LIVIVO - Search results -

Search results

Result 1 - 8 of total 8

Search options

Article ; Online: Cohesin loading and sliding.

Ocampo-Hafalla, Maria T / Uhlmann, Frank

2011 Volume 124, Issue Pt 5, Page(s) 685–691

Abstract: Cohesin is best known as a crucial component of chromosomal stability. Composed of several essential subunits in budding yeast, cohesin forms a ring-like complex that is thought to embrace sister chromatids, thereby physically linking them until their ... ...

Abstract	Cohesin is best known as a crucial component of chromosomal stability. Composed of several essential subunits in budding yeast, cohesin forms a ring-like complex that is thought to embrace sister chromatids, thereby physically linking them until their timely segregation during cell division. The ability of cohesin to bind chromosomes depends on the Scc2-Scc4 complex, which is viewed as a loading factor for cohesin onto DNA. Notably, in addition to its canonical function in sister chromatid cohesion, cohesin has also been implicated in gene regulation and development in organisms ranging from yeast to human. Despite its importance, both as a mediator of sister chromatid cohesion and as a modulator of gene expression, the nature of the association of cohesin with chromosomes that enables it to fulfil both of these roles remains incompletely understood. The mechanism by which cohesin is loaded onto chromosomes, and how cohesin and the related condensin and Smc5-Smc6 complexes promote DNA interactions require further elucidation. In this Commentary, we critically review the evidence for cohesin loading and its subsequent apparent sliding along chromosomes, and discuss the implications gained from cohesin localisation studies for its important functions in chromosome biology.
MeSH term(s)	Adenosine Triphosphatases/metabolism ; Adenosine Triphosphate/metabolism ; Cell Cycle Proteins/chemistry ; Cell Cycle Proteins/metabolism ; Chromatids/metabolism ; Chromosomal Proteins, Non-Histone/chemistry ; Chromosomal Proteins, Non-Histone/metabolism ; Chromosomes/metabolism ; DNA/metabolism ; DNA-Binding Proteins/metabolism ; Humans ; Multiprotein Complexes/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Cohesins
Chemical Substances	Cell Cycle Proteins ; Chromosomal Proteins, Non-Histone ; DNA-Binding Proteins ; Multiprotein Complexes ; SCC2 protein, S cerevisiae ; SCC4 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; condensin complexes ; Adenosine Triphosphate (8L70Q75FXE) ; DNA (9007-49-2) ; Adenosine Triphosphatases (EC 3.6.1.-)
Language	English
Publishing date	2011-02-14
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.073866
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1200: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 14: Show issues

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article: Cohesin loading and sliding

Ocampo-Hafalla, Maria T / Uhlmann, Frank

Journal of cell science. 2011 Mar. 1, v. 124, no. 5

2011

Abstract	Cohesin is best known as a crucial component of chromosomal stability. Composed of several essential subunits in budding yeast, cohesin forms a ring-like complex that is thought to embrace sister chromatids, thereby physically linking them until their timely segregation during cell division. The ability of cohesin to bind chromosomes depends on the Scc2-Scc4 complex, which is viewed as a loading factor for cohesin onto DNA. Notably, in addition to its canonical function in sister chromatid cohesion, cohesin has also been implicated in gene regulation and development in organisms ranging from yeast to human. Despite its importance, both as a mediator of sister chromatid cohesion and as a modulator of gene expression, the nature of the association of cohesin with chromosomes that enables it to fulfil both of these roles remains incompletely understood. The mechanism by which cohesin is loaded onto chromosomes, and how cohesin and the related condensin and Smc5-Smc6 complexes promote DNA interactions require further elucidation. In this Commentary, we critically review the evidence for cohesin loading and its subsequent apparent sliding along chromosomes, and discuss the implications gained from cohesin localisation studies for its important functions in chromosome biology.
Language	English
Dates of publication	2011-0301
Size	p. 685-691.
Publishing place	The Company of Biologists Limited
Document type	Article
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Bonn / Germany

Z 4' 67/94: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

Article: Displacement and re-accumulation of centromeric cohesin during transient pre-anaphase centromere splitting.

Ocampo-Hafalla, Maria T / Katou, Yuki / Shirahige, Katsuhiko / Uhlmann, Frank

Chromosoma

2007 Volume 116, Issue 6, Page(s) 531–544

Abstract: The ring-shaped cohesin complex links sister chromatids until their timely segregation during mitosis. Cohesin is enriched at centromeres where it provides the cohesive counterforce to bipolar tension produced by the mitotic spindle. As a consequence of ... ...

