Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Sahiti Kuppa"'
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
Dynamic states of eIF6 and SDS variants modulate interactions with uL14 of the 60S ribosomal subunit
Autor:
Jonah Elliff, Aparna Biswas, Poonam Roshan, Sahiti Kuppa, Angela Patterson, Jenna Mattice, Mathivanan Chinnaraj, Ryan Burd, Sarah E Walker, Nicola Pozzi, Edwin Antony, Brian Bothner, Sofia Origanti
Publikováno v:
Nucleic Acids Research. 51:1803-1822
Assembly of ribosomal subunits into active ribosomal complexes is integral to protein synthesis. Release of eIF6 from the 60S ribosomal subunit primes 60S to associate with the 40S subunit and engage in translation. The dynamics of eIF6 interaction w
Autor:
Jessica L. Norris, Lindsey O. Rogers, Kara G. Pytko, Rachel L. Dannenberg, Samuel Perreault, Vikas Kaushik, Sahiti Kuppa, Edwin Antony, Mark Hedglin
In humans, DNA polymerase δ (Pol δ) holoenzymes, comprised of Pol δ and the processivity sliding clamp, proliferating cell nuclear antigen (PCNA), carry out DNA synthesis during lagging strand DNA replication, initiation of leading strand DNA repl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::743779c4df651587c9b5d785de182cab
https://doi.org/10.1101/2023.05.09.539896
https://doi.org/10.1101/2023.05.09.539896
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
Autor:
Silvia Hormeno, Oliver J. Wilkinson, Clara Aicart-Ramos, Sahiti Kuppa, Edwin Antony, Mark S. Dillingham, Fernando Moreno-Herrero
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
Hormeno, S, Wilkinson, O J, Aicart-Ramos, C, Kuppa, S, Antony, E, Dillingham, M S & Moreno-Herrero, F 2022, ' Human HELB is a processive motor protein that catalyzes RPA clearance from single-stranded DNA ', Proceedings of the National Academy of Sciences of the United States of America, vol. 119, no. 15, e2112376119 . https://doi.org/10.1073/pnas.2112376119
instname
Hormeno, S, Wilkinson, O J, Aicart-Ramos, C, Kuppa, S, Antony, E, Dillingham, M S & Moreno-Herrero, F 2022, ' Human HELB is a processive motor protein that catalyzes RPA clearance from single-stranded DNA ', Proceedings of the National Academy of Sciences of the United States of America, vol. 119, no. 15, e2112376119 . https://doi.org/10.1073/pnas.2112376119
Human DNA helicase B (HELB) is a poorly characterized helicase suggested to play both positive and negative regulatory roles in DNA replication and recombination. In this work, we used bulk and single-molecule approaches to characterize the biochemic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c00eb3c5b3374c5497a5bb49fe18495e
http://hdl.handle.net/10261/266694
http://hdl.handle.net/10261/266694
Autor:
Joseph S. Beckman, Ryan A. Mehl, Rachel Franklin, Edwin Antony, Subhashis Jana, Sahiti Kuppa, Riley M. Bednar, Richard B. Cooley
Publikováno v:
ACS Chem Biol
The ability to site-specifically modify proteins at multiple sites in vivo will enable the study of protein function in its native environment with unprecedented levels of detail. Here, we present a versatile two-step strategy to meet this goal invol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8219d7a77abf10fd1f1655c4e4a6403f
https://europepmc.org/articles/PMC9377405/
https://europepmc.org/articles/PMC9377405/
Autor:
Edwin Antony, Urvashi Mahajan, Susana Gonzalo, Simona Graziano, Barbara Teodoro-Castro, Alessandro Vindigni, Sahiti Kuppa, Elena Shashkova, Jessica Jackson, Núria Coll-Bonfill
Publikováno v:
The Journal of Biological Chemistry
Lamin A/C provides a nuclear scaffold for compartmentalization of genome function that is important for genome integrity. Lamin A/C dysfunction is associated with cancer, aging, and degenerative diseases. The mechanisms whereby lamin A/C regulates ge
Autor:
Jessica Jackson, Teodoro-Castro B, Alessandro Vindigni, Elena Shashkova, Sahiti Kuppa, Núria Coll-Bonfill, Simona Graziano, Edwin Antony, Urvashi Mahajan, Susana Gonzalo
Lamins provide a nuclear scaffold for compartmentalization of genome function that is important for genome integrity. The mechanisms whereby lamins regulate genome stability remain poorly understood. Here, we demonstrate a crucial role for A-type lam
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::efb1a09dd044a5d29c2a63fead91778d
https://doi.org/10.1101/2021.06.22.449466
https://doi.org/10.1101/2021.06.22.449466
Autor:
Hormeno S, Mark S. Dillingham, Sahiti Kuppa, Oliver J Wilkinson, Clara Aicart-Ramos, Fernando Moreno-Herrero, Edwin Antony
Publikováno v:
bioRxiv
Human HELB is a poorly-characterised helicase suggested to play both positive and negative regulatory roles in DNA replication and recombination. In this work, we used bulk and single molecule approaches to characterise the biochemical activities of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f4e5f9e7164b6c3ebbbdf7ed33d3b5c
https://doi.org/10.1101/2021.05.27.445972
https://doi.org/10.1101/2021.05.27.445972