Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Daniel Achinko"'
Autor:
Manoj Kumar Kashyap, Hiren Karathia, Deepak Kumar, Roberto Vera Alvarez, Jose Vicente Forero-Forero, Eider Moreno, Juliana Velez Lujan, Carlos Ivan Amaya-Chanaga, Newton Medeiros Vidal, Zhe Yu, Emanuela M. Ghia, Paula A. Lengerke-Diaz, Daniel Achinko, Michael Y. Choi, Laura Z. Rassenti, Leonardo Mariño-Ramírez, Stephen M. Mount, Sridhar Hannenhalli, Thomas J. Kipps, Januario E. Castro
Publikováno v:
Molecular Therapy: Nucleic Acids, Vol 35, Iss 2, Pp 102202- (2024)
Splicing factor 3b subunit 1 (SF3B1) is the largest subunit and core component of the spliceosome. Inhibition of SF3B1 was associated with an increase in broad intron retention (IR) on most transcripts, suggesting that IR can be used as a marker of s
Externí odkaz:
https://doaj.org/article/adf59c81f6f94126a63b606708311ab5
Autor:
Anton Dormer, Mahesh Narayanan, Jerome Schentag, Daniel Achinko, Elton Norman, James Kerrigan, Gary Jay, William Heydorn
Publikováno v:
Journal of Pain Research. 16:1487-1498
Autor:
Manoj Kumar Kashyap, Hiren Karathia, Deepak Kumar, Roberto Vera Alvarez, Paula A Lengerke-Diaz, Jose Vicente Forero-Forero, Eider Moreno, Juliana Velez Lujan, Carlos Ivan Amaya-Chanaga, Newton Medeiros Vidal, Zhe Yu, Daniel Achinko, Emanuela M. Ghia, Michael Y. Choi, Laura Z. Rassenti, Leonardo Mariño-Ramírez, Stephen M. Mount, Sridhar Hannenhalli, Thomas J. Kipps, Januario E. Castro
BackgroundAlternative splicing (AS) is a fundamental process in eukaryotes contributing to the diversity of mRNA isoforms with variable ratios of intron/exon. SF3B1 is a pivotal protein of the spliceosome machinery. Mutations in the SF3B1 gene have p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e9780fc833c4337eeaff49ae6153d3bf
https://doi.org/10.21203/rs.3.rs-1622375/v1
https://doi.org/10.21203/rs.3.rs-1622375/v1
Publikováno v:
BMC Proceedings
BMC Proceedings, Vol 6, Iss Suppl 6, p P1 (2012)
BMC Proceedings, Vol 6, Iss Suppl 6, p P1 (2012)
Cathepsin B is a lysosomal papain-like cysteine peptidase that is expressed in all tissues and functions primarily as an exopeptidase through its carboxydipeptidyl activity. Together with other cathepsins, it is involved in the degradation of protein