Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Nilisha Pokhrel"'
Autor:
Jaigeeth Deveryshetty, Rahul Chadda, Jenna R. Mattice, Simrithaa Karunakaran, Michael J. Rau, Katherine Basore, Nilisha Pokhrel, Noah Englander, James A. J. Fitzpatrick, Brian Bothner, Edwin Antony
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-16 (2023)
Abstract Homologous recombination (HR) is an essential double-stranded DNA break repair pathway. In HR, Rad52 facilitates the formation of Rad51 nucleoprotein filaments on RPA-coated ssDNA. Here, we decipher how Rad52 functions using single-particle
Externí odkaz:
https://doaj.org/article/01f000207b0349d299eef6c4244d2fbc
Autor:
Poonam Roshan, Sahiti Kuppa, Jenna R. Mattice, Vikas Kaushik, Rahul Chadda, Nilisha Pokhrel, Brunda R. Tumala, Aparna Biswas, Brian Bothner, Edwin Antony, Sofia Origanti
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-19 (2023)
Abstract Errors in chromosome segregation underlie genomic instability associated with cancers. Resolution of replication and recombination intermediates and protection of vulnerable single-stranded DNA (ssDNA) intermediates during mitotic progressio
Externí odkaz:
https://doaj.org/article/65036afea1644453947715d045612938
Autor:
Sahiti Kuppa, Jaigeeth Deveryshetty, Rahul Chadda, Jenna R. Mattice, Nilisha Pokhrel, Vikas Kaushik, Angela Patterson, Nalini Dhingra, Sushil Pangeni, Marisa K. Sadauskas, Sajad Shiekh, Hamza Balci, Taekjip Ha, Xiaolan Zhao, Brian Bothner, Edwin Antony
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-16 (2022)
The single stranded DNA binding protein RPA coordinates DNA metabolism using multiple protein and DNA interaction domains. Here, the authors show that the chaperone-like protein Rtt105 staples RPA domains to prevent untimely protein interactions.
Externí odkaz:
https://doaj.org/article/e99b58d62524498db2c7354c42751eca
Autor:
Luke A. Yates, Ricardo J. Aramayo, Nilisha Pokhrel, Colleen C. Caldwell, Joshua A. Kaplan, Rajika L. Perera, Maria Spies, Edwin Antony, Xiaodong Zhang
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
Replication Protein A (RPA) coats single stranded DNA (ssDNA) generated during DNA recombination, replication and repair. Here the authors present a structural model suggesting how RPA’s DNA-binding domains promote cooperative assembly of multiple
Externí odkaz:
https://doaj.org/article/8d342a9ef98841d4b568cbf8c3f546c6
Publikováno v:
Water Research X, Vol 1, Iss , Pp - (2018)
Progress towards a more circular phosphorus economy necessitates development of innovative water treatment systems which can reversibly remove inorganic phosphate (Pi) to ultra-low levels (
Externí odkaz:
https://doaj.org/article/5b57cf69cbd640e3b642b86d23a6d6b8
Autor:
Jaigeeth Deveryshetty, Rahul Chadda, Jenna Mattice, Simrithaa Karunakaran, Michael J. Rau, Katherine Basore, Nilisha Pokhrel, Noah Englander, James A.J. Fitzpatrick, Brian Bothner, Edwin Antony
Homologous recombination (HR) is a pathway for the accurate repair of double-stranded DNA breaks, which are resected to yield single-strand DNA (ssDNA). Rad52 promotes HR by facilitating formation of Rad51 nucleoprotein filaments on ssDNA. Using sing
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::93228499994af2205f8e05cdea0fe869
https://doi.org/10.1101/2023.02.05.527205
https://doi.org/10.1101/2023.02.05.527205
Autor:
Sahiti Kuppa, Jaigeeth Deveryshetty, Rahul Chadda, Jenna Mattice, Nilisha Pokhrel, Vikas Kaushik, Angela Patterson, Nalini Dhingra, Sushil Pangeni, Marisa K. Sadauskas, Sajad Shiekh, Hamza Balci, Taekjip Ha, Xiaolan Zhao, Brian Bothner, Edwin Antony
Replication Protein A (RPA) binds to single-stranded DNA (ssDNA) and recruits over three dozen RPA-interacting proteins (RIPs) to coordinate multiple aspects of DNA metabolism including DNA replication, repair, and recombination. Rtt105 is a molecula
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e5a74b6ec7daa2d25b925bf804c690c9
https://doi.org/10.1101/2022.02.05.479199
https://doi.org/10.1101/2022.02.05.479199
Publikováno v:
Journal of Plant Pathology. 105:619-619
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8c6518b8473be682ecfe4eb929e576f5
https://doi.org/10.1007/s42161-023-01328-x
https://doi.org/10.1007/s42161-023-01328-x
Publikováno v:
Methods Mol Biol
Methods in Molecular Biology ISBN: 9781071612897
Methods in Molecular Biology ISBN: 9781071612897
Replication protein A (RPA) is an essential single-stranded DNA (ssDNA)-binding protein that sequesters ssDNA and protects it from nucleolytic degradation. The RPA-ssDNA nucleoprotein acts as a hub to recruit over two dozen DNA metabolic enzymes onto
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bff417016284a692d95f0ef68b1c80de
https://pubmed.ncbi.nlm.nih.gov/33847957
https://pubmed.ncbi.nlm.nih.gov/33847957
Autor:
Brian Bothner, Faiz Ahmad, Edwin Antony, Angela Patterson, Jaigeeth Deveryshetty, Jenna Mattice, Nilisha Pokhrel
Publikováno v:
Nucleic Acids Research
Replication protein A (RPA) binds to single-stranded DNA (ssDNA) and interacts with over three dozen enzymes and serves as a recruitment hub to coordinate most DNA metabolic processes. RPA binds ssDNA utilizing multiple oligosaccharide/oligonucleotid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81cc3ac289dd34c6e42c8eea9c99e22c
https://pubmed.ncbi.nlm.nih.gov/33444457
https://pubmed.ncbi.nlm.nih.gov/33444457