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Book ; Thesis: Entwicklung eines Bestimmungsverfahrens für albumingebundenes Doxorubicin und pharmakokinetische Untersuchung in der Maus

Richly, Heike

2004

Author's details	vorgelegt von Heike Richly
Language	German
Size	96 Bl. : Ill., graph. Darst.
Publishing country	Germany
Document type	Book ; Thesis
Thesis / German Habilitation thesis	Duisburg, Essen, Univ., Diss., 2005
HBZ-ID	HT014417605
Database	Catalogue ZB MED Medicine, Health

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2006 E 1403	order for loan	Magazin

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Article ; Online: Autophagy during ageing - from Dr Jekyll to Mr Hyde.

Wilhelm, Thomas / Richly, Holger

The FEBS journal

2018 Volume 285, Issue 13, Page(s) 2367–2376

Abstract: Autophagy is a ubiquitous catabolic process, which causes cellular bulk degradation through vesicular engulfment of obsolete, damaged or harmful cytoplasmic components. While autophagy regulates cellular homeostasis during development and in youth, there ...

Abstract	Autophagy is a ubiquitous catabolic process, which causes cellular bulk degradation through vesicular engulfment of obsolete, damaged or harmful cytoplasmic components. While autophagy regulates cellular homeostasis during development and in youth, there is mounting evidence that autophagy becomes increasingly dysfunctional with age. Recent work in Caenorhabditis elegans even suggests that late-life dysfunctional autophagy exhibits detrimental effects that drive the ageing process. Other studies link elevated autophagy closely to increased health and longevity. This review aims to put these apparently opposing views into perspective and define our current understanding of the role of autophagy during ageing.
MeSH term(s)	Aging/physiology ; Animals ; Autophagy/physiology ; Caenorhabditis elegans/physiology ; Drosophila melanogaster/physiology ; Humans ; Longevity/physiology ; Saccharomyces cerevisiae/physiology ; Signal Transduction
Language	English
Publishing date	2018-04-16
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.14453
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Article ; Online: H4K20me2: Orchestrating the recruitment of DNA repair factors in nucleotide excision repair.

Chitale, Shalaka / Richly, Holger

Nucleus (Austin, Tex.)

2018 Volume 9, Issue 1, Page(s) 212–215

Abstract: The integrity of the genome is maintained by specific DNA repair pathways. The main pathway removing DNA lesions induced by exposure to UV light is nucleotide excision repair (NER). The DNA damage response at chromatin is accompanied by the recruitment ... ...

Abstract	The integrity of the genome is maintained by specific DNA repair pathways. The main pathway removing DNA lesions induced by exposure to UV light is nucleotide excision repair (NER). The DNA damage response at chromatin is accompanied by the recruitment of DNA repair factors to the lesion site and the deposition of specific histone marks. The function of these histone marks in NER stays for the most part elusive. We have recently reported that the methyltransferase MMSET catalyzes the dimethylation of histone H4 at lysine 20 (H4K20me2) at the lesion site. The deposition of H4K20me2 at DNA damage sites elicits the recruitment of the NER factor XPA providing evidence for an H4K20me2-dependent DNA repair factor recruitment mechanism during lesion recognition in the global-genomic branch of NER. Here we discuss how H4K20me2 might impact on the chromatin conformation and the DNA damage response.
MeSH term(s)	DNA/metabolism ; DNA Damage ; DNA Repair ; Histones/metabolism ; Humans ; Lysine/metabolism ; Methyltransferases/metabolism ; Nucleotides/metabolism
Chemical Substances	Histones ; Nucleotides ; DNA (9007-49-2) ; Methyltransferases (EC 2.1.1.-) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	2018-03-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2619626-8
ISSN	1949-1042 ; 1949-1034
ISSN (online)	1949-1042
ISSN	1949-1034
DOI	10.1080/19491034.2018.1444327
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: A chromatin scaffold for DNA damage recognition: how histone methyltransferases prime nucleosomes for repair of ultraviolet light-induced lesions.

Gsell, Corina / Richly, Holger / Coin, Frédéric / Naegeli, Hanspeter

Nucleic acids research

2020 Volume 48, Issue 4, Page(s) 1652–1668

Abstract: The excision of mutagenic DNA adducts by the nucleotide excision repair (NER) pathway is essential for genome stability, which is key to avoiding genetic diseases, premature aging, cancer and neurologic disorders. Due to the need to process an ... ...

