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115 results on '"MALANGA, MARIA"'

4. Histone shuttling by poly ADP-ribosylation

Author

Althaus, Felix R., Höfferer, Liane, Kleczkowska, Hanna E., Malanga, Maria, Naegeli, Hanspeter, Panzeter, Phyllis L., Realini, Claudio A., Dhalla, Naranjan S., editor, Moss, Joel, editor, and Zahradka, Peter, editor

Published
1994
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8. In vitro induction of H1-H1 histone cross-linking by adenosine diphosphate-ribose polymers

Author

Reale, Anna, Malanga, Maria, Zardo, Guiseppe, Strom, Roberto, Scovassi, A. Ivana, Farina, Benedetta, and Caiafa, Paola

Subjects
Cytochemistry -- Research, Enzymes -- Physiological aspects, Crosslinked polymers -- Physiological aspects, Chromatin -- Physiological aspects, Histones -- Physiological aspects, Polymers -- Physiological aspects, Ribose -- Physiological aspects, Adenosine diphosphate -- Physiological aspects, Biological sciences, Chemistry
Abstract

In vitro induction of H1-H1 histone cross-linking by adenosine diphosphate-ribose polymers is discussed. A study has been made into whether and how ADP-ribose polymers, alone, can affect formation of H1-H1 oligomers, normally present in a condensed chromatin structure. Results indicate ADP-ribose polymers are involved in chromatin decondensation.

Published
2000

13. High-affinity interaction of poly(ADP-ribose) and the human DEK oncoprotein depends upon chain length

Author

Fahrer, Jorg, Popp, Oliver, Malanga, Maria, Beneke, Sascha, Markovitz, David M., Ferrando-May, Elisa, Burkle, Alexander, and Kappes, Ferdinand

Subjects
DNA-ligand interactions -- Analysis, DNA damage -- Analysis, DNA polymerases -- Structure, DNA polymerases -- Chemical properties, Protein binding -- Analysis, Biological sciences, Chemistry
Abstract

Sequence alignment is used for identifying three functional poly(ADP-ribose) (PAR)-binding sites in the DEK primary sequence and has confirmed their functionality in PAR binding studies. The studies have helped in the molecular understanding of the DEK-PAR interplay and have supported the existence of a cellular ePAR codeE represented by PAR chain length.

Published
2010

23. Poly ADP-ribosylation in two L5178Y murine lymphoma sublines differentially sensitive to DNA-damaging agents

Author

KLECZKOWSKA H. E, SZUMIEL I, ALTHAUS F. R., MALANGA, MARIA, University of Zurich, Althaus, F R, Kleczkowska, H. E., Malanga, Maria, Szumiel, I, and Althaus, F. R.

Subjects
570 Life sciences, biology, 2741 Radiology, Nuclear Medicine and Imaging, 10079 Institute of Veterinary Pharmacology and Toxicology, 3614 Radiological and Ultrasound Technology
Published
2002
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35. DNA Damage Signaling through Poly(ADP-Ribose).

Author

Bürkle, Alexander, Malanga, Maria, and Althaus, Felix R.

Abstract

Several lines of evidence reveal that poly(ADP-ribose)polymerase-1 (PARP-1) operates in a DNA damage signaling network. Poly(ADP-ribose) metabolism induced by DNA damage participates in DNA repair and contributes to downstream mechanisms leading to cell cycle arrest, cell survival, cell death, or cell transformation. An important element of these multiple actions is the recruitment of DNA damage checkpoint proteins coordinating DNA repair with downstream events. The focus of this overview is the mechanism by which poly(ADP-ribose)—attached to the automodified PARP-1—interact with DNA damage check-point proteins and how it may reprogram the functions of specific protein domains. Several proteins of the genome surveillance system, e.g., p53, p21, DNA-PK, NF-κB, XRCC1, and XPA are targets of such regulation. In all cass studied, a specific ‘polymer-binding' sequence motif of 20 to 26 amino acids is targeted by poly (ADP-ribose) and this motif overlaps with important functional domains responsible for protein-protein or protein-DNA interactions, nuclear import or export, enzymatic catalysis, or protein degradation. [ABSTRACT FROM AUTHOR]

Published
2006
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36. Inhibition of Poly(ADP-Ribosyl)ation Allows DNA Hypermethylation.

