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Publications by Kazuto Shigematsu

Deletion of N-Terminal Residues 23–88 From Prion Protein (PrP) Abrogates the Potential to Rescue PrP-deficient Mice From PrP-like Protein/Doppel-Induced Neurodegeneration

Journal of Biological Chemistry

English

Related publications

The PrP-like Protein Doppel Binds Copper

Journal of Biological Chemistry

English

Prion Protein (PrP) Synthetic Peptides Induce Cellular PrP to Acquire Properties of the Scrapie Isoform.

Proceedings of the National Academy of Sciences of the United States of America

Multidisciplinary

1995

English

Β-Amyloid 42; Prion Protein (PRNP; PrP; CD230)

Science-Business eXchange

2012

English

A Scrapie-Like Unfolding Intermediate of the Prion Protein Domain PrP(121-231) Induced by Acidic pH

Proceedings of the National Academy of Sciences of the United States of America

Multidisciplinary

1998

English

Knockdown of Prion Protein (PrP) by RNA Interference Weakens the Protective Activity of Wild-Type PrP Against Copper Ion and Antagonizes the Cytotoxicity of fCJD-associated PrP Mutants in Cultured Cells

International Journal of Molecular Medicine

Medicine

Genetics

2011

English

Elucidation of the Molecular Basis of Abnormal Prion Protein (PrP) Formation in a Cell-Free System Using Baculovirus and Insect Cell-Derived Recombinant PrP

Yakugaku Zasshi

Pharmacology

Pharmaceutical Science

2019

English

A 7-kDa Prion Protein (PrP) Fragment, an Integral Component of the PrP Region Required for Infectivity, Is the Major Amyloid Protein in Gerstmann-Sträussler-Scheinker Disease A117V

Journal of Biological Chemistry

English

Endoplasmic Reticulum Stress, PrP Trafficking, and Neurodegeneration

Developmental Cell

Biochemistry

Developmental Biology

English

Prion Infections and Anti-PrP Antibodies Trigger Converging Neurotoxic Pathways

English

Amanote Research

Discover open access scientific publications

Search, annotate, share and cite publications

Publications by Kazuto Shigematsu

Deletion of N-Terminal Residues 23–88 From Prion Protein (PrP) Abrogates the Potential to Rescue PrP-deficient Mice From PrP-like Protein/Doppel-Induced Neurodegeneration

Related publications

The PrP-like Protein Doppel Binds Copper

Prion Protein (PrP) Synthetic Peptides Induce Cellular PrP to Acquire Properties of the Scrapie Isoform.

Β-Amyloid 42; Prion Protein (PRNP; PrP; CD230)

A Scrapie-Like Unfolding Intermediate of the Prion Protein Domain PrP(121-231) Induced by Acidic pH

Knockdown of Prion Protein (PrP) by RNA Interference Weakens the Protective Activity of Wild-Type PrP Against Copper Ion and Antagonizes the Cytotoxicity of fCJD-associated PrP Mutants in Cultured Cells

Elucidation of the Molecular Basis of Abnormal Prion Protein (PrP) Formation in a Cell-Free System Using Baculovirus and Insect Cell-Derived Recombinant PrP

A 7-kDa Prion Protein (PrP) Fragment, an Integral Component of the PrP Region Required for Infectivity, Is the Major Amyloid Protein in Gerstmann-Sträussler-Scheinker Disease A117V

Endoplasmic Reticulum Stress, PrP Trafficking, and Neurodegeneration

Prion Infections and Anti-PrP Antibodies Trigger Converging Neurotoxic Pathways