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Hsp70 chaperones: Cellular functions and molecular mechanism

Cellular and molecular life sciences : CMLS, 2005-03, Vol.62 (6), Article 670

2005

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Hsp70 chaperones: cellular functions and molecular mechanism

Cellular and molecular life sciences : CMLS, 2005-03, Vol.62 (6), p.670-684

2005

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ClpS is an essential component of the N-end rule pathway in Escherichia coli

Nature, 2006-02, Vol.439 (7077), p.753-756

2006

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Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK

FEBS letters, 2004-02, Vol.559 (1), p.181-187

2004

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Protein folding and degradation in bacteria: to degrade or not to degrade? That is the question

Cellular and molecular life sciences : CMLS, 2002-10, Vol.59 (10), p.1607-1616

2002

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DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat‐induced protein damage

The EMBO journal, 1993-11, Vol.12 (11), p.4137-4144

1993

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Three-State Equilibrium of Escherichia coli Trigger Factor

Biological chemistry, 2002-10, Vol.383 (10), p.1611-1619

2002

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Mechanism of substrate recognition by Hsp70 chaperones

Biochemical Society transactions, 2004-08, Vol.32 (Pt 4), p.617-621

2004

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Functional Dissection of Escherichia coli Trigger Factor: Unraveling the Function of Individual Domains

Journal of Bacteriology, 2004-06, Vol.186 (12), p.3777-3784

2004

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Protein Turnover: A CHIP Programmed for Proteolysis

Current biology, 2002-01, Vol.12 (1), p.R26-R28

2002

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Cyanobacterial ClpC/HSP100 Protein Displays Intrinsic Chaperone Activity

The Journal of biological chemistry, 2006-03, Vol.281 (9), p.5468-5475

2006

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The ATP Hydrolysis-Dependent Reaction Cycle of the Escherichia coli Hsp70 System-DnaK, DnaJ, and GrpE

Proceedings of the National Academy of Sciences - PNAS, 1994-10, Vol.91 (22), p.10345-10349

1994

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GPD1 Specifically Marks Dormant Glioma Stem Cells with a Distinct Metabolic Profile

Cell stem cell, 2019-08, Vol.25 (2), p.241-257.e8

2019

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Escherichia coli Trigger Factor is a Prolyl isomerase that Associates with Nascent Polypeptide Chains

Proceedings of the National Academy of Sciences - PNAS, 1996-04, Vol.93 (9), p.4437-4441

1996

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Molecular Basis for Interactions of the DnaK Chaperone with Substrates

Biological chemistry, 2000-09, Vol.381 (9-10), p.877-885

2000

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Integrating protein homeostasis strategies in prokaryotes

Cold Spring Harbor perspectives in biology, 2011-04, Vol.3 (4), p.a004366-a004366

2011

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Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor

The EMBO journal, 2006-06, Vol.25 (11), p.2510-2518

2006

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Stand-alone ClpG disaggregase confers superior heat tolerance to bacteria

Proceedings of the National Academy of Sciences - PNAS, 2018-01, Vol.115 (2), p.E273-E282

2018

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Allosteric Regulation of Hsp70 Chaperones by a Proline Switch

Molecular cell, 2006-02, Vol.21 (3), p.359-367

2006

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Stand-alone CIpG disaggregase confers superior heat tolerance to bacteria

Proceedings of the National Academy of Sciences - PNAS, 2018-01, Vol.115 (2), p.E273

2018

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Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation

Molecular microbiology, 2003-10, Vol.50 (2), p.585-595

2003

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Functional Dissection of Trigger Factor and DnaK: Interactions with Nascent Polypeptides and Thermally Denatured Proteins

Biological chemistry, 2001-08, Vol.382 (8), p.1235-1243

2001

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The Hsp70 and Hsp60 Chaperone Machines

Cell, 1998-02, Vol.92 (3), p.351-366

1998

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Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins

Nature, 2004-09, Vol.431 (7008), p.590-596

2004

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Thermotolerance Requires Refolding of Aggregated Proteins by Substrate Translocation through the Central Pore of ClpB

Cell, 2004-11, Vol.119 (5), p.653-665

2004

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Hsp70 chaperones: Cellular functions and molecular mechanism

Hsp70 chaperones: cellular functions and molecular mechanism

ClpS is an essential component of the N-end rule pathway in Escherichia coli

Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK

Protein folding and degradation in bacteria: to degrade or not to degrade? That is the question

DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat‐induced protein damage

Three-State Equilibrium of Escherichia coli Trigger Factor

Mechanism of substrate recognition by Hsp70 chaperones

Functional Dissection of Escherichia coli Trigger Factor: Unraveling the Function of Individual Domains

Protein Turnover: A CHIP Programmed for Proteolysis

Cyanobacterial ClpC/HSP100 Protein Displays Intrinsic Chaperone Activity

The ATP Hydrolysis-Dependent Reaction Cycle of the Escherichia coli Hsp70 System-DnaK, DnaJ, and GrpE

GPD1 Specifically Marks Dormant Glioma Stem Cells with a Distinct Metabolic Profile

Escherichia coli Trigger Factor is a Prolyl isomerase that Associates with Nascent Polypeptide Chains

Molecular Basis for Interactions of the DnaK Chaperone with Substrates

Integrating protein homeostasis strategies in prokaryotes

Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor

Stand-alone ClpG disaggregase confers superior heat tolerance to bacteria

Allosteric Regulation of Hsp70 Chaperones by a Proline Switch

Stand-alone CIpG disaggregase confers superior heat tolerance to bacteria

Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation

Functional Dissection of Trigger Factor and DnaK: Interactions with Nascent Polypeptides and Thermally Denatured Proteins

The Hsp70 and Hsp60 Chaperone Machines

Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins

Thermotolerance Requires Refolding of Aggregated Proteins by Substrate Translocation through the Central Pore of ClpB

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