Abstract	The ring-shaped cohesin complex links sister chromatids until their timely segregation during mitosis. Cohesin is enriched at centromeres where it provides the cohesive counterforce to bipolar tension produced by the mitotic spindle. As a consequence of spindle tension, centromeric sequences transiently split in pre-anaphase cells, in some organisms up to several micrometers. This 'centromere breathing' presents a paradox, how sister sequences separate where cohesin is most enriched. We now show that in the budding yeast Saccharomyces cerevisiae, cohesin binding diminishes over centromeric sequences that split during breathing. We see no evidence for cohesin translocation to surrounding sequences, suggesting that cohesin is removed from centromeres during breathing. Two pools of cohesin can be distinguished. Cohesin loaded before DNA replication, which has established sister chromatid cohesion, disappears during breathing. In contrast, cohesin loaded after DNA replication is partly retained. As sister centromeres re-associate after transient separation, cohesin is reloaded in a manner independent of the canonical cohesin loader Scc2/Scc4. Efficient centromere re-association requires the cohesion establishment factor Eco1, suggesting that re-establishment of sister chromatid cohesion contributes to the dynamic behaviour of centromeres in mitosis. These findings provide new insights into cohesin behaviour at centromeres.
MeSH term(s)	Anaphase/genetics ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Centromere/genetics ; Centromere/metabolism ; Chromosomal Proteins, Non-Histone/genetics ; Chromosomal Proteins, Non-Histone/metabolism ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Cohesins
Chemical Substances	Cell Cycle Proteins ; Chromosomal Proteins, Non-Histone ; Nuclear Proteins ; Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2007-09-01
Publishing country	Austria
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	203083-4
ISSN	1432-0886 ; 0009-5915
ISSN (online)	1432-0886
ISSN	0009-5915
DOI	10.1007/s00412-007-0118-4
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Ub I Zs.94/5: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article: Displacement and re-accumulation of centromeric cohesin during transient pre-anaphase centromere splitting

Ocampo-Hafalla, Maria T / Katou, Yuki / Shirahige, Katsuhiko / Uhlmann, Frank

Chromosoma. 2007 Dec., v. 116, no. 6

2007

Abstract	The ring-shaped cohesin complex links sister chromatids until their timely segregation during mitosis. Cohesin is enriched at centromeres where it provides the cohesive counterforce to bipolar tension produced by the mitotic spindle. As a consequence of spindle tension, centromeric sequences transiently split in pre-anaphase cells, in some organisms up to several micrometers. This 'centromere breathing' presents a paradox, how sister sequences separate where cohesin is most enriched. We now show that in the budding yeast Saccharomyces cerevisiae, cohesin binding diminishes over centromeric sequences that split during breathing. We see no evidence for cohesin translocation to surrounding sequences, suggesting that cohesin is removed from centromeres during breathing. Two pools of cohesin can be distinguished. Cohesin loaded before DNA replication, which has established sister chromatid cohesion, disappears during breathing. In contrast, cohesin loaded after DNA replication is partly retained. As sister centromeres re-associate after transient separation, cohesin is reloaded in a manner independent of the canonical cohesin loader Scc2/Scc4. Efficient centromere re-association requires the cohesion establishment factor Eco1, suggesting that re-establishment of sister chromatid cohesion contributes to the dynamic behaviour of centromeres in mitosis. These findings provide new insights into cohesin behaviour at centromeres.
Keywords	DNA replication ; Saccharomyces cerevisiae ; breathing ; centromeres ; chromatids ; chromosome translocation ; cohesion ; mitosis ; mitotic spindle apparatus ; yeasts
Language	English
Dates of publication	2007-12
Size	p. 531-544.
Publisher	Springer-Verlag
Publishing place	Berlin/Heidelberg
Document type	Article
ZDB-ID	203083-4
ISSN	1432-0886 ; 0009-5915
ISSN (online)	1432-0886
ISSN	0009-5915
DOI	10.1007/s00412-007-0118-4
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Bonn / Germany

Z 46/355: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Rapid movement and transcriptional re-localization of human cohesin on DNA.

