Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Nikolas H. Chmiel"'
Autor:
Troy E. Messick, Sheila S. David, Leemor Joshua-Tor, Nikolas H. Chmiel, Michael R. Langer, Marie Pierre Golinelli
Publikováno v:
Biochemistry. 41:3931-3942
The Escherichia coli DNA repair enzyme MutY plays an important role in the recognition and repair of 7,8-dihydro-8-oxo-2'-deoxyguanosine-2'-deoxyadenosine (OG*A) mismatches in DNA. MutY prevents DNA mutations caused by the misincorporation of A oppos
Autor:
G. T. Williams, Julie Helen Maynard, Jeremy Peter Cheadle, Nikolas H. Chmiel, D. Rhodri Davies, Angela Hodges, Sheila S. David, Alison L. Livingston, Nicholas I. Fleming, Nada Al-Tassan, Julian R. Sampson
Publikováno v:
Nature Genetics. 30:227-232
Inherited defects of base excision repair have not been associated with any human genetic disorder, although mutations of the genes mutM and mutY, which function in Escherichia coli base excision repair, lead to increased transversions of G:C to T:A1
Publikováno v:
Organic Letters. 2:1341-1344
[formula: see text] The DNA repair adenine glycosylase MutY efficiently recognizes 7-deaza-2'-deoxyadenosine (Z) and its nonpolar isostere 4-methylindole beta-deoxynucleoside (M) opposite 7,8-dihydro-8-oxo-2'-deoxyguanosine (OG) and G in DNA. Both wi
Publikováno v:
Synthesis. 1998:1009-1014
Publikováno v:
ChemInform. 28
Publikováno v:
ChemInform. 29
Publikováno v:
Chmiel, Nikolas H; Rio, Donald C; & Doudna, Jennifer A. (2006). Distinct contributions of KH domains to substrate binding affinity of Drosophila P-element somatic inhibitor protein. RNA-A Publication of the RNA Society, 12(2), 283-291. UC Berkeley: Retrieved from: http://www.escholarship.org/uc/item/0800x6xw
Drosophila P-element somatic inhibitor protein (PSI) regulates splicing of the P-element transposase pre-mRNA by binding a pseudo-splice site upstream of the authentic splice site using four tandem KH-type RNA binding motifs. While the binding domain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d73dc4987274f8b6b8be989905ba0adf
http://www.escholarship.org/uc/item/0800x6xw
http://www.escholarship.org/uc/item/0800x6xw
Publikováno v:
DNA repair. 4(3)
Escherichia coli MutY and its eukaryotic homologues play an important role in preventing mutations by removing adenine from 7,8-dihydro-8-oxo-2′-deoxyguanosine (OG):A mismatches. It has recently been demonstrated that inherited biallelic mutations
Autor:
Sheila S. David, Alison L. Livingston, Nikolas H. Chmiel, Jacqueline K. Barton, Elizabeth M. Boon
MutY, like many DNA base excision repair enzymes, contains a [4Fe4S] 2+ cluster of undetermined function. Electrochemical studies of MutY bound to a DNA-modified gold electrode demonstrate that the [4Fe4S] cluster of MutY can be accessed in a DNA-med
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::343cdbc9502b9ecb2225250a4f82c1e3
https://europepmc.org/articles/PMC240652/
https://europepmc.org/articles/PMC240652/
Publikováno v:
Journal of molecular biology. 327(2)
The oxidized guanine lesion 7,8-dihydro-8-oxo-2'-deoxyguanosine (OG) is highly mutagenic, resulting in G:C to T:A transversion mutations in the absence of repair. The Escherichia coli adenine glycosylase MutY and its human homolog (hMYH) play an impo