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Krzysztof Liberek
Krzysztof Liberek
在 ug.edu.pl 的电子邮件经过验证
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引用次数
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Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK.
K Liberek, J Marszalek, D Ang, C Georgopoulos, M Zylicz
Proceedings of the National Academy of Sciences 88 (7), 2874-2878, 1991
11361991
Chaperones in control of protein disaggregation
K Liberek, A Lewandowska, S Ziętkiewicz
The EMBO journal 27 (2), 328-335, 2008
5402008
Biological role and regulation of the universally conserved heat shock proteins
D Ang, K Liberek, D Skowyra, M Zylicz, C Georgopoulos
The Journal of biological chemistry (Print) 266 (36), 24233-24236, 1991
4191991
Initiation of lambda DNA replication with purified host‐and bacteriophage‐encoded proteins: the role of the dnaK, dnaJ and grpE heat shock proteins.
M Zylicz, D Ang, K Liberek, C Georgopoulos
The EMBO Journal 8 (5), 1601-1608, 1989
3691989
The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a …
K Liberek, D Skowyra, M Zylicz, C Johnson, C Georgopoulos
Journal of Biological Chemistry 266 (22), 14491-14496, 1991
3111991
Role of the Escherichia coli DnaK and DnaJ heat shock proteins in the initiation of bacteriophage lambda DNA replication.
K Liberek, C Georgopoulos, M Zylicz
Proceedings of the National Academy of Sciences 85 (18), 6632-6636, 1988
2591988
The DnaK chaperone modulates the heat shock response of Escherichia coli by binding to the sigma 32 transcription factor.
K Liberek, TP Galitski, M Zylicz, C Georgopoulos
Proceedings of the National Academy of Sciences 89 (8), 3516-3520, 1992
2351992
The growing world of small heat shock proteins: from structure to functions
S Carra, S Alberti, PA Arrigo, JL Benesch, IJ Benjamin, W Boelens, ...
Cell Stress and Chaperones 22 (4), 601-611, 2017
2032017
Structure-function analysis of the zinc finger region of the DnaJ molecular chaperone
B Banecki, K Liberek, D Wall, A Wawrzynów, C Georgopoulos, E Bertoli, ...
Journal of Biological Chemistry 271 (25), 14840-14848, 1996
2031996
Properties of heat shock proteins of Escherichia coli and autoregulation of the heat shock response.
C Georgopoulos
The Biology of Heat Shock Proeins and Molecular Chaperones, 209-249, 1994
1921994
Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation
S Ziȩtkiewicz, J Krzewska, K Liberek
Journal of Biological Chemistry 279 (43), 44376-44383, 2004
1882004
Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding
J Krzewska, T Langer, K Liberek
FEBS letters 489 (1), 92-96, 2001
1762001
Autoregulation of the Escherichia coli heat shock response by the DnaK and DnaJ heat shock proteins.
K Liberek, C Georgopoulos
Proceedings of the National Academy of Sciences 90 (23), 11019-11023, 1993
1681993
Hsp70 displaces small heat shock proteins from aggregates to initiate protein refolding
S Żwirowski, A Kłosowska, I Obuchowski, NB Nillegoda, A Piróg, ...
The EMBO journal 36 (6), 783-796, 2017
1642017
Function, evolution, and structure of J-domain proteins
HH Kampinga, C Andreasson, A Barducci, ME Cheetham, D Cyr, ...
Cell Stress and Chaperones 24, 7-15, 2019
1582019
Properties of the Escherichia coli heat shock proteins and their role in bacteriophage λ growth
C Georgopoulos
Stress proteins in biology and medicine, 1990
1461990
Mitochondrial Hsp70 Ssc1: role in protein folding
Q Liu, J Krzewska, K Liberek, EA Craig
Journal of Biological Chemistry 276 (9), 6112-6118, 2001
1382001
The DnaJ chaperone catalytically activates the DnaK chaperone to preferentially bind the sigma 32 heat shock transcriptional regulator.
K Liberek, D Wall, C Georgopoulos
Proceedings of the National Academy of Sciences 92 (14), 6224-6228, 1995
1331995
Distinct activities of Escherichia coli small heat shock proteins IbpA and IbpB promote efficient protein disaggregation
E Ratajczak, S Ziętkiewicz, K Liberek
Journal of molecular biology 386 (1), 178-189, 2009
1312009
The small heat shock protein IbpA of Escherichia coli cooperates with IbpB in stabilization of thermally aggregated proteins in a disaggregation competent state
M Matuszewska, D Kuczyńska-Wiśnik, E Laskowska, K Liberek
Journal of Biological Chemistry 280 (13), 12292-12298, 2005
1312005
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