Abstract	The excision of mutagenic DNA adducts by the nucleotide excision repair (NER) pathway is essential for genome stability, which is key to avoiding genetic diseases, premature aging, cancer and neurologic disorders. Due to the need to process an extraordinarily high damage density embedded in the nucleosome landscape of chromatin, NER activity provides a unique functional caliper to understand how histone modifiers modulate DNA damage responses. At least three distinct lysine methyltransferases (KMTs) targeting histones have been shown to facilitate the detection of ultraviolet (UV) light-induced DNA lesions in the difficult to access DNA wrapped around histones in nucleosomes. By methylating core histones, these KMTs generate docking sites for DNA damage recognition factors before the chromatin structure is ultimately relaxed and the offending lesions are effectively excised. In view of their function in priming nucleosomes for DNA repair, mutations of genes coding for these KMTs are expected to cause the accumulation of DNA damage promoting cancer and other chronic diseases. Research on the question of how KMTs modulate DNA repair might pave the way to the development of pharmacologic agents for novel therapeutic strategies.
MeSH term(s)	Chromatin/genetics ; Chromatin/radiation effects ; DNA Damage/genetics ; DNA Damage/radiation effects ; DNA Repair/genetics ; DNA Repair/radiation effects ; Genomic Instability/genetics ; Genomic Instability/radiation effects ; Histone Methyltransferases/chemistry ; Histone Methyltransferases/genetics ; Histones/genetics ; Methylation/radiation effects ; Nucleosomes/genetics ; Nucleosomes/radiation effects ; Saccharomyces cerevisiae/genetics ; Signal Transduction/radiation effects ; Ultraviolet Rays
Chemical Substances	Chromatin ; Histones ; Nucleosomes ; Histone Methyltransferases (EC 2.1.1.-)
Language	English
Publishing date	2020-01-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkz1229
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Article ; Online: Nuclear organization of nucleotide excision repair is mediated by RING1B dependent H2A-ubiquitylation.

Chitale, Shalaka / Richly, Holger

Oncotarget

2017 Volume 8, Issue 19, Page(s) 30870–30887

Abstract: One of the major cellular DNA repair pathways is nucleotide excision repair (NER). It is the primary pathway for repair of various DNA lesions caused by exposure to ultraviolet (UV) light, such as cyclobutane pyrimidine dimers (CPDs) and 6-4 ... ...

Abstract	One of the major cellular DNA repair pathways is nucleotide excision repair (NER). It is the primary pathway for repair of various DNA lesions caused by exposure to ultraviolet (UV) light, such as cyclobutane pyrimidine dimers (CPDs) and 6-4 photoproducts. Although lesion-containing DNA associates with the nuclear matrix after UV irradiation it is still not understood how nuclear organization affects NER. Analyzing unscheduled DNA synthesis (UDS) indicates that NER preferentially occurs in specific nuclear areas, viz the nucleolus. Upon inducing localized damage, we observe migration of damaged DNA towards the nucleolus. Employing a LacR-based tethering system we demonstrate that H2A-ubiquitylation via the UV-RING1B complex localizes chromatin close to the nucleolus. We further show that the H2A-ubiquitin binding protein ZRF1 resides in the nucleolus, and that it anchors ubiquitylated chromatin along with XPC. Our data thus provide insight into the sub-nuclear organization of NER and reveal a novel role for histone H2A-ubiquitylation.
Language	English
Publishing date	2017-05-09
Publishing country	United States
Document type	Journal Article
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.16142
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Article ; Online: Regulation of DNA Repair Mechanisms: How the Chromatin Environment Regulates the DNA Damage Response.

Stadler, Jens / Richly, Holger

International journal of molecular sciences

2017 Volume 18, Issue 8

Abstract: Cellular DNA is constantly challenged by damage-inducing factors derived from exogenous or endogenous sources. In order to maintain genome stability and integrity, cells have evolved a wide variety of DNA repair pathways which counteract different types ... ...

