Sabina Kedzierska

Summary

Country: Poland

Publications

  1. ncbi [Role of Escherichia coli molecular chaperones in the protection of bacterial cells against irreversible aggregation induced by heat shock]
    Sabina Kedzierska
    Department of Biochemistry, University of Gdansk, 24 Kladki St, 80 822 Gdansk, Poland
    Postepy Biochem 51:146-53. 2005
  2. ncbi The effect of some antibiotic-resistance-conferring plasmids on the removal of the heat-aggregated proteins from Escherichia coli cells
    S Kedzierska
    Department of Biochemistry, University of Gdansk, Poland
    FEMS Microbiol Lett 176:279-84. 1999
  3. ncbi [Structure, function and mechanisms of action of ATPases from the AAA superfamily of proteins]
    Sabina Kedzierska
    Department of Biochemistry, University of Gdansk, 24 Kładki St, 80 822 Gdansk, Poland
    Postepy Biochem 52:330-8. 2006
  4. ncbi The effect of co-overproduction of DnaK/DnaJ/GrpE and ClpB proteins on the removal of heat-aggregated proteins from Escherichia coli DeltaclpB mutant cells--new insight into the role of Hsp70 in a functional cooperation with Hsp100
    S Kedzierska
    Department of Biochemistry, University of Gdansk, Kladki 24, 80 822, Gdansk, Poland
    FEMS Microbiol Lett 204:355-60. 2001
  5. ncbi DnaK/DnaJ chaperone system reactivates endogenous E. coli thermostable FBP aldolase in vivo and in vitro; the effect is enhanced by GroE heat shock proteins
    S Kedzierska
    Department of Biochemistry, University of Gdansk, Poland
    Cell Stress Chaperones 6:29-37. 2001
  6. ncbi Aggregation of heat-shock-denatured, endogenous proteins and distribution of the IbpA/B and Fda marker-proteins in Escherichia coli WT and grpE280 cells
    Ewa Laskowska
    Department of Biochemistry, University of Gdansk, Kładki 24, 80 822 Gdansk, Poland
    Microbiology 150:247-59. 2004
  7. ncbi Interactions within the ClpB/DnaK bi-chaperone system from Escherichia coli
    Sabina Kedzierska
    Department of Biochemistry, University of Gdansk, Gdansk, Poland
    Arch Biochem Biophys 444:61-5. 2005
  8. ncbi The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock
    Dorota Kuczynska-Wisnik
    Department of Biochemistry, University of Gdask, Kładki 24, 80 822 Gdask, Poland
    Microbiology 148:1757-65. 2002
  9. ncbi Structure and function of the middle domain of ClpB from Escherichia coli
    Sabina Kedzierska
    Department of Biochemistry, University of Gdansk, Gdansk, Poland
    Biochemistry 42:14242-8. 2003
  10. ncbi The amino-terminal domain of ClpB supports binding to strongly aggregated proteins
    Micheal E Barnett
    Department of Biochemistry, Kansas State University, Manhattan, Kansas 66506, USA
    J Biol Chem 280:34940-5. 2005

Collaborators

Detail Information

Publications10

  1. ncbi [Role of Escherichia coli molecular chaperones in the protection of bacterial cells against irreversible aggregation induced by heat shock]
    Sabina Kedzierska
    Department of Biochemistry, University of Gdansk, 24 Kladki St, 80 822 Gdansk, Poland
    Postepy Biochem 51:146-53. 2005
    ..Recently, many studies have been focused on the disaggregation and reactivation of proteins by a bi-chaperone system consisting of DnaK/DnaJ/GrpE and ClpB, an ATPase from the AAA superfamily of proteins...
  2. ncbi The effect of some antibiotic-resistance-conferring plasmids on the removal of the heat-aggregated proteins from Escherichia coli cells
    S Kedzierska
    Department of Biochemistry, University of Gdansk, Poland
    FEMS Microbiol Lett 176:279-84. 1999
    ....
  3. ncbi [Structure, function and mechanisms of action of ATPases from the AAA superfamily of proteins]
    Sabina Kedzierska
    Department of Biochemistry, University of Gdansk, 24 Kładki St, 80 822 Gdansk, Poland
    Postepy Biochem 52:330-8. 2006
    ..They also act as DNA helicases and transcription factors. This review describes the structure, function and mechanisms of action of the most known AAA proteins...
  4. ncbi The effect of co-overproduction of DnaK/DnaJ/GrpE and ClpB proteins on the removal of heat-aggregated proteins from Escherichia coli DeltaclpB mutant cells--new insight into the role of Hsp70 in a functional cooperation with Hsp100
    S Kedzierska
    Department of Biochemistry, University of Gdansk, Kladki 24, 80 822, Gdansk, Poland
    FEMS Microbiol Lett 204:355-60. 2001
    ....
  5. ncbi DnaK/DnaJ chaperone system reactivates endogenous E. coli thermostable FBP aldolase in vivo and in vitro; the effect is enhanced by GroE heat shock proteins
    S Kedzierska
    Department of Biochemistry, University of Gdansk, Poland
    Cell Stress Chaperones 6:29-37. 2001
    ..It is supposed that the denaturation of the thermostable Fda in vivo results rather from a temporary and transient deficit of Hsps than from the direct heat effect...
  6. ncbi Aggregation of heat-shock-denatured, endogenous proteins and distribution of the IbpA/B and Fda marker-proteins in Escherichia coli WT and grpE280 cells
    Ewa Laskowska
    Department of Biochemistry, University of Gdansk, Kładki 24, 80 822 Gdansk, Poland
    Microbiology 150:247-59. 2004
    ....
  7. ncbi Interactions within the ClpB/DnaK bi-chaperone system from Escherichia coli
    Sabina Kedzierska
    Department of Biochemistry, University of Gdansk, Gdansk, Poland
    Arch Biochem Biophys 444:61-5. 2005
    ....
  8. ncbi The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock
    Dorota Kuczynska-Wisnik
    Department of Biochemistry, University of Gdask, Kładki 24, 80 822 Gdask, Poland
    Microbiology 148:1757-65. 2002
    ....
  9. ncbi Structure and function of the middle domain of ClpB from Escherichia coli
    Sabina Kedzierska
    Department of Biochemistry, University of Gdansk, Gdansk, Poland
    Biochemistry 42:14242-8. 2003
    ..The heptad repeats are likely involved in stabilization of an intra-MD helical bundle rather than an intersubunit coiled coil...
  10. ncbi The amino-terminal domain of ClpB supports binding to strongly aggregated proteins
    Micheal E Barnett
    Department of Biochemistry, Kansas State University, Manhattan, Kansas 66506, USA
    J Biol Chem 280:34940-5. 2005
    ..In summary, we provided evidence for an essential role of the N-terminal domain of ClpB in recognition and binding strongly aggregated proteins...