Zobrazeno 1 - 10
of 37
pro vyhledávání: '"Gopinath, Rangam"'
Autor:
Don-Marc Franchini, Chun-Fung Chan, Hugh Morgan, Elisabetta Incorvaia, Gopinath Rangam, Wendy Dean, Fatima Santos, Wolf Reik, Svend K Petersen-Mahrt
Publikováno v:
PLoS ONE, Vol 9, Iss 7, p e97754 (2014)
Base modifications of cytosine are an important aspect of chromatin biology, as they can directly regulate gene expression, while DNA repair ensures that those modifications retain genome integrity. Here we characterize how cytosine DNA deaminase AID
Externí odkaz:
https://doaj.org/article/dfe19d6006ca47379c766b9bf31defc3
Simultaneous in vitro characterisation of DNA deaminase function and associated DNA repair pathways.
Autor:
Don-Marc Franchini, Elisabetta Incorvaia, Gopinath Rangam, Heather A Coker, Svend K Petersen-Mahrt
Publikováno v:
PLoS ONE, Vol 8, Iss 12, p e82097 (2013)
During immunoglobulin (Ig) diversification, activation-induced deaminase (AID) initiates somatic hypermutation and class switch recombination by catalysing the conversion of cytosine to uracil. The synergy between AID and DNA repair pathways is funda
Externí odkaz:
https://doaj.org/article/dfd9a6c414834b2e86a2da703ad6734e
Publikováno v:
PLoS ONE, Vol 7, Iss 8, p e43279 (2012)
Activation induced deaminase (AID) deaminates cytosine to uracil, which is required for a functional humoral immune system. Previous work demonstrated, that AID also deaminates 5-methylcytosine (5 mC). Recently, a novel vertebrate modification (5-hyd
Externí odkaz:
https://doaj.org/article/b634379c999545aeb492b570e319c73d
Autor:
Maria T. Simon, Isabelle Robert, Vincent Heyer, Kerstin-Maike Schmitz, Sara Milosevic, Sarah L. Maslen, Mark Skehel, Katharina L. Willmann, Siim Pauklin, Bernardo Reina-San-Martin, Gopinath Rangam, Svend K. Petersen-Mahrt, Ebe Schiavo
Publikováno v:
The Journal of Experimental Medicine
Antibody diversification requires the DNA deaminase AID to induce DNA instability at immunoglobulin (Ig) loci upon B cell stimulation. For efficient cytosine deamination, AID requires single-stranded DNA and needs to gain access to Ig loci, with RNA
Publikováno v:
Synthesis. :1467-1472
The development of new synthetic probes to study the mechanism of Uracil-DNA glycosylase is described. 4'-C-Alkylated 2'-deoxyuridines were synthesized and incorporated site-specifically into oligonucleotides. These compounds were subsequently employ
Autor:
Elisabetta Incorvaia, Fátima Santos, Hugh Morgan, Svend K. Petersen-Mahrt, Gopinath Rangam, Don-Marc Franchini, Wendy Dean, CF Chan, Wolf Reik
Publikováno v:
PLoS ONE
PLoS ONE, Vol 9, Iss 7, p e97754 (2014)
PLoS ONE, Vol 9, Iss 7, p e97754 (2014)
Base modifications of cytosine are an important aspect of chromatin biology, as they can directly regulate gene expression, while DNA repair ensures that those modifications retain genome integrity. Here we characterize how cytosine DNA deaminase AID
Publikováno v:
Chem. Commun.. :1692-1694
Herein we describe the beneficial impact of immobilized 4'C-modified primer probes on detecting single nucleotide variations in arrayed primer extension by a DNA polymerase.
Autor:
Svend K. Petersen-Mahrt, Heather A. Coker, Gopinath Rangam, Elisabetta Incorvaia, Don-Marc Franchini
Publikováno v:
PLoS ONE, Vol 8, Iss 12, p e82097 (2013)
PLoS ONE
PLoS ONE
During immunoglobulin (Ig) diversification, activation-induced deaminase (AID) initiates somatic hypermutation and class switch recombination by catalysing the conversion of cytosine to uracil. The synergy between AID and DNA repair pathways is funda
Publikováno v:
Rangam, G, Schmitz, K-M, Cobb, A J A & Petersen-Mahrt, S K 2012, ' AID Enzymatic Activity Is Inversely Proportional to the Size of Cytosine C5 Orbital Cloud ', PL o S One, vol. 7, no. 8 . https://doi.org/10.1371/journal.pone.0043279
PLoS ONE
PLoS ONE, Vol 7, Iss 8, p e43279 (2012)
PLoS ONE
PLoS ONE, Vol 7, Iss 8, p e43279 (2012)
Activation induced deaminase (AID) deaminates cytosine to uracil, which is required for a functional humoral immune system. Previous work demonstrated, that AID also deaminates 5-methylcytosine (5 mC). Recently, a novel vertebrate modification (5-hyd
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28ecd9eb0cb919e773991926ae725ea9
https://kclpure.kcl.ac.uk/ws/files/61055862/Aid_Enzymatic_Activity_RANGAM_Accepted18July2012_GOLD_VoR.pdf
https://kclpure.kcl.ac.uk/ws/files/61055862/Aid_Enzymatic_Activity_RANGAM_Accepted18July2012_GOLD_VoR.pdf
Publikováno v:
Chembiochem : a European journal of chemical biology. 10(10)
Finding the right fit: Herein, we report on the development of novel steric probes and present initial insights into their interplay with DNA polymerases. Our findings provide experimental evidence for varied enzyme-substrate interactions that might