List of works - Krzysztof Liberek

A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase

scientific article

ATP hydrolysis is required for the DnaJ-dependent activation of DnaK chaperone for binding to both native and denatured protein substrates

scientific article published on 01 August 1995

Adenosine diphosphate restricts the protein remodeling activity of the Hsp104 chaperone to Hsp70 assisted disaggregation

scientific article published on 25 May 2016

Autoregulation of the Escherichia coli heat shock response by the DnaK and DnaJ heat shock proteins

scientific article published on December 1993

Biological role and regulation of the universally conserved heat shock proteins ⬇️

scientific article published on December 25, 1991

Both ambient temperature and the DnaK chaperone machine modulate the heat shock response in Escherichia coli by regulating the switch between sigma 70 and sigma 32 factors assembled with RNA polymerase

scientific article published on October 1995

Chaperones in control of protein disaggregation

scientific article

Conformational properties of aggregated polypeptides determine ClpB-dependence in the disaggregation process

scientific article published on 26 May 2007

Conformational stability of the full-atom hexameric model of the ClpB chaperone from Escherichia coli

scientific article

Cooperative action of Escherichia coli ClpB protein and DnaK chaperone in the activation of a replication initiation protein

scientific article

Differential inhibition of transcription from sigma70- and sigma32-dependent promoters by rifampicin

scientific article published on 01 November 1998

Dispose to the pole-protein aggregation control in bacteria.

scientific article published on March 2010

Disruption of ionic interactions between the nucleotide binding domain 1 (NBD1) and middle (M) domain in Hsp100 disaggregase unleashes toxic hyperactivity and partial independence from Hsp70.

scientific article published on 11 December 2012

Distinct activities of Escherichia coli small heat shock proteins IbpA and IbpB promote efficient protein disaggregation.

scientific article

Duplicate divergence of two bacterial small heat shock proteins reduces the demand for Hsp70 in refolding of substrates

scientific article published on 25 October 2019

Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK ⬇️

scientific article (publication date: April 1991)

Expression of heat shock protein 72 in peritoneal leukocytes is induced by peritoneal dialysis

scientific article published on 01 May 2007

Formation of the preprimosome protects lambda O from RNA transcription-dependent proteolysis by ClpP/ClpX.

scientific article

Function, evolution, and structure of J-domain proteins

scientific article published on 26 November 2018

Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation.

scientific article published on 16 January 2006

Hsp70 displaces small heat shock proteins from aggregates to initiate protein refolding.

scientific article published on 20 February 2017

Hsp78 chaperone functions in restoration of mitochondrial network following heat stress

scientific article published on 14 February 2006

IbpA the small heat shock protein from Escherichia coli forms fibrils in the absence of its cochaperone IbpB.

scientific article

Importance of N- and C-terminal regions of IbpA, Escherichia coli small heat shock protein, for chaperone function and oligomerization

scientific article

Importance of two ATP-binding sites for oligomerization, ATPase activity and chaperone function of mitochondrial Hsp78 protein 1 1Edited by M. Yaniv ⬇️

scientific article published on December 7, 2001

Initiation of lambda DNA replication reconstituted with purified lambda and Escherichia coli replication proteins

scientific article published on 01 December 1988

Initiation of lambda DNA replication with purified host- and bacteriophage-encoded proteins: the role of the dnaK, dnaJ and grpE heat shock proteins

scientific article published on May 1989

Mitochondrial Hsp70 Ssc1: role in protein folding.

scientific article

Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding

scientific article published on 01 January 2001

On the mechanism of FtsH-dependent degradation of the sigma 32 transcriptional regulator of Escherichia coli and the role of the Dnak chaperone machine

scientific article published in January 1999

Physical interactions between bacteriophage and Escherichia coli proteins required for initiation of lambda DNA replication

scientific article

Purification and biochemical properties of Saccharomyces cerevisiae Mdj1p, the mitochondrial DnaJ homologue

scientific article published on 01 November 1997

Role of a conserved aspartic acid in nucleotide binding domain 1 (NBD1) of Hsp100 chaperones in their activities

scientific article published on 6 December 2011

Role of the Escherichia coli DnaK and DnaJ heat shock proteins in the initiation of bacteriophage lambda DNA replication

scientific article

Selective Hsp70-Dependent Docking of Hsp104 to Protein Aggregates Protects the Cell from the Toxicity of the Disaggregase

scientific article published on 24 April 2019

Small but mighty: a functional look at bacterial sHSPs

scientific article published on 16 April 2020

Small heat shock proteins: multifaceted proteins with important implications for life

scientific article published on 13 February 2019

Structure-function analysis of the zinc finger region of the DnaJ molecular chaperone

scientific article

Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation

scientific article

The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein ⬇️

scientific article published on August 5, 1991

The growing world of small heat shock proteins: from structure to functions

scientific article published on 31 March 2017

The small heat shock protein IbpA of Escherichia coli cooperates with IbpB in stabilization of thermally aggregated proteins in a disaggregation competent state.

