchi, M. Yoshida, N. Murai, 1995, The Journal of biological chemistry.

Folding intermediate binds to the bottom of bullet-shaped holo-chaperonin and is readily accessible to antibody.

H. Taguchi, H. Sasabe, M. Yoshida, 1994, Journal of molecular biology.

Structure of holo‐chaperonin studied with electron microscopy Oligomeric cpn10 on top of two layers of cpn60 rings with two stripes each

H. Taguchi, Masasuke Yoshida, N. Ishii, 1992, FEBS letters.

Comparison of refolding activities between nanogel artificial chaperone and GroEL systems.

H. Taguchi, K. Akiyoshi, Wakiko Asayama, 2008, International journal of biological macromolecules.

Molecular Mechanism of Chaperonin GroEL: The Role of ATP and the Substrate Protein

H. Taguchi, 2006 .

Specific interaction between GroEL and denatured protein measured by compression-free force spectroscopy.

H. Taguchi, A. Ikai, Ryohei Kokawa, 2003, Biophysical journal.

Leu309 Plays a Critical Role in the Encapsulation of Substrate Protein into the Internal Cavity of GroEL*

H. Taguchi, Masasuke Yoshida, K. Yokoyama, 2006, Journal of Biological Chemistry.

Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP

H. Taguchi, Masasuke Yoshida, Y. Makino, 1993, FEBS letters.

GroEL Binds Artificial Proteins with Random Sequences*

H. Taguchi, Masasuke Yoshida, T. Yomo, 2000, The Journal of Biological Chemistry.

Equatorial split of holo‐chaperonin from Thermus thermophilus by ATP and K+

H. Taguchi, Masasuke Yoshida, N. Ishii, 1995, FEBS letters.

Fibrillar Structures of Yeast Prion Sup35 In Vivo

H. Taguchi, S. Kawai-Noma, 2014 .

Strong Growth Polarity of Yeast Prion Fiber Revealed by Single Fiber Imaging*

A. Kishimoto, H. Taguchi, Masasuke Yoshida, 2001, The Journal of Biological Chemistry.

Chaperonin from Thermus thermophilus can protect several enzymes from irreversible heat denaturation by capturing denaturation intermediate.

H. Taguchi, M. Yoshida, 1993, The Journal of biological chemistry.

Calorimetric Observation of a GroEL-Protein Binding Reaction with Little Contribution of Hydrophobic Interaction*

H. Taguchi, Masasuke Yoshida, K. Yutani, 1997, The Journal of Biological Chemistry.

Dynamics of yeast prion aggregates in single living cells

H. Taguchi, Masasuke Yoshida, K. Yasuda, 2006, Genes to cells : devoted to molecular & cellular mechanisms.

Filamentous Morphology in GroE-Depleted Escherichia coli Induced by Impaired Folding of FtsE

H. Taguchi, Kei Fujiwara, 2007, Journal of bacteriology.

In vivo client proteins of the chaperonin GroEL-GroES provide insight into the role of chaperones in protein evolution

H. Taguchi, A. Koike-Takeshita, 2023, Frontiers in Molecular Biosciences.

Crystallization of the chaperonin GroEL-GroES complex from Thermus thermophilus HB8.

H. Taguchi, Masasuke Yoshida, S. Iwata, 2003, Acta crystallographica. Section D, Biological crystallography.

Synchronized Domain-opening Motion of GroEL Is Essential for Communication between the Two Rings*

H. Taguchi, Masasuke Yoshida, T. Hisabori, 2001, The Journal of Biological Chemistry.

Monomeric chaperonin-60 and its 50-kDa fragment possess the ability to interact with non-native proteins, to suppress aggregation, and to promote protein folding.

H. Taguchi, M. Yoshida, Y. Makino, 1994, The Journal of biological chemistry.

Trigger Factor from Thermus thermophilus Is a Zn2+-dependent Chaperone*

H. Taguchi, Masasuke Yoshida, R. Masui, 2004, Journal of Biological Chemistry.

Crystal structure of a symmetric football-shaped GroEL:GroES2-ATP14 complex determined at 3.8Å reveals rearrangement between two GroEL rings.

H. Taguchi, T. Shimamura, T. Arakawa, 2014, Journal of molecular biology.

Kinetic Analysis of Interactions between GroEL and Reduced α-Lactalbumin

H. Taguchi, Masasuke Yoshida, N. Murai, 1995, The Journal of Biological Chemistry.

Effect of electrostatic interactions on the binding of charged substrate to GroEL studied by highly sensitive fluorescence correlation spectroscopy.

H. Taguchi, M. Tamura, M. Yoshida, 2000, Biochemical and biophysical research communications.

Isolation of ubiquitin-E2 (ubiquitin-conjugating enzyme) complexes from erythroleukaemia cells using immunoaffinity techniques.

H. Taguchi, H. Yokosawa, Y. Okawa, 2001, The Biochemical journal.

The effects of induced production of reactive oxygen species in organelles on endoplasmic reticulum stress and on the unfolded protein response in arabidopsis

H. Taguchi, K. Matsuzaki, Y. Kawata, 2015 .

Single-molecule Analyses of the Dynamics of Heat Shock Protein 104 (Hsp104) and Protein Aggregates*

H. Taguchi, Tatsuya Niwa, Momoko Okuda, 2015, The Journal of Biological Chemistry.

Molecularly Engineered "Janus GroEL": Application to Supramolecular Copolymerization with a Higher Level of Sequence Control.

