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Alicja Wawrzynów
Researcher at University of Gdańsk
Publications - 28
Citations - 1734
Alicja Wawrzynów is an academic researcher from University of Gdańsk. The author has contributed to research in topics: Pyridine & Chaperone (protein). The author has an hindex of 18, co-authored 28 publications receiving 1699 citations. Previous affiliations of Alicja Wawrzynów include International Institute of Minnesota & University of Utah.
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Journal ArticleDOI
The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone.
Alicja Wawrzynów,D. Wojtkowiak,Jaroslaw Marszalek,Bogdan Banecki,M. Jonsen,Barbara J. Graves,Costa Georgopoulos,Maciej Zylicz +7 more
TL;DR: It is proposed that the ClpX protein is a bona fide chaperone, whose biological role includes the maintenance of certain polypeptides in a form competent for proteolysis by the ClPP protease.
Journal ArticleDOI
Hsp70 interactions with the p53 tumour suppressor protein
TL;DR: The 70 kDa heat shock‐related proteins comprise a family of highly conserved molecular chaperones that regulate a wide variety of cellular processes during normal and stress conditions, and Hsp70 is one of the most abundant of these proteins, accounting for as much as 1–2% of total cellular protein.
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Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53.
TL;DR: The results presented here provide possible molecular mechanisms that can help to explain the observed in vivo role of molecular chaperones in the stabilization and cellular localization of wild‐type and mutant p53 protein.
Journal ArticleDOI
Structure-Function Analysis of the Zinc Finger Region of the DnaJ Molecular Chaperone
Bogdan Banecki,Krzysztof Liberek,Daniel Wall,Alicja Wawrzynów,Costa Georgopoulos,Enrico Bertoli,Fabio Tanfani,Maciej Zylicz +7 more
TL;DR: These in vitro results correlate well with the in vivo observed partial inhibition of bacteriophage λ growth in a DnaJΔ144-200 mutant background, and show that the Zn(II) ions help to stabilize DnJ's tertiary structure.
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The Clp ATPases define a novel class of molecular chaperones
TL;DR: The recent evidence that the Clp ATPases are indeed molecular chaperones capable of either repairing proteins damaged during stress conditions or activating the initiation proteins for Mu, λ or P1 DNA replication is discussed.