Davidson, Iain F / Goetz, Daniela / Zaczek, Maciej P / Molodtsov, Maxim I / Huis In 't Veld, Pim J / Weissmann, Florian / Litos, Gabriele / Cisneros, David A / Ocampo-Hafalla, Maria / Ladurner, Rene / Uhlmann, Frank / Vaziri, Alipasha / Peters, Jan-Michael

The EMBO journal

2016 Volume 35, Issue 24, Page(s) 2671–2685

Abstract: The spatial organization, correct expression, repair, and segregation of eukaryotic genomes depend on cohesin, ring-shaped protein complexes that are thought to function by entrapping DNA It has been proposed that cohesin is recruited to specific genomic ...

Abstract	The spatial organization, correct expression, repair, and segregation of eukaryotic genomes depend on cohesin, ring-shaped protein complexes that are thought to function by entrapping DNA It has been proposed that cohesin is recruited to specific genomic locations from distal loading sites by an unknown mechanism, which depends on transcription, and it has been speculated that cohesin movements along DNA could create three-dimensional genomic organization by loop extrusion. However, whether cohesin can translocate along DNA is unknown. Here, we used single-molecule imaging to show that cohesin can diffuse rapidly on DNA in a manner consistent with topological entrapment and can pass over some DNA-bound proteins and nucleosomes but is constrained in its movement by transcription and DNA-bound CCCTC-binding factor (CTCF). These results indicate that cohesin can be positioned in the genome by moving along DNA, that transcription can provide directionality to these movements, that CTCF functions as a boundary element for moving cohesin, and they are consistent with the hypothesis that cohesin spatially organizes the genome via loop extrusion.
MeSH term(s)	CCCTC-Binding Factor ; Cell Cycle Proteins/metabolism ; Chromosomal Proteins, Non-Histone/metabolism ; DNA/metabolism ; Humans ; Repressor Proteins/metabolism ; Single Molecule Imaging ; Time Factors ; Transcription, Genetic ; Cohesins
Chemical Substances	CCCTC-Binding Factor ; CTCF protein, human ; Cell Cycle Proteins ; Chromosomal Proteins, Non-Histone ; Repressor Proteins ; DNA (9007-49-2)
Language	English
Publishing date	2016-10-31
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.15252/embj.201695402
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 1808: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 100: Show issues

Order via subito

Details ▾

Article ; Online: An rtt109-independent role for vps75 in transcription-associated nucleosome dynamics.

Selth, Luke A / Lorch, Yahli / Ocampo-Hafalla, Maria T / Mitter, Richard / Shales, Michael / Krogan, Nevan J / Kornberg, Roger D / Svejstrup, Jesper Q

Molecular and cellular biology

2009 Volume 29, Issue 15, Page(s) 4220–4234

Abstract: The histone chaperone Vps75 forms a complex with, and stimulates the activity of, the histone acetyltransferase Rtt109. However, Vps75 can also be isolated on its own and might therefore possess Rtt109-independent functions. Analysis of epistatic ... ...

Abstract	The histone chaperone Vps75 forms a complex with, and stimulates the activity of, the histone acetyltransferase Rtt109. However, Vps75 can also be isolated on its own and might therefore possess Rtt109-independent functions. Analysis of epistatic miniarray profiles showed that VPS75 genetically interacts with factors involved in transcription regulation whereas RTT109 clusters with genes linked to DNA replication/repair. Additional genetic and biochemical experiments revealed a close relationship between Vps75 and RNA polymerase II. Furthermore, Vps75 is recruited to activated genes in an Rtt109-independent manner, and its genome-wide association with genes correlates with transcription rate. Expression microarray analysis identified a number of genes whose normal expression depends on VPS75. Interestingly, histone H2B dynamics at some of these genes are consistent with a role for Vps75 in histone H2A/H2B eviction/deposition during transcription. Indeed, reconstitution of nucleosome disassembly using the ATP-dependent chromatin remodeler Rsc and Vps75 revealed that these proteins can cooperate to remove H2A/H2B dimers from nucleosomes. These results indicate a role for Vps75 in nucleosome dynamics during transcription, and importantly, this function appears to be largely independent of Rtt109.
MeSH term(s)	Acetylation ; Binding Sites/genetics ; Chromatin Immunoprecipitation ; Cluster Analysis ; Gene Expression Profiling ; Genome, Fungal/genetics ; Histone Acetyltransferases/genetics ; Histone Acetyltransferases/metabolism ; Histones/genetics ; Histones/metabolism ; Lysine/genetics ; Lysine/metabolism ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Mutation ; Nucleosomes/metabolism ; Oligonucleotide Array Sequence Analysis ; Protein Binding ; RNA Polymerase II/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Transcription, Genetic
Chemical Substances	Histones ; Molecular Chaperones ; Nucleosomes ; Saccharomyces cerevisiae Proteins ; Vps75 protein, S cerevisiae ; Histone Acetyltransferases (EC 2.3.1.48) ; Rtt109 protein, S cerevisiae (EC 2.3.1.48) ; RNA Polymerase II (EC 2.7.7.-) ; RPB1 protein, S cerevisiae (EC 2.7.7.-) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	2009-05-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.01882-08
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1666: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Targeted deletion of the genes encoding NTH1 and NEIL1 DNA N-glycosylases reveals the existence of novel carcinogenic oxidative damage to DNA.