Abstract	Cellular DNA is constantly challenged by damage-inducing factors derived from exogenous or endogenous sources. In order to maintain genome stability and integrity, cells have evolved a wide variety of DNA repair pathways which counteract different types of DNA lesions, also referred to as the DNA damage response (DDR). However, DNA in eukaryotes is highly organized and compacted into chromatin representing major constraints for all cellular pathways, including DNA repair pathways, which require DNA as their substrate. Therefore, the chromatin configuration surrounding the lesion site undergoes dramatic remodeling to facilitate access of DNA repair factors and subsequent removal of the DNA lesion. In this review, we focus on the question of how the cellular DNA repair pathways overcome the chromatin barrier, how the chromatin environment is rearranged to facilitate efficient DNA repair, which proteins mediate this re-organization process and, consequently, how the altered chromatin landscape is involved in the regulation of DNA damage responses.
Language	English
Publishing date	2017-08-05
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms18081715
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Article ; Online: Shaping chromatin with DICER.

Chitale, Shalaka / Richly, Holger

Oncotarget

2017 Volume 8, Issue 25, Page(s) 39937–39938

Language	English
Publishing date	2017-07-05
Publishing country	United States
Document type	Editorial
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.17773
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Article ; Online: DICER and ZRF1 contribute to chromatin decondensation during nucleotide excision repair.

Chitale, Shalaka / Richly, Holger

Nucleic acids research

2017 Volume 45, Issue 10, Page(s) 5901–5912

Abstract: Repair of damaged DNA relies on the recruitment of DNA repair factors in a well orchestrated manner. As a prerequisite, the chromatin needs to be decondensed by chromatin remodelers to allow for binding of repair factors and for DNA repair to occur. ... ...

Abstract	Repair of damaged DNA relies on the recruitment of DNA repair factors in a well orchestrated manner. As a prerequisite, the chromatin needs to be decondensed by chromatin remodelers to allow for binding of repair factors and for DNA repair to occur. Recent studies have implicated members of the SWI/SNF and INO80 families as well as PARP1 in nucleotide excision repair (NER). In this study, we report that the endonuclease DICER is implicated in chromatin decondensation during NER. In response to UV irradiation, DICER is recruited to chromatin in a ZRF1-mediated manner. The H2A-ubiquitin binding protein ZRF1 and DICER together impact on the chromatin conformation via PARP1. Moreover, DICER-mediated chromatin decondensation is independent of its catalytic activity. Taken together, we describe a novel function of DICER at chromatin and its interaction with the ubiquitin signalling cascade during GG-NER.
MeSH term(s)	Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/growth & development ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans/radiation effects ; Cell Line ; Cell Line, Tumor ; Chromatin/chemistry ; Chromatin/metabolism ; Chromatin Assembly and Disassembly ; DEAD-box RNA Helicases/genetics ; DEAD-box RNA Helicases/metabolism ; DNA Damage ; DNA Repair ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Fibroblasts/cytology ; Fibroblasts/metabolism ; Fibroblasts/radiation effects ; HEK293 Cells ; Histones/genetics ; Histones/metabolism ; Humans ; Oncogene Proteins/genetics ; Oncogene Proteins/metabolism ; Osteoblasts/cytology ; Osteoblasts/metabolism ; Osteoblasts/radiation effects ; Poly (ADP-Ribose) Polymerase-1/genetics ; Poly (ADP-Ribose) Polymerase-1/metabolism ; Ribonuclease III/genetics ; Ribonuclease III/metabolism ; Ubiquitin/genetics ; Ubiquitin/metabolism ; Ultraviolet Rays
Chemical Substances	Chromatin ; DNA-Binding Proteins ; DNAJC2 protein, human ; Histones ; Oncogene Proteins ; Ubiquitin ; PARP1 protein, human (EC 2.4.2.30) ; Poly (ADP-Ribose) Polymerase-1 (EC 2.4.2.30) ; DICER1 protein, human (EC 3.1.26.3) ; Ribonuclease III (EC 3.1.26.3) ; DEAD-box RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2017-06-02
Publishing country	England
Document type	Journal Article
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkx261
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Article ; Online: DICER- and MMSET-catalyzed H4K20me2 recruits the nucleotide excision repair factor XPA to DNA damage sites.