H. Taguchi, T. Aida, Y. Ishida, 2020, Journal of the American Chemical Society.

Acetate overflow metabolism regulates a major metabolic shift after glucose depletion in Escherichia coli

H. Taguchi, T. Shimada, Kan Tanaka, 2021, FEBS letters.

C9orf72-derived arginine-rich poly-dipeptides impede phase modifiers

H. Taguchi, N. Kodera, Mari Nakanishi, 2021, Nature Communications.

Reconstitution of C9orf72 (GGGGCC) repeat-associated non-AUG translation with purified components

H. Taguchi, H. Imataka, M. Ueyama, 2023, bioRxiv.

Nascent polypeptide within the exit tunnel ensures continuous translation elongation by stabilizing the translating ribosome

H. Taguchi, Shintaro Iwasaki, Tatsuya Niwa, 2021, bioRxiv.

[Mechanism of chaperonin function].

H. Taguchi, Masasuke Yoshida, Y. Kawata, 2004, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme.

Protein Nanotube Selectively Cleavable with DNA: Supramolecular Polymerization of "DNA-Appended Molecular Chaperones".

H. Taguchi, T. Aida, Tatsuya Niwa, 2018, Journal of the American Chemical Society.

A tubular biocontainer: metal ion-induced 1D assembly of a molecularly engineered chaperonin.

H. Taguchi, T. Aida, K. Kinbara, 2009, Journal of the American Chemical Society.

Amyloid conformation-dependent disaggregation revealed by a reconstituted yeast prion system

H. Taguchi, Y. Sako, M. Shirouzu, 2020 .

Dynamics of oligomer and amyloid fibril formation by yeast prion Sup35 observed by high-speed atomic force microscopy

H. Taguchi, T. Ando, N. Kodera, 2020, Proceedings of the National Academy of Sciences.

Structure of the Chaperonin-Substrate Complex

H. Taguchi, K. Mitsuoka, A. Koike-Takeshita, 2009 .

FUS regulates RAN translation through modulating the G-quadruplex structure of GGGGCC repeat RNA in C9orf72-linked ALS/FTD

H. Taguchi, L. Petrucelli, K. Nakatani, 2023, bioRxiv.

BODIPY Catalyzes Proximity‐Dependent Histidine Labelling

H. Taguchi, Hiroyuki Nakamura, Tatsuya Niwa, 2022, ChemCatChem.

Novel self-regulation strategy of a small heat shock protein for prodigious and rapid expression on demand

H. Taguchi, Tsukumi Miwa, 2021, Current Genetics.

The beauty and complexity of the small heat shock proteins: a report on the proceedings of the fourth workshop on small heat shock proteins.

H. Taguchi, W. Lau, R. Klevit, 2023, Cell stress & chaperones.

Electrostatic interactions between middle domain motif-1 and the AAA1 module of the bacterial ClpB chaperone are essential for protein disaggregation

H. Taguchi, Kumiko Watanabe, Tatsuya Niwa, 2018, The Journal of Biological Chemistry.

Large-scale aggregation analysis of eukaryotic proteins reveals an involvement of intrinsically disordered regions in protein folding

H. Taguchi, M. Ota, S. Fukuchi, 2018, Scientific Reports.

Translation‐coupled protein folding assay using a protease to monitor the folding status

H. Taguchi, Tatsuya Niwa, Y. Matsuno, 2019, Protein science : a publication of the Protein Society.

The Escherichia coli small heat shock protein IbpA plays a role in regulating the heat shock response by controlling the translation of σ32

H. Taguchi, Tsukumi Miwa, 2023, bioRxiv.

The mRNA binding-mediated self-regulatory function of small heat shock protein IbpA in γ-proteobacteria is conferred by a conserved arginine

H. Taguchi, Yajie Cheng, Tsukumi Miwa, 2023, The Journal of biological chemistry.

In vitro transcription–translation using bacterial genome as a template to reconstitute intracellular profile

H. Taguchi, N. Doi, S. Nomura, 2017, Nucleic acids research.

Molecular cloning, expression, and characterization of chaperonin-60 and chaperonin-10 from a thermophilic bacterium, Thermus thermophilus HB8.

H. Taguchi, M. Yohda, I. Endo, 1995, Journal of biochemistry.

A systematic survey of in vivo obligate chaperonin‐dependent substrates

H. Taguchi, Y. Ishihama, K. Nakahigashi, 2010, The EMBO journal.

Biomolecular robotics for chemomechanically driven guest delivery fuelled by intracellular ATP.

H. Taguchi, T. Aida, K. Kataoka, 2013, Nature chemistry.

A LEA model peptide protects the function of a red fluorescent protein in the dry state

H. Taguchi, M. Sakurai, T. Kikawada, 2018, Biochemistry and biophysics reports.

Self-regulatory function of bacterial small heat shock protein IbpA through mRNA binding is conferred by a conserved arginine

H. Taguchi, Yajie Cheng, Tsukumi Miwa, 2023, bioRxiv.

Flexibility of GroES mobile loop is required for efficient chaperonin function.

H. Taguchi, Masasuke Yoshida, T. Ikegami, 2012, Journal of molecular biology.

Intrinsic Ribosome Destabilization Underlies Translation and Provides an Organism with a Strategy of Environmental Sensing.

H. Taguchi, Tsutomu Suzuki, Koreaki Ito, 2017, Molecular cell.