Chan, Michael K / Ocampo-Hafalla, Maria T / Vartanian, Vladimir / Jaruga, Pawel / Kirkali, Güldal / Koenig, Karen L / Brown, Stuart / Lloyd, R Stephen / Dizdaroglu, Miral / Teebor, George W

DNA repair

2009 Volume 8, Issue 7, Page(s) 786–794

Abstract: We have generated a strain of mice lacking two DNA N-glycosylases of base excision repair (BER), NTH1 and NEIL1, homologs of bacterial Nth (endonuclease three) and Nei (endonuclease eight). Although these enzymes remove several oxidized bases from DNA, ... ...

Abstract	We have generated a strain of mice lacking two DNA N-glycosylases of base excision repair (BER), NTH1 and NEIL1, homologs of bacterial Nth (endonuclease three) and Nei (endonuclease eight). Although these enzymes remove several oxidized bases from DNA, they do not remove the well-known carcinogenic oxidation product of guanine: 7,8-dihydro-8-oxoguanine (8-OH-Gua), which is removed by another DNA N-glycosylase, OGG1. The Nth1-/-Neil1-/- mice developed pulmonary and hepatocellular tumors in much higher incidence than either of the single knockouts, Nth1-/- and Neil1-/-. The pulmonary tumors contained, exclusively, activating GGT-->GAT transitions in codon 12 of K-ras of their DNA. Such transitions contrast sharply with the activating GGT-->GTT transversions in codon 12 of K-ras of the pathologically similar pulmonary tumors, which arose in mice lacking OGG1 and a second DNA N-glycosylase, MUTY. To characterize the biochemical phenotype of the knockout mice, the content of oxidative DNA base damage was analyzed from three tissues isolated from control, single and double knockout mice. The content of 8-OH-Gua was indistinguishable among all genotypes. In contrast, the content of 4,6-diamino-5-formamidopyrimidine (FapyAde) and 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyGua) derived from adenine and guanine, respectively, were increased in some but not all tissues of Neil1-/- and Neil1-/-Nth1-/- mice. The high incidence of tumors in our Nth1-/-Neil1-/- mice together with the nature of the activating mutation in the K-ras gene of their pulmonary tumors, reveal for the first time, the existence of mutagenic and carcinogenic oxidative damage to DNA which is not 8-OH-Gua.
MeSH term(s)	Animals ; Base Sequence ; Brain/metabolism ; Brain/pathology ; DNA Damage ; DNA Glycosylases/genetics ; DNA Glycosylases/metabolism ; DNA Mutational Analysis ; Deoxyribonuclease (Pyrimidine Dimer)/genetics ; Deoxyribonuclease (Pyrimidine Dimer)/metabolism ; Female ; Gas Chromatography-Mass Spectrometry ; Gene Deletion ; Genes, ras/genetics ; Guanine/analogs & derivatives ; Guanine/metabolism ; Kidney/metabolism ; Kidney/pathology ; Liver/metabolism ; Liver/pathology ; Liver Neoplasms/genetics ; Liver Neoplasms/metabolism ; Liver Neoplasms/pathology ; Lung Neoplasms/genetics ; Lung Neoplasms/metabolism ; Lung Neoplasms/pathology ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Inbred Strains ; Mice, Knockout ; Mutation ; Oxidation-Reduction ; Pyrimidines/metabolism
Chemical Substances	7,8-dihydro-8-oxoguanine ; Pyrimidines ; 2,6-diamino-4-hydroxy-5-formamidopyrimidine (133310-38-0) ; 4,6-diamino-5-N-formamidopyrimidine (5122-36-1) ; Guanine (5Z93L87A1R) ; Deoxyribonuclease (Pyrimidine Dimer) (EC 3.1.25.1) ; Nthl1 protein, mouse (EC 3.1.25.1) ; DNA Glycosylases (EC 3.2.2.-) ; Neil1 protein, mouse (EC 3.2.2.-)
Language	English
Publishing date	2009-04-05
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2071608-4
ISSN	1568-7856 ; 1568-7864
ISSN (online)	1568-7856
ISSN	1568-7864
DOI	10.1016/j.dnarep.2009.03.001
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 5555: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Repair of thymine glycol by hNth1 and hNeil1 is modulated by base pairing and cis-trans epimerization.

