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The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS

Nature structural biology, 1996-02, Vol.3 (2), p.170-177

1996

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5 - Structure and Function of Chaperonins in Archaebacteria and Eukaryotic Cytosol

The Chaperonins, 1996, p.107-136

1996

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Absence of lipofuscin in motor neurons of SOD1-linked ALS mice

Proceedings of the National Academy of Sciences - PNAS, 2014-07, Vol.111 (30), p.11055-11060

2014

Volltextzugriff (PDF)

Advances in Protein Chemistry

1, 1945

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Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes

Nature structural & molecular biology, 2006-02, Vol.13 (2), p.147-152

2006

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Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding

Advances in Protein Chemistry, 2001, Vol.59, p.45-72

2001

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An ALS-Associated Mutant SOD1 Rapidly Suppresses KCNT1 (Slack) Na + -Activated K + Channels in Aplysia Neurons

The Journal of neuroscience, 2017-02, Vol.37 (8), p.2258-2265

2017

Volltextzugriff (PDF)

An ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans

PLoS genetics, 2009-01, Vol.5 (1), p.e1000350

2009

Volltextzugriff (PDF)

An ALS-Linked Mutant SOD1 Produces a Locomotor Defect Associated with Aggregation and Synaptic Dysfunction When Expressed in Neurons of Caenorhabditis elegans: e1000350

PLoS genetics, 2009-01, Vol.5 (1)

2009

Volltextzugriff (PDF)

ANALYSIS OF A CANDIDATE MOUSE IV (INVERSUS VISCERUM) GENE. • 123

Pediatric research, 1996-04, Vol.39, p.23-23

1996

Volltextzugriff (PDF)

Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space

Cell, 1992-03, Vol.68 (6), p.1163-1175

1992

Volltextzugriff (PDF)

Aqueductal stenosis leading to hydrocephalus-an unusual manifestation of neurofibromatosis

American journal of medical genetics, 1983-03, Vol.14 (3), p.577-581

1983

Volltextzugriff (PDF)

Archaeal-like chaperonins in bacteria

Proceedings of the National Academy of Sciences - PNAS, 2010-11, Vol.107 (47), p.20269-20274

2010

Volltextzugriff (PDF)

ATP-Bound States of GroEL Captured by Cryo-Electron Microscopy

Cell, 2001-12, Vol.107 (7), p.869-879

2001

Volltextzugriff (PDF)

ATP-triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP 7 is not the rate-limiting step of the GroEL/GroES reaction cycle

FEBS letters, 2010-03, Vol.584 (5), p.951-953

2010

Volltextzugriff (PDF)

ATP‐triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP7 is not the rate‐limiting step of the GroEL/GroES reaction cycle

FEBS letters, 2010-03, Vol.584 (5), p.951-953

2010

Volltextzugriff (PDF)

ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin

Cell, 2012-03, Vol.149 (1), p.113-123

2012

Volltextzugriff (PDF)

A biochemical screen for GroEL/GroES inhibitors

Bioorganic & medicinal chemistry letters, 2014-02, Vol.24 (3), p.786-789

2014

Volltextzugriff (PDF)

A carboxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic phenotype in Escherichia coli K-12

Journal of Bacteriology, 1994-11, Vol.176 (22), p.6980-6985

1994

Volltextzugriff (PDF)

cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains

Proceedings of the National Academy of Sciences - PNAS, 2009-02, Vol.106 (6), p.1772-1777

2009

Volltextzugriff (PDF)

A cDNA clone for the precursor of rat mitochondrial ornithine transcarbamylase: comparison of rat and human leader sequences and conservation of catalytic sites

Nucleic acids research, 1985-02, Vol.13 (3), p.943-952

1985

Volltextzugriff (PDF)

Cell biology Sight at the end of the tunnel

Nature, 2004-09, Vol.431 (7008), p.520-522

Horwich, Arthur

2004

Volltextzugriff (PDF)

Chaperone Rings in Protein Folding and Degradation

Proceedings of the National Academy of Sciences - PNAS, 1999-09, Vol.96 (20), p.11033-11040

1999

Volltextzugriff (PDF)

Chaperoned Protein Disaggregation—The ClpB Ring Uses Its Central Channel

Cell, 2004-11, Vol.119 (5), p.579-581

Horwich, Arthur L.

2004

Volltextzugriff (PDF)

Chaperonin-assisted protein folding: a chronologue

Quarterly reviews of biophysics, 2020-01, Vol.53, p.e4-e4, Article e4

2020

Volltextzugriff (PDF)

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The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS

5 - Structure and Function of Chaperonins in Archaebacteria and Eukaryotic Cytosol

Absence of lipofuscin in motor neurons of SOD1-linked ALS mice

Advances in Protein Chemistry

Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes

Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding

An ALS-Associated Mutant SOD1 Rapidly Suppresses KCNT1 (Slack) Na + -Activated K + Channels in Aplysia Neurons

An ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans

An ALS-Linked Mutant SOD1 Produces a Locomotor Defect Associated with Aggregation and Synaptic Dysfunction When Expressed in Neurons of Caenorhabditis elegans: e1000350

ANALYSIS OF A CANDIDATE MOUSE IV (INVERSUS VISCERUM) GENE. • 123

Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space

Aqueductal stenosis leading to hydrocephalus-an unusual manifestation of neurofibromatosis

Archaeal-like chaperonins in bacteria

ATP-Bound States of GroEL Captured by Cryo-Electron Microscopy

ATP-triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP 7 is not the rate-limiting step of the GroEL/GroES reaction cycle

ATP‐triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP7 is not the rate‐limiting step of the GroEL/GroES reaction cycle

ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin

A biochemical screen for GroEL/GroES inhibitors

A carboxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic phenotype in Escherichia coli K-12

cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains

A cDNA clone for the precursor of rat mitochondrial ornithine transcarbamylase: comparison of rat and human leader sequences and conservation of catalytic sites

Cell biology Sight at the end of the tunnel

Chaperone Rings in Protein Folding and Degradation

Chaperoned Protein Disaggregation—The ClpB Ring Uses Its Central Channel

Chaperonin-assisted protein folding: a chronologue

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