Lista de obras - Yoshiaki Furukawa - Dominio Público Uruguay

A copper-deficient form of mutant Cu/Zn-superoxide dismutase as an early pathological species in amyotrophic lateral sclerosis.

artículo científico publicado en 2018

A misfolded dimer of Cu/Zn-superoxide dismutase leading to pathological oligomerization in amyotrophic lateral sclerosis.

artículo científico publicado en 2016

A molecular mechanism realizing sequence-specific recognition of nucleic acids by TDP-43.

artículo científico publicado en 2016

A primary role for disulfide formation in the productive folding of prokaryotic Cu,Zn-superoxide dismutase

artículo científico publicado en 2014

A seeded propagation of Cu, Zn-superoxide dismutase aggregates in amyotrophic lateral sclerosis.

artículo científico

A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions

artículo científico publicado en 2011

Abnormal protein oligomers for neurodegeneration

artículo científico publicado en 2017

Aggregation of FET Proteins as a Pathological Change in Amyotrophic Lateral Sclerosis

artículo científico publicado en 2016

Amyotrophic lateral sclerosis mutations have the greatest destabilizing effect on the apo- and reduced form of SOD1, leading to unfolding and oxidative aggregation.

artículo científico publicado en 2005

An essential role of N-terminal domain of copper chaperone in the enzymatic activation of Cu/Zn-superoxide dismutase

artículo científico publicado en 2017

Biochemical and morphological classification of disease-associated alpha-synuclein mutants aggregates

artículo científico publicado en 2018

Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis

artículo científico publicado en 2008

Conformational Disorder of the Most Immature Cu, Zn-Superoxide Dismutase Leading to Amyotrophic Lateral Sclerosis.

artículo científico

Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria

artículo científico publicado en 2006

Copper Homeostasis as a Therapeutic Target in Amyotrophic Lateral Sclerosis with SOD1 Mutations

artículo científico publicado en 2016

Cross-seeding fibrillation of Q/N-rich proteins offers new pathomechanism of polyglutamine diseases

artículo científico publicado en 2009

Cysteine residues in Cu,Zn-superoxide dismutase are essential to toxicity in Caenorhabditis elegans model of amyotrophic lateral sclerosis.

artículo científico publicado en 2015

Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice

artículo científico publicado en 2006

Disulfide scrambling describes the oligomer formation of superoxide dismutase (SOD1) proteins in the familial form of amyotrophic lateral sclerosis.

artículo científico publicado en 2012

Does wild-type Cu/Zn-superoxide dismutase have pathogenic roles in amyotrophic lateral sclerosis?

artículo científico publicado en 2020

Electron transfer reaction in a single protein molecule observed by total internal reflection fluorescence microscopy.

artículo científico publicado en 2005

Electron transfer reactions in Zn-substituted cytochrome P450cam.

artículo científico publicado en 2000

Elimination of TDP-43 inclusions linked to amyotrophic lateral sclerosis by a misfolding-specific intrabody with dual proteolytic signals.

artículo científico publicado en 2018

Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria.

artículo científico publicado en 2003

Functional diversity of protein fibrillar aggregates from physiology to RNA granules to neurodegenerative diseases.

artículo científico

Identification of a novel zinc-binding protein, C1orf123, as an interactor with a heavy metal-associated domain

artículo científico publicado en 2018

Immunochemical characterization on pathological oligomers of mutant Cu/Zn-superoxide dismutase in amyotrophic lateral sclerosis

artículo científico publicado en 2017

Intracellular seeded aggregation of mutant Cu,Zn-superoxide dismutase associated with amyotrophic lateral sclerosis

artículo científico publicado en 2013

Intranuclear aggregation of mutant FUS/TLS as a molecular pathomechanism of amyotrophic lateral sclerosis

artículo científico publicado en 2013

Investigation of the electron-transfer mechanism by cross-linking between Zn-substituted myoglobin and cytochrome b(5).

artículo científico publicado en 2002

Local unfolding of Cu, Zn superoxide dismutase monomer determines the morphology of fibrillar aggregates

artículo científico publicado en 2011

Molecular properties of TAR DNA binding protein-43 fragments are dependent upon its cleavage site ⬇️

artículo científico publicado el 16 de septiembre de 2011

Mutant huntingtin fragment selectively suppresses Brn-2 POU domain transcription factor to mediate hypothalamic cell dysfunction

artículo científico publicado en 2010

Mutation-dependent polymorphism of Cu,Zn-superoxide dismutase aggregates in the familial form of amyotrophic lateral sclerosis

artículo científico publicado en 2010

Oxidation-state-dependent protein docking between cytochrome c and cytochrome b(5): high-pressure laser flash photolysis study.

artículo científico publicado en 2002

Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS.

artículo científico publicado en 2004

Pathological roles of wild-type cu, zn-superoxide dismutase in amyotrophic lateral sclerosis.

artículo científico publicado en 2012

Post-aggregation oxidation of mutant huntingtin controls the interactions between aggregates.

artículo científico publicado en 2012

Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis.

artículo científico publicado en 2006

Redox environment is an intracellular factor to operate distinct pathways for aggregation of Cu,Zn-superoxide dismutase in amyotrophic lateral sclerosis.

artículo científico publicado en 2013

Regulatory Role of RNA Chaperone TDP-43 for RNA Misfolding and Repeat-Associated Translation in SCA31.

artículo científico publicado en 2017

Screening of Drugs Inhibiting In vitro Oligomerization of Cu/Zn-Superoxide Dismutase with a Mutation Causing Amyotrophic Lateral Sclerosis

artículo científico publicado en 2016

Tau protein assembles into isoform- and disulfide-dependent polymorphic fibrils with distinct structural properties.

artículo científico publicado en 2011

The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status

scientific article published on 23 August 2004

Wild-type Cu/Zn-superoxide dismutase is misfolded in cerebrospinal fluid of sporadic amyotrophic lateral sclerosis

scientific article published on 19 November 2019

Lista de obras de Yoshiaki Furukawa

A copper-deficient form of mutant Cu/Zn-superoxide dismutase as an early pathological species in amyotrophic lateral sclerosis.

A misfolded dimer of Cu/Zn-superoxide dismutase leading to pathological oligomerization in amyotrophic lateral sclerosis.

A molecular mechanism realizing sequence-specific recognition of nucleic acids by TDP-43.

A primary role for disulfide formation in the productive folding of prokaryotic Cu,Zn-superoxide dismutase

A seeded propagation of Cu, Zn-superoxide dismutase aggregates in amyotrophic lateral sclerosis.

A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions

Abnormal protein oligomers for neurodegeneration

Aggregation of FET Proteins as a Pathological Change in Amyotrophic Lateral Sclerosis

Amyotrophic lateral sclerosis mutations have the greatest destabilizing effect on the apo- and reduced form of SOD1, leading to unfolding and oxidative aggregation.

An essential role of N-terminal domain of copper chaperone in the enzymatic activation of Cu/Zn-superoxide dismutase

Biochemical and morphological classification of disease-associated alpha-synuclein mutants aggregates

Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis

Conformational Disorder of the Most Immature Cu, Zn-Superoxide Dismutase Leading to Amyotrophic Lateral Sclerosis.

Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria

Copper Homeostasis as a Therapeutic Target in Amyotrophic Lateral Sclerosis with SOD1 Mutations

Cross-seeding fibrillation of Q/N-rich proteins offers new pathomechanism of polyglutamine diseases

Cysteine residues in Cu,Zn-superoxide dismutase are essential to toxicity in Caenorhabditis elegans model of amyotrophic lateral sclerosis.

Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice

Disulfide scrambling describes the oligomer formation of superoxide dismutase (SOD1) proteins in the familial form of amyotrophic lateral sclerosis.

Does wild-type Cu/Zn-superoxide dismutase have pathogenic roles in amyotrophic lateral sclerosis?

Electron transfer reaction in a single protein molecule observed by total internal reflection fluorescence microscopy.

Electron transfer reactions in Zn-substituted cytochrome P450cam.

Elimination of TDP-43 inclusions linked to amyotrophic lateral sclerosis by a misfolding-specific intrabody with dual proteolytic signals.

Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria.

Functional diversity of protein fibrillar aggregates from physiology to RNA granules to neurodegenerative diseases.

Identification of a novel zinc-binding protein, C1orf123, as an interactor with a heavy metal-associated domain

Immunochemical characterization on pathological oligomers of mutant Cu/Zn-superoxide dismutase in amyotrophic lateral sclerosis

Intracellular seeded aggregation of mutant Cu,Zn-superoxide dismutase associated with amyotrophic lateral sclerosis

Intranuclear aggregation of mutant FUS/TLS as a molecular pathomechanism of amyotrophic lateral sclerosis

Investigation of the electron-transfer mechanism by cross-linking between Zn-substituted myoglobin and cytochrome b(5).

Local unfolding of Cu, Zn superoxide dismutase monomer determines the morphology of fibrillar aggregates

Molecular properties of TAR DNA binding protein-43 fragments are dependent upon its cleavage site ⬇️

Mutant huntingtin fragment selectively suppresses Brn-2 POU domain transcription factor to mediate hypothalamic cell dysfunction

Mutation-dependent polymorphism of Cu,Zn-superoxide dismutase aggregates in the familial form of amyotrophic lateral sclerosis

Oxidation-state-dependent protein docking between cytochrome c and cytochrome b(5): high-pressure laser flash photolysis study.

Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS.

Pathological roles of wild-type cu, zn-superoxide dismutase in amyotrophic lateral sclerosis.

Post-aggregation oxidation of mutant huntingtin controls the interactions between aggregates.

Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis.

Redox environment is an intracellular factor to operate distinct pathways for aggregation of Cu,Zn-superoxide dismutase in amyotrophic lateral sclerosis.

Regulatory Role of RNA Chaperone TDP-43 for RNA Misfolding and Repeat-Associated Translation in SCA31.

Screening of Drugs Inhibiting In vitro Oligomerization of Cu/Zn-Superoxide Dismutase with a Mutation Causing Amyotrophic Lateral Sclerosis

Tau protein assembles into isoform- and disulfide-dependent polymorphic fibrils with distinct structural properties.

The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status

Wild-type Cu/Zn-superoxide dismutase is misfolded in cerebrospinal fluid of sporadic amyotrophic lateral sclerosis