Chitale, Shalaka / Richly, Holger

The Journal of cell biology

2017 Volume 217, Issue 2, Page(s) 527–540

Abstract: Ultraviolet (UV) irradiation triggers the recruitment of DNA repair factors to the lesion sites and the deposition of histone marks as part of the DNA damage response. The major DNA repair pathway removing DNA lesions caused by exposure to UV light is ... ...

Abstract	Ultraviolet (UV) irradiation triggers the recruitment of DNA repair factors to the lesion sites and the deposition of histone marks as part of the DNA damage response. The major DNA repair pathway removing DNA lesions caused by exposure to UV light is nucleotide excision repair (NER). We have previously demonstrated that the endoribonuclease DICER facilitates chromatin decondensation during lesion recognition in the global-genomic branch of NER. Here, we report that DICER mediates the recruitment of the methyltransferase MMSET to the DNA damage site. We show that MMSET is required for efficient NER and that it catalyzes the dimethylation of histone H4 at lysine 20 (H4K20me2). H4K20me2 at DNA damage sites facilitates the recruitment of the NER factor XPA. Our work thus provides evidence for an H4K20me2-dependent mechanism of XPA recruitment during lesion recognition in the global-genomic branch of NER.
MeSH term(s)	Biocatalysis ; Cell Line, Tumor ; DEAD-box RNA Helicases/metabolism ; DNA Damage ; DNA Repair ; HEK293 Cells ; Histone-Lysine N-Methyltransferase/metabolism ; Histones/metabolism ; Humans ; Lysine/metabolism ; Repressor Proteins/metabolism ; Ribonuclease III/metabolism ; Ultraviolet Rays ; Xeroderma Pigmentosum Group A Protein/metabolism
Chemical Substances	Histones ; Repressor Proteins ; XPA protein, human ; Xeroderma Pigmentosum Group A Protein ; Histone-Lysine N-Methyltransferase (EC 2.1.1.43) ; NSD2 protein, human (EC 2.1.1.43) ; DICER1 protein, human (EC 3.1.26.3) ; Ribonuclease III (EC 3.1.26.3) ; DEAD-box RNA Helicases (EC 3.6.4.13) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	2017-12-12
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.201704028
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Article ; Online: On-site remodeling at chromatin: How multiprotein complexes are rebuilt during DNA repair and transcriptional activation.

Papadopoulou, Thaleia / Richly, Holger

BioEssays : news and reviews in molecular, cellular and developmental biology

2016 Volume 38, Issue 11, Page(s) 1130–1140

Abstract: In this review, we discuss a novel on-site remodeling function that is mediated by the H2A-ubiquitin binding protein ZRF1. ZRF1 facilitates the remodeling of multiprotein complexes at chromatin and lies at the heart of signaling processes that occur at ... ...

Abstract	In this review, we discuss a novel on-site remodeling function that is mediated by the H2A-ubiquitin binding protein ZRF1. ZRF1 facilitates the remodeling of multiprotein complexes at chromatin and lies at the heart of signaling processes that occur at DNA damage sites and during transcriptional activation. In nucleotide excision repair ZRF1 remodels E3 ubiquitin ligase complexes at the damage site. During embryonic stem cell differentiation, it contributes to retinoic acid-mediated gene activation by altering the subunit composition of the Mediator complex. We postulate that ZRF1 operates in conjunction with cellular remodeling machines and suggest that on-site remodeling might be a hallmark of many chromatin-associated signaling pathways. We discuss yet unexplored functions of ZRF1-mediated remodeling in replication and double strand break repair. In conclusion, we postulate that on-site remodeling of multiprotein complexes is essential for the timing of chromatin signaling processes.
MeSH term(s)	Animals ; Chromatin Assembly and Disassembly ; DNA Repair ; DNA-Binding Proteins/metabolism ; Humans ; Multiprotein Complexes/metabolism ; Oncogene Proteins/metabolism ; Transcriptional Activation
Chemical Substances	DNA-Binding Proteins ; DNAJC2 protein, human ; Multiprotein Complexes ; Oncogene Proteins
Language	English
Publishing date	2016-11
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	50140-2
ISSN	1521-1878 ; 0265-9247
ISSN (online)	1521-1878
ISSN	0265-9247
DOI	10.1002/bies.201600094
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