Ocampo-Hafalla, Maria T / Altamirano, Alvin / Basu, Ashis K / Chan, Michael K / Ocampo, Jose Eliseo A / Cummings, Archie / Boorstein, Robert J / Cunningham, Richard P / Teebor, George W

DNA repair

2006 Volume 5, Issue 4, Page(s) 444–454

Abstract: Oxidation of thymine yields 5,6-dihydroxy-5,6-dihydrothymine (thymine glycol. Tg) which, as cis 5S,6R and 5R,6S 2'-deoxyribonucleoside diastereoisomers (dTg1, dTg2), are in equilibrium with their trans 5S,6S and 5R,6R epimers. The stereoselective ... ...

Abstract	Oxidation of thymine yields 5,6-dihydroxy-5,6-dihydrothymine (thymine glycol. Tg) which, as cis 5S,6R and 5R,6S 2'-deoxyribonucleoside diastereoisomers (dTg1, dTg2), are in equilibrium with their trans 5S,6S and 5R,6R epimers. The stereoselective excision of Tg from DNA by the mammalian orthologs of E. coli DNA N-glycosylase/AP lyases Nth and Nei was reported using substrates in which Tg opposed adenine. Since we showed that Tg is the major product of oxidation of 5-methylcytosine, we asked if the opposing purine influenced stereospecific enzymatic excision. The human ortholog hNth1 released Tg2 much more rapidly than Tg1 regardless of the opposing purine. In contrast, hNeil1 released Tg non-stereoselectively, but the rate of excision was much greater when Tg opposed guanine. Remarkably, the kinetics of excision of Tg by hNth1 and hNeil1 were biphasic, describing a double exponential curve which yielded two rate constants. We suggest that the greater rate constant describes the rate of enzymatic excision of Tg. The smaller rate constant represents the equilibrium constant for the cis and trans epimerization of dTg1 and dTg2 in high molecular weight DNA. Thus, only one of the epimers of dTg1 and dTg2 are enzymatically processed but it is not yet known whether it is cis or trans. Thus, base excision repair of Tg in mammals is mediated by at least two DNA N-glycosylase/AP lyases which are affected by the nature of the diastereoisomer of dTg, the rate of cis-trans epimerization of each diastereoisomer, and the nature of the opposing purine.
MeSH term(s)	Base Pairing ; Catalysis ; DNA Damage ; DNA Glycosylases/metabolism ; DNA Repair ; Deoxyribonuclease (Pyrimidine Dimer)/metabolism ; Deoxyribose/chemical synthesis ; Escherichia coli Proteins/metabolism ; Humans ; Isomerism ; Kinetics ; Oligonucleotides/chemical synthesis ; Purines/metabolism ; Substrate Specificity ; Thymine/analogs & derivatives ; Thymine/chemistry ; Thymine/metabolism
Chemical Substances	Escherichia coli Proteins ; Oligonucleotides ; Purines ; thymine glycol (2943-56-8) ; Deoxyribose (533-67-5) ; Deoxyribonuclease (Pyrimidine Dimer) (EC 3.1.25.1) ; NTH protein, E coli (EC 3.1.25.1) ; NTHL1 protein, human (EC 3.1.25.1) ; DNA Glycosylases (EC 3.2.2.-) ; NEIL1 protein, human (EC 3.2.2.-) ; Thymine (QR26YLT7LT)
Language	English
Publishing date	2006-04-08
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2071608-4
ISSN	1568-7856 ; 1568-7864
ISSN (online)	1568-7856
ISSN	1568-7864
DOI	10.1016/j.dnarep.2005.12.004
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 5555: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito