Maciej Zylicz

D-Index & Metrics D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines.

Discipline name Citations Publications World Ranking National Ranking

Biology and Biochemistry D-index 50 Citations 10,311 76 World Ranking 13037 National Ranking 5539

Research.com Recognitions

Awards & Achievements

2011 - German National Academy of Sciences Leopoldina - Deutsche Akademie der Naturforscher Leopoldina – Nationale Akademie der Wissenschaften Genetics/Molecular Biology and Cell Biology

2007 - Polish Academy of Science

2001 - Member of Academia Europaea

1999 - Prize of the Foundation for Polish Science - Nagroda Fundacji na rzecz Nauki Polskiej for research on regulatory proteins constituting part of the system protecting cells against undesirable changes in their external environment

Member of the European Molecular Biology Organization (EMBO)

Overview

What are the main themes of his work throughout his whole career to date

Maciej Zylicz conducts interdisciplinary study in the fields of Gene and In vitro through his works. In his research, Maciej Zylicz undertakes multidisciplinary study on In vitro and Gene. His research on Escherichia coli often connects related areas such as Escherichia coli Proteins. His research on Escherichia coli Proteins often connects related topics like Escherichia coli. He performs multidisciplinary study on Heat shock protein and GroEL in his works. In his study, Maciej Zylicz carries out multidisciplinary GroEL and Heat shock protein research. He performs multidisciplinary studies into Molecular biology and Transfection in his work. Maciej Zylicz integrates Biochemistry and Microbiology in his research. Maciej Zylicz combines Microbiology and Biochemistry in his studies.

Maciej Zylicz most often published in these fields:

Gene (100.00%)
Escherichia coli (83.33%)
Heat shock protein (66.67%)

This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.

Best Publications

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

Krzysztof Liberek;Jaroslaw Marszalek;Debbie Ang;Costa Georgopoulos.
Proceedings of the National Academy of Sciences of the United States of America (1991)

1076 Citations

High guanine and cytosine content increases mRNA levels in mammalian cells.

Grzegorz Kudla;Leszek Lipinski;Leszek Lipinski;Fanny Caffin;Aleksandra Helwak;Aleksandra Helwak.
PLOS Biology (2006)

441 Citations

The dnaK protein modulates the heat-shock response of Escherichia coli

Kit Tilly;Niki McKittrick;Maciej Zylicz;Costa Georgopoulos.
Cell (1983)

434 Citations

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

Debbie Ang;Krzysztof Liberek;Krzysztof Liberek;Dorota Skowyra;Maciej Zylicz.
Journal of Biological Chemistry (1991)

407 Citations

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 (1989)

377 Citations

The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication.

Daniel Wall;Maciej Zylicz;Costa Georgopoulos.
Journal of Biological Chemistry (1994)

365 Citations

Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli.

Diana Wojtkowiak;Costa Georgopoulos;Maciej Zylicz.
Journal of Biological Chemistry (1993)

334 Citations

The dnaK protein of Escherichia coli possesses an ATPase and autophosphorylating activity and is essential in an in vitro DNA replication system.

Maciej Zylicz;Jonathan H. Lebowitz;Roger McMacken;Costa Georgopoulos.
Proceedings of the National Academy of Sciences of the United States of America (1983)

332 Citations

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.

Krzysztof Liberek;Dorota Skowyra;Maciej Zylicz;Claudia Johnson.
Journal of Biological Chemistry (1991)

331 Citations

The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone.

A. Wawrzynow;D. Wojtkowiak;J. Marszalek;B. Banecki.
The EMBO Journal (1995)

301 Citations

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