Zobrazeno 1 - 10
of 97
pro vyhledávání: '"ASHOK S. BHAGWAT"'
Autor:
Philip Barbulescu, Chetan K. Chana, Matthew K. Wong, Ines Ben Makhlouf, Jeffrey P. Bruce, Yuqing Feng, Alexander F. A. Keszei, Cassandra Wong, Rukshana Mohamad-Ramshan, Laura C. McGary, Mohammad A. Kashem, Derek F. Ceccarelli, Stephen Orlicky, Yifei Fang, Huihui Kuang, Mohammad Mazhab-Jafari, Rossanna C. Pezo, Ashok S. Bhagwat, Trevor J. Pugh, Anne-Claude Gingras, Frank Sicheri, Alberto Martin
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-19 (2024)
Abstract A diverse antibody repertoire is essential for humoral immunity. Antibody diversification requires the introduction of deoxyuridine (dU) mutations within immunoglobulin genes to initiate somatic hypermutation (SHM) and class switch recombina
Externí odkaz:
https://doaj.org/article/67ed2463e18d49fc9638e7762e1de9a6
Autor:
Yasha Butt, Ramin Sakhtemani, Rukshana Mohamad-Ramshan, Michael S. Lawrence, Ashok S. Bhagwat
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-13 (2024)
Abstract The APOBEC3 enzymes convert cytosines in single-stranded DNA to uracils to protect against viruses and retrotransposons but can contribute to mutations that diversify tumors. To understand the mechanism of mutagenesis, we map the uracils res
Externí odkaz:
https://doaj.org/article/820624b331134de1a53888915fff2f2b
Autor:
Adam Langenbucher, Danae Bowen, Ramin Sakhtemani, Elodie Bournique, Jillian F. Wise, Lee Zou, Ashok S. Bhagwat, Rémi Buisson, Michael S. Lawrence
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
The APOBEC mutation signature contributes to a significant percentage of human cancers. Here the authors via biochemical and computational analyses shed light on how DNA primary sequence and secondary structure jointly influence A3A substrate optimal
Externí odkaz:
https://doaj.org/article/0df7d51a696e4dfaa11c6266dbb37d50
Autor:
Ramin Sakhtemani, Madusha L W Perera, Daniel Hübschmann, Reiner Siebert, Michael S Lawrence, Ashok S Bhagwat
Publikováno v:
Nucleic Acids Research. 50:5145-5157
Activation-induced deaminase (AID) is a DNA-cytosine deaminase that mediates maturation of antibodies through somatic hypermutation and class-switch recombination. While it causes mutations in immunoglobulin heavy and light chain genes and strand bre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a7b0bef94359c234f1c720d1e41f567
https://doi.org/10.1093/nar/gkac296
https://doi.org/10.1093/nar/gkac296
Publikováno v:
PLoS Genetics, Vol 14, Iss 7, p e1007516 (2018)
Recombination and mutagenesis are elevated by active transcription. The correlation between transcription and genome instability is largely explained by the topological and structural changes in DNA and the associated physical obstacles generated by
Externí odkaz:
https://doaj.org/article/85e0d7d26afc48aa8b90fb882a5aa5a4
Autor:
Jessica A. Stewart, Javier M. Di Noia, Amy Hin Yan Tong, Diana Nakib, Maribel Berru, Alberto Martin, Katherine Chan, Noé Seija Desivo, Gholam Ali Kardar, James R. Carlyle, Daniel Durocher, Rukshana Mohamad-Ramshan, Yuqing Feng, Jason Moffat, Madusha L. W. Perera, Rossanna C. Pezo, Alejandro Álvarez-Quilón, Philip Barbulescu, Ashok S. Bhagwat, Gavin Li, Conglei Li
Publikováno v:
Nature
Activation-induced cytidine deaminase (AID) catalyses the deamination of deoxycytidines to deoxyuracils within immunoglobulin genes to induce somatic hypermutation and class-switch recombination1,2. AID-generated deoxyuracils are recognized and proce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e9900ef9c698a316ab01d156a02d6c7
https://doi.org/10.1038/s41586-021-04144-4
https://doi.org/10.1038/s41586-021-04144-4
A novel class of chemicals that react with abasic sites in DNA and specifically kill B cell cancers.
Publikováno v:
PLoS ONE, Vol 12, Iss 9, p e0185010 (2017)
Most B cell cancers overexpress the enzyme activation-induced deaminase at high levels and this enzyme converts cytosines in DNA to uracil. The constitutive expression of this enzyme in these cells greatly increases the uracil content of their genome
Externí odkaz:
https://doaj.org/article/4f4fe82052ae4e32bfee8ea4e7590c50
Publikováno v:
Virology
APOBEC3 family of DNA-cytosine deaminases inactivate and mutate several human viruses. We constructed a human cell line that is inducible for EGFP-tagged APOBEC3A and found A3A predominantly in the nuclei. When these cells were infected with Herpes S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46e040408891992697b13946cafc598a
https://doi.org/10.1016/j.virol.2019.08.012
https://doi.org/10.1016/j.virol.2019.08.012
Autor:
Ashok S. Bhagwat, Ramin Sakhtemani, Vimukthi Senevirathne, Roger Pique-Regi, Jessica A. Stewart, Madusha L. W. Perera, Michael S. Lawrence
Publikováno v:
J Biol Chem
Activation-induced deaminase (AID) and apolipoprotein B mRNA-editing enzyme catalytic subunit (APOBEC) enzymes convert cytosines to uracils, creating signature mutations that have been used to predict sites targeted by these enzymes. Mutation-based t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::651723b17ec5a24e3a2ee52fd952f322
https://doi.org/10.1074/jbc.ra119.008053
https://doi.org/10.1074/jbc.ra119.008053
Autor:
Jessica A, Stewart, Ashok S, Bhagwat
Publikováno v:
DNA Repair. 118:103381
Murine FAM72A, mFAM72A, binds the nuclear form of uracil-DNA glycosylase, mUNG2, inhibits its activity and causes its degradation. In immunoprecipitation assays the human paralog, hFAM72A, binds hUNG2 and is a potential anti-cancer drug target becaus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61cec1de1386d07b1fa01e166f7c441f
https://doi.org/10.1016/j.dnarep.2022.103381
https://doi.org/10.1016/j.dnarep.2022.103381