scientific article

List of works by Krzysztof Liberek

A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase

ATP hydrolysis is required for the DnaJ-dependent activation of DnaK chaperone for binding to both native and denatured protein substrates

Adenosine diphosphate restricts the protein remodeling activity of the Hsp104 chaperone to Hsp70 assisted disaggregation

Autoregulation of the Escherichia coli heat shock response by the DnaK and DnaJ heat shock proteins

Biological role and regulation of the universally conserved heat shock proteins ⬇️

Both ambient temperature and the DnaK chaperone machine modulate the heat shock response in Escherichia coli by regulating the switch between sigma 70 and sigma 32 factors assembled with RNA polymerase

Chaperones in control of protein disaggregation

Conformational properties of aggregated polypeptides determine ClpB-dependence in the disaggregation process

Conformational stability of the full-atom hexameric model of the ClpB chaperone from Escherichia coli

Cooperative action of Escherichia coli ClpB protein and DnaK chaperone in the activation of a replication initiation protein

Differential inhibition of transcription from sigma70- and sigma32-dependent promoters by rifampicin

Dispose to the pole-protein aggregation control in bacteria.

Disruption of ionic interactions between the nucleotide binding domain 1 (NBD1) and middle (M) domain in Hsp100 disaggregase unleashes toxic hyperactivity and partial independence from Hsp70.

Distinct activities of Escherichia coli small heat shock proteins IbpA and IbpB promote efficient protein disaggregation.

Duplicate divergence of two bacterial small heat shock proteins reduces the demand for Hsp70 in refolding of substrates

Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK ⬇️

Expression of heat shock protein 72 in peritoneal leukocytes is induced by peritoneal dialysis

Formation of the preprimosome protects lambda O from RNA transcription-dependent proteolysis by ClpP/ClpX.

Function, evolution, and structure of J-domain proteins

Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation.

Hsp70 displaces small heat shock proteins from aggregates to initiate protein refolding.

Hsp78 chaperone functions in restoration of mitochondrial network following heat stress

IbpA the small heat shock protein from Escherichia coli forms fibrils in the absence of its cochaperone IbpB.

Importance of N- and C-terminal regions of IbpA, Escherichia coli small heat shock protein, for chaperone function and oligomerization

Importance of two ATP-binding sites for oligomerization, ATPase activity and chaperone function of mitochondrial Hsp78 protein 1 1Edited by M. Yaniv ⬇️

Initiation of lambda DNA replication reconstituted with purified lambda and Escherichia coli replication proteins

Initiation of lambda DNA replication with purified host- and bacteriophage-encoded proteins: the role of the dnaK, dnaJ and grpE heat shock proteins

Mitochondrial Hsp70 Ssc1: role in protein folding.

Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding

On the mechanism of FtsH-dependent degradation of the sigma 32 transcriptional regulator of Escherichia coli and the role of the Dnak chaperone machine

Physical interactions between bacteriophage and Escherichia coli proteins required for initiation of lambda DNA replication

Purification and biochemical properties of Saccharomyces cerevisiae Mdj1p, the mitochondrial DnaJ homologue

Role of a conserved aspartic acid in nucleotide binding domain 1 (NBD1) of Hsp100 chaperones in their activities

Role of the Escherichia coli DnaK and DnaJ heat shock proteins in the initiation of bacteriophage lambda DNA replication

Selective Hsp70-Dependent Docking of Hsp104 to Protein Aggregates Protects the Cell from the Toxicity of the Disaggregase

Small but mighty: a functional look at bacterial sHSPs

Small heat shock proteins: multifaceted proteins with important implications for life

Structure-function analysis of the zinc finger region of the DnaJ molecular chaperone

Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation

The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein ⬇️

The growing world of small heat shock proteins: from structure to functions

The small heat shock protein IbpA of Escherichia coli cooperates with IbpB in stabilization of thermally aggregated proteins in a disaggregation competent state.