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Chemistry

D-Index
89
Citations
27043
World Ranking
2184
National Ranking
119

Overview

Yuji Goto is affiliated with Osaka University in Japan and has contributed extensively to the fields of Medicine and Biochemistry, Genetics and Molecular Biology. Their research spans multiple subfields, including Molecular Biology, Physiology, Neurology, Genetics, and Biomaterials.

The research topics covered by Yuji Goto include:

  • Alzheimer's disease research and treatments
  • Protein Structure and Dynamics
  • Parkinson's Disease Mechanisms and Treatments
  • Amyloidosis: Diagnosis, Treatment, Outcomes
  • Prion Diseases and Protein Misfolding
  • Enzyme Structure and Function
  • Supramolecular Self-Assembly in Materials

Yuji Goto's frequent coauthors include:

  • K. Yamaguchi
  • Kichitaro Nakajima
  • Masatomo So
  • Kensuke Ikenaka
  • Hideki Mochizuki

Publications by Yuji Goto have appeared prominently in the following venues:

  • Journal of Biological Chemistry
  • bioRxiv (Cold Spring Harbor Laboratory)
  • Biophysical Journal
  • Chemistry - A European Journal
  • Nucleic Acids Research

Among their recent papers are:

  • "BeStSel: webserver for secondary structure and fold prediction for protein CD spectroscopy" (2022) published in Nucleic Acids Research
  • "Breakdown of supersaturation barrier links protein folding to amyloid formation" (2021) published in Communications Biology
  • "Current Understanding of the Structure, Stability and Dynamic Properties of Amyloid Fibrils" (2021) published in International Journal of Molecular Sciences
  • "Two-step screening method to identify α-synuclein aggregation inhibitors for Parkinson's disease" (2022) published in Scientific Reports
  • "Isoelectric point-amyloid formation of α-synuclein extends the generality of the solubility and supersaturation-limited mechanism" (2020) published in Current Research in Structural Biology

Best Publications

  • Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy

    András Micsonai;Frank Wien;Linda Kernya;Young Ho Lee

  • BeStSel: a web server for accurate protein secondary structure prediction and fold recognition from the circular dichroism spectra.

    András Micsonai;Frank Wien;Éva Bulyáki;Judit Kun

  • Mechanism of acid induced folding of proteins

    Yuji Goto;Nobuaki Takahashi;Anthony L. Fink

  • Acid-induced folding of proteins

    Yuji Goto;Linda J. Calciano;Anthony L. Fink

  • Classification of Acid Denaturation of Proteins: Intermediates and Unfolded States

    Anthony L. Fink;Linda J. Calciano;Yuji Goto;Takuzo Kurotsu

  • Conformational states in .beta.-lactamase: molten-globule states at acidic and alkaline pH with high salt

    Yuji Goto;Anthony L. Fink

  • Trifluoroethanol-induced stabilization of the alpha-helical structure of beta-lactoglobulin: implication for non-hierarchical protein folding.

    Kentaro Shiraki;Ken Nishikawa;Yuji Goto

  • BeStSel: webserver for secondary structure and fold prediction for protein CD spectroscopy

    Unknown

  • Clustering of Fluorine-Substituted Alcohols as a Factor Responsible for Their Marked Effects on Proteins and Peptides

    Dong-Pyo Hong;Masaru Hoshino;Ryoichi Kuboi;Yuji Goto

  • Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence.

    Tadato Ban;Daizo Hamada;Kazuhiro Hasegawa;Hironobu Naiki

  • A toxic monomeric conformer of the polyglutamine protein.

    Yoshitaka Nagai;Takashi Inui;Takashi Inui;Takashi Inui;H Akiko Popiel;Nobuhiro Fujikake

  • Mapping the core of the beta(2)-microglobulin amyloid fibril by H/D exchange.

    Masaru Hoshino;Hidenori Katou;Yoshihisa Hagihara;Yoshihisa Hagihara;Kazuhiro Hasegawa

  • Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation

    Yuichi Yoshimura;Yuxi Lin;Hisashi Yagi;Young-Ho Lee

  • Molten globule of cytochrome c studied by small angle X-ray scattering.

    Mikio Kataoka;Yoshihisa Hagihara;Ken'ichi Mihara;Yuji Goto

  • Direct observation of Aβ amyloid fibril growth and inhibition

    Tadato Ban;Masaru Hoshino;Satoshi Takahashi;Daizo Hamada

  • Group additive contributions to the alcohol-induced alpha-helix formation of melittin: implication for the mechanism of the alcohol effects on proteins.

    Nami Hirota;Kazuko Mizuno;Yuji Goto

  • Protein folding by the effects of macromolecular crowding

    Nobuhiko Tokuriki;Masataka Kinjo;Shigeru Negi;Masaru Hoshino

  • 3D structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR

    Kentaro Iwata;Toshimichi Fujiwara;Yoh Matsuki;Hideo Akutsu

  • Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein

    Unknown

  • Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering.

    M. Kataoka;K. Kuwajima;F. Tokunaga;Y. Goto

  • Cooperative α‐helix formation of β‐lactoglobulin and melittin induced by hexafluoroisopropanol

    Unknown

  • Low Concentrations of Sodium Dodecyl Sulfate Induce the Extension of β2-Microglobulin-Related Amyloid Fibrils at a Neutral pH†

    Suguru Yamamoto;Kazuhiro Hasegawa;Itaru Yamaguchi;Shinobu Tsutsumi

  • Structural and kinetic characterization of early folding events in β-lactoglobulin

    Kazuo Kuwata;Ramachandra Shastry;Hong Cheng;Masaru Hoshino

Frequent Co-Authors

Hironobu Naiki
Hironobu Naiki University of Fukui
Satoshi Takahashi
Satoshi Takahashi Tohoku University
Kunihiro Kuwajima
Kunihiro Kuwajima Tokyo University of Science
Teizo Kitagawa
Teizo Kitagawa University of Hyogo
Mikio Kataoka
Mikio Kataoka Nara Institute of Science and Technology
Anthony L. Fink
Anthony L. Fink University of California, Santa Cruz
Saburo Aimoto
Saburo Aimoto Osaka University
Hideki Mochizuki
Hideki Mochizuki Osaka University
Toshiharu Hase
Toshiharu Hase Osaka University
Tomoji Kawai
Tomoji Kawai Osaka University

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