Author

Szyf, Moshe, Reale, Anna, Zardo, Giuseppe, Malanga, Maria, Zlatanova, Jordanka, and Caiafa, Paola

Abstract

This chapter emphasizes that along the chain of events that induce DNA methylation-dependent chromatin condensation, a post-synthetic modification other than histone acetylation, poly(ADP-ribosyl)ation, participates in the establishment and maintenance of methylation-free regions of chromatin. In fact, several lines of in vitro and in vivo evidence have shown that poly(ADP-ribosyl)ation is involved in the control of DNA methylation pattern, protecting genomic DNA from full methylation. More recent studies have provided some clues to the understanding of the molecular mechanism(s) connecting poly(ADP-ribosyl)ation with DNA methylation. We aim here to demonstrate the direct correlation existing between inhibition of poly(ADP-ribose) polymerases and DNA hypermethylation, and to describe some possible mechanisms underlying this molecular link. We will then present our hypothesis that the inhibition of the poly(ADP-ribosyl)ation process in the cell may be responsible for the anomalous hypermethylation of oncosuppressor gene promoters during tumorigenesis and to suggest the possibility that an active poly(ADP-ribosyl)ation process is also involved in maintaining the unmethylated state of CpG islands in normal cells. [ABSTRACT FROM AUTHOR]

Published
2005
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41. Histone shuttling by poly ADP-ribosylation

Author

Althaus, Felix R., primary, H�fferer, Liane, additional, Kleczkowska, Hanna E., additional, Malanga, Maria, additional, Naegeli, Hanspeter, additional, Panzeter, Phyllis L., additional, and Realini, Claudio A., additional

Published
1994
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45. Poly ADP-ribosylation: A DNA break signal mechanism.

Author

Althaus, Felix, Kleczowska, Hanna, Malanga, Maria, Müntener, Cedric, Pleschke, Jutta, Ebner, Maria, and Auer, Bernhard

Abstract

Recent evidence obtained with transgenic knockout mice suggests that the enzyme poly(ADP-ribose)polymerase (PARP) does not play a direct role in DNA break processing [1, 2]. Nevertheless, inactivation of the catalytic or the DNA nick-binding functions of PARP affects cellular responses to genotoxins at the level of cell survival, sister chromatid exchanges and apoptosis [2, 3]. In the present report, we conceptualize the idea that PARP is part of a DNA break signal mechanism [4, 5]. In vitro screening studies revealed the existence of a protein family containing a polymer-binding motif of about 22 amino acids. This motif is present in p53 protein as well as in MARCKS, a protein involved in the regulation of the actin cytoskeleton. Biochemical analyses showed that these sequences are directly targeted by PARP-associated polymers in vitro, and this alters several molecular functions of p53- and MARCKS protein. PARP-deficient knockout mice from transgenic mice were found to exhibit several phenotypic features compatible with altered DNA damage signaling, such as downregulation and lack of responsiveness of p53 protein to genotoxins, and morphological changes compatible with MARCKS-related cytoskeletal dysfunction. The knockout phenotype could be rescued by stable expression of the PARP gene. - We propose that PARP-associated polymers may recruit signal proteins to sites of DNA breakage and reprogram their functions. [ABSTRACT FROM AUTHOR]

Published
1999
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48. In vivo ADP-ribosylation of specific proteins

Author

FARAONE MENNELLA, MARIA ROSARIA, MALANGA, MARIA, FARINA, BENEDETTA, E. , Leone, K.Decker, W.Stoffel, H.G.Zachau, FARAONE MENNELLA, MARIA ROSARIA, Malanga, Maria, E., Leone, and Farina, Benedetta

Subjects
ADP-ribosylation, histones, non-histones
Published
1986

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